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TCID	Name	Organismal Type	Example
2.A.4.1.1	Cd²⁺, Zn²⁺, Co²⁺ efflux permease (also binds Cu²⁺ and Ni²⁺) (Anton et al., 2004)	Bacteria	CzcD of Ralstonia metallidurans (previously Alcaligenes eutrophus)
2.A.4.1.2	Zn²⁺, Co²⁺ efflux permease	Bacteria	ZntA of Staphylococcus aureus
2.A.4.1.3	Cd²⁺ or Zn²⁺:H⁺ + K⁺ antiporter, CzcD	Bacteria	CzcD of Bacillus subtilis
2.A.4.1.4	Zn²⁺ (Km=105 μM), Cd²⁺ (Km=90 μM):proton (Km=20 nM) antiport metal ion efflux permease, ZitB (Chao and Fu, 2004a); Zn²⁺ (Km=1.4 μM; Anton et al., 2004). It also takes up Ni²⁺ and Cu²⁺ (Rahman et al., 2008).	Bacteria	ZitB of E. coli (P75757)
2.A.4.1.5	The major Zn²⁺ resistance determinant, ZitA (Grover and Sharma, 2006 Grover and Sharma, 2006)	Bacteria	ZitA of Mycobacterium smegmatis (A0QQH3)
2.A.4.1.6	Mitochondrial metal transporter 2	Fungi	MMT2 of Saccharomyces cerevisiae
2.A.4.2.1	Mitochondrial Co²⁺/Zn²⁺ uptake (into mitochondria) permease. A single mutation (N45I) increases the specificity for Fe²⁺ and decreases it for Co²⁺ (Lin et al., 2008).	Yeast	Cotl of Saccharomyces cerevisiae
2.A.4.2.2	Vacuolar Zn²⁺, Cd²⁺ uptake (into vacuoles) permease (Zn²⁺/Cd²⁺:H⁺ antiporter). A single mutation (N44I) changes the specificity from Zn²⁺ to Fe²⁺ (Lin et al., 2008). Lin et al. (2009) have identified transmembrane residues that determine metal specificity.	Yeast	Zrclp (ZnrP) of Saccharomyces cerevisiae
2.A.4.2.3	Plasma membrane Zn²⁺ efflux permease	Animals	ZnT1 of Rattus norvegicus
2.A.4.2.4	Zn²⁺ exporter, CDF-1	Animals	CDF-1 of Caenorhabditis elegans (Q95QW4)
2.A.4.2.5	solute carrier family 30, member 10	Animals	SLC30A10 of Homo sapiens
2.A.4.2.6	Zinc transporter 1 (ZnT-1) (Solute carrier family 30 member 1)	Animals	SLC30A1 of Homo sapiens
2.A.4.3.1	Vesicular Zn²⁺ uptake (into endosomal/lysosomal vesicles) permease, ZnT2. There are two isoforms due to alternative splicing, 35 kDa (plasma membrane localized) and 42 kDa (endosome/secretory compartment localized) (Lopez and Kelleher, 2009).	Animals	ZnT2 of Rattus norvegicus
2.A.4.3.2	Vesicular Zn²⁺ uptake (into synaptic vesicles) permease, ZnT3 (SLC30A subfamily). ZnT-3 regulates presynaptic Erk1/2 signaling and hippocampus-dependent memory (Sindreu et al., 2011).	Animals	SLC30A3 of Homo sapiens
2.A.4.3.3	Mammary epithelia/brain Zn²⁺ transporter ZnT4 (the cause of inherited zinc deficiency in the lethal milk (lm) syndrome of mice, due to a nonsense mutation at codon 297 (arg) in the ZnT4 gene) (Huang and Gitschier, 1997).	Animals	ZnT4 of Mus musculus (O35149)
2.A.4.3.4	Plant root and leaf vacuolar Zn²⁺ transporter, ZAT-1 or MTP1 (metal tolerance protein 1) (Desbrosses-Fonrouge et al., 2005). Loss of the histidine-rich loop stimulates transport activity (Kawachi et al., 2008). The barley orthologue has broader metal specificity (Podar et al., 2012). Critical residues for function, ion selectivity and structure have been identified (Kawachi et al., 2012).	Plants	MTP1 of Arabidopsis thaliana (Q9ZT63)
2.A.4.3.5	Homodimeric solute carrier family 30 (zinc transporter), member 8, ZnT8. An inherited R325W mutant gives aberant zinc transport in pancreatic beta cells (Weijers 2010).	Animals	SLC30A8 of Homo sapiens
2.A.4.3.6	solute carrier family 30 (zinc transporter), member 2	Animals	SLC30A2 of Homo sapiens
