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TCID	Name	Organismal Type	Example
2.A.1.1: The Sugar Porter (SP) Family
2.A.1.1.1	Galactose:H⁺ symporter (also transports xylose) (Hernández-Montalvo et al., 2001). Relative substrate affinities of wild-type and mutant forms of the E. coli sugar transporter GalP have been determined by solid-state NMR (Patching et al., 2008).	Bacteria	GalP of E. coli (P0AEP1)
2.A.1.1.2	Arabinose (xylose; galactose):H⁺ symporter	Bacteria	AraE of E. coli (P0AE24)
2.A.1.1.3	Xylose:H⁺ symporter. Also transports and binds D-glucose and 6-bromo-6-deoxy-D-glucose. The 3-d structure is known (Sun et al. 2012). Most of the sugar-binding residues are conserved with the human Glut-1, 2, 3 and 4 homologues.	Bacteria	XylE of E. coli (P0AGF4)
2.A.1.1.4	Glucose uniporter	Bacteria	Glf of Zymomonas mobilis
2.A.1.1.5	Hexose uniporter	Yeast	HxtO of Saccharomyces cerevisiae
2.A.1.1.6	Galactose, glucose uniporter (also transports xylose)	Yeast	Gal2 of Saccharomyces cerevisiae
2.A.1.1.7	Quinate:H⁺ symporter	Fungi	Qay of Neurospora crassa
2.A.1.1.8	Myoinositol:H⁺ symporter	Yeast	ITR1 of Saccharomyces cerevisiae
2.A.1.1.9	Lactose, galactose:H⁺ symporter	Yeast	LacP of Kluyveromyces lactis
2.A.1.1.10	Maltose:H⁺ symporter	Yeast	MAL6 of Saccharomyces cerevisiae
2.A.1.1.11	General α-glucoside H⁺ symporter (Trehalose, maltose turanose, isomaltose, α-methyl-glucoside, maltotriose, palatinose, trehalose and melezitose): H⁺ symporter, Gtr3 or Agt1 (Smit et al., 2008).	Yeast	AGT1 of Saccharomyces cerevisiae
2.A.1.1.12	Glucose uniporter (also transports dehydro-ascorbate; Maulén et al., 2003). Down-regulated in the brains of Alzheimer's disease patients (Liu et al., 2008b).	Animals	Gtr3 (Glut3) of Rattus norvegicus (rat)
2.A.1.1.13	Fructose uniporter	Animals	SLC2A5 of Homo sapiens
2.A.1.1.14	Hexose:H⁺ symporter	Plants	Hup1 of Chlorella kessleri
2.A.1.1.15	Putative sugar transporter	Archaea	Porter of Sulfolobus solfataricus
2.A.1.1.16	Low-affinity hexose (glucose, fructose, mannose, 2-deoxyglucose) uniporter. The evolution of hexose transporters in kinetoplastid protozoans has been studied (Pereira and Silber 2012).	Protozoa	Gtr2 (D2) of Leishmania donovani
2.A.1.1.17	Glucose transporter	Protozoa	Th2A of Trypanosoma brucei
2.A.1.1.18	Glucose/mannose/fructose transporter and high affinity sensor, Snf3p (regulates glucose transport via other systems)	Yeast	Snf3p of Saccharomyces cerevisiae
2.A.1.1.19	Glucose transporter and low affinity sensor, Rgt2p (regulates glucose transport in conjunction with Snf3p)	Yeast	Rgt2p of Saccharomyces cerevisiae
2.A.1.1.20	Myoinositol:H⁺ symporter, MIT	Protozoa	MIT of Leishmania donovani; most similar to ITRI of Saccharomyces cerevisiae
2.A.1.1.21	Hexose:H⁺ symporter, Ght2 (Glucose > Fructose)	Yeast	Ght2 of Schizosaccharomyces pombe
2.A.1.1.22	Hexose:H⁺ symporter, Ght6 (Fructose > Glucose)	Yeast	Ght6 of Schizosaccharomyces pombe
2.A.1.1.23	Gluconate:H⁺ symporter, Ght3	Yeast	Ght3 of Schizosaccharomyces pombe
2.A.1.1.24	Hexose (Glucose and Fructose) transporter, PfHT1	Protozoa	PfHT1 of Plasmodium falciparum
2.A.1.1.25	Myoinositol:H⁺ symporter, HMIT (also transport other inositols including scyllo-, muco- and chiro-, but not allo-inositol) (Aouameur et al., 2007). Expressed in the golgi of the hippocampus and cortex. May also transport inositoltriphosphate (Di Daniel et al., 2009).	Animals	SLC2A13 of Homo sapiens
2.A.1.1.26	Major myoinositol:H⁺ symporter, IolT	Bacteria	IolT (YdjK) of Bacillus subtilis
2.A.1.1.27	Minor myoinositol:H⁺ symporter, IolF	Bacteria	IolF of Bacillus subtilis
2.A.1.1.28	The erythrocyte/brain hexose facilitator, Gtr1 or Glut1. Also transports D-glucose, dehydroascorbate, and the flavonone, quercetin, via one channel and water via a distinct channel. Sugar transport has been suggested to function via a sliding mechanism involving several sugar binding sites (Cunningham et al., 2006). (Receptor for human T-cell leukemia virus (HTLV)) (Manel et al., 2003). Regulated by stomatin to take up dehydroascorbate (Montel-Hagen et al., 2008). Mutations cause Glut1 deficiency syndrome, a human encephalopathy that results from decreased glucose flux through the blood brain barrier (Pascual et al., 2008). Mueckler and Makepeace (2009) have presented a model of the exofacial substrate-binding site and helical folding of Glut1. Glut 1, 2, 4 and 9 are functional both in the plasma membrane and the endoplasmic reticulum (Takanaga and Frommer, 2010). Down-regulated in the brains of Alzheimer's disease patients (Liu et al., 2008b). Metabolic stress rapidly stimulates blood-brain barrier endothelial cell sugar transport by acute up-regulation of plasma membrane GLUT1 levels, possibly involving an AMP-activated kinase activity (Cura and Carruthers, 2010). Serves as a receptor for entry of human T-cell leukemia virus type-1 (HTLV-1) along with neuropilin-1 (923aas; 2 TMSs) (O14786) and heparan sulfate proteoglycans (HSPGs) (Hoshino, 2012).	Animals	SLC2A1 of Homo sapiens
2.A.1.1.29	Glucosamine/glucose uniporter, Glut-2 (may also transport dehydroascorbate (Mardones et al., 2011; Maulén et al., 2003), and cotransport water against an osmotic gradient (Naftalin, 2008))	Animals	SLC2A2 of Homo sapiens
2.A.1.1.30	Low affinity, constitutive, glucose (hexose; xylose) uniporter, Hxt4 (LGT1) (also transports arsenic trioxide [As(OH)₃] as do Hxtl, 3, 5, 7 and 9) (Liu et al., 2004)	Yeast	Hxt4 of Saccharomyces cerevisiae
2.A.1.1.31	High affinity, glucose-repressible, glucose (hexose) uniporter (Hxt6/Hxt7). Hydrophobic residue side chains in TMS5 determine substrate affinity (Kasahara et al., 2011).	Yeast	Hxt6/Hxt7 of Saccharomyces cerevisiae Hxt6 (P39003)
2.A.1.1.32	Glucose/fructose:H⁺ symporter, GlcP (Zhang et al., 1989)	Bacteria	GlcP of Synechocystis sp. (P15729)
2.A.1.1.33	Fructose:H⁺ symporter, Frt1 (Diezemann and Boles, 2003)	Yeast	Frt1 of Kluyveromyces lactis (CAC79614)
2.A.1.1.34	The broad specificity sugar/sugar alcohol (myo-inositol, glycerol, ribose, sorbitol, mannitol, xylitol, erythritol, etc) H⁺ symporter, AtPLT5 (transports a wide range of hexoses, pentoses, tetroses, sugar alcohols and a sugar acid, but not disaccharides) (Reinders et al., 2005) (expressed in roots, leaves and floral organs) (Klepek et al., 2004)	Plants	AtPLT5 of Arabidopsis thaliana (Q8VZ80)
2.A.1.1.35	The major glucose (or 2-deoxyglucose) uptake transporter, GlcP (van Wezel et al., 2005)	Bacteria	GlcP of Streptomyces coelicolor (Q7BEC4)
2.A.1.1.36	The low affinity, glucose-inducible glucose transporter, MstE (Forment et al., 2006)	Fungi	MstE of Aspergillus nidulans (Q400D8)
2.A.1.1.37	The glucose/fructose facilitator, Glut7 (SLC2A7) (a single mutation, I314V, results in loss of fructose transport but retention of glucose transport (Manolescu et al., 2005)	Animals	SLC2A7 of Homo sapiens
2.A.1.1.38	The glycerol:H⁺ symporter, Stl1p (Ferreira et al., 2005)	Yeast	Stl1p of Saccharomyces cerevisiae (NP_010825)
2.A.1.1.39	The high affinity glucose transporter, Hgt1 (Baruffini et al., 2006)	Yeast	Hgt1 of Kluyveromyces lactis (P49374)
2.A.1.1.40	The xylose facilitator, Xylhp (Nobre et al., 1999)	Yeast	Xylhp of Debaryomyces hansenii (AAR06925)
2.A.1.1.41	The D-xylose:H⁺ symporter, XylT (K_m=220 μM; inhibited competitively by 6-deoxyglucose (K_i=220 μM), but not by other sugars tested) (Chaillou et al., 1998)	Bacteria	XylT of Lactobacillus brevis (O52733)
2.A.1.1.42	The D-glucose:H⁺ symporter, GlcP (glucose uptake is inhibited by 2-deoxyglucose, mannose and galactose) (Parche et al., 2006)	Bacteria	GlcP of Bifidobacterium longum (AAN25419)
2.A.1.1.43	The monosaccharide (MST) (glucose > mannose > galactose > fructose):H⁺ symporter, MST1 (Schussler et al., 2006).	Fungi	MST1 of Geosiphon pyriformis (A0ZXK6)
2.A.1.1.44	The hexose (glucose and fructose but not galactose) transporter (Glut11; SLC2A11) (Scheepers et al., 2005)	Animals	SLC2A11 of Homo sapiens
2.A.1.1.45	Vacuolar (tonoplast) glucose transporter1, Vgt1 (important for seed germination and flowering) (Aluri and Büttner, 2007)	Plants	Vgt1 of Arabidopsis thaliana (Q8L6Z8)
2.A.1.1.46	The blastocyst/testis glucose transporter, Glut8 (Doege et al., 2000) (insulin stimulated in blastocysts) (Carayannopoulos et al., 2000).	Animals	Glut8 of Mus musculus (Q9JIF3)
2.A.1.1.47	The liver, kidney, and other tissue embryonic uric acid transporter, Glut9 (SLC2A9) (Wright et al. 2010). Mutations in this transporter cause severe renal hyperuricemia.	Animals	Glut9 of Mus musculus (Q5ERC7)
2.A.1.1.48	The pentose/hexose transporter (sugar transport protein 2), STP2. (Expressed during pollen maturation and early stages of gametophyte development) (Truernit et al., 1999)	Plants	STP2 of Arabidopsis thaliana (Q9LNV3)
2.A.1.1.49	The sink-specific, stress-regulated monosaccharide uptake porter, STP4. (Induced upon wounding or infection with bacteria or fungi; expressed in roots and flowers) (Truernit et al., 1996)	Plants	STP4 of Arabidopsis thaliana (Q39228)
2.A.1.1.50	The glucose/fructose:H⁺ symporter, STP13. Expressed in vascular tissues and induced during programmed cell death (Norholm et al., 2006)	Plants	STP13 of Arabidopsis thaliana (Q94AZ2)
2.A.1.1.51	Glucose/xylose: H⁺ symporter, Gsx1 (Leandro et al., 2006)	yeast	Gsx1 of Candida intermedia (Q2MEV7)
2.A.1.1.52	The glucose transport protein, GTP1 (Skelly et al., 1994)	Animals	GTP1 of Schistosoma mansoni (Q26579)
2.A.1.1.53	Myo-Inositol uptake porter, IolT1 (Km=0.2mM) (Krings et al., 2006).	Bacteria	IolT1 of Corynebacterium glutamicum (Q8NTX0)
2.A.1.1.54	Myo-Inositol (Km=0.45mM) uptake porter, IolT2 (Krings et al., 2006)	Bacteria	IolT2 of Corynebacterium glutamicum (Q8NL90)
2.A.1.1.55	L-arabinose:proton symporter, AraE (Sa-Nogueira and Ramos, 1997). Also transports xylose, galactose and α-1,5 arabinobiose (Ferreira and Sá-Nogueira, 2010).	Bacteria	AraE of Bacillus subtilis (P96710)
2.A.1.1.56	High affinity monosaccharide (K_M ≈ 20 �M):H⁺ symporter, Stp6 (takes up glucose, 3-O-methylglucose, mannose, fructose, galactose and to a lesser extent, xylose and ribulose. (Scholz-Starke et al., 2003)	Plants	Stp6 of Arabidopsis thaliana (Q9SFG0)
2.A.1.1.57	High affinity (15 μM) glucose (monosaccharides including xylose):H⁺ symporter, MstA (Jørgensen et al., 2007).	Fungi	MstA of Aspergillus niger (Q8J0V1)
2.A.1.1.58	Low affinity glucose:H⁺ symporter, MstC (Jørgensen et al., 2007).	Fungi	MstC of Aspergillus niger (Q8J0U9)
2.A.1.1.59	The glucose transporter, GLUT10, was originally believed to be responsible for Type 2 diabetes. It is now believed to be responsible for arterial tortuosity, a rare autosomal recessive connective tissue disease (Callewaert et al., 2007). GLUT10 transports glucose and 2-deoxy glucose (K_m=0.3 mM), and is inhibited by galactose and phloretin (Coucke et al., 2006).	Animals	SLC2A10 of Homo sapiens
2.A.1.1.60	The major hexose transporter, Htr1 (mediates the active uptake of hexoses by sugar:H⁺ symport. Can transport glucose, 3-O-methylglucose, fructose, xylose, mannose, galactose, fucose, 2-deoxyglucose and arabinose. Confers sensitivity to galactose in seedlings. K_m=20 uM for glucose) (Stadler et al., 2003; Boorer et al., 1994)	Plants	Htr1 of Arabidopsis thaliana (P23586)
2.A.1.1.61	High affinity monosaccharide (K_m = 25 �M) transporter (takes up glucose, galactose, mannose, xylose and 3-O-methylglucose, but not fructose and ribose), STP11 (expressed in pollen tubes) (Schneidereit et al., 2005)	Plants	STP11 of Arabidopsis thaliana (Q9FMX3)
2.A.1.1.62	High affinity (0.24mM) plasma membrane myoinositol-specific H⁺ symporter, INT4 (Schneider et al., 2006)	Plants	INT4 of Arabidopsis thaliana (O23492)
2.A.1.1.63	Low affinity inositol (myoinsoitol (Km = 1 mM), scylloinositol, d-chiroinositol and mucoinositol):H⁺ symporter (expressed in the anther tapetum, the vasculature, and the leaf mesophyll (Schneider et al., 2007)	Plants	INT2 of Arabidopsis thaliana (Q9C757)
2.A.1.1.64	The hexose sensor, Hxs1 (believed to be non-transporting) (Stasyk et al., 2008)	Yeast	Hxs1 of Hansenula polymorpha (B1PM37)
2.A.1.1.65	Glucose permease GlcP (Pimentel-Schmitt et al., 2008) (most similar to 2.A.1.1.32)	Bacteria	GlcP of Mycobacterium smegmatis (A0QZX3)
2.A.1.1.66	The tonoplast H⁺:Inositol symporter 1, Int1 (mediates efflux from the tonoplast to the cytoplasm (Schneider et al., 2008) (most similar to 2.A.1.1.63 and 2.A.1.1.62).	Plants	Int1 of Arabidopsis thaliana (Q8VZR6)
2.A.1.1.67	Glucose/xylose facilitator-1, GXF1 (functions by sugar uniport; low affinity (Leandro et al., 2008)	Yeast	GXF1 of Candida intermedia (Q2MDH1)
2.A.1.1.68	The Glucose Transporter/Sensor Rgt2	Yeast	Rgt2 Pichia stipitis�(A3M0N3)
2.A.1.1.69	Sugar & polyol transporter 1 (SPT1): broad specificity; takes up glucose (Schilling and Oesterhelt, 2007). Loss of the first 3 TMSs of the 12 TMSs does not prevent sugar uptake or sugar recognition but lowers substrate affinity & transport rate, and abolished H⁺ symport (Schilling and Oesterhelt, 2007).	Red algae	SPT1 of Galdieria sulphuraria (A1Z264)
2.A.1.1.70	MFS Permease	Fungi	MFS Permease of Phaeosphaeria nodurum
2.A.1.1.71	Hexose (glucose) transporter, GT4 (D2) (almost identical to 2.A.1.1.16)	Trypanosomatidae	Hexose transporter, GT4 of Leishmania mexicana (B1PLM1)
2.A.1.1.72	The kidney basolateral voltage-driven urate efflux transporter (URATv1) (orthologue of 2.A.1.1.47) (Anzai et al., 2008). Human SLC2A9a and SLC2A9b isoforms mediate electrogenic transport of urate with different characteristics in the presence of hexoses (Witkowska et al., 2012).	Animals	SLC2A9 of Homo sapiens
2.A.1.1.73	Glycerol uptake permease (Glycerol:H⁺ symporter) Stl1. (Involved in salt stress relief) (Kayingo et al. 2009) (similar to Stl1 of S. cerevisiae (2.A.1.1.38))	Yeast	Stl1 of Candida albicans (Q5A8J5)
2.A.1.1.74	The putative L-rhamnose porter, RhaY	Firmicutes, Actinobacteria	RhaY of Listeria monocytogenes (Q926Q9)
2.A.1.1.75	The fructose/xylose:H⁺symporter, PMT1 (polyol monosaccharide transporter-1). Also transports other substrates at lower rates. PMT2 is largely of the same sequence and function. Both are present in pollen and young xylem cells (Klepek et al., 2005).	Plants	PMT1 of Arabidopsis thaliana (Q9XIH7)
2.A.1.1.76	Glucose transporter, GT1. GT1, 2, and 3 are homologues. GT2 and GT3 transport ribose as well as glucose at different rates. GT3 transports ribose with 6-fold lower efficiency due to two threonines in GT3 that are alanines in GT2. They are in two loops between TMSs 3, 4, and 7, 8 (Naula et al., 2010).	Eukaryota	GT1 of Leishmania mexicana (Q9F315)
2.A.1.1.77	The D-glucose/D-ribose transporter, LmGT2 (Most similar to 1.A.1.1.18) (Naula et al., 2010).	Protozoa	LmGT2 of Leishmania mexicana (O61059)
2.A.1.1.78	The glucose transporter, LmGT3 (homologous to LmGT2 (1.A.1.1.75)). Two threonine residues located in the hydrophilic loops connecting TMSs 3 & 4 and 7 & 8 of GT3 prevent transport of D-ribose. Changing these two residues to alanine (as in GT2) allows transport of ribose. Thus, loops 3-4 and 7-8 partially determine substrate specificity (Naula et al., 2010).	Protozoa	LmGT3 of Leishmania mexicana (O61060)
2.A.1.1.79	Polyol (xylitol):H⁺ symporter, PLT4 (Kalliampakou et al., 2011)	Plants	PLT4 of Lotus japonicus (Q1XF07)
2.A.1.1.80	Insulin-responsive facilitative glucose transporter in skeletal and cardiac muscle, adipose, and other tissues, Glut4 (GTR4; SLC2A4; 509aas). Defects in Glut4 cause noninsulin-dependent diabetes mellitus (NIDDM). Hyperinsulinemia leads to uncoupled insulin regulation of the GLUT4 glucose transporter and the FoxO1 transcription factor (Gonzalez et al., 2011). The first luminal loop confers insulin responsiveness to GLUT4 (Kim and Kandror, 2012). Exercise increases Glut4 synthesis in a process involving several protein kinases, the Glut4 enhancer factor (GEF; SLC2A4 regulator; Q9NR83), and the myocyte enhancing factor 2 (MEF2; NP_001139257). (McGee and Hargreaves 2006; Wright 2007; Zorzano et al. 2005)	Animals	SLC2A4 of Homo sapiens
2.A.1.1.81	The glucose uptake porter, GluP (Araki et al., 2011).	Bacteria	GluP of Rhodococcus jostii (Q0SE66)
2.A.1.1.82	The cellobiose/cellodextrin transporter, Cdt-1 (Galazka et al., 2010)	Fungi	Cdt-1 of Neurospora crassa (Q7SCU1)
2.A.1.1.83	The cellobiose/cellodextrin transporter, Cdt-2	Fungi	Cdt2 of Neurospora crassa (Q7SD12)
2.A.1.1.84	The heteromeric TMT1/TMT2 glucose/sucrose:H⁺ antiporter. Catalyzes glucose/sucrose antiport into vacuoles (Schulz et al., 2011).	Plants	The TMT1/2 sugar:H⁺ anti-porter of Arabidopsis thaliana. TMT1 (Q96290). TMT2 (Q8LPQ8).
