ID S39A1_HUMAN Reviewed; 324 AA. AC Q9NY26; B4DDY7; Q5T4K1; Q8N2H7; Q9BTV0; Q9UBI7; Q9Y2Z7; Q9Y380; DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 27-MAR-2024, entry version 179. DE RecName: Full=Zinc transporter ZIP1; DE AltName: Full=Solute carrier family 39 member 1; DE AltName: Full=Zinc-iron-regulated transporter-like; DE AltName: Full=Zrt- and Irt-like protein 1; DE Short=ZIP-1; DE Short=hZIP1; GN Name=SLC39A1 {ECO:0000312|HGNC:HGNC:12876}; GN Synonyms=IRT1, ZIP1, ZIRTL {ECO:0000303|PubMed:10610721}; GN ORFNames=CGI-08, CGI-71; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), AND TISSUE RP SPECIFICITY. RX PubMed=10610721; DOI=10.1006/geno.1999.5993; RA Lioumi M., Ferguson C.A., Sharpe P.T., Freeman T., Marenholz I., RA Mischke D., Heizmann C., Ragoussis J.; RT "Isolation and characterization of human and mouse ZIRTL, a member of the RT IRT1 family of transporters, mapping within the epidermal differentiation RT complex."; RL Genomics 62:272-280(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SUBCELLULAR LOCATION. RX PubMed=11696349; DOI=10.1016/s0014-5793(01)02950-7; RA Milon B., Dhermy D., Pountney D., Bourgeois M., Beaumont C.; RT "Differential subcellular localization of hZip1 in adherent and non- RT adherent cells."; RL FEBS Lett. 507:241-246(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=10810093; DOI=10.1101/gr.10.5.703; RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.; RT "Identification of novel human genes evolutionarily conserved in RT Caenorhabditis elegans by comparative proteomics."; RL Genome Res. 10:703-713(2000). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Thyroid, and Urinary bladder; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=16303743; DOI=10.1093/dnares/12.2.117; RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y., RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., RA Isogai T.; RT "Signal sequence and keyword trap in silico for selection of full-length RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA RT libraries."; RL DNA Res. 12:117-126(2005). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Kidney, Lung, Muscle, and Placenta; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [9] RP FUNCTION, TRANSPORTER ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR RP LOCATION, AND TISSUE SPECIFICITY. RX PubMed=11301334; DOI=10.1074/jbc.m101772200; RA Gaither L.A., Eide D.J.; RT "The human ZIP1 transporter mediates zinc uptake in human K562 RT erythroleukemia cells."; RL J. Biol. Chem. 276:22258-22264(2001). RN [10] RP FUNCTION, AND TRANSPORTER ACTIVITY. RX PubMed=12888280; DOI=10.1016/s0162-0134(03)00249-6; RA Franklin R.B., Ma J., Zou J., Guan Z., Kukoyi B.I., Feng P., Costello L.C.; RT "Human ZIP1 is a major zinc uptake transporter for the accumulation of zinc RT in prostate cells."; RL J. Inorg. Biochem. 96:435-442(2003). RN [11] RP INDUCTION. RX PubMed=16153295; DOI=10.1186/1476-4598-4-32; RA Franklin R.B., Feng P., Milon B., Desouki M.M., Singh K.K., RA Kajdacsy-Balla A., Bagasra O., Costello L.C.; RT "hZIP1 zinc uptake transporter down regulation and zinc depletion in RT prostate cancer."; RL Mol. Cancer 4:32-32(2005). RN [12] RP FUNCTION, TRANSPORTER ACTIVITY, MUTAGENESIS OF HIS-158; HIS-160; HIS-190 RP AND HIS-217, AND SUBCELLULAR LOCATION. RX PubMed=16844077; DOI=10.1016/j.bbamem.2006.06.005; RA Milon B., Wu Q., Zou J., Costello L.C., Franklin R.B.; RT "Histidine residues in the region between transmembrane domains III and IV RT of hZip1 are required for zinc transport across the plasma membrane in PC-3 RT cells."; RL Biochim. Biophys. Acta 1758:1696-1701(2006). