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TCID	Name	Organismal Type	Example
2.A.3.1: The Amino Acid Transporter (AAT) Family
2.A.3.1.1	Phenylalanine:H⁺ symporter	Bacteria	PheP of E. coli
2.A.3.1.2	Lysine:H⁺ symporter	Bacteria	LysP of E. coli
2.A.3.1.3	Aromatic amino acid:H⁺ symporter	Bacteria	AroP of E. coli
2.A.3.1.4	γ-aminobutyrate:H⁺ symporter (also transports a variety of pyridine carboxylates)	Bacteria	GabP of E. coli
2.A.3.1.5	β-alanine/γ-aminobutyrate:H⁺ symporter	Bacteria	GabP of Bacillus subtilis
2.A.3.1.6	Proline-specific permease (ProY)	Bacteria	ProY of Salmonella typhimurium
2.A.3.1.7	D-Serine/D-alanine/glycine/D-cycloserine:H⁺ symporter (regulated by the small RNA, GcvB; Pulvermacher et al., 2009).	Bacteria	CycA of E. coli (P0AAE0)
2.A.3.1.8	Asparagine permease (AnsP)	Bacteria	AnsP of Salmonella typhimurium
2.A.3.1.9	Histidine permease HutT	Bacteria	HutT of Pseudomonas putida
2.A.3.1.10	S-Methylmethionine permease, MmuP	Bacteria	MmuP of E. coli
2.A.3.1.11	L-Arginine permease, RocE	Bacteria	RocE of Bacillus subtilis
2.A.3.1.12	Aromatic amino acid permease, AroP (Wehrmann et al., 1995)	Bacteria	AroP of Corynebacterium glutamicum (Q46065)
2.A.3.1.13	Putrescine importer, PuuP (Kurihara et al., 2005)	Bacteria	PuuP of E. coli (P76037)
2.A.3.2: The Basic Amino Acid/Polyamine Antiporter (APA) Family
2.A.3.2.1	Putrescine:ornithine antiporter; putrescine:H⁺ symporter	Bacteria	PotE of E. coli (P0AAF1)
2.A.3.2.2	Cadaverine:lysine antiporter [Catalyzes cadaverine uptake via H⁺ symport (Km=21μM) and cadaverine export (Km=300 μM) via cadaverine:lysine antiport.] (Soksawatmaekhin et al., 2004)	Bacteria	CadB of E. coli (P0AAE8)
2.A.3.2.3	Arginine:ornithine antiporter	Bacteria	ArcD of Pseudomonas aeruginosa
2.A.3.2.4	Lysine permease	Bacteria	LysI of Corynebacterium glutamicum
2.A.3.2.5	Homodimeric electrogenic arginine (Km=80μM):agmatine antiporter involved in extreme acid resistance (Fang et al., 2007; Gong et al., 2003; Iyer et al., 2003). A projection structure at 6.5 Å resolution has been published (Casagrande et al., 2008), and the 3.2 Å resolution X-ray structure was determined by Fang et al., 2009 and Gao et al., 2009.	Bacteria	YjdE (AdiC) of E. coli (P39269)
2.A.3.2.6	Putative lysine uptake permease, YvsH (Rodionov et al., 2003)	Bacteria	YvsH of Bacillus subtilis (CAA11718)
2.A.3.3: The Cationic Amino Acid Transporter (CAT) Family
2.A.3.3.1	System Y+ high affinity basic amino acid transporter (CAT1) (ecotropic retrovival leukemia virus receptor (ERR)) (transports arginine, lysine and ornithine; Na⁺-independent)	Mammals	CAT1(ERR) of Mus musculus
2.A.3.3.2	Low affinity basic amino acid transporter (CAT2) (T-cell early activation protein (TEA)) (transports arginine, lysine and ornithine; Na⁺-independent) (Habermeier et al., 2003)	Mammals	CAT2(TEA) of Mus musculus
2.A.3.3.3	Amino acid transporter, AAT1	Plants	AAP1 of Arabidopsis thaliana
2.A.3.3.4	The amino acid transporter, CAT6. Mediates electrogenic transport of large neutral and cationic amino acids in preference to other amino acids. Present in lateral root primordia, flowers and seeds (Hammes et al., 2006)	Plants	CAT6 of Arabidopsis thaliana (Q9LZ20)
2.A.3.3.5	The brain L-cationic (Arg, Lys, Orn, 2,4-diamino-n-butyrate) transporter, CAT3 (capacity of trans-stimulation by internal Arg) (Ito and Groudine, 1997)	Animals	CAT3 of Mus musculus (P70423)
2.A.3.4: The Amino Acid/Choline Transporter (ACT) Family
2.A.3.4.1	Choline permease	Yeast	Ctr (Hnm1) of Saccharomyces cerevisiae