2.A.1.1.85	Zebrafish Slc2A10 (Glut10) facilitative glucose transporter.	Animals	Zebrafish Glut10 of Danio rerio (A8KB28)
2.A.1.1.86	The sea bream facilitative glucose transporter 1 (GLUT1) (Balmaceda-Aguilera et al., 2012).	Animals	Glut1 of Sparus aurata (H9BPB6)
2.A.1.1.87	solute carrier family 2 (facilitated glucose transporter), member 12	Animals	SLC2A12 of Homo sapiens
2.A.1.1.88	solute carrier family 2 (facilitated glucose transporter), member 6	Animals	SLC2A6 of Homo sapiens
2.A.1.1.89	Solute carrier family 2, facilitated glucose transporter member 8 (Glucose transporter type 8) (GLUT-8) (Glucose transporter type X1)	Animals	SLC2A8 of Homo sapiens
2.A.1.1.90	Solute carrier family 2, facilitated glucose transporter member 14 (Glucose transporter type 14) (GLUT-14)	Animals	SLC2A14 of Homo sapiens
2.A.1.1.91	Solute carrier family 2, facilitated glucose transporter member 3 (Glucose transporter type 3, brain) (GLUT-3)	Animals	SLC2A3 of Homo sapiens
2.A.1.1.92	Inner membrane metabolite transport protein YdjE	Bacteria	YdjE of E. coli
2.A.1.1.93	Vacuolar protein sorting-associated protein 73	Fungi	VPS73 of Saccharomyces cerevisiae
2.A.1.1.94	Putative metabolite transport protein YDL199C	Fungi	YDL199C of Saccharomyces cerevisiae
2.A.1.1.95	Inner membrane metabolite transport protein YgcS	Bacteria	�YgcS of E. coli
2.A.1.1.96	Probable metabolite transport protein YBR241C	Fungi	YBR241C of Saccharomyces cerevisiae
2.A.1.1.97	Sugar transporter ERD6 (Early-responsive to dehydration protein 6) (Sugar transporter-like protein 1)	Plants	ERD6 of Arabidopsis thaliana
2.A.1.1.98	Sugar transporter ERD6-like 6	Plants	At1g75220 of Arabidopsis thaliana
2.A.1.1.99	Facilitated trehalose transporter Tret1-1 (DmTret1-1)	Animals	Tret1-1 of Drosophila melanogaster
2.A.1.1.100	Probable metabolite transport protein YFL040W	Fungi	YFL040W of Saccharomyces cerevisiae
2.A.1.1.101	Probable metabolite transport protein YDR387C	Fungi	YDR387C of Saccharomyces cerevisiae
2.A.1.1.102	Plastidic glucose transporter 4 (AtpGlcT)	Plants	At5g16150 of Arabidopsis thaliana
2.A.1.1.103	D-xylose-proton symporter-like 3, chloroplastic	Plants	At5g59250 of Arabidopsis thaliana
2.A.1.1.104	Myo-inositol transporter 2	Fungi	ITR2 of Saccharomyces cerevisiae
2.A.1.1.105	Hexose transporter HXT11 (Low-affinity glucose transporter LGT3)	Fungi	HXT11 of Saccharomyces cerevisiae
2.A.1.1.106	Probable metabolite transport protein CsbC	Bacilli	CsbC of Bacillus subtilis
2.A.1.1.107	Hexose transporter HXT15	Fungi	HXT15 of Saccharomyces cerevisiae
2.A.1.1.108	Low-affinity glucose transporter HXT1	Fungi	HXT1 of Saccharomyces cerevisiae
2.A.1.1.109	Hexose transporter HXT14	Fungi	HXT14 of Saccharomyces cerevisiae
2.A.1.1.110	Hexose transporter HXT13	Fungi	HXT13 of Saccharomyces cerevisiae
2.A.1.1.111	High-affinity glucose transporter HXT2	Fungi	HXT2 of Saccharomyces cerevisiae
2.A.1.1.112	High-affinity glucose transporter Ght1 (Hexose transporter 1)	Yeast	Ght1 of Schizosaccharomyces pombe
2.A.1.1.113	Putative metabolite transport protein YyaJ	Bacilli	YyaJ of Bacillus subtilis
2.A.1.1.114	Putative metabolite transport protein YaaU	Bacteria	YaaU of Escherichia coli
2.A.1.1.115	Putative metabolite transport protein YdjK	Bacteria	YdjK of Escherichia coli
2.A.1.2: The Drug:H⁺ Antiporter-1 (12 Spanner) (DHA1) Family
2.A.1.2.1	Pyridoxine, pyridoxal, pyridoxamine, amiloride:H⁺ cotransporter (Km (pyridoxine) = 22 μM) (Stolz et al., 2005). Also takes up thiamine (Vogl et al., 2008).	Yeast	Bsu1 (Car1) of Schizosaccharomyces pombe (P33532)
2.A.1.2.2	Cycloheximide:H⁺ antiporter	Yeast	CyhR of Candida maltosa
2.A.1.2.3	Chloramphenicol:H⁺ antiporter; multidrug exporter; isopropyl β-thiogalactoside exporter	Bacteria	CmlA of Pseudomonas aeruginosa
2.A.1.2.4	Tetracycline:H⁺ antiporter	Bacteria	TetA of E. coli
2.A.1.2.5	Multidrug (14- and 15-membered macrolides, lincosamides, streptogramins, tetracyclines, daunomycin, ethidium bromide, etc.):H⁺ antiporter, LmrP. Two proton translocation pathways have been proposed (Bapna et al., 2007), but Schaedler and van Veen, 2010 have provided evidence that a flexible cation binding site in LmrP is associated with variable proton coupling. Basic residues R260 and K357 affect the conformational dynamics of LmrP (Wang and van Veen, 2012). Basic residues, R260 and K357 control the conformational dynamics of the protein (Wang and van Veen 2012). Also specifically catalyzes Ca²⁺:3H⁺ antiport with an affinity of 7 μM (Zhang et al. 2012). Two carboxylates (Asp-235 and Glu-327) are critical for Ca²⁺ binding.	Gram-positive bacteria	LmrP of Lactococcus lactis
2.A.1.2.6	(Benomyl, cycloheximide, methotrexate, fluconazole, etc.):H⁺ antiporter, CaMDR1 (Basso et al., 2010; Cannon et al., 1998). MDR1 catalyzes efflux of commonly used azoles. The central cytoplasmic loop is critical for MDR function, but does not impart substrate specificity (Mandal et al., 2012).	Yeast	CaMDR1 of Candida albicans
2.A.1.2.7	(Bicyclomycin, sulfathiazole, tetracycline, fosfomycin, acriflavin, etc.):H⁺ antiporter. Also exports L-cysteine (Yamada et al., 2006).	Gram-negative bacteria	Bcr of E. coli
2.A.1.2.8	(Spermidine; fluoroquinolones, acriflavin, chloramphenicol, ethidium bromide, etc.):H⁺ antiporter	Gram-positive bacteria	Blt of Bacillus subtilis
2.A.1.2.9	(Hydrophobic uncoupler e.g., CCCP, benzalkonium, SDS):H⁺ antiporter. The 3-d structure (3.5Å resolution) has been determined (Yin et al., 2006; see also Science (2007) 317, 1682).	Gram-negative bacteria	EmrD of E. coli
2.A.1.2.10	Quinolone (and other drug):H⁺ antiporter	Bacteria	NorA of Staphylococcus aureus (P0A0J7)
2.A.1.2.11	Monoamine transporter; drug (doxorubicin, ethidium bromide-6-G):H⁺ antiporter	Animals	VMAT1 of Rattus norvegicus
2.A.1.2.12	Chromaffin granule monoamine (and drug) transporter, VAT1	Animals	SLC18A1 of Homo sapiens
2.A.1.2.13	Vesicular acetylcholine:H⁺ antiporter, UNC-17/VAChT. Mutants grow slowly and are uncoordinated, but the defect can be corrected by mutation of an interacting monotopic protein, SUP-1 (Mathews et al. 2012).	Animals	Unc17 of Caenorhabditis elegans
2.A.1.2.14	Putative arabinose efflux porter	Bacteria	AraJ of E. coli
2.A.1.2.15	Arabinose (and isopropyl β-D-thio- galactopyranoside):H⁺ antiporter, YdeA	Bacteria	YdeA of E. coli
2.A.1.2.16	Polyamines (spermine, spermidine, putrescene); paraquat; methylgloxal bis(guanylhydrazone):H⁺ antiporter (in the plasma membrane) (activated by phosphorylation) (Uemura et al., 2005)	Yeast	TPO1 (YLL028w) of Saccharomyces cerevisiae
2.A.1.2.17	Fluconazole:H⁺ antiporter	Yeast	Flr1 of Saccharomyces cerevisiae
2.A.1.2.18	Lactose and melibiose (>>IPTG) efflux pump, SotB	Bacteria	SotB of Erwinia chrysanthemi
2.A.1.2.19	The multidrug (chloramphenicol, tetra- cycline, norfloxacin, doxorubicin, trimethoprim, acriflavin, ethidium bromide, tetraphenylphosphonium, TPP, benzalkonium, ciprofloxacin, thiamphenicol, IPTG) resistance exporter, MdfA (catalyzes both electrogenic and electroneutral transport) (Adler and Bibi, 2004). Can function as a Na (K)/H antiporter (Lewinson and Bibi 2001; Higgins, 2007). For review of MdfA see Lewinson et al., 2006. The conformational switch accompanying transport is induced by promiscuous binding of substrates and/or inhibitors to the binding pocket (Fluman et al., 2009). Normally extrudes monovalent cationic drugs in exchange for a single proton, but it transports divalent cationic drugs poorly. It can be mutated to antiport a divalent cationic drug for 2 protons (Tirosh et al., 2012).	Bacteria	MdfA of E. coli (P0AEY8)
2.A.1.2.20	Putative MDR efflux pump, MdtG (YceE) (under SoxSR control) (Fàbrega et al., 2010). (May confer fosfomycin- and fluoroquinolone-resistance)	Bacteria	MdtG of E. coli
2.A.1.2.21	The norfloxacin/enoxacin resistance protein, YceL	Bacteria	YceL of E. coli (P69367)
2.A.1.2.22	The chloramphenicol resistance protein, YidY	Bacteria	YidY of E. coli
2.A.1.2.23	The fructose-specific facilitator (uniporter), Ffz1 (Pina et al., 2004)	Yeast	Ffz1 of Zygosaccharomyces bailii (CAD56485)
2.A.1.2.24	The multidrug resistance efflux pump, CgMDR (exports fluoroquinolones and chloramphenicol) (Vardy et al., 2005)	Bacteria	CgMDR of Corynebacterium glutamicum (NP_600365)
2.A.1.2.25	The purine base/nucleoside (nucleosides: inosine, adenosine and guanosine; bases: hypoxanthine adenine, guanine 2-fluoroadenine) efflux pump, YdhL (PbuE) (Johansen et al., 2003; Nygaard and Saxild, 2005; Zakataeva et al., 2007).	Bacteria	PbuE of Bacillus subtilis (O05504)
2.A.1.2.26	The purine ribonucleoside (inosine, adenosine, guanosine, 6-mercaptopurine ribonucleoside) efflux pump (H⁺ antiporter), NepI (YicM) (Gronskiy et al., 2005)	Bacteria	NepI of E. coli (P0ADL1)
2.A.1.2.27	The alcaligin siderophore exporter, AlcS (Brickman and Armstrong, 2005)	Bacteria	AlcS of Bordetella pertussis (CAE42734)
2.A.1.2.28	The vesicular acetylcholine transporter, VAChT (pumps acetylcholine into synaptic vesicles). The acetyl choline and vesamicol binding sites are near the luminal end of the transport pathway (Khare et al. 2010).	Animals	SLC18A3 of Homo sapiens
2.A.1.2.29	The vesicular monoamine transporter, VMAT2 (pumps dopamine, norepinephrine, serotonin and histamine into synaptic vesicles). VMAT2 physically and functionally interacts with the enzymes responsible for dopamine synthesis (Cartier et al., 2010). Molecular hinge points mediating alternating access have been identified (Yaffe et al. 2013).	Animals	VMAT1 (SLC18A2) of Homo sapiens
2.A.1.2.30	The hippocampus abundant transcript-like 1 protein, HIATL1 (putative drux exporter)	Animals	HIATL1 of Homo sapiens (NP_115947)
2.A.1.2.31	The multidrug transporter, QDR2, required for resistance to quinidine, barban, cisplatin, and bleomycin; may have a role in potassium uptake	Bacteria	QDR2 of Saccharomyces cerevisiae (P40474)
2.A.1.2.32	The chloramphenicol resistance protein, Chl^R	Bacteria	Chl^R of Streptomyces lividans (P31141)
2.A.1.2.33	The Hol1 MFS transporter (Mutation allows the uptake of histidinol and other cations (Wright et al., 1996). The N-terminal 200 residues show 22% identity with 2.A.1.2.1 and 2.A.1.2.16).	Yeast	Hol1 of Saccharomyces cerevisiae (P53389)
2.A.1.2.34	The MDR efflux pump, PmrA (exports fluoroquinolone and other compounds) and other components including the antimicrobial peptide, colistin (Pamp et al., 2008).	Bacteria	PmrA of Streptococcus pneumoniae (P0A4K4)
2.A.1.2.35	The caffeine resistance protein 5 (Caf5) (Benko et al., 2004)	Bacteria	Caf5 of Schizosaccharomyces pombe (O94528)
2.A.1.2.36	The multidrug resistance protein Aqr1 (YNL065w) (exports short chain monocarboxylates but not more hydrophobic acids such as octonate and quinidine. Also exports ketoconazole and crystal violet (Tenreiro et al., 2002)).	Yeast	Aqr1 of Saccharomyces cerevisiae (P53943)
2.A.1.2.37	The legiobactin (siderophore) exporter (most similar to 2.A.1.2.9; 23% identity) (Allard et al., 2006)	Gram-negative bacterium	IbtB of Legionella pneumophila LbtA (Q45RG2) LbtB (Q5WX21)
2.A.1.2.38	Tetracycline-specific exporter, TetA39 (most like 2.A.1.2.4) (Thompson et al., 2007).	Bacteria	TetA39 of Acinetobacter spp. (Q56RY7)
2.A.1.2.39	Tetracycline-specific exporter, TetA41 (most like 2.A.1.2.4) (Thompson et al., 2007).	Bacteria	TetA41 of Serratia marcescens (Q5JAK9)
2.A.1.2.40	The dityrosine exporter, Dtr1 (required for formation of the outer layer of the cell wall (Morishita and Engebrecht, 2008)).	Yeast	Dtr1 of Saccharomyces cerevisiae (P38125)
2.A.1.2.41	The tetracycline resistance determinant, TetA42 from a deep terrestrial subsurface bacterium (Brown et al., 2008).	Bacteria	TetA42 of Micrococcus sp. SMCC G8878 (B2YGG2)
2.A.1.2.42	The multidrug efflux pump, EmrD-3 (exports ethidium, linezolid, tetraphenylphosphonium chloride, rifampin, erythromycin, minocycline, trimethoprim, chloramphenicol, and rhodamine) (Smith et al., 2009).	Bacteria	EmrD-3 of Vibrio cholerae (Q9KMQ3)
2.A.1.2.43	The multidrug efflux pump, Qdr3 (exports polyamines, quinidine, barban, cisplatin and bleomycin). The two halves of the protein each have an N-terminal. 150 residue hydrophilic region found in many fungi followed by a 200 residue, 6 TMS, transmembrane region. This suggests that an intragenic duplication event gave rise to 12 TMS proteins independently of most other MFS carriers, but this has not been demonstrated, possibly because of extensive sequence divergence of the second half.	Fungi	Qdr3 of Saccharomyces cerevisiae (P38227)
2.A.1.2.44	Diglucosyl-diacylglycerol exporter or flippase, LtaA (lipoteichoic acid protein A) (Gründling and Schneewind, 2007)	Firmicutes	LtaA of Staphylococcus aureus (Q2FZP8)
2.A.1.2.45	The fructose-specific uniporter, Ffz1 (69% identical to Ffz2 (2.A.1.2.46) and 66% identical to (2.A.1.2.23) (Leandro et al., 2011).	Yeast	Ffz1 of Zygosaccharomyces rouxii (C5E4Z7)
2.A.1.2.46	The fructose/glucose uniporter, Ffz2 (64% identical to 2.A.1.2.23). Both sugars are transported with similar affinities and efficiencies (Leandro et al., 2011).	Yeast	Ffz2 of Zygosaccharomyces rouxii (C5DX43)
2.A.1.2.47	The multidrug resistance efflux pump, HsMDR (YfmO2; Vardy et al., 2005).	Archaea	HsMDR of Halobacterium sp. NRC-1 (Q9HS33)
2.A.1.2.48	tetracycline exporter	Eukaryotes	tet^R exporter of Aspergillus niger (A2QTF4)
2.A.1.2.49	Putative tetracycline resistance protein	Archaea	Putative tet resistance pump of Pyrobaculum aerophilum (Q8ZUX8)
2.A.1.2.50	MFS porter	Slime molds	MFS porter of Dictyostelium purpureum (F0ZU09)
2.A.1.2.51	Chloramphenicol (specific) resistance pump, CraA (43% identical to MdfA of E. coli) (Roca et al., 2009).	Bacteria	CraA of Acinetobacter baumannii (A3M9E9)
2.A.1.2.52	Puromycin resistance MDR protein, MdtM (Soo et al., 2011)	Bacteria	MdtM of E. coli (P39386)
2.A.1.2.53	MDR pump, SLC22A18 in lung cancer cells (Lei et al., 2012).	Animals	SLC22A18 of Homo sapiens
2.A.1.2.54	LigA-like protein	Bacteria	LigA-like protein of Streptomyces coelicolor (Q9KYE9)
2.A.1.2.55	Peptide exporter (Ala-Gln and Ala-branched chain amino and dipeptides) (Hayashi et al., 2010).	Bacteria	YdeE of E. coli (P31126)
2.A.1.2.56	NCL7. Neuronal ceroid lipofuscinosis, a neuro-degenerative genetic disease, is caused by mutations in at least 8 different human genes, one of which, CLN7 (MFSD8), is associated with late infantile NCL. CLN7 is localized to lysosomes (Sharifi et al., 2010).	Animals	NCL7 of Homo sapiens (Q8NHS3)
2.A.1.2.57	MFS-type transporter SLC18B1 (Solute carrier family 18 member B1)	Animals	C6orf192 of Homo sapiens
2.A.1.2.58	Protein ZINC INDUCED FACILITATOR 1	Plants	ZIF1 of Arabidopsis thaliana
2.A.1.2.59	Ucharacterized MFS-type transporter C330.07c; YJ87	Yeast	YJ87 of Schizosaccharomyces pombe
2.A.1.2.60	Inner membrane transport protein, YajR	Bacteria	YajR of E. coli
2.A.1.2.61	SPX domain-containing membrane protein At1g63010	Plants	At1g63010 of Arabidopsis thaliana
2.A.1.2.62	Inner membrane transport protein, YdhC	Bacteria	YdhC of Escherichia coli
2.A.1.2.63	Probable drug/proton antiporter YHK8	Fungi	YHK8 of Saccharomyces cerevisiae
2.A.1.2.64	Polyamine transporter 4	Fungi	TPO4 of Saccharomyces cerevisiae
2.A.1.2.65	Inner membrane transport protein YdhP	Bacteria	YdhP of Escherichia coli
2.A.1.2.66	Polyamine transporter 3	Fungi	TPO3 of Saccharomyces cerevisiae
2.A.1.2.67	Polyamine transporter 2	Fungi	TPO2 of Saccharomyces cerevisiae
2.A.1.2.68	Tetracycline resistance protein, class B (TetA(B)) (Metal-tetracycline/H(+) antiporter)	Bacteria	TetA of Escherichia coli
2.A.1.2.69	Uncharacterized MFS-type transporter YttB	Bacilli	YttB of Bacillus subtilis
2.A.1.2.70	Multidrug resistance protein 1 (Multidrug-efflux transporter 1)	Bacilli	Bmr of Bacillus subtilis
2.A.1.2.71	Uncharacterized MFS-type transporter Rv2456c/MT2531	Bacteria	Rv2456c of Mycobacterium tuberculosis
2.A.1.2.72	Major facilitator superfamily domain-containing protein 9	Animals	Mfsd9 of Mus musculus
2.A.1.2.73	Major facilitator superfamily domain-containing protein 10 (Tetracycline transporter-like protein)	Animals	Mfsd10 of Mus musculus
2.A.1.2.74	Multidrug resistance protein MdtL	Proteobacteria	MdtL of Shewanella sp.