2.A.4.3.7	Zinc transporter 4 (ZnT-4) (Solute carrier family 30 member 4)	Animals	SLC30A4 of Homo sapiens
2.A.4.4.1	Heteromeric nuclear/ER Zn²⁺ uptake permease, Msc2/Zrg17 (Ellis et al., 2005)	Yeast	Msc2/Zrg17 heteromeric Zn²⁺ transporter of Saccharomyces cerevisiae Msc2 (Q03455) Zrg17 (P53735)
2.A.4.4.2	Zn²Transporter, LbrM31	Euglenoza	LbrM31 of Leishmania braziliensis (A4HJM3)
2.A.4.4.3	Golgi/secretory granule Zn² uptake (into Golgi or granules) permease, ZnT5 or ZTL1 (ZnT5 forms heterooligomers with ZnT6) (Ellis et al., 2005; Ishihara et al., 2006) (Variant B catalyzes bidirectional transport (Valentine et al., 2007) )	Animals	SLC30A5 of Homo sapiens
2.A.4.4.4	Golgi/secretory granule Zn²⁺ uptake (into Golgi or granules) permease, ZnT6 (ZnT6 forms heterooligomers with ZnT5) (Ellis et al., 2005; Ishihara et al., 2006)	Animals	SLC30A6 of Homo sapiens
2.A.4.4.5	Golgi/secretory granule Zn²⁺ uptake (into Golgi or granules) permease, ZnT7 (Ishihara et al., 2006)	Animals	SLC30A7 of Homo sapiens
2.A.4.4.6	Metal tolerance protein C2 (AtMTPc2) (AtMTP5)	Plants	MTPC2 of Arabidopsis thaliana
2.A.4.5.1	Golgi/endomembrane Mn²⁺-specific CDF transporter (394 aas) (Peiter et al., 2007)	Plants	MTP11.1 of Populus trichocarpa (A4ZUV2)
2.A.4.6.1	CDF transporter, ZnT9 of unknown specificity (568 aas) (Montanini et al., 2007)	Animals	SLC30A9 of Homo sapiens
2.A.4.7.1	Zn²⁺/Cd²⁺/Hg²⁺/Fe²⁺:H⁺ antiporter, YiiP or FieF (Chao and Fu, 2004b; Grass et al., 2005; Wei et al., 2004; Wei and Fu, 2006). The structure (3.8 Å resolution) reveals a homodimer interconnected at the cytoplasmic domain through four Zn²⁺ ions. A 6 TMS bundle features of a tetrahedral Zn²⁺ binding site (Lu and Fu, 2007).	Bacteria	YiiP of E. coli (P69380)
2.A.4.7.2	Metal tolerance protein C1 (AtMTPc1) (AtMTP6)	Plants	MTPC1 of Arabidopsis thaliana
2.A.4.7.3	Putative magnetosome membrane iron transporter, MamB. Forms a stable complex with MamM which stabilizes MamB. MamB also interacts with other proteins including the PDZ1 domain of MamE (Q6NE61). Both MamB and MamM are essential for magnetite biomineralization and are involved in several steps in magnetosome formation, but only MamB is essential for formation of magnetosome membrane vesicles (Uebe et al. 2011). Implicated in iron uptake due to homology with other CDF transporters.	Bacteria	MamB of Magnetospirillum gryphiswaldense
2.A.4.7.4	Putative magnetosome membrane iron transporter, MamM. Forms a stable complex with MamB which it stabilizes. MamB also interacts with other proteins including the PDZ1 domain of MamE (Q6NE61; see 2.A.4.7.3). Both MamB and MamM are essential for magnetite biomineralization and are involved in several steps in magnetosome formation, but only MamB is essential for formation of magnetosome membrane vesicles (Uebe et al. 2011). Implicated in iron uptake due to homology with other CDF transporters.	Bacteria	MamM of Magnetospirillum gryphiswaldense
2.A.4.7.5	Cd²⁺/Zn²⁺ efflux pump, YiiP or FieF. A low resolution structure in the open configuration has been determined by cryoelectron microscopy (Coudray et al. 2013).	Proteobacteria	YiiP of Shewanella oneidensis (Q8E919)
2.A.4.8.1	CDF Family homologue with MMT1 domain	Actinobacteria	CDF porter of Streptomyces coelicolor
2.A.4.8.2	CDF Family member	Actinobacteria	CDF cation efflux carrier of Mycobacterium tuberculosis