TCID | Name | Domain | Kingdom/Phylum | Protein(s) |
---|---|---|---|---|
2.A.5.1.1 | High affinity zinc-regulated zinc uptake transporter, Zrt1 of 376 aas and 8 TMSs. May be a transceptor with both transport and receptor (signal transduction) functions (Diallinas 2017; Schothorst et al. 2017). Activated at the transcriptional level by Yap1 and Ace1 (Gomes et al. 2005). Zrt1 may also transport, or influence the uptake of Cd2+ (Gomes et al. 2005). | Eukaryota |
Fungi, Ascomycota | Zrt1 of Saccharomyces cerevisiae |
2.A.5.1.2 | Iron regulated Fit1-mediated plasma membrane high affinity Fe2+ uptake transporter, Irt1, of 347 aas and 9 TMSs (also takes up Co2+, Mn2+, Zn2+ and possibly Cd2+) (Korshunova et al., 1999; Schaaf et al., 2006; Halimaa et al. 2014). It is targetted to the plasma membrane by Sorting nexin1 (Snx1; Q9FG38) (Ivanov et al. 2014). Root-to-shoot iron partitioning in Arabidopsis requires the IRON-REGULATED TRANSPORTER1 (IRT1) protein but not its iron(II) transport function (Quintana et al. 2022). | Eukaryota |
Viridiplantae, Streptophyta | Irt1 of Arabidopsis thaliana |
2.A.5.1.3 | Zinc/iron uptake transporter, Zip1 (Grass et al., 2005; Grotz et al., 1998) | Eukaryota |
Viridiplantae, Streptophyta | Zip1 of Arabidopsis thaliana (O81123) |
2.A.5.1.4 | Iron-regulated Fit1-mediated (coregulated with Irt1) vacuolar high-affinity Fe2+ efflux (from the vacuole into the cytoplasm) transporter, Irt2 (also transports Zn2+ (Schaaf et al., 2006). The archetypical IRT proteins from angiosperms likely emerged before the origin of land plants during early streptophyte algae terrestrialization, a process that required the evolution of Fe acquisition in terrestrial subaerial settings (Rodrigues et al. 2023). | Eukaryota |
Viridiplantae, Streptophyta | Irt2 of Arabidopsis thaliana (O81850) |
2.A.5.1.5 | Zinc (Zn2+) uptake transporter, ZIP8 (Ueno et al. 2010) | Eukaryota |
Viridiplantae, Streptophyta | ZIP8 of Oryza sativa (A3BI11) |
2.A.5.1.6 | The Zn2+/Cd2+ transporter, ZNT1 (Nishida et al., 2011). The histidine-rich loop between TMSs 3 and 4 binds Cu2+ > Zn2+ > Ni2+ (Potocki et al. 2014). Expression of particular transmembrane transporters (e.g., members of the ZIP (ZNT1) and NRAMP (NRAMP4) families) leads to metal tolerance and accumulation in plants (Fasani et al. 2021). | Eukaryota |
Viridiplantae, Streptophyta | ZNT1 of Thlaspi caerulescens (Q9M7J1) |
2.A.5.1.7 | The Zn2+/Cd2+ transporter ZNT2 (Nishida et al., 2011) | Eukaryota |
Viridiplantae, Streptophyta | ZNT2 of Thlaspi caerulescens (Q92XE7) |
2.A.5.1.8 | Zinc-regulated transporter 1 (High-affinity zinc transport (uptake) protein Zrt1) (Boch et al. 2008). | Eukaryota |
Fungi, Ascomycota | Zrt1 of Schizosaccharomyces pombe |
2.A.5.1.9 | Eukaryota |
Evosea | ZntC of Dictyostelium discoideum | |
2.A.5.1.10 | ZIP family porter of 392 aas | Eukaryota |
Oomycota | ZIP family member of Phytophthora infestans (strain T30-4) (Potato late blight fungus) |
2.A.5.1.11 | Ferrous iron (Fe2+) transporting ZIP family member, LIT1, required for intracellular growth and virulence (Huynh et al. 2006). Also transports other metal ions less efficiently. Residues involved in targetting and activity have been identified including His108, 283 and 309 (Jacques et al. 2010). | Eukaryota |