2.A.1.2.75	Tetracycline resistance protein, class E (TetA(E))	Bacteria	TetA of Escherichia coli
2.A.1.2.76	Major facilitator copper transporter 1, Mfc1. Takes up copper in meiotic sporulating cells; present in the forespore membrane. Induced under copper limitation. Required for normal forespore development and spore copper-dependent amine oxidase activity (Beaudoin et al. 2011).	Yeast	Mfc1 of Schizosaccharomyces pombe
2.A.1.2.77	CefT confers phenyacetate resistance (Fern�ndez-Aguado et al. 2012).� It has been reported to be a hydrophilic beta-lactam transporter that is involved in the secretion of hydrophilic beta-lactams containing an α-aminoadipic acid side chain (isopenicillin N, penicillin N and deacetylcephalosporin C) (Cesareo et al. 2007; Ull�n et al. 2002).	Fungi	CefT of Acremonium chrysogenum
2.A.1.2.78	The PaaT (PenT) exporter. PaaT is involved in penicillin production, possibly through the translocation of side-chain precursors (phenylacetate and phenoxyacetate) from the cytosol to the peroxisomal lumen across the peroxisomal membrane of P. chrysogenum. It has a Pex19 (peroxisome biogenesis factor 19) binding sequence (residues 258 - 269) accounting for its peroxysomal location (Fernández-Aguado et al. 2012; Yang et al. 2012).	Fungi	PaaT of Penicillum chysogenum (notatum)
2.A.1.3: The Drug:H⁺ Antiporter-2 (14 Spanner) (DHA2) Family
2.A.1.3.1	The main boron exporter in yeast, Atr1 (Kaya et al. 2009) (Aminotriazole, 4-nitroquinoline-N-oxide, etc.):H⁺ antiporter. Also exports L-cysteine (Yamada et al., 2006).	Yeast	Atr1 of Saccharomyces cerevisiae
2.A.1.3.2	(CCCP, nalidixic acid, rhodamine 6G, methylviologen, deoxycholate, growth inhibitory steroid hormones (estradiol and progesterone) (Elkins and Mullis, 2006) SDS, organomercurials, etc.):H⁺ antiporter	Gram-negative bacteria	EmrB of E. coli (P0AEJ0)
2.A.1.3.3	(Acriflavin, ethidium bromide, fluoroquinolones, etc.):H⁺ antiporter (Li et al. 2004; Rodrigues et al. 2011).	Gram-positive bacteria	LfrA of Mycobacterium smegmatis
2.A.1.3.4	(Mono- and divalent organocation):H⁺ antiporter. Transmembrane helix 12 of QacA lines the bivalent cationic drug binding pocket (Hassan et al., 2007).	Gram-positive bacteria	QacA of Staphylococcus aureus (P0A0J9)
2.A.1.3.5	(Pristinamycin I and II, rifamycin, etc.):H⁺ antiporter	Gram-positive bacteria	Ptr of Streptomyces pristinaespiralis
2.A.1.3.6	Me²⁺�tetracycline:2H⁺ or 2K⁺ antiporter (the optimal Me²⁺ = Co²⁺) (Also transports Na⁺ or K⁺out in exchange for 2H⁺.)	Bacteria	TetK of Staphylococcus aureus (P02983)
2.A.1.3.7	Actinorhodin:H⁺ antiporter, ActVa or ActA (Tahlan et al., 2007)	Gram-positive bacteria	ActVa of Streptomyces coelicolor
2.A.1.3.8	Cephamycin:H⁺ antiporter	Gram-positive bacteria	CmcT of Nocardia lactamdurans
2.A.1.3.9	Lincomycin:H⁺ antiporter	Gram-positive bacteria	LmrA of Streptomyces lincolnensis
2.A.1.3.10	Methylenomycin:H⁺ antiporter	Gram-positive bacteria	MmrB of Bacillus subtilis
2.A.1.3.11	Puromycin:H⁺ antiporter	Gram-positive bacteria	Pur8 of Streptomyces lipmanii
2.A.1.3.12	Tetracenomycin:H⁺ antiporter	Gram-positive bacteria	TcmA of Streptomyces glaucescens
2.A.1.3.13	Unconjugated bile acid uptake transporter	Bacteria	BaiG of Eubacterium sp. strain VPI 12708
2.A.1.3.14	Methylviologen (paraquat):H⁺ antiporter (also exports ethidium bromide, acriflavin, malachite green, pyonine B and benzyl viologen)	Bacteria	SmvA of Salmonella typhimurium
2.A.1.3.15	Rifamycin:H⁺ antiporter	Bacteria	RifP of Amycolatopsis mediterranei
2.A.1.3.16	The Me²⁺·tetracycline:2H⁺ antiporter (Me²⁺ = Co²⁺, Mg²⁺, Mn²⁺) (also probably a Na⁺ or K⁺:2H⁺ antiporter) (Wang et al. 2000).	Bacteria	TetA(L) of Bacillus subtilis
2.A.1.3.17	The trimethoprim-sensitivity protein, YebQ (increases sensitivity to trimethoprim)	Bacteria	YebQ of E. coli
2.A.1.3.18	Efflux pump for plant-bacterial signaling molecules, phytoalexins, flavenoids and salicylate as well as drugs, RmrB	Bacteria	RmrB of Rhizobium etli
2.A.1.3.19	Paraquot efflux pump, PqrB (Cho et al., 2003)	Bacteria	PqrB of Streptomyces coelicolor (AAG45950)
2.A.1.3.20	Long chain fatty acid efflux pump, FarB (Lee et al., 2003) (exports antimicrobial long chain fatty acids; functions with MFP auxillary protein, FarA (TC# 8.A.1.1.2)) (Lee et al., 2006)	Bacteria	FarB of Neisseria gonorrhoeae (AAD54074)
2.A.1.3.21	Siderophore, achromobactin efflux pump, YhcA (Franza et al., 2005)	Bacteria	YhcA of Erwinia (Pectobacterium) chrysanthemi (AAL14569)
2.A.1.3.22	The Tet38 tetracycline-resistance protein of Staphylococcus aureus (Truong-Bolduc et al., 2005)	Bacteria	Tet38 of Staphylococcus aureus (AAV80464)
2.A.1.3.23	The NorB multidrug resistance pump (exports hydrophilic quinolones, ethidium bromide, cetrimide, sparfloxacin, moxifloxacin and tetracycline) (Truong-Bolduc et al., 2005)	Bacteria	NorB of Staphylococcus aureus (BAB42529)
2.A.1.3.24	The VceAB multidrug (hydrophobic compounds including deoxycholate (DOC), antibiotics, such as chloramphenicol and nalidixic acid, and the proton motive force uncoupler, cyanide carbonyl m-chlorophenylhydrazone (CCCP)) resistance pump (functions with outer membrane VceC (TC#1.B.17.3.6) or OprM (2.A.6.2.21), an OMF family member; The C-terminal domain of the Pseudomonas aeruginosa OprM and the alpha-helical hairpin domain of Vibrio cholerae VceA play important roles in recognition/specificity/recruitment in the assembly of a functional, VceAB-OprM chimeric efflux pump (Bai et al., 2010).	Bacteria	VceAB of Vibrio cholerae VceB (MFS), NP_231054 VceA (MFP), NP_231053
2.A.1.3.25	Actinorhodin (blue pigmented antibiiotic) transporter, ActII-2	Bacteria	ActII-2, Actinorhodin transporter of Streptomyces coelicolor (P46105).
2.A.1.3.26	Novobiocin/deoxycholate exporting MDR efflux pump, YegB (Baranova and Nikaido, 2002)	Bacteria	YegB of E. coli (P36554)
2.A.1.3.27	The vacuolar basic amino acid (Arg, Lys, His) transporter, Vba3 (Shimazu et al., 2005)	Yeast	Vba3 of Saccharomyces cerevisiae (P25594)
2.A.1.3.28	MDR multidrug efflux pump, EbrE (involved in colony growth, dependent on Ca²⁺, Mg²⁺, Na⁺ and K⁺) (Lee et al., 2007)	Bacteria	EbrE of Streptomyces lividans (Q939A4)
2.A.1.3.29	The metal:tetracycline/oxytetracycline resistance efflux pump, TctB (563 aas)	Bacteria	TctB of Streptomyces rimosus (O69070)
2.A.1.3.30	Lincomycin resistance protein; Lincomycin:H⁺ antiporter, LmrB	Bacteria	LmrB of Bacillus subtilis (O35018)
2.A.1.3.31	The hydrophilic fluroquinolones efflux pump, QepA (Perichon et al., 2008). Exports hyrdophilic quinolones, norfloxacin, and ciprofloxacin.	Bacteria	QepA of E. coli (A5H8A5)
2.A.1.3.32	Landomycin A efflux pump, LanJ (Otash et al., 2008)	Bacteria	LanJ of Streptomyces cyanogenus (Q9ZGB6)
2.A.1.3.33	Multidrug (including novobiocin, streptomycin, and actinomycin D) resistance porter, MdtP (YusP)	Bacteria	MdtP of Bacillus subtilis (O32182)
2.A.1.3.34	The P55 drug efflux pump (Rv141Oc) (extrudes drugs including rifampicin and clifazimine, first- and second-line anti-tuberculosis drugs. CCCP and valinomycin inhibited drug resistance) (Ramón-García et al., 2009). P55 also exports malachite green, ethidium bromide, isoniazid and ethambutol (Bianco et al. 2011). Functions together with the outer membrane lipoprotein porin, LprG, also called P27 and Lpp-27 (Bianco et al. 2011; Farrow and Rubin 2008). Required together with LprG for normal colony morphology and sliding motility, possibly due to alterred cell wall composition (Farrow and Rubin 2008). Required together with LprG for normal colony morphology and sliding motility, possibly due to alterred cell wall composition (Farrow and Rubin 2008).	Bacteria	P55 drug efflux pump of Mycobacterium tuberculosis (P71678)
2.A.1.3.35	The 14 TMS FmtC (MrpF) protein, involved in methecillin resistance. Residues 1-550 comprise a 14TMS MFS permease domain while residues 551-840 comprise a "phosphatidylglycerol lysyl transferase" (or synthetase) domain (DUF2156). Also called "Lysyl cardiolipid synthase". More distantly related to lysyl-tRNA synthetases. Similar to 2.A.1.3.44 in all these respects.	Bacteria	FmtC of Staphylococcus aureus (D1QCY9)
2.A.1.3.36	EmrKY-TolC MDR efflux pump. (also exports cysteine (Yamada et al., 2006)) (similar to 2.A.1.3.2)	Bacteria	EmrKY-TolC of E. coli EmrK (MFP) (C5W790) EmrY (MFS) (C5W789)
2.A.1.3.37	The uridine/deoxyuridine/5-fluorouridine uptake transporter, UriP (llmg_0856) (480aas; 14TMSs) (Martinussen et al., 2010)	Bacteria	UriP of Lactococcus lactis (A2RJJ9)
2.A.1.3.38	MFS porter of unknown function	Bacteria	MFS porter of Streptomyces viridochromogenes (D9X7X8)
2.A.1.3.39	The antimicrobial efflux pump, LmrS. Exports linezolid and tetraphenylphosphonium chloride (TPCL) > sodium dodecyl sulfate (SDS), trimethoprim, and chloramphenicol. (most similar to LmrB (2.A.1.3.30)) (Floyd et al., 2010).	Bacteria	LmrS of Staphylococcus aureus (Q5HE38)
2.A.1.3.40	The phenazine resistance pump. Also exports D-alanyl-griseoluteic acid; possibly in conjunction with a chaperone protein, EhpR. The crystal structure of EhpR is known (Yu et al., 2011). Note: Phenazines are toxic redox active secondary metabolites that many bacteria secrete.	Bacteria	EhpJ of Panloea (Enterobacter) agglomerans (O32600)
2.A.1.3.41	Rv0585c; 795aas: 1 - 220aas, TMSs 1-6; 221-490aas, kinase domain; 491-795, TMS: 7-14. The C-terminal 8 TMS hydrophobic domain is homologous to an N-terminal domain in fused Mg²⁺-ATPases (3.A.3.4.3 and 3.A.3.4.4) and members of family 9.B.3.	Bacteria	Rv0585c of Mycobacterium tuberculosis (O53781)
2.A.1.3.42	Putative oxacillin resistance-associated protein, FmtC (872 aas; 14 N-terminal TMSs (residues 1-530) plus a largely hydrophilic DUF2156 domain (residues 531-872). Similar throughout its length to FmtC of Staphylococcus aureus (2.A.1.3.37). Residues 67-326 (TMSs 2-8) are homologous to residues 527-786 (TMSs 8-14) in Rv0585c of Mycobacterium tuberculosis (2.A.1.3.43). Residues 6-314 are also homologous to an extra hydrophobic domain in Mg²⁺ P-type ATPases (3.A.3.4.3 and 3.A.3.4.4). The C-terminal domain belongs to the DUF2156 superfamily. Homologues of the hydrophilic domain retrieved with NCBI BLAST searches are annotated as "putative" lysylphosphatidyl-glycerol synthetase. Some include full length MFS fusion proteins.	Bacteria	FmtC of Brucella melitensis (D1F3T8)
2.A.1.3.43	MFS efflux pump, AmvA (AedF). Mediates drug, dye, detergent, antibiotic and disinfectant resistance (Rajamohan et al., 2010; Hassan et al. 2011). 98.6% identical to AdeF (2.A.1.3.46).	Bacteria	AmvA of Acinetobacter baumannii (C4PAW9)
2.A.1.3.44	MDR pump, AdeF (AmvA) exports ethidium, DAPI, and chlorhexidine (Hassan et al. 2011). 98.6% identical to AmvA (2.A.1.3.45).	Bacteria	AdeF of Acinetobacter baumannii (A3M6E0)
2.A.1.3.45	Putative MFS permease TMSs 10-13 (shows limited sequence similarity with TMSs 2-5 in 9.B.111.1.1 and 9.B.111.1.2).	Bacteria	MFS permease of Bilophila wadsworthia (E5Y3Y1)
2.A.1.3.46	The phenicol (florfenicol/chloramphenicol) exporter, FexB (Liu et al., 2012)	Firmicutes	FexB of Enterococcus faecium (G9FS16)
2.A.1.3.47	The trichothecene efflux pump, TRI12 (Alexander et al., 1999; Wuchiyama et al., 2000). See also Fang et al. (2012).	Fungi	TRI12 of Fusarium sporotrichioides (Q9C1B3)
2.A.1.3.48	Probable multidrug-efflux transporter Rv1634/MT1670	Bacteria	Rv1634 of Mycobacterium tuberculosis
2.A.1.3.49	Multidrug resistance protein Stp (Spectinomycin tetracycline efflux pump)	Bacteria	Stp of Myconbacterium tuberculosis
2.A.1.3.50	Multidrug resistance protein 3 (Multidrug-efflux transporter 3)	Bacilli	Bmr3 of Bacillus subtilis
2.A.1.3.51	Probable transport protein HsrA (High-copy suppressor of RspA)	Bacteria	HsrA of Escherichia coli
2.A.1.3.52	Drug resistance protein YOR378W	Fungi	YOR378W of Saccharomyces cerevisiae
2.A.1.3.53	Azole resistance protein 1	Fungi	AZR1 of Saccharomyces cerevisiae
2.A.1.3.54	Protein SGE1 (10-N-nonyl acridine orange resistance protein) (Crystal violet resistance protein)	Fungi	SGE1 of Saccharomyces cerevisiae
2.A.1.3.55	Uncharacterized MFS-type transporter YubD	Bacilli	YubD of Bacillus subtilis
2.A.1.3.56	Uncharacterized MFS-type transporter YvmA	Bacilli	yvmA of Bacillus subtilis
2.A.1.3.57	Uncharacterized MFS-type transporter YwoD	Bacilli	YwoD of Bacillus subtilis
2.A.1.3.58	Uncharacterized MFS-type transporter YfiU	Bacilli	YfiU of Bacillus subtilis
2.A.1.3.59	MDR efflux pump, NorC (Truong-Bolduc et al. 2006).	Firmicutes	NorC of Staphylococcus aureus
2.A.1.3.60	MDR efflux pump, SdrM.� Exports norfloxacin, acriflavin and ethidium bromide (Yamada et al. 2006).	Firmicutes	SdrM of Staphylococcus aureus
2.A.1.3.61	MDR efflux pump, MdeA. Exports hoechst 33342, doxorubicin, daunorubicin, tetraphenyl phosphonium, ethidium bromide and rhodamine 6G (Yamada et al. 2006).	Firmicutes	MdeA of Staphylococcus aureus
2.A.1.3.62	MDR efflux pump, AedC (Hassan et al. 2011). Shown to export chloramphenicol and tetracycline.	Proteobacteria	AedC of Acinetobacter baumannii
2.A.1.3.63	Iron homeostasis protein, AedD; may function in siderophore export (Hassan et al. 2011).	Proteobacteria	AedD of Acinetobacter baumannii
2.A.1.4: The Organophosphate:P_i Antiporter (OPA) Family
2.A.1.4.1	Sugar-P:P_i antiporter (transports many sugar-phosphates - both 1- and 6-P esters)	Bacteria	UhpT of E. coli (P0AGC0)
2.A.1.4.2	P-glycerate:P_i antiporter	Bacteria	PgtP of Salmonella typhimurium
2.A.1.4.3	Glycerol-P:P_i antiporter (may function by a 'rocker switch' mechanism; Law et al., 2007). The 3-d structure is known (3.3Å resolution) (Huang et al., 2003; Lemieux et al., 2005; Lemieux, 2007).	Bacteria	GlpT of E. coli
2.A.1.4.4	Hexose-P:P_i antiporter regulatory protein; senses external glucose-6-P and transports it with high affinity and low efficiency	Bacteria	UhpC of E. coli
