ZNT5_HUMAN
ID ZNT5_HUMAN Reviewed; 765 AA.
AC Q8TAD4; B7ZM89; Q6UX54; Q7L4M4; Q8TDG3; Q9BVY8; Q9H9H1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Zinc transporter 5;
DE Short=ZnT-5;
DE AltName: Full=Solute carrier family 30 member 5;
DE AltName: Full=ZnT-like transporter 1;
DE Short=hZTL1;
GN Name=SLC30A5; Synonyms=ZNT5, ZNTL1, ZTL1; ORFNames=UNQ863/PRO1879;
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 [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=11904301; DOI=10.1074/jbc.m200910200;
RA Kambe T., Narita H., Yamaguchi-Iwai Y., Hirose J., Amano T., Sugiura N.,
RA Sasaki R., Mori K., Iwanaga T., Nagao M.;
RT "Cloning and characterization of a novel mammalian zinc transporter, zinc
RT transporter 5, abundantly expressed in pancreatic beta cells.";
RL J. Biol. Chem. 277:19049-19055(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Small intestine;
RX PubMed=11937503; DOI=10.1074/jbc.m200577200;
RA Cragg R.A., Christie G.R., Phillips S.R., Russi R.M., Kuery S.,
RA Mathers J.C., Taylor P.M., Ford D.;
RT "A novel zinc-regulated human zinc transporter, hZTL1, is localized to the
RT enterocyte apical membrane.";
RL J. Biol. Chem. 277:22789-22797(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND INDUCTION.
RC TISSUE=Heart;
RX PubMed=15276077; DOI=10.1016/j.bcp.2004.05.024;
RA Devergnas S., Chimienti F., Naud N., Pennequin A., Coquerel Y.,
RA Chantegrel J., Favier A., Seve M.;
RT "Differential regulation of zinc efflux transporters ZnT-1, ZnT-5 and ZnT-7
RT gene expression by zinc levels: a real-time RT-PCR study.";
RL Biochem. Pharmacol. 68:699-709(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Teratocarcinoma, and Trachea;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon endothelium;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 104-765 (ISOFORM 1).
RC TISSUE=Brain, Placenta, and Uterus;
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 [10]
RP FUNCTION, AND INTERACTION WITH ZNT6.
RX PubMed=15994300; DOI=10.1074/jbc.m506902200;
RA Suzuki T., Ishihara K., Migaki H., Ishihara K., Nagao M.,
RA Yamaguchi-Iwai Y., Kambe T.;
RT "Two different zinc transport complexes of cation diffusion facilitator
RT proteins localized in the secretory pathway operate to activate alkaline
RT phosphatases in vertebrate cells.";
RL J. Biol. Chem. 280:30956-30962(2005).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15525635; DOI=10.1074/jbc.m411247200;
RA Suzuki T., Ishihara K., Migaki H., Matsuura W., Kohda A., Okumura K.,
RA Nagao M., Yamaguchi-Iwai Y., Kambe T.;
RT "Zinc transporters, ZnT5 and ZnT7, are required for the activation of
RT alkaline phosphatases, zinc-requiring enzymes that are
RT glycosylphosphatidylinositol-anchored to the cytoplasmic membrane.";
RL J. Biol. Chem. 280:637-643(2005).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [13]
RP SUBUNIT.
RX PubMed=19521526; DOI=10.1371/journal.pone.0005896;
RA Salazar G., Falcon-Perez J.M., Harrison R., Faundez V.;
RT "SLC30A3 (ZnT3) oligomerization by dityrosine bonds regulates its
RT subcellular localization and metal transport capacity.";
RL PLoS ONE 4:e5896-e5896(2009).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [16]
RP INDUCTION.
RX PubMed=25582195; DOI=10.1128/mcb.01298-14;
RA Ogo O.A., Tyson J., Cockell S.J., Howard A., Valentine R.A., Ford D.;
RT "The zinc finger protein ZNF658 regulates the transcription of genes
RT involved in zinc homeostasis and affects ribosome biogenesis through the
RT zinc transcriptional regulatory element.";
RL Mol. Cell. Biol. 35:977-987(2015).