2.A.3.4.2	γ-aminobutyric acid (GABA) permease, GabA	Yeast, fungi	GabA of Emericella nidulans
2.A.3.4.3	γ-aminobutyric acid (GABA) permease, Uga4 (also transports polyamines) (Uemura et al., 2007)	Yeast	Uga4 of Saccharomyces cerevisiae (NP_010071)
2.A.3.4.4	The 7-keto-8-aminopelargonic acid (KAPA) transporter, Bio5 (Phalip et al., 1999)	Fungi	Bio5 of Saccharomyces cerevisiae (P53744)
2.A.3.4.5	The polyamine (putrescine > spermidine > spermine) exporter, Top5p (Ykl174c) [found in the golgi or post-golgi secretory vesicles; induction:spermine > spermidine > putrescene]	Yeast	Top5p of Saccharomyces cerevisiae (NP_012747)
2.A.3.4.6	The thiamine (vitamin B1) transporter, Thi9 (SPAC9.10). Uptake is inhibited by pyrithiamine, oxythiamine, amprolium, and the thiazole part of thiamine indicating that these compounds are substrates of Thi9 (Vogl et al., 2008).	Yeast	Thi9 of Schizosaccharomyces pombe (Q9UT18)
2.A.3.5: The Ethanolamine Transporter (EAT) Family
2.A.3.5.1	Ethanolamine import permease	Bacteria	Ethanolamine permease of Rhodococcus erythropolis
2.A.3.5.2	Probable methylamine import permease	Archaea	Methylamine permease of Methanosarcina acetivorans MA0143
2.A.3.6: The Archaeal/Bacterial Transporter (ABT) Family
2.A.3.6.1	Putative cationic amino acid permease	Archaea	Cat-1 of Archaeoglobus fulgidus
2.A.3.6.2	The putative permease, MtbP (MA2426) (possibly a methyl amine uptake porter; D.J. Ferguson, personal communication) (12 putative TMSs)	Archaea	MtbP of Methanoscarina acetivorans (Q8TN67).
2.A.3.6.3	ApcT, a proton coupled broad specificity amino acid transporter. 3-d structure available at 2.3Å resolution (3GIA_A; Shaffer et al., 2009).	Archaea	ApcT of Methanocaldococcus jannaschii (Q58026)
2.A.3.7: The Glutamate:GABA Antiporter (GGA) Family
2.A.3.7.1	Glutamate:γ-aminobutyrate antiporter	Bacteria	GadC of Lactococcus lactis
2.A.3.7.2	The GadC homologue	Bacteria	YcaM of E.coli (P75835)
2.A.3.8: The L-type Amino Acid Transporter (LAT) Family (Many LAT family members function as heterooligomers with rBAT and/or 4F2hc (TC #8.A.9))
2.A.3.8.1	L-type neutral amino acid transporter, LAT1 (Na⁺-independent) (prefers amino acids with branched or aromatic side chains: Phe, Ile, Leu, Val, Trp, His; catalyzes obligatory exchange with μM affinities on the outside and mM affinities on the inside [1000x difference]). Both LAT1 and LAT2 (2.A.3.8.6) catalyze uptake of S-nitroso-L-cysteine. These and other LAT family members are specifically inhibited by 2-aminobicyclo[2.2.1]heptane-2-carboxylic acid (Li and Whorton, 2005). Mediates tryptophan:kynurenine exchange (Kaper et al., 2007).	Animals	LAT1 of Rattus norvegicus (Q63016)
2.A.3.8.2	L-type neutral amino acid transporter, ASUR4 (Na⁺-independent)	Animals	ASUR4 of Xenopus laevis (O13020)
2.A.3.8.3	The schistosome neutral and cationic amino acid transporter, SPRM1lc (Na⁺-independent), (takes up phe, arg, lys, ala, gln, his, trp and leu; functions with SPRM1hc (TC# 8.A.9.3.1) (Krautz-Peterson et al., 2007)	Animals	SPRM1lc of Schistosoma mansoni (Q26594)
2.A.3.8.4	L-methionine transporter, MUP1	Yeast	MUP1 of Saccharomyces cerevisiae (P50276)
2.A.3.8.5	Cystine/glutamate antiporter, xCT (requires the 4F2hc protein (TC #8.A.9.2.1))	Animals	xCT of Mus musculus (Q9WTR6)
2.A.3.8.6	L-type neutral amino acid transporter, LAT2 (Na⁺-independent with broad specificity for all L-isomers of neutral amino acids; preferred substrate: Phe, His, Trp, Ile, Val, Leu, Gln, Cys, Ser; catalyzes obligatory exchange with μM affinities on the outside and mM affinities on the inside [1000x difference]). Both LAT2 and LAT1 (2.A.3.8.1) catalyze uptake of S-nitro-L-cysteine (Li and Whorton, 2005).	Animals	LAT2 of Rattus norvegicus (Q9WVR6)