Euglenozoa | LIT1 of Leishmania major |
2.A.5.1.12 | Root iron transporter IRT1 of 364 aas and 9 TMSs. Has an uncleaved signal peptide that targets the protein to the endoplasmic reticulum for transport to the plasma membrane (Zhang et al. 2014). | Eukaryota |
Viridiplantae, Streptophyta | IRT1 of Malus xiaojinensis (apple) |
2.A.5.1.13 | Ferrous iron (Fe2+) uptake transporter of 347 aas and 9 TMSs. Transports iron and possibly Cd2+ in this hyperaccumulating plant. Induced by iron deficiency and cadmium excess (Plaza et al. 2007). | Eukaryota |
Viridiplantae, Streptophyta | IRT1 of Noccaea caerulescens (Alpine penny-cress) (Thlaspi caerulescens) |
2.A.5.1.14 | Low affinity zinc-regulated zinc uptake transporter, Zrt2 of 422 aas and 7 TMSs. Active in zinc-replete cells and is time-, temperature- and concentration-dependent. It prefers zinc over other metals as its substrate (Zhao and Eide 1996). | Eukaryota |
Fungi, Ascomycota | Zrt2 of Saccharomyces cerevisiae |
2.A.5.1.15 | Zinc transporter, Zrt1 of 468 aas and 7 TMSs. Receives Zn2+ from the secreted, extracellular zincophore protein, Pra1 for uptake of the metal. The binding site in Pra1 is in the C-terminal region of this 299 aa protein (Łoboda and Rowińska-Żyrek 2017). Pra1 is a cell surface protein with a single N-terminal TMS involved in the host-parasite interaction during candidal infection. With MP65, it represents a major component of the biofilm matrix. It sequesters zinc from host tissues and mediates leukocyte adhesion and migration (Citiulo et al. 2012). | Eukaryota |
Fungi, Ascomycota | Zrt1/Pra1 of Candida albicans and Candida dubliniensis (Yeast) |
2.A.5.1.16 | Zinc uptake transporter of 352 aas and 8 TMSs. RaZIP1 is a high-affinity plasma membrane transporter specialized in Zn2+ uptake, but also taking up Cd2+ with lower affinity (Leonhardt et al. 2018). | Eukaryota |
Fungi, Basidiomycota | Zip1 of Russula atropurpurea |
2.A.5.1.17 | Zinc/Iron/Cadmium ion transporter protein IRT1 of 355 aas and 9 TMSs. Regulated by MAP kinase 4 which therefore regulates cell death in the presence of Cd2+ (Zhang et al. 2019). | Eukaryota |
Viridiplantae, Streptophyta | IRT1 of Nicotiana tabacum (Common tobacco) |
2.A.5.1.18 | ZIP1 of 358 aas and 9 TMSs in a 4 + 5 TMS arrangement. It transports Zn2+ and is induced by the absence of this ion in the medium (López-Millán et al. 2004). | Eukaryota |
Viridiplantae, Streptophyta | ZIP1 of Medicogo truncatula |
2.A.5.1.19 | ZIP5 of 374 aas and 9 TMSs in a 4 + 5 arrangement. It transports both Zn2+ and Fe2+ and is up regulated in medium deficient for Zn2+ and Mn2+. | Eukaryota |
Viridiplantae, Streptophyta | ZIP5 of Medicago truncatula |
2.A.5.1.20 | ZIP4 of 372 aas and 9 TMSs in a 4 + 5 TMS arrangement. Zip4 transports Mn2+ and is induced by the absence of Zn2+ in the external medium (López-Millán et al. 2004). | Viridiplantae, Streptophyta | ZIP4 of Medicago truncatula | |
2.A.5.1.21 | Zinc-regulated zinc transporting Zrt2 of 370 aas and 8 TMSs in a 3 + 5 TMS arrangement. It contains an extra-membrane disordered loop, corresponding to the amino acid sequence 126-215. Three Zrt2+ regions in this loop bind Zn2+ and Cu2+ with comparable affinities below pH 5, and therefore, may equally contribute to metal acquisition under the most acidic conditions in which the Zrt2 transporter is expressed (Bellotti et al. 2022). | Eukaryota |