2.A.1.4.5	Microsomal glucose-6-P:Pi antiporter (glycogen storage disease (GSD1b and 1c); Gierke's disease protein) (SLC37A2; in mice, associated with white adipose tissue obesity and expressed at high levels in macrophage) (4 isoforms present in humans; Chen et al., 2008)	Animals	SLC37A4 of Homo sapiens
2.A.1.4.6	Glucose-6-P:P_i antiporter, Hpt (may also transport other organophosphates including C₃ organophosphates).	Bacteria	Hpt of Chlamydia pneumoniae (spQ9Z7N9 & gi9979188) & pirA72050
2.A.1.4.7	Putative glycerol-3-phosphate (G-3-P) transporter, G3PP (most similar to TC# 2.A.1.4.6, 22% identity)	Animals	SLC37A1 of Homo sapiens
2.A.1.4.8	solute carrier family 37 (glycerol-3-phosphate transporter), member 2	Animals	SLC37A2 of Homo sapiens
2.A.1.4.9	solute carrier family 37 (glycerol-3-phosphate transporter), member 3	Animals	SLC37A3 of Homo sapiens
2.A.1.5: The Oligosaccharide:H⁺ Symporter (OHS) Family
2.A.1.5.1	Lactose:H⁺ symporter, LacY. Transports lactose, melibiose and TMG. Crystal structures and modeling reveal the cytoplasmic open state and the periplasmic open state (PDB ID: 1PV7; Abramson et al., 2003; Pendse et al., 2010). The membrane lipid composition determines the topology of LacY (Dowhan and Bogdanov, 2011). Smirnova et al. (2011) have provided evidence that the opening of the periplasmic cavity in LacY is the limiting step for sugar binding. Evidence for an alternating sites mechanism of transport has been summarized (Smirnova et al., 2011). Eames and Kortemme (2012) have shown that when considering expression of the lac operon, LacY function (H⁺ transport) and not protein production is the primary origin of cost fitness. Homology threading of several MFS porters based on the LacY 3-d structure has been reported (Kasho et al., 2006). The alternating-access mechanism has been suggested to arise from inverted topological repeats (Radestock and Forrest, 2011; Madej et al. 2012 Madej et al. 2012).	Bacteria	LacY of E. coli
2.A.1.5.2	Raffinose:H⁺ symporter, RafB, can be mutated to transport maltose (Van Camp et al., 2007).	Bacteria	RafB of E. coli
2.A.1.5.3	Sucrose:H⁺ symporter, CscB, also transports maltose (Peng et al. 2009).	Bacteria	CscB of E. coli
2.A.1.5.4	Melibiose:H⁺ symporter, MelY (Shinnick et al., 2003). Transports melibiose and lactose, but not TMG (Tavoulari and Frillingos, 2007)	Bacteria	MelY of Enterobacter cloacae
2.A.1.6: The Metabolite:H⁺ Symporter (MHS) Family
2.A.1.6.1	Citrate:H⁺ symporter	Bacteria	CitA of Klebsiella pneumoniae
2.A.1.6.2	α-Ketoglutarate:H⁺ symporter	Bacteria	KgtP of E. coli (P0AEX3)
2.A.1.6.3	Dicarboxylate:H⁺ symporter	Bacteria	PcaT of Pseudomonas putida
2.A.1.6.4	(Poline/glycine-betaine):(H⁺/Na⁺) symporter (also transports taurine, ectoine, pipecolate, proline-betaine, N,N-dimethylglycine, carnitine, and 1-carboxymethyl-pyridinium) (subject to osmotic activation). Transmembrane helix I and periplasmic loop 1 are involved in osmosensing and osmoprotectant transport (Keates et al., 2010).	Bacteria	ProP of E. coli (P0C0L7)
2.A.1.6.5	4-Methyl-o-phthalate:H⁺ symporter	Bacteria	MopB of Burkholderia cepacia
2.A.1.6.6	Shikimate:H⁺ symporter	Bacteria	ShiA of E. coli
2.A.1.6.7	The citrate/tricarballylate:H⁺ symporter (CitA or TcuC); probably orthologous to 2.A.1.6.1 (Lewis et al., 2004)	Bacteria	TcuC of Salmonella enterica serovar Typhimurium LT2 (P0A2G3)
2.A.1.6.8	The acetate/monochloroacetate (haloacid) permease, Deh4p (Km = 5.5 mμM for acetate; 9 mμM for monochloroacetate) (Yu et al., 2007; Su and Tsang 2012).	Bacteria	Deh4 of Burkholderia cepacia or sp. MBA4 (Q7X4L6)
2.A.1.6.9	YdfJ. Can function as an inward rectifying K⁺ channel when expressed in animal cells as measured by whole cell patch clamping. Blocked by barium and protopine (Tang et al., 2011).	Bacteria	YdfJ of E. coli (P77228)
2.A.1.6.10	Inner membrane metabolite transport protein YhjE	Bacteria	YhjE of Escherichia coli
2.A.1.6.11	Acetate/haloacid transporter, Dehp2.� Transports acetate, chloroacetate, bromoacetate, 2-chloropropionate, and possibly with low affinity, glycolate, lactate and pyruvate (based on weak inhibition results).� Inducible by chloroacetate (Su and Tsang 2012).� This protein is 79% identical to its paralogue, Deh4p (TC# 2.A.1.6.8) which differs in that it shows lower apparent affinity for 2-chloropropionate.	Bacteria	Dehp2 of Burkholderia caribensis (formerly sp. MBA4)
2.A.1.6.12	The putative thiazole transporter, ThiU. Regulatyed by TPP riboswitch (Rodionov et al. 2002)	Pasteurellales	ThiU of Haemophilus influenzae (P44699)
2.A.1.7: The Fucose: H⁺ Symporter (FHS) Family
2.A.1.7.1	L-Fucose:H⁺ symporter. The x-ray structure (3.1Å resolution) with an outward open, amphipathic cavity has been solved. Asp46 and Glu135 can undergo cycles of protonation (Dang et al., 2010).	Bacteria	FucP of E. coli
2.A.1.7.2	Glucose/galactose porter	Bacteria	Ggp of Brucella abortus (P0C105)
2.A.1.7.3	Glucose/Mannose/Xylose: H⁺ symporter (Paulsen et al., 1998; G.Gosset, personal communication).	Bacteria	GlcP of Bacillus subtilis
2.A.1.7.4	Rat kidney Na⁺-dependent glucose (methyl α-glucoside) transporter, NaGLT1 (glucose:Na⁺:Na⁺=1:1) (Horiba et al., 2003)	Animals	NaGLT1 of Rattus norvegicus (BAC57446)
2.A.1.7.5	2-Deoxy-D-ribose porter, DeoP (Christensen et al., 2003)	Bacteria	DeoP of Salmonella typhimurium LT-2 (gi 16767076)
2.A.1.7.6	Sucrose permease, ScrT (Rodionov et al., 2010)	Bacteria	ScrT of Shewanella frigidimarina (ABI73814)
2.A.1.7.7	The Na⁺-dependent sugar transporter, HP1174 (transports glucose, galactose, mannose and 2-deoxyglucose (Psakis et al. 2009)). (most similar to 2.A.1.7.2; 49% identity)	Bacteria	HP1174 of Helicobacter pylori (O25788)
2.A.1.7.8	N-acetylglucosamine porter, NagP (Rodionov et al. 2010).	Proteobacteria	NagP of Shewanella oneidensis (Q8EBL0)
2.A.1.7.9	The putative N-acetylgalactosamine porter, AgaP (Leyn et al. 2012).	Proteobacteria	AgaP of Shewanella amazonensis (A1S4V0)
2.A.1.7.10	The putative glucose porter, GlcP (Rodionov et al., 2010).	Proteobacteria	GlcP of Shewanella amazonensis (A1S5F4)
2.A.1.7.11	The putative mannose porter, ManP^l (Rodionov et al., 2010).	Proteobacteria	ManP^l of Shewanella amazonensis (A1S297)
2.A.1.7.12	The putative trehalose porter, TreT (Rodionov et al., 2010)	Proteobacteria	TreT of Shewanella frigidimarina (Q07XD1)
2.A.1.7.13	Bypass of stop codon protein 6	Fungi	BSC6 of Saccharomyces cerevisiae S288c
2.A.1.7.14	Protein TsgA	Bacteria	TgsA of E. coli
2.A.1.7.15	Major facilitator superfamily domain-containing protein 4-A	Animals	Mfsd4a of Danio rerio
2.A.1.7.16	The putative mannose porter, ManP (Rodionov D.A., personal communication). Regulated by mannose regulon ManR.	Bacteroidetes	ManP (Q8A5Y0) of Bacteroides thetaiotaomicron
2.A.1.7.17	The putative fructose porter, FruP (Rodionov D.A., personal communication). Regulated by fructose oligosaccharide utilization regulon.	Bacteroidetes	FruP (Q8A6W8) of Bacteroides thetaiotaomicron
2.A.1.7.18	The putative N-acetylglucosamine porter, NagP (Rodionov D.A., personal communication). Regulated by heparin utilization regulon.	Bacteroidetes	NagP (Q89YS8) of Bacteroides thetaiotaomicron
2.A.1.7.19	Uncharacterized MFS permease	Chlamydiae	MFS permease of Parachlamydia acanthamoebae
2.A.1.8: The Nitrate/Nitrite Porter (NNP) family
2.A.1.8.1	Nitrate/H⁺ symporter (K1) Nitrate/nitrite antiporter (K2)	Bacteria	NarK (NarK1-K2) of E. coli
2.A.1.8.2	Nitrate uptake porter	Bacteria	NasA of Bacillus subtilis
2.A.1.8.3	Nitrate/nitrite uptake porter	Bacteria	NrtP of Synechococcus PCC7002
2.A.1.8.4	Nitrate transporter	Diatoms	Nitrate porter of Cylindrotheca fusiformis
2.A.1.8.5	Nitrate transporter, CrnA/NrtA (Unkles et al., 1991). The nitrate signature sequences (NS1 and NS2) in TMSs 5 and 11 and arg residues in TMSs 2 and 8 may influence substrate binding (Unkles et al., 2012).	Fungi	CrnA of Emericella nidulans
2.A.1.8.6	Nitrate transporter	Algae	Nitrate porter of Chlamydomonas reinhardtii
2.A.1.8.7	High affinity Nitrate/nitrite uptake transporter, Nar4.	Algae	Nar4 of Chlamydomonas reinhardtii (A8J4P3)
2.A.1.8.8	NO₂^- extrusion, NO₃^-/NO₂^- exchange permease, NarK1	Bacteria	NarK1 of Thermus thermophilus HB8
2.A.1.8.9	NO₂^- extrusion, NO₃^-/NO₂^- exchange permease, NarK2	Bacteria	NarK2 of Thermus thermophilus HB8
2.A.1.8.10	NO₃^-/NO₂^- transporter (NO₃^- uptake permease; NO₂^- exporter) (NO₃^-/NO₂^- antiporter ?) (stress-induced; Clegg et al., 2006)	Bacteria	NarU of E. coli
2.A.1.8.11	The 24 TMS, 2 domain, NarK1-NarK2 porter (NarK1 = a NO₃^-/H⁺ symporter; NarK2 = a NO₃^-/NO₂^- antiporter). NarK1 is a nitrate/proton symporter with high affinity for nitrate while NarK2 is a nitrate/nitrite antiporter with lower affinity for nitrate (Goddard et al., 2008). Each transporter requires two conserved arginine residues for activity. A transporter consisting of inactivated NarK1 fused to active NarK2 has a dramatically increased affinity for nitrate compared with NarK2 alone, implying a functional interaction between the two domains (Goddard et al., 2008).	Bacteria	NarK1/NarK2 of Roseobacter denitrificans (Q166T6)
2.A.1.8.12	The root cortical and epidermal cell, high affinity, plasma membrane, NO₃^- uptake transporter, NRT2.1 (Wirth et al., 2007). Also functions in nitrate sensing and signaling (Miller et al., 2007; Girin et al., 2010). Activity only occurs when NRT2.1 is complexed with NAR2.1 (WR3; 8.A.20.1.1) in a 2:2 tetrameric complex (Yong et al., 2010). NAR2.1 has an N-terminal and a C-terminal TMS and has been annotated as a calcineurin-like phosphoesterase family member (Yong et al., 2010).	Plants	NRT2.1 of Arabidopsis thaliana (O82811)
2.A.1.8.13	High affinity nitrate uptake porter, NrtB (Unkles et al., 1991; 2011)	Fungi	NrtB of Emericella (Aspergillus) nidulans (Q8X193)
2.A.1.8.14	Nitrate/nitrite uptake porter, NapA (Wang et al., 2000)	Cyanobacteria	NapA of Trichodesmium sp. WH 9601 (Q9RA38)
2.A.1.8.15	Probable nitrate transporter NarT	Bacteria	NarT of Staphylococcus carnosus
2.A.1.9: The Phosphate: H⁺ Symporter (PHS) Family
2.A.1.9.1	High affinity P_i uptake porter (also functions in Mn²⁺ homeostasis); may transport a phosphate · Mn²⁺ complex (Jensen et al., 2003). Also takes up selenite (Lazard et al., 2010).	Yeast	Pho84 of Saccharomyces cerevisiae (P25297)
2.A.1.9.2	P_i uptake porter, Pho84	Fungi	Pho-84 of Neurospora crassa (Q7RVX9)
2.A.1.9.3	P_i uptake porter. Four close paralogues in Medicago truncatula (PT1-4), all localized to roots, show differing affinities for phosphate (Liu et al. 2008).	Plants	PT1 of Solanum tuberosum
2.A.1.9.4	Pht1;2(1;4) (PT2), a low affinity Pi uptake transporter, functioning throughout the plant (Ai et al., 2009) (76% identical to 2.A.1.9.3).	Plants	Pht1;2(1;4) of Oryza sativa (Q01MW8)
2.A.1.9.5	Pht1;6 (PT6), a high affinity Pi uptake transporter, functioning thoughout the plant (Ai et al., 2009) (75% identical to 2.A.1.9.3)	Plants	Pht1;6 (PT6) of Oryza sativa (Q8H6H0)
2.A.1.9.6	Phosphate transporter-5, PT5. Catalyzes phosphate:H⁺ symport (Liu et al., 2008).	Plants	PT5 of Medicago truncatula (A5H2U6)
2.A.1.9.7	Probable metabolite transport protein GIT1	Fungi	GIT1 of Saccharomyces cerevisiae
2.A.1.9.8	Putative inorganic phosphate transporter C23D3.12	Yeast	SPAC23D3.12 of Schizosaccharomyces pombe
2.A.1.9.9	Inorganic phosphate transporter 1-1 (AtPht1;1) (H(+)/Pi cotransporter)	Plants	PHT1-1 of Arabidopsis thaliana
2.A.1.10: The Nucleoside: H⁺ Symporter (NHS) Family
2.A.1.10.1	Nucleoside porter, NupG. Guanosine, inosine, cytidine and thymidine but not uridine, adenosine and xanthosine are transported (Patching et al. 2005).	Bacteria	NupG of E. coli (P0AFF4)
2.A.1.10.2	Xanthosine porter, XapB. Xanthosine, inosine, adenosine, cytidine and thymidine but not guanosine and uridine are transported (Seeger et al. 1995; Nørholm and Dandanell 2001 Nørholm and Dandanell 2001).	Bacteria	XapB of E. coli
2.A.1.10.3	Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-glucosyltransferase (EC 2.4.1.256) (Alpha-1,2-glucosyltransferase ALG10-A) (Alpha-2-glucosyltransferase ALG10) (Asparagine-linked glycosylation protein 10) (Dolichyl-phosphoglucose-dependent glucosyltransferase ALG10)	Fungi	DIE2 of Saccharomyces cerevisiae
2.A.1.10.4	Putative nucleoside transporter YegT	Bacteria	yegT of Escherichia coli
2.A.1.11: The Oxalate:Formate Antiporter (OFA) Family
2.A.1.11.1	The oxalate:formate antiporter	Bacteria	OxlT of Oxalobacter formigenes
2.A.1.11.2	Putative MFS transporter of 399 aas; 12 TMSs.	Bacteria	MFS porter of Pseudomonas aeruginosa (Q9I458)
2.A.1.11.3	Inner membrane protein yhjX	Bacteria	yhjX of Escherichia coli
2.A.1.11.4	Uncharacterized membrane protein YJL163C	Fungi	YJL163C of Saccharomyces cerevisiae
2.A.1.11.5	Uncharacterized MFS-type transporter YcxA (ORF5)	Bacilli	YcxA of Bacillus subtilis
2.A.1.11.6	Uncharacterized MFS-type transporter YbfB	Bacilli	YbfB of Bacillus subtilis
2.A.1.12: The Sialate:H⁺ Symporter (SHS) Family
2.A.1.12.1	The sialic acid porter	Bacteria	NanT of E. coli
2.A.1.12.2	The lactate/pyruvate:H⁺ symporter. Residues in the substrate translocation pathway have been reported (Soares-Silva et al., 2011).	Yeast	Jen1 (YKL217w) of Saccharomyces cerevisiae
2.A.1.13: The Monocarboxylate Porter (MCP) Family (Halestrap, 2011)