2.A.3.8.7	y+LAT1 (transports neutral amino acids (i.e., Leu) in symport with Na⁺, Li⁺ or H⁺ in 1:1 stoichiometry; transports basic amino acids (i.e., Lys) by facilitated diffusion without a symported cation). Also transports the neurotoxicant, methylmercury-L-cysteine by molecular mimicry. Causes the Lysinuric protein intolerance condition in humans (Q9UM01) (Broer, 2008).	Animals	y+LAT1 of Rattus norvegicus (Q9QZ66)
2.A.3.8.8	Aspartate/glutamate Na⁺-independent transporter, AGT1	Animals	AGT1 of Mus musculus (Q91WN3)
2.A.3.8.9	Heteromeric amino acid transporter #1 (transports most neutral aas with highest rates for Ala and Ser (Km≈100 μM)). They function by obligatory aa:aa exchange (Veljkovic et al., 2004b).	Animals	AAT1 of Caenorhabditis elegans (Q19834)
2.A.3.8.10	Aromatic amino acid exchanger, AAT-9 (Veljkovic et al., 2004b)	Animals	AAT-9 of Caenorhabditis elegans (Q9NA91)
2.A.3.8.11	The aromatic-preferring amino acid transporter (ArpAT). Functions with rBAT or 4F2hc (8.A.9) and transports preferentially tyr and 3,4-dihydroxyphenylalanine (L-DOPA), but also ala, glu, ser, cys and arg by a Na⁺-independent mechanism (present in mouse, rat, dog and chicken, but silenced in humans and chimps)(Fernández et al., 2005; Sato et al., 2005)	Animals	ArpAT of Mus musculus (Q50E62)
2.A.3.8.12	The Ser/Thr exchange transporter (SteT) (also transports aromatic amino acids with lower efficiency) (Reig et al., 2007)	Bacteria	SteT of Bacillus subtilis (O34739)
2.A.3.8.13	The Asc-type small neutral D- and L-amino acid:H⁺ symport transporter-1, Asc-1 (Slc7a10). Also transports amino acid related compounds. Heterodimeric; associates with 4F2hc (TC# 8.A.9.2.1) Most highly expressed in brain and lung, but to a lesser degree in placenta and small intestine. (Fukasawa et al., 2000)	Animals	Asc-1 of Mus musculus (P63115)
2.A.3.8.14	The Asc-type small neutral L-amino acid:H⁺ symport transporter-2 (Asc-2). Does not associate with 4F2hc or rBAT, but probably associates with some comparable heavy chain. Doesn't transport some substrates of Asc-1 such as α-aminoisobutyric acid and β-alanine (Chairoungdua et al., 2001)	Animals	Asc-2 of Mus musculus (Q8VIE6)
2.A.3.8.15	The b^0,+ amino acid (cystine) transporter associated with the cystinuria-related type II membrane glycoprotein, BAT1 which forms a heterodimer with rBAT (TC# 8.A.9.1.1). Present in the apical membrane of renal proximal tubules (Chairoungdua et al., 1999)	Animals	BAT1 of Rattus norvegicus (P82252)
2.A.3.9: The Spore Germination Protein (SGP) Family
2.A.3.9.1	Spore germination protein A2 (AB) (amino acid [L-alanine] receptor)	Gram-positive bacteria	GerAB of Bacillus subtilis
2.A.3.9.2	Spore germination protein B2 (BB) (amino acid [D-alanine and L-asparagine] receptor)	Gram-positive bacteria	GerBB of Bacillus subtilis
2.A.3.9.3	Spore germination protein K2 (KB) (probable amino acid receptor)	Gram-positive bacteria	GerKB of Bacillus subtilis
2.A.3.10: The Yeast Amino Acid Transporter (YAT) Family
2.A.3.10.1	High affinity histidine permease (also implicated in Mn²⁺ efflux; Co²⁺, Ni²⁺, Zn²⁺ and Cu²⁺ uptake)	Yeast, fungi	Hip1 of Saccharomyces cerevisiae (P06775)
2.A.3.10.2	General amino acid permease (all L-amino acids and some D-amino acids as well as β-alanine and GABA)	Yeast	Gap1 of Saccharomyces cerevisiae (P19145)