CC -!- FUNCTION: Functions as a zinc transporter. May be a transporter of zinc
CC into beta cells in order to form insulin crystals. Partly regulates
CC cellular zinc homeostasis. Required with ZNT7 for the activation of
CC zinc-requiring enzymes, alkaline phosphatases (ALPs). Transports zinc
CC into the lumens of the Golgi apparatus and vesicular compartments where
CC ALPs locate, thus, converting apoALPs to holoALPs. Required with ZNT6
CC and ZNT7 for the activation of TNAP. {ECO:0000269|PubMed:11904301,
CC ECO:0000269|PubMed:11937503, ECO:0000269|PubMed:15276077,
CC ECO:0000269|PubMed:15525635, ECO:0000269|PubMed:15994300}.
CC -!- SUBUNIT: Homodimer. Homodimerization could enhance the zinc transport
CC efficiency (PubMed:19521526). Forms heterooligomers with ZNT6.
CC {ECO:0000269|PubMed:15994300, ECO:0000269|PubMed:19521526}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000269|PubMed:11904301, ECO:0000269|PubMed:11937503,
CC ECO:0000269|PubMed:15525635}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:11904301, ECO:0000269|PubMed:11937503,
CC ECO:0000269|PubMed:15525635}. Note=Perimeter of granules, localizes to
CC the brush border membrane of the enterocyte. Concentrated in early
CC compartments of the secretory pathway such as COPII-coated vesicles.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8TAD4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TAD4-2; Sequence=VSP_030254, VSP_030255, VSP_030256;
CC Name=3;
CC IsoId=Q8TAD4-3; Sequence=VSP_043673, VSP_043674;
CC Name=4;
CC IsoId=Q8TAD4-4; Sequence=VSP_045115, VSP_043673, VSP_043674;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Highly expressed in
CC pancreas, liver and kidney. Expressed abundantly in insulin-containing
CC beta cells, undetectable in other endocrine cell types including
CC glucagon-secreting alpha cells and most acinar cells.
CC {ECO:0000269|PubMed:11904301, ECO:0000269|PubMed:11937503}.
CC -!- INDUCTION: Down-regulated by ZNF658 in response to zinc.
CC {ECO:0000269|PubMed:15276077, ECO:0000269|PubMed:25582195}.
CC -!- MISCELLANEOUS: The histidine-rich loop is essential for ZNT5 and ZNT6
CC heterooligomeric complexes to activate TNAP.
CC -!- SIMILARITY: Belongs to the cation diffusion facilitator (CDF)
CC transporter (TC 2.A.4) family. SLC30A subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14258.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF461760; AAL96437.1; -; mRNA.
DR EMBL; AF439324; AAL84188.1; -; mRNA.
DR EMBL; AY089991; AAM09099.1; -; mRNA.
DR EMBL; AY358505; AAQ88869.1; -; mRNA.
DR EMBL; AK022818; BAB14258.1; ALT_INIT; mRNA.
DR EMBL; AK292925; BAF85614.1; -; mRNA.
DR EMBL; BX537394; CAD97636.1; -; mRNA.
DR EMBL; AC010273; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471137; EAW51307.1; -; Genomic_DNA.
DR EMBL; CH471137; EAW51309.1; -; Genomic_DNA.
DR EMBL; BC000808; AAH00808.1; -; mRNA.
DR EMBL; BC008198; AAH08198.2; -; mRNA.
DR EMBL; BC017441; AAH17441.1; -; mRNA.
DR EMBL; BC130452; AAI30453.1; -; mRNA.
DR EMBL; BC130454; AAI30455.1; -; mRNA.
DR EMBL; BC144349; AAI44350.1; -; mRNA.
DR CCDS; CCDS34173.1; -. [Q8TAD4-3]
DR CCDS; CCDS3996.1; -. [Q8TAD4-1]
DR CCDS; CCDS58955.1; -. [Q8TAD4-4]
DR RefSeq; NP_001238898.1; NM_001251969.1. [Q8TAD4-4]
DR RefSeq; NP_075053.2; NM_022902.4. [Q8TAD4-1]
DR RefSeq; NP_076960.1; NM_024055.4. [Q8TAD4-3]
DR AlphaFoldDB; Q8TAD4; -.
DR SMR; Q8TAD4; -.
DR BioGRID; 122346; 135.
DR IntAct; Q8TAD4; 28.
DR MINT; Q8TAD4; -.
DR STRING; 9606.ENSP00000379836; -.
DR DrugBank; DB14533; Zinc chloride.
DR DrugBank; DB14548; Zinc sulfate, unspecified form.
DR TCDB; 2.A.4.4.3; the cation diffusion facilitator (cdf) family.