2.A.1.13.1	The proton-linked monocarboxylate (lactate, pyruvate, mevalonate, branched chain oxo acids, β-hydroxybutyrate, γ-hydroxybutyrate, butyrate, acetoacetate acetate and formate) uptake/efflux porter (Moschen et al. 2012). Activity is stimulated by direct interaction with carbonic anhydrase isoform II (Becker et al., 2005). This transporter interacts physically with the chaperone protein Basigin (CD147; TC #8.A.23.1.1) which is required both for targetting to the plasma membrane and for activity. Mct-2 uses a different chaperone protein, GP70. Mct-1 also transports the methionine hydroxy analogue 2-hydroxy (4-methylthio) butanate (Martin-Venegas et al., 2007). Activity is stimulated by binding of carbonic anhydrase II (Becker and Deitmer, 2008). MCT1, 3 and 4 require the ancillary protein, basigin (P35613; 8.A.23.1.1) for plasma membrane localization (Ovens et al., 2010).	Animals	MCT1 (SLC16A1) of Homo sapiens
2.A.1.13.2	The low affinity aromatic amino acid (Tyr, Trp, Phe) transporter, TAT1, MCT10, Slc16a10. Also transports N-methyl amino acids. Essential for aromatic amino acid homeostasis in various tissues of mice (Mariotta et al. 2012).	Animals	Tat1 of Rattus norvegicus
2.A.1.13.3	The thyroid hormone transporter, MCT8 (transports L- and D-isomers of thyroxine (T4), 3,3',5-triiodothyronine (T3), 3,3'5'-triiodothyronine (rT3) and 3,3'-diiodothyronine [Km values = 2-5 μM; Leu, Phe, Trp and Tyr were not transported]) (Friesema et al., 2003). Loss of function mutations in MCT8 leads to Allan-Herndon-Dudley syndrome, severe X-linked psychomotor retardation and elevated serum T3 levels (Jansen et al., 2008). Essential molecular determinants for thyroid hormone transport and their structural implications are presented by Kinne et al. (2010). Induced by retinoic acid (Kogai et al., 2010). Mediates energy-independent bidirectional transport. MCT8 is specific for L-iodothyronines and requires at least one iodine atom per aromatic ring. Thyronamines, decarboxylated metabolites of iodothyronines, triiodothyroacetic acid and tetraiodothyroacetic acid, TH derivatives lacking both chiral center and amino group, are not substrates (Kinne et al., 2010). A deficiency causes altered thyroid morphology and a persistent high triiodothyronine/thyroxine ratio after thyroidectomy (Wirth et al., 2011). Primary and secondary thyroid hormone transporters have been reviewed (Kinne et al., 2011).	Animals	MCT8 of Mus musculus (O70324)
2.A.1.13.4	The high affinity (17 μM) facilitated diffusion, riboflavin-regulated riboflavin uptake system, Mch5 (Reihl and Stolz, 2005)	Yeast	Mch5 of Saccharomyces cerevisiae (NP_014951)
2.A.1.13.5	Monocarboxylate transporter-2 (MCT2). Transports γ-hydroxybutyrate (Wang and Morris, 2007). MCT2 requires the ancillary protein, embigin (Q6PCB8; 8.A.23.1.2) for plasma membrane localization (Ovens et al., 2010).	Animals	MCT2 (SLC16A7) of Homo sapiens
2.A.1.13.6	Plasma membrane proton-linked monocarboxylate transporter, MCT4 (SLC16A3). Catalyzes the rapid plasma membrane transport of many monocarboxylates such as lactate, pyruvate, branched-chain oxo acids derived from leucine, valine and isoleucine, and the ketone bodies acetoacetate, beta-hydroxybutyrate and acetate	Animals	MCT4 (SLC16A3) of Homo sapiens
2.A.1.13.7	Monocarboxylate transporter-4 (MCT4). Lactate transport via the monocarboxylate transporter isoform 4 is non enzymatically stimulated by carbonic anhydrase II (Becker et al., 2010). MCT1, 3 and 4 require the ancillary protein, basigin (P35613; 8.A.23.1.1) for plasma membrane localization (Ovens et al., 2010).	Animals	SLC16A4 of Homo sapiens
2.A.1.13.8	Monocarboxylate transporter, MCTI0. Transports thyroid horomones (Visser et al., 2010). Primary and secondary thyroid hormone transporters have been reviewed (Kinne et al., 2011).	Animals	SLC16A10 of Homo sapiens
2.A.1.13.9	Short chain monocarboxylate (lactate) transporter 3, MCT3. MCT1, 3 and 4 require the ancillary protein, basigin (P35613; 8.A.23.1.1) for plasma membrane localization (Ovens et al., 2010).	Animals	SLC16A8 of Homo sapiens
2.A.1.13.10	MCT8 (SLC16a2) monocarboxylate thyroid hormone transporter 8 (Arjona et al., 2011). The X-linked mental retardation Allan-Herndon-Dudley syndrome (AHDS) protein (Schweizer and Köhrle 2012). AHDS is accompanied by several severe physiological symptoms (Boccone et al. 2010).	Animals	SLC16A2 of Homo sapiens
2.A.1.13.11	solute carrier family 16, member 5 (monocarboxylic acid transporter 6)	Animals	SLC16A5 of Homo sapiens
2.A.1.13.12	solute carrier family 16, member 14 (monocarboxylic acid transporter 14)	Animals	SLC16A14 of Homo sapiens
2.A.1.13.13	solute carrier family 16, member 11 (monocarboxylic acid transporter 11)	Animals	SLC16A11 of Homo sapiens
2.A.1.13.14	solute carrier family 16, member 12 (monocarboxylic acid transporter 12)	Animals	SLC16A12 of Homo sapiens
2.A.1.13.15	Monocarboxylate transporter 7 (MCT 7) (Monocarboxylate transporter 6) (MCT 6) (Solute carrier family 16 member 6)	Animals	SLC16A6 of Homo sapiens
2.A.1.13.16	Monocarboxylate transporter 9 (MCT 9) (Solute carrier family 16 member 9)	Animals	SLC16A9 of Homo sapiens
2.A.1.13.17	Monocarboxylate transporter 13 (MCT 13) (Solute carrier family 16 member 13)	Animals	SLC16A13 of Homo sapiens
2.A.1.13.18	Probable transporter MCH2	Fungi	MCH2 of Saccharomyces cerevisiae S288c
2.A.1.13.19	Probable transporter MCH4	Fungi	MCH4 of Saccharomyces cerevisiae
2.A.1.14: The Anion:Cation Symporter (ACS) Family
2.A.1.14.1	Glucarate porter	Bacteria	GudT of Bacillus subtilis
2.A.1.14.2	Hexuronate (glucuronate; galacturonate) porter	Bacteria	ExuT of E. coli (P0AA78)
2.A.1.14.3	Putative tartrate porter	Bacteria	TtuB of Agrobacterium vitis
2.A.1.14.4	Dipeptide (e.g., Gly-Leu), allantoate, ureidosuccinate, allantoin porter (Cai et al., 2007).	Yeast	Dal5 of Saccharomyces cerevisiae
2.A.1.14.5	Phthalate porter	Bacteria	Pht1 of Pseudomonas putida
2.A.1.14.6	Na:P_i symporter, NPT1 or SLC17A1. (Renal chloride-dependent polyspecific anion exporter; transports organic acids such as p-aminohippurate, ureate, and acetylsalicylate (asprin)). Catalyzes ureate excretion. A mutant form shows increased risk of gout in humans.	Animals	Npt1 of Mus musculus
2.A.1.14.7	Galactonate transporter	Bacteria	DgoT (YidT) of E. coli (P0AA76)
2.A.1.14.8	Phthalate porter	Bacteria	OphD of Burkholderia cepacia
2.A.1.14.9	Putative p-hydroxyphenylacetate porter	Bacteria	HpaX of Salmonella dublin
2.A.1.14.10	Lysosomal sialate transporter (Salla disease and infantile sialate storage disease protein (Morin et al., 2004)). Also transports glucuronic acid and aspartate. Structure-function studies have identify crucial residues and substrate-induced conformational changes (Courville et al., 2010). Also called SLC17A5. The substrate binding pocket has been identified based on modeling studies (Pietrancosta et al., 2012).	Animals	SLC17A5 of Homo sapiens
2.A.1.14.11	Plasma membrane, high affinity nicotinate permease, Tna1	Yeast	Tna1 of Saccharomyces cerevisiae
2.A.1.14.12	Plasma membrane, high affinity biotin:H⁺ symporter, Vht1	Yeast	Vht1 of Saccharomyces cerevisiae
2.A.1.14.13	Broad specificity brain synaptic vesicle anion:Na⁺ symporter (transports glutamate, phosphate, chloride, etc.)(BNPI, EAT-4, VGLUT1) Chloride and ketone bodies regulate VGLUT activities (Omote et al., 2011).	Animals	BNPI of Rattus norvegicus
2.A.1.14.14	Probable D-galactarate (glucarate?):H symporter, GarP or YhaU. May also function as a glucarate:glycerate antiporter (Moraes and Reithmeier 2012).	Bacteria	GarP (YhaU) of E. coli
2.A.1.14.15	Apical membrane renal proximal tubule. Voltage-driven but Na⁺-independent organic anion transporter, OAT_v1 (transports p-aminohippurate; probably transports organic anions but not cations and not inorganic phosphate. It may catalyze excretion of various drugs, xenobiotics, and their metabolites) (Jutabha et al., 2003)	Animals	OAT_v1 of Sus scrofa (Q7YQJ7)
2.A.1.14.16	The broad specificity brain synaptic vesicle anion transporter (transports glutamate in a Δψ-dependent fashion requiring Cl^- but phosphate by a Na⁺-dependent mechanism via a different pathway/mechanism (Juge et al., 2006). VGLUT1-3 concentrate glutamate into synaptic vesicles before its exocytotic release.	Animals	VGLUT2 of Rattus norvegicus (Q9JI12)
2.A.1.14.17	Pantothenate:H⁺ symporter, Liz1 (mutants cause abnormal mitosis due to a defect in ribonucleotide reductase) (Stolz et al., 2004)	Yeast	Liz1 of Schizosaccharomyces pombe (O43000)
2.A.1.14.18	Pantothenate:H⁺ symporter, Fen2	Yeast	Fen2 of Saccharomyces cerevisiae (P25621)
2.A.1.14.19	Plasma membrane, high affinity vitamin H transporter 1 (H⁺:biotin symporter), Vht1 (Stolz, 2003)	Yeast	Vht1 of Schizosaccharomyces pombe (O13880)
2.A.1.14.20	Endoplasmic reticular cysteine transporter, Yct1 (Kaur and Bachhawat, 2007)	Yeast	Yct1 of Saccharomyces cerevisiae (Q12235)
2.A.1.14.21	The vesicular purine nucleotide (ADP, ATP, GTP) transporter. (Found in synaptic vesicles and chromafin granules, SLC17A9 (Sawada et al., 2008)).	Animals	SLC17A9 of Homo sapiens
2.A.1.14.22	The chloroplast thylakoid Na⁺:phosphate symporter, ANTR1 (512aas) (Pavón et al., 2008). Residues essential for function have been identified (Ruiz-Pavón et al., 2010). Functionally important amino acids have been identified (Ruiz-Pavón et al., 2010).	Plants	ANTR1 of Arabidopsis thaliana (O82390)
2.A.1.14.23	Vesicular glutamate transporter #3 (VGLUT3) [Its absence in mice causes sensorineural deafness and seizures]. 70% identical to VGLUT2 (TC# 2.A.1.14.16) (Gras et al., 2002). VGLUT1-3 concentrate glutamate into synaptic vesicles before its exocytotic release and contribute to the regulation of serotonergic transmission and anxiety (Amilhon et al., 2010).	Animals	VGLUT3 of Mus musculus (Q8BFU8)
2.A.1.14.24	Intestinal mucosal sodium/phosphate symporter, SLC17A4. Maintains phosphate homeostasis; mediates intestinal absorption, bone deposition and resorption and renal excretion.	Animals	SLC17A4 of Homo sapiens
2.A.1.14.25	The putative D-mannuronate porter, AlgT (Rodionov et al., 2010).	Proteobacteria	AlgT of Shewanella frigidimarina (Q07YH1)
2.A.1.14.26	The plasma membrane Lethal (2)01810 glutamate uptake porter (K_m=0.07μM) (Inhibited by aspartate) (Shim et al., 2011)	Animals	L(2)01810 of Drosophila melanogaster (F2YPN7)
2.A.1.14.27	solute carrier family 17 (sodium phosphate), member 1	Animals	SLC17A1 of Homo sapiens
2.A.1.14.28	solute carrier family 17 (sodium phosphate), member 3	Animals	SLC17A3 of Homo sapiens
2.A.1.14.29	Sodium-dependent phosphate transport protein 3 (Na(+)/PI cotransporter 3) (Sodium/phosphate cotransporter 3) (Solute carrier family 17 member 2)	Animals	SLC17A2 of Homo sapiens
2.A.1.14.30	Vesicular glutamate transporter 1 (VGluT1) (Brain-specific Na(+)-dependent inorganic phosphate cotransporter) (Solute carrier family 17 member 7)	Animals	SLC17A7 of Homo sapiens
2.A.1.14.31	Vesicular glutamate transporter 2 (VGluT2) (Differentiation-associated BNPI) (Differentiation-associated Na(+)-dependent inorganic phosphate cotransporter) (Solute carrier family 17 member 6)	Animals	SLC17A6 of Homo sapiens
2.A.1.14.32	Vesicular glutamate transporter 3 (VGluT3) (Solute carrier family 17 member 8)	Animals	SLC17A8 of Homo sapiens
2.A.1.14.33	L-galactonate transporter, YjjL	Bacteria	YjjL of Escherichia coli
2.A.1.14.34	Putative inorganic phosphate cotransporter	Animals	Picot of Drosophila melanogaster
2.A.1.14.35	Inner membrane transport protein RhmT	Bacteria	RhmT of Escherichia coli
2.A.1.14.36	Thiamine pathway transporter THI73	Fungi	THI73 of Saccharomyces cerevisiae
2.A.1.14.37	Probable transporter SEO1	Fungi	SEO1 of Saccharomyces cerevisiae
2.A.1.14.38	Uncharacterized transporter YIL166C	Fungi	YIL166C of Saccharomyces cerevisiae
2.A.1.14.39	Uncharacterized transporter YybO	Bacilli	YybO of Bacillus subtilis
2.A.1.14.40	Glucarate transporter, GudP.� Encoded in an operon with GudD, a glucarate dehydratase (Moraes and Reithmeier 2012).	Bacteria	GudP of E. coli
2.A.1.15: The Aromatic Acid:H⁺ Symporter (AAHS) Family
2.A.1.15.1	4-Hydroxybenzoate/protocatachuate porter	Bacteria	PcaK of Pseudomonas putida
2.A.1.15.2	3-Hydroxyphenyl propionate porter	Bacteria	MhpT of E. coli
2.A.1.15.3	2,4-Dichlorophenoxyacetate porter	Bacteria	TfdK of Ralstonia eutropha
2.A.1.15.4	cis,cis-muconate porter, MucK	Bacteria	MucK of Acinetobacter sp. ADP1
2.A.1.15.5	Benzoate porter, BenK	Bacteria	BenK of Acinetobacter sp. ADPP1
2.A.1.15.6	Vanillate porter, VanK	Bacteria	VanK of Acinetobacter sp. ADP1
2.A.1.15.7	Niacin uptake porter NiaP (Jeanguenin et al. 2012)	Bacteria	YceI of Bacillus subtilis (O34691)
2.A.1.15.8	Probable 1-hydroxy-2-naphthoate transporter, orf1 (Iwabuchi and Harayama, 1997).	Bacteria	Orf1 of Nocardioides sp. (O24723)
2.A.1.15.9	Probable 4-methylmuconolactone transporter, MmlH (Erb et al., 1998)	Bacteria	MmlH of Ralstonia eutropha (O51798)
2.A.1.15.10	The gentisate (2,5-dihydroxybenzoate) uptake porter, GenK (does not take up either benzoate or 3-hydoxybenzoate).	Bacteria	GenK of Corynebacterium glutamicum (Q8NLB7)
2.A.1.15.11	The Vanillate porter, VanK	Bacteria	VanK of Corynebacterium glutamicum (Q6M372)
2.A.1.15.12	Inner membrane transport protein YdiM	Bacteria	YdiM of Escherichia coli
2.A.1.15.13	Inner membrane transport protein YdiN (Similar to 2.A.1.15.12)	Bacteria	YdiN of Escherichia coli
2.A.1.15.14	Synaptic vesicle 2-related protein (SV2-related protein)	Animals	Sv2p of Mus musculus
2.A.1.15.15	MFS Homologue	Actinobacteria	MFS homologue of Streptomyces coelicolor (Q9RL01)
2.A.1.15.16	MFS uptake permease. The gene is adjacent to a putative SAM-dependent methyl transferase, one homologue of which is a puromycin methyl transferase. Perhaps the transport substrate is a drug that is modified by methylation for detoxification purposes.	δ-Proteobacteria	MFS uptake permease of Myxococcus xanthus