Fungi, Ascomycota | Zrt2 of Candida albicans |
2.A.5.1.22 | Zinc (ZrfC) transporter of 522 aas and 9 TMSs in a 1 (N-terminal) + 3 (central; residues 200 - 300) + 5 TMSs (C-terminal). Aspergillus fumigatus, one of the most widespread opportunistic human fungal pathogens, adapts to zinc limitation by secreting a 310 amino acid Aspf2 zincophore, able to specifically bind Zn2+ and deliver it to ZrfC. Garstka et al. 2022 focused on the thermodynamics of Zn2+ complexes with unstructured regions of Aspf2; basing on a variety of spectrometric and potentiometric data, they show that the C-terminal part has the highest Zn(II)-binding affinity among the potential binding sites, and Ni2+ does not compete with Zn2+ binding to this region. The 14 amino acid Aspf2 C-terminus coordinates Zn2+ via two Cys thiolates and two His imidazoles (Garstka et al. 2022). The Aspf2 zincophore protein is a member of the Asp F2 family (TC# 8.A.190). | Eukaryota |
Fungi, Ascomycota | ZrfC/Aspf2 of Aspergillus fumigatus |
2.A.5.2.1 | Golgi Mn2+ homeostasis protein (probably pumps Mn2+ into cytoplasm), ATX2 (Eide, D.J, 1998) | Eukaryota |
Fungi, Ascomycota | ATX2 of Saccharomyces cerevisiae |
2.A.5.3.1 | Growth arrest-inducible protein, ZIP2 of 309 aas. Zinc dyshomeostasis leads to augmented production of proinflammatory cytokines, promoting chronic inflammation and increasing the susceptibility to age-related diseases. ZIP2 plays a role in the immune system, especially during zinc deficiency, while a polymorphism in the coding region of ZIP2 (Gln/Arg/Leu) is associated with severe carotid artery disease (Giacconi et al. 2015). | Eukaryota |
Metazoa, Chordata | SLC39A2 of Homo sapiens |
2.A.5.3.2 | Zn2+ uptake transporter, Zip1 (abundantly expressed; involved in zinc homeostasis rather than acquisition of dietary Zn2+) (Gaither and Eide, 2000). Mouse Zip1, 2 and 3 play important noncompensatory roles under conditions of zinc deficiency (Kambe et al. 2008). | Eukaryota |
Metazoa, Chordata | SLC39A1 of Homo sapiens |
2.A.5.3.3 | Zn2+ uptake transporter, Zip3 (poorly expressed; involved in Zn2+ homeostasis) (Dufner-Beattie et al., 2003). This protein plays an ancillary role in zinc homeostasis in mice (Dufner-Beattie et al. 2005). | Eukaryota |
Metazoa, Chordata | SLC39A3 of Homo sapiens |
2.A.5.3.4 | Zinc transporter 1 (ZRT/IRT-like protein 1) (OsZIP1) | Eukaryota |
Viridiplantae, Streptophyta | ZIP1 of Oryza sativa |
2.A.5.3.5 | Zinc transporter ZIP1 (DrZIP1) (Solute carrier family 39 member 1) (Zrt- and Irt-like protein 1) (ZIP-1) | Eukaryota |
Metazoa, Chordata | Slc39a1 of Danio rerio |
2.A.5.3.6 | Zip1 (ZIP42C.1) Zn2+ uptake transporter of 352 aas; Zn/Fe regulated (Lye et al. 2013; Dechen et al. 2015). | Eukaryota |
Metazoa, Arthropoda | Zip1 of Drosophila melanogaster (Fruit fly) |
2.A.5.3.7 | ZIP family member of 437 aas | Eukaryota |
Apicomplexa | ZIP protein of Cryptosporidium parvum |
2.A.5.3.8 | Zip3 or Zip89B Zinc uptake porter of 495 aas. | Eukaryota |
Metazoa, Arthropoda | Zip3 of Drosophila melanogaster |
2.A.5.3.9 | Putative zinc transporter of 298 aas and 8 TMSs. | Eukaryota |