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). CC -!- FUNCTION: Transporter for the divalent cation Zn(2+). Mediates the CC influx of Zn(2+) into cells from extracellular space (PubMed:11301334, CC PubMed:12888280, PubMed:16844077). Functions as the major importer of CC zinc from circulating blood plasma into prostate cells CC (PubMed:12888280). {ECO:0000269|PubMed:11301334, CC ECO:0000269|PubMed:12888280, ECO:0000269|PubMed:16844077}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Zn(2+)(in) = Zn(2+)(out); Xref=Rhea:RHEA:29351, CC ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:11301334, CC ECO:0000269|PubMed:12888280, ECO:0000269|PubMed:16844077}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29352; CC Evidence={ECO:0000305|PubMed:11301334}; CC -!- ACTIVITY REGULATION: Inhibited by Ni(2+) ions. Fe(2+) ions do not CC inhibit zinc uptake. {ECO:0000269|PubMed:11301334}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=3.5 uM for Zn(2+) {ECO:0000269|PubMed:11301334}; CC -!- INTERACTION: CC Q9NY26; P21964: COMT; NbExp=3; IntAct=EBI-726491, EBI-372265; CC Q9NY26; Q07325: CXCL9; NbExp=3; IntAct=EBI-726491, EBI-3911467; CC Q9NY26; P49447: CYB561; NbExp=3; IntAct=EBI-726491, EBI-8646596; CC Q9NY26; Q96CV9: OPTN; NbExp=3; IntAct=EBI-726491, EBI-748974; CC Q9NY26; Q9H2L4: TMEM60; NbExp=3; IntAct=EBI-726491, EBI-2852148; CC Q9NY26; A5PKU2: TUSC5; NbExp=3; IntAct=EBI-726491, EBI-11988865; CC Q9NY26; Q96EC8: YIPF6; NbExp=3; IntAct=EBI-726491, EBI-751210; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11301334, CC ECO:0000269|PubMed:11696349, ECO:0000269|PubMed:16844077}; Multi-pass CC membrane protein {ECO:0000255}. Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:11696349}; Multi-pass membrane protein CC {ECO:0000255}. Note=Shows a vesicular localization corresponding CC partially to the endoplasmic reticulum in several epithelial cell CC lines. {ECO:0000269|PubMed:11696349}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9NY26-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9NY26-2; Sequence=VSP_056522; CC -!- TISSUE SPECIFICITY: Ubiquitous (PubMed:10610721, PubMed:11301334). CC Expressed in most adult and fetal tissues including the epidermis. CC {ECO:0000269|PubMed:10610721, ECO:0000269|PubMed:11301334}. CC -!- INDUCTION: Down-regulated in prostate cancer. CC {ECO:0000269|PubMed:16153295}. CC -!- MISCELLANEOUS: Inhibited by Ni(2+) ions. Fe(2+) ions do not inhibit CC zinc uptake. CC -!- SIMILARITY: Belongs to the ZIP transporter (TC 2.A.5) family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD27717.1; Type=Frameshift; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/46571/SLC39A1"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AJ243649; CAB59979.1; -; mRNA. DR EMBL; AJ243650; CAB59980.1; -; Genomic_DNA. DR EMBL; AJ271671; CAB82784.1; -; mRNA. DR EMBL; AF132942; AAD27717.1; ALT_FRAME; mRNA. DR EMBL; AF151829; AAD34066.1; -; mRNA. DR EMBL; AK075257; BAC11502.1; -; mRNA. DR EMBL; AK074943; BAG52035.1; -; mRNA. DR EMBL; AK293389; BAG56898.1; -; mRNA. DR EMBL; AL358472; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471121; EAW53259.1; -; Genomic_DNA. DR EMBL; CH471121; EAW53261.1; -; Genomic_DNA. DR EMBL; CH471121; EAW53264.1; -; Genomic_DNA. DR EMBL; CH471121; EAW53265.1; -; Genomic_DNA. DR