2.A.1.15.17	Fused protein with N-terminal transmembrane region of 7 putative TMSs and a C-terminal hydrophilic domain homologous to SAM-dependent spermidine synthase.� The N-terminus of this protein shows extensive sequence similarity with 2.A.1.15.16 but shows weak similarity with other MFS permeases.	γ-Proteobacteria	Fused protein of Thiocapsa marina
2.A.1.16: The Siderophore-Iron Transporter (SIT) Family
2.A.1.16.1	Siderophore-iron (ferrioxamine):H⁺ sym- porter, Sit1 (Arn3) (in vesicles)	Yeast	Sit1 (YEL065w) of Saccharomyces cerevisiae
2.A.1.16.2	The ferric enterobactin:H⁺ symporter, Enb1	Yeast	Enb1 (YOL158c) of Saccharomyces cerevisiae
2.A.1.16.3	The ferric triacetylfusarinine C:H⁺ symporter, Taf1	Yeast	Taf1 (YHL047c) of Saccharomyces cerevisiae
2.A.1.16.4	The ferrichrome:H⁺ symporter, Arn1p (Moore et al., 2003)	Yeast	Arn1 of Saccharomyces cerevisiae (NP_011823)
2.A.1.16.5	Siderophore iron transporter 2	Yeast	str2 of Schizosaccharomyces pombe
2.A.1.16.6	Siderophore iron transporter 1, Str1	Yeast	Str1 of Schizosaccharomyces pombe
2.A.1.16.7	Ferri-siderophore transporter, MirB. Transports hydroxamate siderophores such as triacetylfusarinine C (TAFC) (Raymond-Bouchard et al. 2012).	Fungi	MirB of Emericella nidulans
2.A.1.17: The Cyanate Porter (CP) Family
2.A.1.17.1	Cyanate transport system, CynX. Encoded with cyanate aminohydrolase, CynS, and carbonic anhydrase, CynT (Moraes and Reithmeier 2012).	Bacteria	CynX of E. coli
2.A.1.17.2	Glucose transporter, OEOE_0819. Does not transport fructose (Kim et al., 2011)	Firmicutes	OEOE_0819 of Oenococcus onei (Q04FN1)
2.A.1.17.3	Inner membrane transport protein YeaN	Bacteria	YeaN of Escherichia coli
2.A.1.18: The Polyol Porter (PP) Family
2.A.1.18.1	D-Arabinitol:H⁺ symporter	Bacteria	DalT of Klebsiella pneumoniae
2.A.1.18.2	Ribitol:H⁺ symporter	Bacteria	RbtT of Klebsiella pneumoniae
2.A.1.18.3	Alpha-ketoglutarate permease	Bacilli	CsbX of Bacillus subtilis
*2.A.1.19: The Organic Cation Transporter (OCT) Family (The SLC22A family including OCT1-3, OCTN1-3 and OAT1-5 of H. sapiens)*
2.A.1.19.1	The basolateral multivalent, potential-sensitive, organic cation (tetramethyl-ammonium; N'-methylnicotinamide; cationic drugs, xenobiotics, vitamins, neuro-transmitters, etc.) transporter (uni-porter)-1, Oct1	Animals	Oct1 of Rattus norvegicus (Q63089)
2.A.1.19.2	The ergothionine/organic cation porter, OctN1 (SLC22A4). Associated with rheumatoid arthritis (Barton et al., 2005).	Animals	OctN1 of Homo sapiens (O14546)
2.A.1.19.3	The polyspecific organic cation (L- and D-carnitine, butyryl-L-carnitine, acetyl carnitine, γ-butyro-betaine, glycinebetaine, β-lactam antibiotics with a quaternary nitrogen such as cephaloridine, and others):Na symporter, OctN2 (SLC22A5). Associated with Crohn''s disease (Barton et al., 2005) as well as primary carnitine deficiency. The protein in glycosylated on extracytoplasmic asparagines, and these residues are in a region important for function and turnover (Filippo et al. 2011).	Animals	SLC22A5 of Homo sapiens
2.A.1.19.4	The polyspecific organic anion, cation and neutral molecule transporter, Oat1 (Slc22a6) (transports neutral compounds such as cardiac glycosides [i.e., ouabain] and steroids [i.e., aldosterone; cortisol; dexamethasone]; cationic compounds such as N-propylajmalinium, and anionic compounds such as p-aminohippurate, dicarboxylates, cyclic nucleotides, prostaglandins, urate, β-lactam antibiotics, nonsteroidal anti-inflammatory drugs, diuretics, bile salts and steroid conjugates [i.e., estrone-3-sulfate and estradiol-17-glucuronide]) transporter (H⁺ symporter or uniporter) Probably catalyzes organic anion (uptake):dicarboxylate (efflux) antiport in the basolateral membrane of kidney proximal tubules) (Eraly et al., 2003a,b). A 3-dimensional model of OAT1 has led to the identification of residues involved in differential transport of substrates such as p-aminohippurate and cidofovir (Perry et al., 2006). Oat1 transports many antiviral agents (Truong et al., 2008). The human orthologue (Q4U2R8; 563aas) has been shown to be a multispecific organic anion transporter on the basolateral membrane of the proximal tubule in human kidney (Hosoyamada et al. 1999). A substrate binding hinge domain is required for transport-related structural changes (Egenberger et al., 2012). Transports environmental toxins and clinically important drugs including anti-HIV therapeutics, anti-tumor drugs, antibiotics, anti-hypertensives, and anti-inflammatories (Duan et al., 2011). hOAT1 has two GXXXG motifs in TMSs 2 and 5 which play critical roles in stability (Duan et al., 2011).	Animals	Oat1 of Rattus norvegicus (O35956)
2.A.1.19.5	The putative apical polyspecific organic cation transporter (cation:H⁺ or cation:cation antiporter), Oct2 (substrates include monoamine neurotransmitters such as dopamine, noradrenaline, adrenaline and 5-hydroxytryptamine) (Oct2 exhibits some properties of an ion channel with an inner diameter of ~4 �. Selectivity: Cs⁺ > Rb⁺ > K⁺ > Na⁺ ≈ Li⁺ (Schmitt and Koepsell, 2005)) Chloride dependent, but a single mutation (R466K) abolishes this dependency (Rizwan et al., 2007). Also transports ochratoxin (Rizwan et al., 2007) and cisplatin and oxaliplatin (Yonezama et al., 2006).	Animals	Oct2 of Sus scrofa (O02713)
2.A.1.19.6	The polyspecific potential-sensitive organic cation uptake transporter, Oct3 (transport substrates include the neurotoxin 1-methyl-4-phenylpyridinium and monoamine neurotransmitters such as dopamine). Mediates paraquat (herbicide) neurotoxicity (Rappold et al., 2011).	Animals	Oct3 of Rattus norvegicus (O88446)
2.A.1.19.7	The polyspecific organic anion (and cation) (anions: p-aminohippurate, ochratoxin A, estrone sulfate, anionic drugs, anionic neurotransmitter metabolites; cation: cimetidine) transporter, Oat3 (slc22a8) (catalyzes organic anion (uptake): dicarboxylate (efflux) antiport in the basolateral membrane of the renal proximal tubule) (Eraly et al., 2003a,b); transports many antiviral agents (Truong et al., 2008).	Animals	Oat3 of Rattus norvegicus (Q9R1U7)
2.A.1.19.8	The human organic cation transporter, SLC22A17.� The rat orthologue may be inactive (Bennett et al. 2011).	Animals	SLC22A17 of Homo sapiens
2.A.1.19.9	The osteosclerosis protein, Roct (organic anion transporter 3, Oat3) (Slc22a8) (catalyzes organic anion (uptake):di-carboxylate (efflux) antiport in the basolateral membrane of the renal proximal tubule) (Eraly et al., 2003a,b); transports glutathione and many antiviral agents (Truong et al., 2008).	Animals	Roct (Oat3) of Mus musculus (O88909)
2.A.1.19.10	The apical proximal tubular kidney/placenta organic anion transporter 4, Oat4 (Slc22a11) (transports estrone sulfate (K_m = 1 �M), dehydroepiandrosterone sulfate (K_m = 60�M), many anionic drugs, diuretics, bile salts, and ochratoxin A) (catalyzes Na⁺-independent efflux).	Animals	SLC22A11 of Homo sapiens
2.A.1.19.11	The apical proximal tubular renal urate:anion exchanger, URAT1 (Slc22a12) (catalyzes Na⁺-independent anion efflux (secretion)) (Eraly et al., 2003a,b; Anzai and Endou, 2011) (regulated by PDZK1 protein; Anzai et al., 2004). Also transports orotate, a precursor of pyrimidine biosynthesis (Miura et al., 2011). Mutations in URAT1 cause hereditary renal hypouricemia.	Animals	SLC22A12 of Homo sapiens
2.A.1.19.12	The high affinity L-carnitine transporter, CT2 (present in the luminal membranes of epididymal epithelia and Sertoli cells of the testis) (Enomoto et al., 2002b)	Animals	SLC22A16 of Homo sapiens
2.A.1.19.13	The organic cation transporter, Oct1 (transports L-carnitine; expressed in vascular tissues of various organs and at sites of lateral root formation) (Lelandais-Briere et al, 2007)	Plants	Oct1 of Arabidopsis thaliana (Q9CAT6)
2.A.1.19.14	Brush boarder glycosylated urate (Km= 1.2 mM) tranporter. Inhibited by 50 μM benzbromarone, 1 mM probenecid and 10 mM lactate which may also be transported and trans-stimulate urate uptake. May be orthologous to 2.A.1.19.11. (Hosoyamada et al., 2004).	Animals	URAT1 of Mus musculus (Q8CFZ5)
2.A.1.19.15	The liver multispecific organic anion transporter, NLT or OAT2. Transports salicylate, K_M=90�M, acetylsalicylate, prostaglandin E2, dicarboxylate, p-aminohippurate, etc. (Sekine et al., 1998)	Animals	NLT of Rattus norvegicus (Q63314)
2.A.1.19.16	The organic anion transporter, Oat6 (binding and transport rates for 40 anionic substrates were studied and compared with these for Oat1 (TC# 1.A.1.19.4) (Kaler et al., 2007); transports many antiviral agents (Truong et al., 2008).	Animals	Oat6 of Mus musculus (Q80UJ1)
2.A.1.19.17	Kidney organic cation transporter-like 3 ORCTL-3 (OAT10; SLC22A13) (Bahn et al., 2008) (transports nicotinate, p-aminohippurate and urate; K_M=20-40 mμM) via exchange for lactate).	Animals	SLC22A13 of Homo sapiens
2.A.1.19.18	Oranic anion transporter, Oat7 (exchanges sulfate conjugates (steroids) and other anions for butyrate) (Shin et al., 2007)	Animals	SLC22A9 of Homo sapiens
2.A.1.19.19	The rat kidney basolateral potential-driven symport carrier, Oct2 (transports tetraethylammonium and many other organic cations) (Sweet and Pritchard 1999).	animals	Oct2 of Rattus norvegicus (Q9R0W2)
2.A.1.19.20	Prostaglandin (PGE2, PGE2α, and PGD(2)) -specific organic anion transporter. Exhibits Na⁺ -independent and saturable transport. Shows narrow substrate selectivity and high affinity (Shiraya et al., 2010).	Animals	OAT-PG of Homo sapiens (Q8R0S9)
2.A.1.19.21	solute carrier family 22, member 24	Animals	SLC22A24 of Homo sapiens
2.A.1.19.22	solute carrier family 22, member 14	Animals	SLC22A14 of Homo sapiens
2.A.1.19.23	solute carrier family 22, member 31	Animals	SLC22A31 of Homo sapiens
2.A.1.19.24	Solute carrier family 22 member 3 (Extraneuronal monoamine transporter) (EMT) (Organic cation transporter 3)	Animals	SLC22A3 of Homo sapiens
2.A.1.19.25	Solute carrier family 22 member 7 (Novel liver transporter) (Organic anion transporter 2) (hOAT2)	Animals	SLC22A7 of Homo sapiens
2.A.1.19.26	Solute carrier family 22 member 4 (Ergothioneine transporter) (ET transporter) (Organic cation/carnitine transporter 1)	Animals	SLC22A4 of Homo sapiens
2.A.1.19.27	Solute carrier family 22 member 10 (Organic anion transporter 5)	Animals	SLC22A10 of Homo sapiens
2.A.1.19.28	Solute carrier family 22 member 23. The rat orthologue may be inactive (Bennett et al. 2011).	Animals	SLC22A23 of Homo sapiens
2.A.1.19.29	Solute carrier family 22 member 1 (Organic cation transporter 1) (hOCT1)	Animals	SLC22A1 of Homo sapiens
2.A.1.19.30	Solute carrier family 22 member 2 (Organic cation transporter 2) (hOCT2)	Animals	SLC22A2 of Homo sapiens
2.A.1.19.31	Solute carrier family 22 member 6 (Organic anion transporter 1) (hOAT1) (PAH transporter) (hPAHT) (Renal organic anion transporter 1) (hROAT1)	Animals	SLC22A6 of Homo sapiens
2.A.1.19.32	Solute carrier family 22 member 15 (Fly-like putative transporter 1) (Flipt 1)	Animals	SLC22A15 of Homo sapiens
2.A.1.19.33	Solute carrier family 22 member 25 (Organic anion transporter UST6)	Animals	SLC22A25 of Homo sapiens
2.A.1.19.34	Solute carrier family 22 member 8 (Organic anion transporter 3) (hOAT3)	Animals	SLC22A8 of Homo sapiens
2.A.1.19.35	Solute carrier family 22 member 20 (Organic anion transporter 6)	Animals	SLC22A20 of Homo sapiens
2.A.1.19.36	Organic cation transporter protein. OrcT	Animals	OrcT of Drosophila melanogaster
2.A.1.19.37	Organic cation transporter 1 (CeOCT1)	Worm	Oct-1 of Caenorhabditis elegans
2.A.1.19.38	Uncharacterized MFS-type transporter PB1E7.08c	Yeast	SPAPB1E7.08c of Schizosaccharomyces pombe
2.A.1.19.39	Organic cation/carnitine transporter 6 (AtOCT6)	Plants	OCT6 of Arabidopsis thaliana
2.A.1.20: The Sugar Efflux Transporter (SET) Family
2.A.1.20.1	Efflux system for lactose, glucose, aromatic glucosides and galactosides, cellobiose, maltose, α-methylglucoside, and isopropyl β-thiogalactosides (IPTG); amino-glycosides, streptomycin and kanamycin, weakly expelled	Bacteria	SetA (YabM) of E. coli
2.A.1.20.2	Efflux system for lactose and glucose, but not IPTG or galactose	Bacteria	SetB (YeiO) of E. coli
2.A.1.20.3	Putative efflux system for unknown substrates (none of those exported by SetA and SetB are exported by SetC)	Bacteria	SetC (YicK) of E. coli
2.A.1.20.4	Efflux system for arabinose and IPTG (>>lactose), SotA	Bacteria	SotA of Erwinia chrysanthemi
2.A.1.21: The Drug:H⁺ Antiporter-3 (12 Spanner) (DHA3) Family
2.A.1.21.1	The macrolide (erythromycin; oleando-mycin; azithromycin) efflux, MefA	Bacteria	MefA of Streptococcus pyogenes
2.A.1.21.2	The multidrug (erythromycin, tetracycline, puromycin, bleomycin) resistance protein, Cmr	Bacteria	Cmr of Corynebacterium glutamicum
2.A.1.21.3	The tetracycline resistance determinant, TetV	Bacteria	TetV of Mycobacterium smegmatis
2.A.1.21.4	Multidrug resistance efflux pump, Tap	Bacteria	Tap of Mycobacterium fortuitum
2.A.1.21.5	The putative bacilysin exporter, BacE	Bacteria	BacE of Bacillus subtilis (P39642)
2.A.1.21.6	The tetracycline resistance efflux pump, TetA(P) (Bannam et al., 2004) (21% identity (e^-07) with 2.A.1.21.5 and 22% identity (2xe^-7) with 2.A.1.2.10). It may be the link between DHA1 and DHA3.	Bacteria	TetA (P) of Clostridium perfringens (Q46305)
2.A.1.21.7	The Staphyloferrin A (siderophore) exporter, NWMN-2081 (Beasley et al. 2009).	Bacteria	NWMN-2081 of Staphylococcus aureus (A6QJ21)
2.A.1.21.8	The putative macrolide exporter, TIGR00900 (most similar to 2.A.1.21.1).	Bacteria	TIGR00900 of Bacillus clausii (Q5WAS7)
2.A.1.21.9	MFS carrier of unknown function	Archaea	MFS carrier of Thermoplasma acidophilum (Q9HLP1)
2.A.1.21.10	MFS porter	Archaea	MFS porter of Sulfolobus islandicus (D2PCQ8)
2.A.1.21.11	MFS porter	Bacteria	MFS porter of Stackebrandtia nassauensis (D3Q871)
2.A.1.21.12	Probable multidrug-efflux transporter Rv1258c/MT1297	Bacteria	Rv1258c of Mycobacterium tuberculosis