Evosea | Zn2+ transporter of Entamoeba histolytica |
2.A.5.3.10 | Zinc transporter 11, ZnT11, of 349 aas and 9 TMSs (Yu et al. 2020). | Eukaryota |
Viridiplantae, Streptophyta | ZnT11 of Solanum tuberosum (potato) |
2.A.5.3.11 | Zinc (Zn2+) transporter, ZIP1, of 358 aas and 8 TMSs in a 3 + 5 TMS arrangement. | Eukaryota |
Apicomplexa | ZIP1 of Plasmodium falciparum |
2.A.5.3.12 | ZIP domain-containing protein of 325 aas and 8 TMSs in a 3 + 5 TMS arrangement. | Eukaryota |
Apicomplexa | Zip, zinc- and iron-transporting protein of Plasmodium falciparum |
2.A.5.3.13 | Zinc transporter 2, ZIP2, of 340 aas and 9 TMSs in a 4 + 5 TMS arrangement. SpZIP2 participates in the uptake and accumulation of Cd2+ into cells and might contribute to Cd2+ hyperaccumulation in S. plumbizincicola (Han et al. 2022). | Eukaryota |
Viridiplantae, Streptophyta | ZIP2 of Sedum plumbizincicola |
2.A.5.4.1 | Zip4 dietary Zn2+ uptake transporter of 647 aas and 7 TMSs in a 1 (N-terminus) +3 (middle) +3 (C-terminal) TMS arrangement (Acrodermatitis enteropathica zinc-deficiency disease protein) (Dufner-Beattie et al., 2003). The large cytoplasmic loop is an intrinsically disordered zinc binding domain (Bafaro et al. 2015). A modeled ZIP4 dimer possibly resembles the twelve TMS monomeric PiPT of the MFS, as a likely structural homologue (Antala et al. 2015). Zip4 zinc transporter mutations linked to acrodermatitis enteropathica disrupt function and cause mistrafficking (Kuliyev et al. 2021). A missense variant of SLC39A4 (Zip4) is found in a litter of turkish van cats with acrodermatitis enteropathica (Kiener et al. 2021). hZIP4 is the primary Zn2+ importer in the intestine, but it is also expressed in a variety of organs such as the pancreas and brain. It and a mutant form have been expressed in yeast (Liu et al. 2022). The transmembrane domains mediate oligomerization of the human ZIP4 transporter in vivo (Liu et al. 2022). A "divide and conquer" strategy has been applied to ZIP4 to study the extracellular domain (ECD) and the transmembrane domain separately, which has led to the first ECD structure in the entire ZIP family. Duan and Zhang 2023 provided detailed protocols for the expression, purification, and crystallization of ZIP4-ECD from a mammalian species. | Eukaryota |
Metazoa, Chordata | SLC39A4 of Homo sapiens |
2.A.5.4.2 | Zinc transporter, LIV1 (essential for the nuclear localization of the zinc-finger protein Snail, a master regulator of the epithelial-mesenchymal transition in zebrafish gastrulation) (Yamashita et al., 2004) | Eukaryota |
Metazoa, Chordata | LIV1 in Danio rerio (Q6L8F3) |
2.A.5.4.3 | Zip7 Golgi Zn2+ uptake (into the cytoplasm) transporter (Ke4, Slc39a7) (Huang et al., 2005). This protein can substitute for Iar1, the indole acetic acid-alanine resistance protein, of A. thaliana (Lasswell et al., 2000) | Eukaryota |
Metazoa, Chordata | SLC39A7 of Homo sapiens |
2.A.5.4.4 | Bidirectional endoplasmic reticular Zn2+ transporter, Yke4 (346 aas; Kumanovics et al., 2006) | Eukaryota |
Fungi, Ascomycota | Yke4 (YIL023c) of Saccharomyces cerevisiae (P40544) |