DR iPTMnet; Q8TAD4; -.
DR PhosphoSitePlus; Q8TAD4; -.
DR BioMuta; SLC30A5; -.
DR DMDM; 74723898; -.
DR EPD; Q8TAD4; -.
DR jPOST; Q8TAD4; -.
DR MassIVE; Q8TAD4; -.
DR MaxQB; Q8TAD4; -.
DR PaxDb; Q8TAD4; -.
DR PeptideAtlas; Q8TAD4; -.
DR PRIDE; Q8TAD4; -.
DR ProteomicsDB; 7251; -.
DR ProteomicsDB; 73861; -. [Q8TAD4-1]
DR ProteomicsDB; 73862; -. [Q8TAD4-2]
DR ProteomicsDB; 73863; -. [Q8TAD4-3]
DR Antibodypedia; 23894; 48 antibodies from 13 providers.
DR DNASU; 64924; -.
DR Ensembl; ENST00000380860.8; ENSP00000370241.4; ENSG00000145740.20. [Q8TAD4-3]
DR Ensembl; ENST00000396591.8; ENSP00000379836.3; ENSG00000145740.20. [Q8TAD4-1]
DR Ensembl; ENST00000502979.1; ENSP00000421251.1; ENSG00000145740.20. [Q8TAD4-4]
DR GeneID; 64924; -.
DR KEGG; hsa:64924; -.
DR MANE-Select; ENST00000396591.8; ENSP00000379836.3; NM_022902.5; NP_075053.2.
DR UCSC; uc003jvg.4; human. [Q8TAD4-1]
DR CTD; 64924; -.
DR DisGeNET; 64924; -.
DR GeneCards; SLC30A5; -.
DR HGNC; HGNC:19089; SLC30A5.
DR HPA; ENSG00000145740; Low tissue specificity.
DR MIM; 607819; gene.
DR neXtProt; NX_Q8TAD4; -.
DR OpenTargets; ENSG00000145740; -.
DR PharmGKB; PA134865113; -.
DR VEuPathDB; HostDB:ENSG00000145740; -.
DR eggNOG; KOG1484; Eukaryota.
DR GeneTree; ENSGT00940000155754; -.
DR HOGENOM; CLU_2072337_0_0_1; -.
DR InParanoid; Q8TAD4; -.
DR OMA; FDPPNIN; -.
DR OrthoDB; 1507860at2759; -.
DR PhylomeDB; Q8TAD4; -.
DR TreeFam; TF315217; -.
DR PathwayCommons; Q8TAD4; -.
DR Reactome; R-HSA-264876; Insulin processing.
DR Reactome; R-HSA-435368; Zinc efflux and compartmentalization by the SLC30 family.
DR SignaLink; Q8TAD4; -.
DR BioGRID-ORCS; 64924; 11 hits in 1079 CRISPR screens.
DR ChiTaRS; SLC30A5; human.
DR GenomeRNAi; 64924; -.
DR Pharos; Q8TAD4; Tbio.
DR PRO; PR:Q8TAD4; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q8TAD4; protein.
DR Bgee; ENSG00000145740; Expressed in buccal mucosa cell and 194 other tissues.
DR ExpressionAtlas; Q8TAD4; baseline and differential.
DR Genevisible; Q8TAD4; HS.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IDA:BHF-UCL.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0030141; C:secretory granule; IDA:MGI.
DR GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
DR GO; GO:0046873; F:metal ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; NAS:UniProtKB.
DR GO; GO:0005385; F:zinc ion transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0006882; P:cellular zinc ion homeostasis; IDA:UniProtKB.
DR GO; GO:0006824; P:cobalt ion transport; IDA:MGI.
DR GO; GO:0030070; P:insulin processing; TAS:Reactome.
DR GO; GO:0030001; P:metal ion transport; IBA:GO_Central.
DR GO; GO:0010155; P:regulation of proton transport; NAS:UniProtKB.
DR GO; GO:0010043; P:response to zinc ion; IDA:UniProtKB.
DR GO; GO:1904257; P:zinc ion import into Golgi apparatus; IBA:GO_Central.
DR GO; GO:0071577; P:zinc ion transmembrane transport; TAS:Reactome.
DR GO; GO:0006829; P:zinc ion transport; IDA:UniProtKB.
DR Gene3D; 1.20.1510.10; -; 1.