2.A.1.21.13	Uncharacterized MFS-type transporter yjbB	Bacilli	YjbB of Bacillus subtilis
2.A.1.21.14	Uncharacterized MFS-type transporter Mb0038c	Actinobacteria	Mb0038c of Mycobacterium bovis
2.A.1.21.15	MFS Homologue	Actinobacteria	MFS homologue of Streptomyces coelicolor (Q9X9Y0)
2.A.1.21.16	MFS Homologue	Actinobacteria	MFS homologue of Streptomyces coelicolor (Q9X8T4)
2.A.1.21.17	Uncharacterized MFS-type transporter YxaM	Bacilli	YxaM of Bacillus subtilis
2.A.1.21.18	Uncharacterized protein	Actinobacteria	Uncharacterized protein of Streptomyces coelicolor
2.A.1.21.19	Uncharacterized Major Facilitator	Actinobacteria	UMF of Streptomyces coelicolor
2.A.1.21.20	Unidentified Major Facilitator	Proteobacteria	UMF of Pseudomonas syringae
2.A.1.21.21	Unidentified major facilitator	Actinobacteria	UMF of Saccharomonospora marina
2.A.1.22: The Vesicular Neurotransmitter Transporter (VNT) Family (Related to the SP Family (TC #2.1.1))
2.A.1.22.1	Synaptic vesicle neurotransmitter (e.g., dopamine) transporter	Animals	SV2 of Rattus norvegicus
2.A.1.23: The Conjugated Bile Salt Transporter (BST) Family
2.A.1.23.1	Conjugated bile salt:H⁺ symporter, CbsT1	Bacteria	CbsT1 of Lactobacillus johnsonii 100-100
2.A.1.23.2	Taurocholate:cholate antiporter, CbsT2	Bacteria	CbsT2 of Lactobacillus johnsonii 100-100 (AAC34380)
2.A.1.24: The Unknown Major Facilitator-1 (UMF1) Family
2.A.1.24.1	58.8 KDa protein, YCL038c	Yeast	YCL038c of Saccharomyces cerevisiae
2.A.1.24.2	Putative vacuolar amino acid efflux porter, Atg22 (Autophagy-related protein-22)	Yeast	Atg22 of Schizosaccharomyces pombe (Q09812)
2.A.1.24.3	MFS permease	Bacteria	MFS permease of Chloroflexus aurantiacus (A9WGR7)
2.A.1.24.4	MFS permease	Bacteria	MFS permease of Myxococcus xanthus (Q1CWQ3)
2.A.1.25: The Peptide-Acetyl-Coenzyme A Transporter (PAT) Family
2.A.1.25.1	The endoplasmic reticular/golgi acetyl-CoA:CoA antiporter 1, ACATN/ACATN1 (SLC33A1). Allows acetylation of sialic acid residues in gangliosides and lysine residues in membrane proteins. It is associated with neurodegenerative disorders such as sporadic amyotrophic laterial sclerosis (ALS) and Spastic Paraplegia 42, and it is essential for motor neuron viability (Hirabayashi et al. 2013).	Animals	SLC33A1 of Homo sapiens
2.A.1.25.2	Cell wall degradation product (peptides and glycopeptides including N-acetylglucosaminyl β-1,4-anhydro-N-acetyl-muramyl-tripeptide) as well as penicillin derivative uptake porter, AmpG	Bacteria	AmpG of E. coli (P0AE16)
2.A.1.25.3	The AmpG peptidoglycan uptake porter; part of the peptidoglycan recycling pathway (Garcia and Dillard, 2008)	Bacteria	AmpG of Neisseria gonorrhoeae (Q5F6G0)
2.A.1.25.4	Major facilitator superfamily domain-containing protein 3	Animals	Mfsd3 of Rattus norvegicus
2.A.1.25.5	Transporter of N-acetylglucosamine anhydrous N-acetylmuramyl peptides, AmpG (Kong et al. 2010). Necessary for induction of β-lactam resistance (Zhang et al. 2010).	Bacteria	AmpG of Pseudomonas aeruginosa
2.A.1.25.6	The Ferripyochelin uptake permease, FptX (Michel et al., 2007). Also transports N-acetylglucosamine anhydrous N-acetylmuramyl peptides and is called AmpP or AmpGh1 (Kong et al. 2010). However, it does not play a role in the induction of β-lactam resistance (Zhang et al. 2010).	Bacteria	FptX or AmpP of Pseudomonas aeruginosa (Q9HWG8)
2.A.1.26: The Unknown Major Facilitator-2 (UMF2) Family
2.A.1.26.1	41.4 KDa Protein, YcaD	Bacteria	YcaD of E. coli
2.A.1.26.2	MFS porter, YfkF; possible drug exporter	Bacteria	YfkF of Bacillus subtilis (O34929)
2.A.1.27: The Phenyl Propionate Permease (PPP) Family
2.A.1.27.1	The phenylpropionate porter, HcaT	Bacteria	HcaT (YfhS) of E. coli
2.A.1.28: The Feline Leukemia Virus Subgroup C Receptor (FLVCR) Family
2.A.1.28.1	Cell surface receptor (c-receptor) for anemia-inducing feline leukemia virus subgroup C (FLCVR); functions in haem export in haemopoietic cells (Latunde-Dada et al., 2006; Khan and Quigley, 2011). May cause Diamond-Blackfan anemia when defective (Keel et al., 2008). Mutations of FLVCR1 in posterior column ataxia and retinitis pigmentosa result in the loss of heme export activity (Yanatori et al., 2012). Heme accumulation causes toxicity.	Animals	C-receptor of Homo sapiens
2.A.1.28.2	The MFS-Domain7 protein (516aa) (the MFS-D7 mRNA is expressed in many human tissues, especially in lungs and testis).	Animals	MFSD7 of Mus musculus
2.A.1.28.3	Unknown major facilitator	Bacteria	UMF of Coriobacterium glomerans (F2NBU7)
2.A.1.28.4	The Fowler syndrome-associated protein, feline leukemia virus subgroup C receptor-related protein 2, is a heme importer (Duffy et al., 2010).	Animals	FLVC2 of Homo sapiens (Q9UPI3)
2.A.1.28.5	MFS porter	Bacteria	MFS porter of Leptospira biflexa (B0SL69)
2.A.1.28.6	Electrogenic DIRC2 (Disrupted in renal carcinoma 2) (glycosylated and proteolytically processed (Savalas et al., 2011)). Targeted to lysosomes via an N-terminal dileueine motif.	Animals	DIRC2 of Homo sapiens (Q96SL1)
2.A.1.28.7	Feline leukemia virus subgroup C receptor-related protein 1	Animals	FLVCR1 of Felis catus
2.A.1.29: The Unknown Major Facilitator-3 (UMF3) Family
2.A.1.29.1	Archaeal open reading frame	Archaea	Orf of Archaeoglobus fulgidus
2.A.1.29.2	Archaeal open reading frame	Archaea	Orf of Aeropyrum pernix
2.A.1.29.3	Bacterial unknown major facilitator	Bacteria	UMF3 member of Frankia sp. Eul1c (E3J3E7)
2.A.1.30: The Putative Abietane Diterpenoid Transporter (ADT) Family
2.A.1.30.1	Putative abietane uptake permease (in gene cluster for degradation of abietane diterpenoids), DitE	Bacteria	DitE of Pseudomonas abietaniphila BKME-9
2.A.1.31: The Nickel Resistance (Nre) Family
2.A.1.31.1	The Ni²⁺ efflux pump, NreB (Ni²⁺ inductible)	Bacteria	NreB of Achromobacter xylosoxidans plasmid pTOM
2.A.1.31.2	The Ni²⁺ resistance protein, NrsD	Bacteria	NrsD of Synechocystis PCC6803
2.A.1.31.3	The unknown porter, YfiS	Bacteria	YfiS of Bacillus subtilis (O31561)
2.A.1.32: The Putative Aromatic Compound/Drug Exporter (ACDE) Family
2.A.1.32.1	Putative aromatic compound/drug exporter. Enhances expression of the sigma X gene that functions to modify the cell envelope (Turner and Helmann, 2000). yitG is reported to be a mutator gene that inhibits transition base substitutions (Sasaki and Kurusu, 2004).	Bacilli	YitG of Bacillus subtilis
2.A.1.32.2	Bacillibactin exporter, YmfE (199aas; 6TMSs) (Miethke et al., 2008) (resembles the 2^nd half of YitG of B. subtilis (2.A.1.32.1). The sequence provided under acc# O31763 is only a fragment of the full length gene.	Bacteria	YmfE of Bacillus subtilis (O31763)
2.A.1.32.3	Multidrug efflux protein YfmO	Bacilli	YfmO of Bacillus subtilis
2.A.1.33: The Putative YqgE Transporter (YqgE; UMF4) Family
2.A.1.33.1	MFS homologue, YqgE. Co-transcribed with ftsI, encoding the peptidoglycan transpeptidase that crosslinks peptidoglycan strands, releasing free D-alanine. Possibly YqgE is a D-alanine uptake porter.	Bacteria; Archaea	YqgE of Bacillus subtilis (P54487)
2.A.1.33.2	UMF4 family member	Bacteria	UMF4 family member form Bacteroides ovatus (A7LYG9)
2.A.1.33.3	UMF4 family member (encoded near an α-glucuronidase; GH31 family; divergently transcribed).	Archaea	UMF4 family member of Sulfolobus tokodaii (Q96XI6)
2.A.1.34: The Sensor Kinase-MFS Fusion (SK-MFS) Family
2.A.1.34.1	Sensor kinase (N-terminal 400 residues)/MFS fusion protein. The N-terminal domain resembles the sensor kinase of 414 aas of Anaeromyxobacter sp. KJ (ACG71775).	Bacteria	Fusion protein of Bordetella pertussis (Q7VWI9)
2.A.1.35: The Fosmidomycin Resistance (Fsr) Family
2.A.1.35.1	The fosmidomycin resistance (Fsr) protein (confers fosmidomycin, trimethoprim and carbonylcyanide m-chlorophenylhydrazone (CCCP) resistance)	Bacteria	Fsr of E. coli
2.A.1.35.2	The cationic microbial peptide resistance (RosA) protein	Bacteria	RosA of Yersinia enterocolitica
2.A.1.36: The Acriflavin-sensitivity (YnfM) Family
2.A.1.36.1	The acriflavin-sensitivity protein, YnfM (increases sensitivity to acriflavin specifically)	Bacteria	YnfM of E. coli
2.A.1.36.2	Hypothetical MFS carrier	Bacteria	MFS carrier of Serratia proteamaculans (A8GHT9)
2.A.1.36.3	Putative uncharacterized transporter YgaY	Bacteria	YgaY of Escherichia coli
2.A.1.38: The Enterobactin (Siderophore) Exporter (EntS) Family
2.A.1.38.1	The enterobactin (siderophore) exporter, EntS (Bleuel et al., 2005)	Bacteria	EntS (YbdA) of E. coli
2.A.1.38.2	The putative siderophore exporter (DUF 894; Pfam 05977), VabS	Bacteria	VabS of Listonella anguillarum (Q0E7C5)
2.A.1.38.3	Enterobactin exporter, EntS (Crouch et al., 2008) (probably orthologous to 2.A.1.38.1).	Bacteria	EntS of Salmonella typhimurium (Q8ZR35)
2.A.1.39: The Vibrioferrin (Siderophore) Exporter (PrsC) Family
2.A.1.39.1	The vibrioferrin (siderophore) exporter, PrsC (Tanabe et al., 2003)	Bacteria	PrsC of Vibrio parahaemolyticus (BAC16546)
2.A.1.40: Major Facilitator Superfamily Domain-containing Protein Family
2.A.1.40.1	Major facilitator superfamily domain-containing protein 5	Animals	Mfsd5 of Danio rerio
2.A.1.40.2	Major facilitator superfamily domain-containing protein 5	Animals	MFSD5 of Pongo abelii
2.A.1.41: The Putative Bacteriochlorophyll Delivery (BCD) Family
2.A.1.41.1	Putative pigment transporter (Young and Beatty, 1998)	Photosynthetic bacteria	LhaA of Rhodobacter capsulatus
2.A.1.41.2	Putative pigment transporter (Young and Beatty, 1998)	Photosynthetic bacteria	PucC of Rhodobacter capsulatus
2.A.1.41.3	Putative bacteriochlorophyll synthase	Photosynthetic bacteria	Bch2 of Rhodobacter capsulatus
2.A.1.42: The Lysophospholipid Transporter (LplT) Family
2.A.1.42.1	The lysophospholipid transporter, LplT (Harvat et al., 2005)	Bacteria	LplT of E. coli (NP_417312)
2.A.1.42.2	The putative lysophospholipid transporter-2-acyl glycerophosphoethanolamine acyl transferase/acyl ACP synthetase (LplT-Pls-ACS) fusion protein (Harvat et al., 2005).	Bacteria	The fused LplT-PlsC-ACS of Bradyrhizobium japonicum (BAC47589)
2.A.1.43: The Putative Magnetosome Permease (PMP) Family
2.A.1.43.1	The putative magnetosomal permease, MamH (Schubbe et al., 2003)	Bacteria	MamH of Magnetospirillum gryphiswaldense (Q6NE63)
2.A.1.43.2	The putative magnetosome (Fe?) permease fused to a C-terminal YedZ-like domain (von Rozycki et al., 2004). This protein has 649 aas and 18 TMSs with a C-terminal YedZ domain and is therefore in the YedZ superfamily.	Bacteria	PMP of Magnetospirillum magneticum (Q2W8K5)
2.A.1.44: The L-Amino Acid Transporter-3 (LAT3) Family (also called the SLC43 family)
2.A.1.44.1	The L-amino acid transporter-3, LAT3 (transports neutral amino acids such as L-leucine, L-isoleucine, L-valine, and L-phenylalanine by a Na⁺-independent, electroneutral, facilitated diffusion process; also transports amino acid alcohols) (Prostate cancer up-regulated gene product)	Animals	SLC43A1 of Homo sapiens
2.A.1.44.2	L-amino acid transporter-4 (LAT4) has the same specificity and is 57% identity to LAT3. Na⁺, Cl^- and pH independent; not trans-stimulated; two kinetic components, a low affinity component sensitive to NEM, and a high affinity component insensitive to NEM. Found in the basolateral membrane of epithelial cells in the distal tubule and collecting duct of the kidney and the crypt cells in the intestine (Bodoy et al., 2005).	Animals	SLC43A2 of Homo sapiens
2.A.1.44.3	solute carrier family 43, member 3	Animals	SLC43A3 of Homo sapiens
2.A.1.45: The 2,4-diacetylphloroglucinol (PHL) Exporter (PHL-E) Family
2.A.1.45.1	The 2,4-diacetylphloroglucinol resistance/general stress porter, PhlE (Abbas et al., 2004)	Bacteria	PhlE of Pseudomonas fluorescens (CAD65845)
2.A.1.46: The Unknown Major Facilitator-5 (UMF5) Family
2.A.1.46.1	Probable transporter	Bacteria	Probable transporter of Bordetella pertussis (Q7W0Q7)
2.A.1.46.2	Putative transporter	Bacteria	Putative transporter of Tropheryma whipplei (Q83N16)
2.A.1.46.3	Putative drug resistance UMF5 family member	Eukaryotes	Putative MDR pump of Leishmania infantum
2.A.1.46.4	UMF15 family member	Archaea	UMF5 homologue of Methanosphaerula palustris (B8GFY3)
2.A.1.46.5	Putative quinolone resistance protein	Bacteria	MFS porter of Bacillus cereus (C2UR80)
2.A.1.46.6	UPF0226 protein YfcJ	Bacteria	YjcJ of E. coli
2.A.1.46.7	UPF0226 protein, YhhS	Bacteria	YhhS of E. coli
2.A.1.47: The Unknown Major Facilitator-6 (UMF6) Family
2.A.1.47.1	Putative transporter	Bacteria	Putative transporter of Lactobacillus plantarum (NP_784357)
2.A.1.47.2	UMF6 family member	Fermicutes	MFS carrier of Streptococcus suis (A4VY05)
2.A.1.47.3	Possible antibiotic peptide exporter (encoded in an operon together with lantibiotic biosynthesis enzymes)	Fermicutes	UMF6 family member of Streptococcus pneumoniae (B2IRN2)
2.A.1.48: The Vacuolar Basic Amino Acid Transporter (V-BAAT) Family
2.A.1.48.1	The vacuolar basic amino acid (histidine, lysine and arginine) transporter, Vba1 (catalyzes uptake into the vacuoles (equivalent to efflux from the cytoplasm)) (most similar to family 2.A.1.3; DHA2; 13-14 putative TMSs) (Shimazu et al., 2005)	Yeast	Vba1 of Saccharomyces cerevisiae (NP_013806)
2.A.1.48.2	The vacuolar basic amino acid (Arg, Lys, His) transporter, Vba2 (Shimazu et al., 2005)	Yeast	Vba2 of Saccharomyces cerevisiae (P38358)
2.A.1.48.3	Vacuolar G0 arrest protein, Fnx1; involved in amino acid (e.g., his, lys, ile, asn, etc) uptake into the vacuole (Chardwiriyapreecha et al., 2008).	Yeast	Fnx1 of Schizosaccharomyces pombe (Q09752)
2.A.1.48.4	Vacuolar amino acid uptake system, Fnx2 (Chardiwiriyapreecha et al., 2008)	Yeast	Fnx2 of Schizosaccharomyces pombe (O59726)
2.A.1.48.5	Vacuolar basic amino acid transporter 4	Fungi	VBA4 of Saccharomyces cerevisiae S288c