2.A.5.4.5 | Zip14 Zn2+/Fe2+/Mn2+/Cd2+ uptake transporter (mobilized to the sinusoidal membrane of the hepatocyte during acute inflammation) (Jenkitkasemwong et al. 2012; Pinilla-Tenas et al., 2011); KM for Fe2+= 0.002 μM. The prion gene family may have descended from an ancestral LZT gene (Ehsani et al. 2012). The gene is upregulated by iron loading (Nam et al. 2013). LIV-1 ZIP ectodomain shedding in prion-infected mice resembles the cellular response to transition metal starvation (Ehsani et al. 2012). Zip14 promotes cellular assimilation of iron from transferrin (Zhao et al. 2010) and also plays a role in maintaining manganese homeostasis (Xin et al. 2017). SLC39A14 is essential for efficient Mn2+ uptake by the liver and pancreas, and its deficiency results in impaired Mn2+ excretion and accumulation of the metal in other tissues (Jenkitkasemwong et al. 2018). Mutations cause hypermanganesemia associated with infantile onset dystonia (Juneja et al. 2018). . | Eukaryota |
Metazoa, Chordata | SLC39A14 of Homo sapiens |
2.A.5.4.6 | Zinc transporter, Zip10 (plays an essential role in the migratory activity of highly metastatic breast cancer cells) (Kagara et al., 2007). May be an evolutionary precursor of prion proteins in mammals (Schmitt-Ulms et al. 2009). | Eukaryota |
Metazoa, Chordata | SLC39A10 of Homo sapiens |
2.A.5.4.7 | The indole acetic acid-alanine resistance protein 1, Iar1 (Lasswell et al., 2000) | Eukaryota |
Viridiplantae, Streptophyta | Iar1 of Arabidopsis thaliana (Q9M647) |
2.A.5.4.8 | The divalent cation (M2+): bicarbonate (HCO3-) transporter (M2+:HCO3- = 1:2). Transports Cd2+ and Zn2+, and probably Cu2+, Pb2+, and Hg2+ (based on competitive inhibition studies (Liu et al., 2008)) | Eukaryota |
Metazoa, Chordata | Zip8 of Mus musculus (Q91W10) |
2.A.5.4.9 | Probable Zn2+ transporter, Zip13 (SLC39A13). Mice deficient in Zn transporter Slc39a13/Zip13 show changes in bone, teeth and connective tissue reminiscent of the clinical spectrum of human Ehlers-Danlos syndrome (EDS) (Fukada et al., 2008). | Eukaryota |
Metazoa, Chordata | Zip13 of Mus musculus (Q8BZH0) |
2.A.5.4.10 | Zn2+ transporter, Zip5 (540aas; 1+3+3 TMSs; processed to a 3+3 TMS protein) (Basolateral membrane; carries out serosal to mucosal transport) | Eukaryota |
Metazoa, Chordata | SLC39A5 of Homo sapiens |
2.A.5.4.11 | The Zn2+ and Cd2+ uptake porter, ZipB (nonsaturable; electrogenic) (Lin et al. 2010). Water-mediated zinc transport through the ZipB channel sugests an essential role of solvated water molecules in driving zinc coordination dynamics and transmembrane crossing (Gupta et al. 2019). The 3D structure is known for a close ortholog (83% identity) from Bordetella bronchiseptica (Zhang et al. 2023). | Bacteria |
Pseudomonadota | ZipB of Bordetella bronchispetica (Q2KXZ6) |
2.A.5.4.12 | ZIP13 Zn influx porter, an 8TMS homodimer with N- and C-termini facing the lumen of the Golgi. Important for connective tissue development. Its loss causes the Spondylocheiro dysplastic form of Ehlers-Danlos syndrome (Bin et al., 2011). | Eukaryota |
Metazoa, Chordata | SLC39A13 of Homo sapiens |
2.A.5.4.13 | Solute carrier family 39, SLC39 (zinc transporter), member 6, ZIP6. May be an evoltionary precursor of mammalian prion proteins (Schmitt-Ulms et al. 2009). | Eukaryota |
Metazoa, Chordata | SLC39A6 of Homo sapiens |
2.A.5.4.14 | solute carrier family 39 (zinc transporter), member 12 | Eukaryota |