DR InterPro; IPR002524; Cation_efflux.
DR InterPro; IPR027469; Cation_efflux_TMD_sf.
DR InterPro; IPR045316; Msc2-like.
DR PANTHER; PTHR45755; PTHR45755; 1.
DR Pfam; PF01545; Cation_efflux; 1.
DR SUPFAM; SSF161111; SSF161111; 1.
DR TIGRFAMs; TIGR01297; CDF; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Golgi apparatus; Ion transport;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport; Zinc; Zinc transport.
FT CHAIN 1..765
FT /note="Zinc transporter 5"
FT /id="PRO_0000314293"
FT TOPO_DOM 1..32
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 54..56
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 78..98
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 120
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 142..152
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 174..193
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 215..238
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260..267
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 268..288
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 289..303
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 304..324
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 325..342
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 343..363
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 364..418
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 419..439
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 440..448
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 449..469
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 470..483
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 484..504
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 505..520
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 521..541
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 542..592
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 593..613
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 614..617
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 618..638
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 639..765
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 542..578
FT /note="His-rich loop"
FT REGION 551..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT VAR_SEQ 1..171
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11937503"
FT /id="VSP_030254"
FT VAR_SEQ 29..69
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_045115"
FT VAR_SEQ 92..118
FT /note="WIKIFKHAVAGCIISLLWFFGLTLCGP -> IIGSLKIPGRKEFKDKKLNDP
FT RKLVGN (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043673"
FT VAR_SEQ 119..765
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043674"
FT VAR_SEQ 667..694
FT /note="IQKIEGLISYRDPHFWRHSASIVAGTIH -> VLYVISSLLSSLKITFLKSL
FT LEVKQTTK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11937503"
FT /id="VSP_030255"
FT VAR_SEQ 695..765
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11937503"
FT /id="VSP_030256"
FT CONFLICT 303
FT /note="R -> C (in Ref. 5; BAB14258)"
FT /evidence="ECO:0000305"
FT CONFLICT 321
FT /note="T -> A (in Ref. 2; AAL84188)"
FT /evidence="ECO:0000305"
FT CONFLICT 328
FT /note="L -> P (in Ref. 2; AAL84188)"
FT /evidence="ECO:0000305"
FT CONFLICT 483
FT /note="R -> Q (in Ref. 5; BAB14258)"
FT /evidence="ECO:0000305"
FT CONFLICT 628..629
FT /note="FI -> ST (in Ref. 4; AAQ88869)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 765 AA; 84047 MW; CD96BB6D710DF42D CRC64;
MEEKYGGDVL AGPGGGGGLG PVDVPSARLT KYIVLLCFTK FLKAVGLFES YDLLKAVHIV
QFIFILKLGT AFFMVLFQKP FSSGKTITKH QWIKIFKHAV AGCIISLLWF FGLTLCGPLR
TLLLFEHSDI VVISLLSVLF TSSGGGPAKT RGAAFFIIAV ICLLLFDNDD LMAKMAEHPE
GHHDSALTHM LYTAIAFLGV ADHKGGVLLL VLALCCKVGF HTASRKLSVD VGGAKRLQAL
SHLVSVLLLC PWVIVLSVTT ESKVESWFSL IMPFATVIFF VMILDFYVDS ICSVKMEVSK
CARYGSFPIF ISALLFGNFW THPITDQLRA MNKAAHQEST EHVLSGGVVV SAIFFILSAN
ILSSPSKRGQ KGTLIGYSPE GTPLYNFMGD AFQHSSQSIP RFIKESLKQI LEESDSRQIF
YFLCLNLLFT FVELFYGVLT NSLGLISDGF HMLFDCSALV MGLFAALMSR WKATRIFSYG
YGRIEILSGF INGLFLIVIA FFVFMESVAR LIDPPELDTH MLTPVSVGGL IVNLIGICAF
SHAHSHAHGA SQGSCHSSDH SHSHHMHGHS DHGHGHSHGS AGGGMNANMR GVFLHVLADT
LGSIGVIVST VLIEQFGWFI ADPLCSLFIA ILIFLSVVPL IKDACQVLLL RLPPEYEKEL
HIALEKIQKI EGLISYRDPH FWRHSASIVA GTIHIQVTSD VLEQRIVQQV TGILKDAGVN
NLTIQVEKEA YFQHMSGLST GFHDVLAMTK QMESMKYCKD GTYIM