2.A.1.49: The Endosomal Spinster (Spinster) Family
2.A.1.49.1	The spinster protein, spin1 or spns1 gene product (involved in synaptic growth regulation; interacts with Bcl-2/Bcl-xL, affecting programmed cell death) (Nakano et al., 2001; Sanyal and Ramaswami, 2002; Yanagisawa et al., 2003). Probably transports sphingosine-1-phosphate (Fukuhara et al. 2012).	Animals	Spinster of Drosophila melanogaster (AAG43825)
2.A.1.49.2	The spinster homologue, Spin1 or Spns1 gene (interacts with Bc1-2/Bc1-XL to induce a caspase-independent autophagic cell death; may be required for embryogenesis) (Yanagisawa et al., 2003). Probable spingosine-1-phosphate (or sphingolipid) transporter (Nijnik et al. 2012).	Animals	Spin1 of Homo sapiens (Q9H2V7)
2.A.1.49.3	Probable sphingosine-1-phosphate (or sphingolipid) transporter, spinster homologue 3 (by similarity).	Plants	Spinster homologue 3 of Arabidopsis thaliana (F4IKF6)
2.A.1.49.4	Protein Spinster homolog 2 (Protein two of hearts)	Animals	Spns2 of Danio rerio
2.A.1.49.5	Probable sphingosine-1-phosphate or sphingolipid transporter, Spinster homolog 1 (by similarity).	Plants	At5g65687 of Arabidopsis thaliana
2.A.1.49.6	Sphingosine-1-phosphate transport protein, Spinster 2. Involved in immune development and lymphocyte trafficing (Nijnik et al. 2012; Fukuhara et al. 2012 ).�	Animals	SPNS2 of Homo sapiens
2.A.1.49.7	Bacterial Spinster homologue; possible sphingosine-1-phosphate transporter (by similarity only).	Proteobacteria	Spinster homologue of Myxococcus xanthus
2.A.1.49.8	Bacterial spinster homologue.� Possible sphingosine-1-phosphate transporter (by similarity only).	Acidobacteria	Spinster homologue of Terriglobus saanensis
2.A.1.50: The Proton Coupled Folate Transporter/Heme Carrier Protein (PCFT/HCP) Family
2.A.1.50.1	The apical intestinal and choroid plexus proton-coupled, high affinity folate transporter, the hereditary folate malabsorption protein, PCFT/HCP1 (Shin et al. 2010). Also reported to mediate heme-iron uptake from the gut lumen with duodenal epithelial cells (Shayeghi et al., 2005; Latunde-Dada et al., 2006; Subramanian et al., 2008, Shin et al., 2012b), but it shows a higher affinity for folate than heme) (Qiu et al., 2006). Responsible for folate uptake by choroid plexus epithelial cells (Wollack et al., 2007) and placenta (Yasuda et al., 2008). The rat orthologue (Q5EBA8) catalyzes H-dependent folate uptake in the intestine (Inoue et al., 2008). Responsible for the rare autosomal recessive disorder, hereditary folate malabsorption (Zhao and Goldman, 2007). PCFT/ICP1, when mutated, is the cause of Hereditary Folate Malabsorption in humans (Qiu et al., 2006; Shin et al., 2012). Evidence for a 12 TMS topology has been presented (Zhao et al., 2010; Qiu et al., 2006; Zhao et al., 2011). Downregulated in Chronic Kidney Disease (CKD) in heart, liver, and brain causing malabsorption (Bukhari et al., 2011). An IGXXG motif in TMS5 is important for folate binding and a GXXXG motif is involved in dimerization (Zhao et al., 2012). Inhibited by bicarbonate, bisulfite, nitrite and other anions (Zhao et al. 2013).	Animals	SLC46A1 of Homo sapiens
2.A.1.50.2	Thymic stromal cotransporter, TSCOT (Kim et al. 2000)	Animals	SLC46A2 of Homo sapiens
2.A.1.50.3	solute carrier family 46, member 3	Animals	SLC46A3 of Homo sapiens
2.A.1.51: The Unknown Major Facilitator 7 (UMF7) Family
2.A.1.51.1	Putative permease	Bacteria	Putative transporter of Azoarcus sp. EbN1 (CAI06874)
2.A.1.51.2	YjiJ MFS porter	Bacteria	YjiJ of E. coli (D6IHN4)
2.A.1.51.3	MFS permease	Bacteria	MFS permease of Thermus thermophilus (F6DF77)
2.A.1.52: The Unknown Major Facilitator-8 (UMF8) Family
2.A.1.52.1	The putative permease, YihN (most like NarK and UhpC, 21% identity)	Bacteria	YihN of E. coli (P32135)
2.A.1.52.2	YqcE putative transporter	Bacteria	YqcE pf E. coli (F4TJX1)
2.A.1.52.3	MFS permease	Bacteria	MFS permease of Propionibacterium acnes
2.A.1.53: The Proteobacterial Intraphagosomal Amino Acid Transporter (Pht) Family
2.A.1.53.1	The threonine uptake permease, PhtA (Sauer et al., 2005) (required for maximal growth in macrophages and Acanthamoeba castellanii)	Gamma proteobacteria	PhtA of Legionella pneumophila (YP_094583)
2.A.1.53.2	The valine uptake permease, PhtJ (required for maximal growth in macrophages and Acanthamoeba castellanii) (Chen et al., 2008)	Gamma proteobacteria	PhtJ of Legionella pneumophila (YP_095910)
2.A.1.53.3	The putative MFSDI transporter (463aas; 12 TMSs)	Animals	MFSDI of Homo sapiens (A6NID9)
2.A.1.54: The Unknown (Archaeal/Bacterial) Major Facilitator-9 (UMF9) Family
2.A.1.54.1	The archaeal uptake permease, MMP0835 (function unknown) (31% I, 49% S with PhtA)	Archaea	MMP0835 of Methanococcus maripaludis (CAF30391)
2.A.1.54.2	UMF-9	Bacteria	UMF9 of Geobacter sulfurreducens (Q747F2)
2.A.1.55: The Iron � Pyridine Thiocarboxylic Acid Transporter (PDTC-T) Family
2.A.1.55.1	The iron (Fe³⁺) � pyridine-2,6-bis(thiocarboxylic acid (PDTC)) uptake transporter, PdTE. Functions with the OMR, PdtK, 1.B.14.8.2 (most similar to 2.A.1.25.2, AmpG).	Bacteria	PdtE of Pseudomonas putida (ABC8353)
2.A.1.56: The 1,3-Dihydroxybenzene Transporter (DHB-T) Family
2.A.1.56.1	The 1,3-dihydroxybenzene (resorcinol) uptake permease, MFS_1 (Darley et al., 2007)	Bacteria	MFS_1 of Azoarcus anaerobius (YP_285101)
2.A.1.57: The Ferripyochelin Transporter (FptX) Family
2.A.1.58: The N-Acetylglucosamine Transporter (NAG-T) Family
2.A.1.58.1	The N-acetylglucosamine:H⁺ symporter, Ngt1 (Alvarez and Konopka, 2007)	Yeast	Ngt1 of Candida albicans (Q5A7S4)
2.A.1.58.2	May contribute to coordination of muscle contraction as regulatory subunit of a nonessential potassium channel complex. Subunit structure: May form a complex with sup-9 and sup-10 where unc-93 and sup-10 act as regulatory subunits of the two pore potassium channel sup-9.	Animals	Unc-93 of Caenorhabditis elegans (Q93380)
2.A.1.58.3	UNC93-like protein MFSD11 (Major facilitator superfamily domain-containing protein 11) (Protein ET)	Animals	MFSD11 of Mus musculus
2.A.1.59: Unidentified Major Facilitator-10 (UMF10) Family (mostly from Archaea but some from bacteria)
2.A.1.59.1	UMF10a of unknown function, (COG2270).	Archaea	UMF10a of Methanococcus aeolicus (A6UVW2)
2.A.1.59.2	UMF10b (in an operon with a sensor kinase/response regulator pair and an 8 TMS rhomboid protease)	Bacteria	UMF10b of Nostoc punctiforme (B2JBG5)
2.A.1.59.3	MFS permease, AF1541	Archaea	AF1541 of Archaeoglobus fulgidus (O28731)
2.A.1.59.4	MFS permease, LepA	Bacteria	LepA of Hydrogenivirga sp.128-5-R1-1 (A8UT57)
2.A.1.60: The Rhizopine-related MocC (MocC) Family
2.A.1.60.1	The rhizopine related transporter, MocC (could either transport a precursor for rhizopine biosynthesis into bacteroids or the finished product from the bacteroids) (Murphy et al., 1993)	Bacteria	MocC of Sinorhizobium meliloti (Q07609)
2.A.1.60.2	Inner membrane protein YbjJ	Bacteria	YbjJ of Escherichia coli
2.A.1.60.3	The multidrug (quinolone; tetarcycline) resistance pump, TcrA (Chang et al. 2011).	Bacteria	TcrA of Stenotrophomonas maltophilia (F2WVP9)
2.A.1.61: The Microcin C51 Immunity Protein (MccC) Family
2.A.1.61.1	The MccC microcin C51 immunity protein (exports the peptide-nucleotide 'Trojan horse' antibiotic) (Fomenko et al., 2003; Kazakov et al., 2007)	Bacteria	MccC of E. coli (Q83Y57)
2.A.1.62: The Unidentified Major Facilitator-11 (UMF11) Family
Possibly involved in transport of amino acids and their derivatives.
2.A.1.62.1	The UMF11 homologue	Bacteria	UMF11 of Staphylococcus aureus (A8YZ14)
2.A.1.62.2	Putative Macrolide efflux pump (P-MEP), possibly involved in transport of amino acids and their derivatives.	Bacteria	P-MEP of Fusobacterium sp. 7_1 (C3WVU9)
2.A.1.62.3	UMF11 (links UMF11 with UMF13)	Bacteria	UMF11 of Bacillus clausii (Q5WGH2)
2.A.1.63: The Unidentified Major Facilitator-12 (UMF12) Family
2.A.1.63.1	The UMF12 protein	Archaea	UMF12 of Methanosarcina barkeri (Q467Y6)
2.A.1.63.2	UMF12 Possible amino acid exporter	Archaea	UMF12 of Methanosarcina mazei (Q8PRW9)
2.A.1.63.3	Possible nucleotide or oligonucleotide uptake porter, UMF12	Bacteria	UMF12 of Deinococcus radiodurans (Q9RXM0)
2.A.1.63.4	MFS carrier	Eukaryotes	MFS carrier of Saccharomyces cerevisiae K7 (P47159)
2.A.1.64: The Unidentified Major Facilitator-13 (UMF13) Family
2.A.1.64.1	The UMF13 protein	Firmicutes	UMF13 of Streptococcus thermophilus (Q5M4L1)
2.A.1.64.2	Uncharacterized protein RP255	Bacteria	RP255 of Rickettsia prowazekii
2.A.1.65: The Unidentified Major Facilitator-14 (UMF14) Family
2.A.1.65.1	The putative MFS carrier, Sugar Baby (Sug, isoform D); has a hydrophilic domain between TMSs 3 and 4. Overexpression causes an increased lifespan by 17%.	Animals	Sugar Baby of Drosophila melanogaster (Q7KUF9)
2.A.1.65.2	Unknown MFS homologue; e^-6 with 2.A.1.5 family members; has a hydrophilic domain between TMSs 3 and 4.	Animals	UMF14 of Culex quinquefasciatus (B0W435)
2.A.1.65.3	Unknown MFS homologue UMF14 ( 833 aas, 12 TMSs in a 3+9 arrangement )	Animals	UMF14 of Anopheles gambiae (Q7Q0Z9)
2.A.1.65.4	UMF14 homologue	Animals	UMF14 pf Saccoglossus kowalevskii (UPI0001CBA96A)
2.A.1.65.5	MFS porter	Animals	MFS porter of Daphnia pulex (E9I268)
2.A.1.65.6	Macrophage MHC Class I receptor 2, Mmr2 or MFSD6	Animals	Mmr2 of Mus musculus (Q8CBH5)
2.A.1.65.7	MFS porter	Plants	MFS porter of Chlorella variablis (E1ZG13)
2.A.1.65.8	MFS permease	Bacteria	MFS permease of Thermoanaerobacter tengcongensis (Q8R7B7)
2.A.1.65.9	Maltose permease	Bacteria	MalA of Geobacillus stearothermophilus
2.A.1.65.10	Major facilitator superfamily domain-containing protein 6-like	Animals	MFSD6L of Homo sapiens
2.A.1.66: The Unidentified Major Facilitator-15 (UMF15) Family
2.A.1.66.1	MFS permease of unknown function (First half resembles 2.A.1.3.7 (e^-11) and 2.A.1.15.3 (e^-8)). Very likely to be a galactoside/galactose transporter; encoded within a gene cluster with β-galactosidase and galactose metabolic genes.	Archaea	MFS permease of Thermofilum pendens (A1RW34)
2.A.1.66.2	Putative 4-hydroxybenzoate uptake transporter, MFS_1 (in an operon with 2,3-diketo-5-methylthiopentyl-1-phosphate enolase-phosphatase of the methionine salvage pathway), using S-adenyl methionine (SAM) as substrate. May transport SAM.	Bacteria	MFS1 of Leptospira interrogans (Q8F7L4)
2.A.1.66.3	UMF15 Homologue	Eukaryotes (Stramenophiles)	UMF15 homologue of Thalassiosira pseudonana (B8BU21)
2.A.1.67: The Unidentified Major Facilitator-16 (UMF16) Family
2.A.1.67.1	MFS permease of unknown function (second half distantly resembles the first half of 2.A.1.41.3/e value of 0.001)	Bacteria	UMF16 of Kribbella flavida (D2PP09)
2.A.1.67.2	MFS porter	Bacteria	MFS porter of Arthrobacter aurescens (A1R564)
2.A.1.67.3	MFS porter	Bacteria	MFS porter of Erwinia pyrifoliae (D0FNI7)
2.A.1.67.4	MFS porter	Bacteria	MFS porter of Propionibacterium acnes (D1YEI1)
2.A.1.67.5	Duplicated MFS permease (901 amino acyl residues; ~24 TMSs)	Algae	Duplicated MFS permease of Chlamydomonas reinhardtii
2.A.1.68: The Glucose Transporter (GT) Family
2.A.1.68.1	The glucose transporter, OEOE_1574 does not transport fructose (Kim et al., 2011).	Firmicutes	OEOE_1574 of Oenococcus onei (Q04DP6)
2.A.1.69: Unidentified Major Facilitator-17 (UMF17) Family
2.A.1.69.1	The UMF17A porter	Bacteria	UMF17A porter of Streptomyces coelicolor (Q9KZY0)
2.A.1.70: Unidentified Major Facilitaor-18 (UMF18) Family
2.A.1.70.1	UMF18A	Bacteria	UMF18A of Streptomyces coelicolor (Q9L223)
2.A.1.70.2	UMF18B	Bacteria	UMF18B of Saccharomonospora azurea (G4JJZ0)
2.A.1.70.3	UMF18C	Bacteria	UMF18C of Salinispora tropica (A4X2L1)
2.A.1.71: The Valanimycin-resistance (Val-R) Family
2.A.1.71.1	The Valanimycin-resistance determinant, VlmF (probably a valanimycin:H�antiporter (Ma et al., 2000))	Bacteria	VlmF of Streptomyces viridifaciens (Q9LA76)
2.A.1.71.2	The UMF19a porter	Bacteria	UMF19a porter of Streptomyces coelicolor (Q93J85)
2.A.1.71.3	Major facilitator superfamily domain-containing protein 5	Animals	mfsd5 of Xenopus tropicalis
2.A.1.72: The Unidentified Major Facilitator-20 (UMF20) Family
2.A.1.72.1	The UMF20A porter	Bacteria	UMF20A of Streptomyces coelicolor (Q9RL01)
2.A.1.73: The Unidentified Major Facilitator-21 (UMF21) Family
2.A.1.73.1	The UMF21A porter	Bacteria	UMF21A porter of Streptomyces coelicolor (Q9L102)
2.A.1.74: The Unidentified Major Facilitator-22 (UMF22) Family
2.A.1.74.1	UMF22a porter	Bacteria	UMF22 porter of Streptomyces coelicolor (Q9S243)
2.A.1.75: The Unidentified Major Faciilitator-23 (UMF23) Family
2.A.1.75.1	Probable transporter MCH1 (Monocarboxylate transporter homolog 1)	Fungi	MCH1 of Saccharomyces cerevisiae
2.A.1.75.2	MFS PUTATIVE monocarboxylic acid transporter, UMF23B	Fungi	Mct of Coccidioides posadasii (E9CYW5)
2.A.1.75.3	Uncharacterized major facilitator, UMF23C	Yeast	UMF23C of Candida albicans
2.A.1.75.4	Uncharacterized major facilitator UMF23D	Amoeba	UMF23D of Naegleria gruberi
2.A.1.76: The Uncharacterized Major Facilitator 24 Family
2.A.1.76.1	Uncharacterized protein, UMF24A	Bacteria	UMF24A of Mycoplasma pneumoniae
2.A.1.76.2	Uncharacterized Mycoplama MFS carrier, UMF24B	Bacteria	UMF24B of Mycoplasma capricolum
2.A.1.76.3	Uncharacterized MFS carrier, UMF24C	Bacteria	UMF24C of Lactobacillus salivarius
2.A.1.76.4	Uncharacterized MFS permease	Bacteria	MFS porter of Mycoplasma galisepticum
2.A.1.76.5	Uncharacterized protein Mhp246	Bacteria	Mhp246 of Mycoplasma hyopneumoniae
2.A.1.77: Uncharacterized Major Facilitator-25 (UMF25) Family
2.A.1.77.1	Unknown Major Facilitator UMF25a	Bacteria	UMF25a of Rhodopirellula baltica
2.A.1.77.2	Unknown Major Facilitator, UMF25b	Bacteria	UMF25b of Planctomyces limnophilus