Metazoa, Chordata | SLC39A12 of Homo sapiens |
2.A.5.4.15 | Zinc/iron/manganese/cadmium/selenium transporter ZIP8 (BCG-induced integral membrane protein in monocyte clone 103 protein) (Solute carrier family 39 member 8 (SLC39A8; Zrt- and Irt-like protein 8) (Jenkitkasemwong et al. 2012). Functions in Cd2+ and Mn2+ uptake, cell toxicity and hypertension (Zhang et al. 2015). Also transports selenium (Liang et al. 2021). Four amino acid residues, V33, G38, S335, and I340 of hZIP8 are mutated in patients with congenital disorders of glycosylation (CDG), caused by low blood Mn2+ levels (Fujishiro et al. 2022). Among the four mutations observed in ZIP8-mutated CDG patients, the S335T and I340N mutations in TMS5 abolished Mn2+- and Cd2+-transport activity, while V33M and G35R mutations did not. Artificial mutations in the metal-binding motif EEXXH in TMS5, which exists in most ZIP transporters, abolished the Mn2+- and Cd2+-transport activity of hZIP8 (Fujishiro et al. 2022). Loss of hepatic manganese transporter ZIP8 disrupts serum transferrin glycosylation and the glutamate-glutamine cycle (Powers et al. 2023). ZIP8 plays a role in systemic iron homeostasis but does not modulate the severity of inflammatory lung injury or the host defense against a common bacterial cause of pneumonia (Zhang et al. 2023). | Eukaryota |
Metazoa, Chordata | SLC39A8 of Homo sapiens |
2.A.5.4.16 | Eukaryota |
Metazoa, Arthropoda | Foi of Drosophila melanogaster | |
2.A.5.4.17 | Zinc importer, ZupT of 291 aas and 6 TMSs (Herzberg et al. 2014). | Bacteria |
Pseudomonadota | ZupT of Cupriavidus metallidurans (Ralstonia metallidurans) |
2.A.5.4.18 | Zinc transporter, ZIPT-7.1; regulates sperm activation in nematodes. In spermatids, inactive ZIPT-7.1 localizes to the intracellular membranous organelles, which contain higher levels of zinc than the cytoplasm. When sperm activation is triggered, ZIPT-7.1 activity increases, releasing zinc from internal stores. The resulting increase in cytoplasmic zinc promotes activatioin (Zhao et al. 2018).
| Eukaryota |
Metazoa, Nematoda | ZIPT-7.1 of Caenorhabditis elegans |
2.A.5.4.19 | ZIP Zinc transporter of 231 aas and 8 TMSs | Archaea |
Candidatus Lokiarchaeota | ZIP transporter of Lokiarchaeum sp. GC14_75 |
2.A.5.4.20 | Zinc/Iron transporter, Zip13 (gene: Zip99c) of 355 aas and 8 TMSs. A conserved motif in TMS4 is DNXXH instead of the usual HNXXD; only the former motif, not the latter, allows iron transport (Zhao and Zhou 2019). | Eukaryota |
Metazoa, Arthropoda | Zip13 of Drosophila melanogaster (Fruit fly) |
2.A.5.5.1 | Broad specificity heavy metal divalent cation uptake transporter, ZupT (Fe2+, Co2+, Mn2+, Cd2+ and Zn2+ are transported) (Grass et al., 2005). Point mutations change the specificity and kinetics of metal uptake (Taudte and Grass, 2010). Important for virulence in Salmonella (Karlinsey et al., 2010). ZupT has an asymmetric binuclear metal center in the transmembrane domain; one metal-binding site, M1, binds zinc, cadmium, and iron, while the other, M2, binds iron only and with higher affinity than M1. Using site-specific mutagenesis and transport activity measurements in whole cells and proteoliposomes, Roberts et al. 2021 showed that zinc is transported from M1, while iron is transported from