2.A.3.10.3	Proline permease	Yeast	Put4 of Saccharomyces cerevisiae (P15380)
2.A.3.10.4	Arginine permease	Yeast	Can1 of Saccharomyces cerevisiae (P04817)
2.A.3.10.5	High affinity glutamine permease	Yeast	Gnp1 of Saccharomyces cerevisiae (P48813)
2.A.3.10.6	Leu/Val/Ile amino acid permease	Yeast	Bap2 of Saccharomyces cerevisiae (P38084)
2.A.3.10.7	Asn/Gln permease	Yeast	Agp1 of Saccharomyces cerevisiae (P25376)
2.A.3.10.8	Tryptophan permease	Yeast	Tat2 of Saccharomyces cerevisiae (P38967)
2.A.3.10.9	Val/Tyr/Trp permease	Yeast	Val1 (Tat1) of Saccharomyces cerevisiae (P38085)
2.A.3.10.10	Lysine permease	Yeast	Lyp1 of Saccharomyces cerevisiae (P32487)
2.A.3.10.11	Basic amino acid permease	Yeast	Alp1 of Saccharomyces cerevisiae (P38971)
2.A.3.10.12	Leucine sensor/transcription factor. Mutants hyper- and hyposensitive to inducer (Poulsen et al., 2008) suggest a sensor mechanism involving outward and inward facing conformations.	Yeast	Ssy1 of Saccharomyces cerevisiae (Q03770)
2.A.3.10.13	Dicarboxylic amino acid permease	Yeast	Dip5 of Saccharomyces cerevisiae (P53388)
2.A.3.10.14	General amino acid permease with broad specificity, Agp3	Yeast	Agp3 of Saccharomyces cerevisiae (P43548)
2.A.3.10.15	S-adenosylmethionine uptake permease, SAM3 (also takes up polyamines, glutamate, lysine and the toxic S-adenosylmethionine analogue sinefungin) (Uemura et al., 2007; Zheng et al., 2007).	Yeast	Agp3 (YPL274w) of Saccharomyces cerevisiae (Q08986)
2.A.3.10.16	S-methylmethionine uptake permease, Mmp1	Yeast	Mmp1 (YLL061w) of Saccharomyces cerevisiae (Q12372)
2.A.3.10.17	General amino acid uptake permease, GAP1	Fungi	GAP1 of Hebeloma cylindrosporum (Q8J266)
2.A.3.10.18	The aromatic amino acid and leucine permease, ArlP (may be a general amino acid permease for neutral and basic [but not acidic] amino acids)	Fungi	ArlP of Penicillium chrysogenum (Q8NKC4)
2.A.3.10.19	The high affinity polyamine (spermidine > putrescine)/carnitine, low affinity amino acid transporter, AGP2 (Aouida et al., 2005) (but see Uemura et al., 2007 for contradicting evidence)	Yeast	AGP2 of Saccharomyces cerevisiae (P38090)
2.A.3.10.20	The high affinity basic amino acid (Arg, Lys, His) transporter, Can1 (Matijekova and Sychrova, 1997)	Yeast	Can1 of Candida albicans (P43059)
2.A.3.10.21	The basic amino acid (canavanine sensitivity) transporter, Cat1 (Aspuria and Tamanoi, 2008).	Yeast	Cat1 of Schizosaccharomyces pombe (Q9URZ4)
2.A.3.10.22	Arbuscular mycorrhizal fungal proline:H⁺ symporter, AAP1 (binds and probably transports nonpolar, hydrophobic amino acids) (Cappellazzo et al., 2008).	Fungi	AAP1 of Glomus mosseae (Q2VQZ4)
2.A.3.11: The Aspartate/Glutamate Transporter (AGT) Family
2.A.3.11.1	The aspartate uptake permease, YveA (also transports L-aspartate hydroxamate and glutamate, and possibly asparagine and glutamine; Lorca et al., 2003)	Bacteria and archaea	YveA of Bacillus subtilis
2.A.3.12: The Polyamine:H⁺ Symporter (PHS) Family
2.A.3.12.1	The plasma membrane polyamine (putrescine, spermidine):H⁺ uptake symporter, LmPOT1 (inhibited by pentamidine and protonophores) (Hasne and Ullmann, 2005)	Protozoans	POT1 of Leishmania major (AAW52506)
2.A.3.13: The Amino Acid Efflux (AAE) Family
2.A.3.13.1	The probable hydrophobic amino acid efflux transporter, YjeH (possibly exports L-methionine and other neutral, hydrophobic amino acids; R. Figge, personal communication)	Bacteria	YjeH of E. coli (P39277)
2.A.3.13.2	The Ceftriaxone resistance porter, YjeH (Hu et al., 2007).	Proteobacteria	YjeH of Salmonella enterica (serovar Typhimurium) (Q8ZKC0)