EMBL; CH471121; EAW53267.1; -; Genomic_DNA. DR EMBL; BC002563; AAH02563.1; -; mRNA. DR EMBL; BC003152; AAH03152.1; -; mRNA. DR EMBL; BC007886; AAH07886.1; -; mRNA. DR EMBL; BC014303; AAH14303.1; -; mRNA. DR CCDS; CCDS1055.1; -. [Q9NY26-1] DR RefSeq; NP_001258886.1; NM_001271957.1. [Q9NY26-1] DR RefSeq; NP_001258887.1; NM_001271958.1. [Q9NY26-1] DR RefSeq; NP_001258888.1; NM_001271959.1. [Q9NY26-1] DR RefSeq; NP_001258889.1; NM_001271960.1. [Q9NY26-1] DR RefSeq; NP_001258890.1; NM_001271961.1. DR RefSeq; NP_055252.2; NM_014437.4. [Q9NY26-1] DR AlphaFoldDB; Q9NY26; -. DR SMR; Q9NY26; -. DR BioGRID; 118050; 49. DR IntAct; Q9NY26; 29. DR MINT; Q9NY26; -. DR STRING; 9606.ENSP00000357612; -. DR DrugBank; DB14533; Zinc chloride. DR DrugBank; DB14548; Zinc sulfate, unspecified form. DR TCDB; 2.A.5.3.2; the zinc (zn(2+))-iron (fe(2+)) permease (zip) family. DR PhosphoSitePlus; Q9NY26; -. DR SwissPalm; Q9NY26; -. DR BioMuta; SLC39A1; -. DR DMDM; 37090460; -. DR EPD; Q9NY26; -. DR jPOST; Q9NY26; -. DR MassIVE; Q9NY26; -. DR MaxQB; Q9NY26; -. DR PaxDb; 9606-ENSP00000357612; -. DR PeptideAtlas; Q9NY26; -. DR ProteomicsDB; 3906; -. DR ProteomicsDB; 83153; -. [Q9NY26-1] DR Pumba; Q9NY26; -. DR Antibodypedia; 20389; 121 antibodies from 27 providers. DR DNASU; 27173; -. DR Ensembl; ENST00000310483.10; ENSP00000309710.6; ENSG00000143570.19. [Q9NY26-1] DR Ensembl; ENST00000356205.9; ENSP00000348535.4; ENSG00000143570.19. [Q9NY26-1] DR Ensembl; ENST00000368621.5; ENSP00000357610.1; ENSG00000143570.19. [Q9NY26-1] DR Ensembl; ENST00000368623.7; ENSP00000357612.3; ENSG00000143570.19. [Q9NY26-1] DR Ensembl; ENST00000617697.4; ENSP00000479421.1; ENSG00000143570.19. [Q9NY26-1] DR Ensembl; ENST00000621013.4; ENSP00000484182.1; ENSG00000143570.19. [Q9NY26-1] DR GeneID; 27173; -. DR KEGG; hsa:27173; -. DR MANE-Select; ENST00000356205.9; ENSP00000348535.4; NM_001271958.2; NP_001258887.1. DR UCSC; uc001fdi.5; human. [Q9NY26-1] DR AGR; HGNC:12876; -. DR CTD; 27173; -. DR DisGeNET; 27173; -. DR GeneCards; SLC39A1; -. DR HGNC; HGNC:12876; SLC39A1. DR HPA; ENSG00000143570; Low tissue specificity. DR MIM; 604740; gene. DR neXtProt; NX_Q9NY26; -. DR OpenTargets; ENSG00000143570; -. DR PharmGKB; PA37465; -. DR VEuPathDB; HostDB:ENSG00000143570; -. DR eggNOG; KOG1558; Eukaryota. DR GeneTree; ENSGT00940000157062; -. DR InParanoid; Q9NY26; -. DR OMA; FGFAPLC; -. DR OrthoDB; 5482951at2759; -. DR PhylomeDB; Q9NY26; -. DR TreeFam; TF317098; -. DR PathwayCommons; Q9NY26; -. DR Reactome; R-HSA-442380; Zinc influx into cells by the SLC39 gene family. DR SignaLink; Q9NY26; -. DR BioGRID-ORCS; 27173; 28 hits in 1163 CRISPR screens. DR ChiTaRS; SLC39A1; human. DR GeneWiki; SLC39A1; -. DR GenomeRNAi; 27173; -. DR Pharos; Q9NY26; Tbio. DR PRO; PR:Q9NY26; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q9NY26; Protein. DR Bgee; ENSG00000143570; Expressed in placenta and 97 other cell types or tissues. DR ExpressionAtlas; Q9NY26; baseline and differential. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; TAS:ProtInc. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0022890; F:inorganic cation transmembrane transporter activity; TAS:ProtInc. DR GO; GO:0005102; F:signaling receptor binding; IEA:Ensembl. DR GO; GO:0005385; F:zinc ion transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IEA:Ensembl. DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl. DR GO; GO:0060173; P:limb development; IEA:Ensembl. DR GO; GO:0006812; P:monoatomic cation transport; TAS:ProtInc. DR GO; GO:0071577; P:zinc ion transmembrane transport; IDA:UniProtKB. DR InterPro; IPR003689; ZIP. DR PANTHER; PTHR11040:SF58; ZINC TRANSPORTER ZIP1; 1. DR PANTHER; PTHR11040; ZINC/IRON TRANSPORTER; 1. DR Pfam; PF02535; Zip; 1. DR Genevisible; Q9NY26; HS. PE 1: Evidence at protein level; KW Alternative splicing; Cell membrane; Endoplasmic reticulum; Ion transport; KW Membrane; Reference proteome; Transmembrane; Transmembrane helix; KW Transport; Zinc; Zinc transport. FT CHAIN 1..324 FT /note="Zinc transporter ZIP1" FT /id="PRO_0000068763" FT TOPO_DOM 1..30 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 31..51 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 52..68 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 69..89 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 90..104 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 105..125 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 126..179 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 180..200 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 201..206 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 207..227 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 228..237 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 238..258 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 259..272 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 273..293 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 294..303 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 304..324 FT /note="Helical" FT /evidence="ECO:0000255" FT VAR_SEQ 1..106 FT /note="MGPWGEPELLVWRPEAVASEPPVPVGLEVKLGALVLLLVLTLLCSLVPICVL FT RRPGANHEGSASRQKALSLVSCFAGGVFLATCLLDLLPDYLAAIDEALAALHVT -> M FT KAQ (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056522" FT MUTAGEN 158 FT /note="H->A: Does not affect membrane localization; when FT associated with A-160. Decreases zinc uptake; when FT associated with A-160." FT /evidence="ECO:0000269|PubMed:16844077" FT MUTAGEN 160 FT /note="H->A: Does not affect membrane localization; when FT associated with A-158. Decreases zinc uptake; when FT associated with A-158." FT /evidence="ECO:0000269|PubMed:16844077" FT MUTAGEN 190 FT /note="H->A: Does not affect membrane localization. FT Decreases zinc uptake." FT /evidence="ECO:0000269|PubMed:16844077" FT MUTAGEN 217 FT /note="H->A: Does not affect membrane localization. FT Decreases zinc uptake." FT /evidence="ECO:0000269|PubMed:16844077" FT CONFLICT 10..18 FT /note="LVWRPEAVA -> HGVAPRGGT (in Ref. 3; AAD34066)" FT /evidence="ECO:0000305" FT CONFLICT 16 FT /note="A -> S (in Ref. 8; AAH03152)" FT /evidence="ECO:0000305" FT CONFLICT 47..50 FT /note="VPIC -> GSIG (in Ref. 1; CAB59979/CAB59980)" FT /evidence="ECO:0000305" FT CONFLICT 55 FT /note="P -> T (in Ref. 1; CAB59979/CAB59980)" FT /evidence="ECO:0000305" FT CONFLICT 120 FT /note="F -> V (in Ref. 3; AAD27717/AAD34066)" FT /evidence="ECO:0000305" FT CONFLICT 302 FT /note="R -> G (in Ref. 4; BAC11502)" FT /evidence="ECO:0000305" SQ SEQUENCE 324 AA; 34250 MW; 884C168AA8E8C0DF CRC64; MGPWGEPELL VWRPEAVASE PPVPVGLEVK LGALVLLLVL TLLCSLVPIC VLRRPGANHE GSASRQKALS LVSCFAGGVF LATCLLDLLP DYLAAIDEAL AALHVTLQFP LQEFILAMGF FLVLVMEQIT LAYKEQSGPS PLEETRALLG TVNGGPQHWH DGPGVPQASG APATPSALRA CVLVFSLALH SVFEGLAVGL QRDRARAMEL CLALLLHKGI LAVSLSLRLL QSHLRAQVVA GCGILFSCMT PLGIGLGAAL AESAGPLHQL AQSVLEGMAA GTFLYITFLE ILPQELASSE QRILKVILLL AGFALLTGLL FIQI //