M2. The two sites share a common bridging ligand, a conserved glutamate residue. M1 and M2 have ligands from highly conserved motifs in transmembrane domains 4 and 5. Additionally, M2 has a ligand from transmembrane domain 6, a glutamate residue, which is conserved in the gufA subfamily of ZIP transporters, including ZupT and the human ZIP11. Unlike cadmium, iron transport from M2 does not inhibit the zinc transport activity but slightly stimulates it. This stimulated activity is mediated through the bridging carboxylate ligand. The binuclear zinc-iron binding center in ZupT has likely evolved to enable the transport of essential metals from two different sites without competition; a similar mechanism of metal transport is likely to be found in the gufA subfamily of ZIP transporter proteins (Roberts et al. 2021). | Bacteria |
Pseudomonadota | ZupT of E. coli (P0A8H3) |
2.A.5.5.2 | Zinc transporter ZIP11 (Solute carrier family 39 member 11) (Zrt- and Irt-like protein 11) (ZIP-11). In mice, Zip11 mRNA is abundantly expressed in testes and the digestive system including stomach, ileum and cecum. Analysis of cellular zinc content, metallothionein levels, and cell viability under high or low zinc conditions in cells transfected with a murine Zip11 expression plasmid, suggest that Zip11 is a zinc importer (Yu et al. 2013). ZIP11 may have a zinc and iron binuclear transport center for iorn and zinc (Roberts et al. 2021). | Eukaryota |
Metazoa, Chordata | SLC39A11 of Homo sapiens |
2.A.5.5.3 | Zinc-regulated transporter 3, Zrt3 (Vacuolar membrane zinc transporter) | Eukaryota |
Fungi, Ascomycota | Zrt3 of Saccharomyces cerevisiae |
2.A.5.5.4 | Probable zinc transporter zip2 | Eukaryota |
Fungi, Ascomycota | zip2 of Schizosaccharomyces pombe |
2.A.5.5.5 | Zinc transporter ZupT | Bacteria |
Verrucomicrobiota | ZupT of Akkermansia muciniphila |
2.A.5.5.6 | ZIP11, Zinc permease of 251 aas and 8 TMSs (Hudek et al. 2013). Transports zinc as well as cadmium, cobalt, copper, manganese and nickel. | Bacteria |
Cyanobacteriota | Zinc/Iron permease of Nostoc punctiforme |
2.A.5.5.7 | Zip family protein of 651 aas, ZIL2 | Eukaryota |
Viridiplantae, Chlorophyta | ZIL2 of Chlamydomonas reinhardtii (Chlamydomonas smithii) |
2.A.5.5.8 | Zip family homologue of 553 aas and 16 TMSs | Eukaryota |
Viridiplantae, Chlorophyta | ZIP family homologue of Volvox carteri |
2.A.5.5.10 | ZIP family Zinc/Iron transporter with 267 aas and 7 or 8 TMSs | Bacteria |
Thermodesulfobacteriota | ZIP of Desulfovibrio vulgaris |
2.A.5.5.11 | ZupT zinc transporter of 277 aas and 7 or 8 TMSs. | Bacteria |
Thermodesulfobacteriota | ZupT of Desulfovibrio vulgaris |
2.A.5.5.12 | Fe2+/Zn2+ transporter, ZupT, of 226 aas and 8 - 10 TMSs (Chanket et al. 2024). | Bacteria |
Bacillota | ZupT of Clostridioides difficile (strain 630) (Peptoclostridium difficile) |
2.A.5.6.1 | Zip family member, ZIP9 (SLC39A9) (307aas; 8 TMSs). The orthologue, Zip9, in the atlantic croaker (Micropogonias undulatus) is an androgen receptor that mediates testosterone-induced apoptosis of female ovarian follicle cells (Berg et al. 2014). SLC39A9 and PIK3C3 as crucial entry factors for Ebola virus infection (Gong et al. 2024). | Eukaryota |
Metazoa, Chordata | SLC39A9 of Homo sapiens |