ID S39A7_HUMAN Reviewed; 469 AA. AC Q92504; B0UXF6; Q5STP8; Q9UIQ0; DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2001, sequence version 2. DT 27-MAR-2024, entry version 192. DE RecName: Full=Zinc transporter SLC39A7; DE AltName: Full=Histidine-rich membrane protein Ke4 {ECO:0000303|PubMed:14525538}; DE AltName: Full=Really interesting new gene 5 protein; DE AltName: Full=Solute carrier family 39 member 7; DE AltName: Full=Zrt-, Irt-like protein 7 {ECO:0000303|PubMed:15705588}; DE Short=ZIP7 {ECO:0000303|PubMed:15705588}; GN Name=SLC39A7; Synonyms=HKE4 {ECO:0000303|PubMed:14525538}, RING5; 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], AND VARIANT GLY-280. RC TISSUE=Kidney; RX PubMed=8812499; DOI=10.1006/geno.1996.0405; RA Ando A., Kikuti Y.Y., Shigenari A., Kawata H., Okamoto N., Shiina T., RA Chen L., Ikemura T., Abe K., Kimura M., Inoko H.; RT "cDNA cloning of the human homologues of the mouse Ke4 and Ke6 genes at the RT centromeric end of the human MHC region."; RL Genomics 35:600-602(1996). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLY-280. RA Vergara A., Lana I., Corella A., de Miguel C., Migliaccio M., Encio I.; RT "Molecular cloning and characterization of the human KE4 gene and 5' RT flanking region."; RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [4] 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Skin; 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 [6] RP FUNCTION, TRANSPORTER ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. RX PubMed=14525538; DOI=10.1042/bj20031183; RA Taylor K.M., Morgan H.E., Johnson A., Nicholson R.I.; RT "Structure-function analysis of HKE4, a member of the new LIV-1 subfamily RT of zinc transporters."; RL Biochem. J. 377:131-139(2004). RN [7] RP FUNCTION, TRANSPORTER ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, RP AND INDUCTION. RX PubMed=15705588; DOI=10.1074/jbc.m412188200; RA Huang L., Kirschke C.P., Zhang Y., Yu Y.Y.; RT "The ZIP7 gene (Slc39a7) encodes a zinc transporter involved in zinc RT homeostasis of the Golgi apparatus."; RL J. Biol. Chem. 280:15456-15463(2005). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Platelet; RX PubMed=18088087; DOI=10.1021/pr0704130; RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., RA Schuetz C., Walter U., Gambaryan S., Sickmann A.; RT "Phosphoproteome of resting human platelets."; RL J. Proteome Res. 7:526-534(2008). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-275 AND SER-276, AND 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 [10] RP FUNCTION, PHOSPHORYLATION AT SER-275 AND SER-276, MUTAGENESIS OF SER-275 RP AND SER-276, AND SUBUNIT. RX PubMed=22317921; DOI=10.1126/scisignal.2002585; RA Taylor K.M., Hiscox S., Nicholson R.I., Hogstrand C., Kille P.; RT "Protein kinase CK2 triggers cytosolic zinc signaling pathways by RT phosphorylation of zinc channel ZIP7."; RL Sci. Signal. 5:RA11-RA11(2012). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [13] RP FUNCTION, TRANSPORTER ACTIVITY, ACTIVITY REGULATION, PHOSPHORYLATION AT RP SER-275 AND SER-276, AND MUTAGENESIS OF SER-275; SER-276; SER-293 AND RP THR-294. RX PubMed=28205653; DOI=10.1039/c6mt00286b; RA Nimmanon T., Ziliotto S., Morris S., Flanagan L., Taylor K.M.; RT "Phosphorylation of zinc channel ZIP7 drives MAPK, PI3K and mTOR growth and RT proliferation signalling."; RL Metallomics 9:471-481(2017). RN [14] RP FUNCTION, TRANSPORTER ACTIVITY, AND SUBCELLULAR LOCATION. RX PubMed=29980658; DOI=10.1124/mol.118.112557; RA Woodruff G., Bouwkamp C.G., de Vrij F.M., Lovenberg T., Bonaventure P., RA Kushner S.A., Harrington A.W.; RT "The Zinc Transporter SLC39A7 (ZIP7) Is Essential for Regulation of RT Cytosolic Zinc Levels."; RL Mol. Pharmacol. 94:1092-1100(2018). RN [15] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=30237509; DOI=10.1038/s41418-018-0192-6; RA Fauster A., Rebsamen M., Willmann K.L., Cesar-Razquin A., Girardi E., RA Bigenzahn J.W., Schischlik F., Scorzoni S., Bruckner M., Konecka J., RA Hoermann K., Heinz L.X., Boztug K., Superti-Furga G.; RT "Systematic genetic mapping of necroptosis identifies SLC39A7 as modulator RT of death receptor trafficking."; RL Cell Death Differ. 26:1138-1155(2019). RN [16] RP METHYLATION. RX PubMed=33563959; DOI=10.1038/s41467-020-20670-7; RA Davydova E., Shimazu T., Schuhmacher M.K., Jakobsson M.E., RA Willemen H.L.D.M., Liu T., Moen A., Ho A.Y.Y., Malecki J., Schroer L., RA Pinto R., Suzuki T., Groensberg I.A., Sohtome Y., Akakabe M., Weirich S., RA Kikuchi M., Olsen J.V., Dohmae N., Umehara T., Sodeoka M., Siino V., RA McDonough M.A., Eijkelkamp N., Schofield C.J., Jeltsch A., Shinkai Y., RA Falnes P.O.; RT "The methyltransferase METTL9 mediates pervasive 1-methylhistidine RT modification in mammalian proteomes."; RL Nat. Commun. 12:891-891(2021). RN [17] RP VARIANTS AGM9 ALA-190; PRO-217; LYS-363; 372-GLN--GLU-469 DEL; ILE-395; RP 451-GLU--GLU-469 DEL AND ALA-458, CHARACTERIZATION OF VARIANTS AGM9 ALA-190 RP AND LYS-363, FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=30718914; DOI=10.1038/s41590-018-0295-8; RA Anzilotti C., Swan D.J., Boisson B., Deobagkar-Lele M., Oliveira C., RA Chabosseau P., Engelhardt K.R., Xu X., Chen R., Alvarez L., RA Berlinguer-Palmini R., Bull K.R., Cawthorne E., Cribbs A.P., RA Crockford T.L., Dang T.S., Fearn A., Fenech E.J., de Jong S.J., RA Lagerholm B.C., Ma C.S., Sims D., van den Berg B., Xu Y., Cant A.J., RA Kleiner G., Leahy T.R., de la Morena M.T., Puck J.M., Shapiro R.S., RA van der Burg M., Chapman J.R., Christianson J.C., Davies B., McGrath J.A., RA Przyborski S., Santibanez Koref M., Tangye S.G., Werner A., Rutter G.A., RA Padilla-Parra S., Casanova J.L., Cornall R.J., Conley M.E., Hambleton S.; RT "An essential role for the Zn2+ transporter ZIP7 in B cell development."; RL Nat. Immunol. 20:350-361(2019). RN [18] RP FUNCTION. RX PubMed=33608508; DOI=10.1038/s41419-021-03482-5; RA Chen P.H., Wu J., Xu Y., Ding C.C., Mestre A.A., Lin C.C., Yang W.H., RA Chi J.T.; RT "Zinc transporter ZIP7 is a novel determinant of ferroptosis."; RL Cell Death Dis. 12:198-198(2021). CC -!- FUNCTION: Transports Zn(2+) from the endoplasmic reticulum (ER)/Golgi CC apparatus to the cytosol, playing an essential role in the regulation CC of cytosolic zinc levels (PubMed:14525538, PubMed:15705588, CC PubMed:29980658, PubMed:28205653). Acts as a gatekeeper of zinc release CC from intracellular stores, requiring post-translational activation by CC phosphorylation, resulting in activation of multiple downstream CC pathways leading to cell growth and proliferation (PubMed:29980658, CC PubMed:22317921, PubMed:28205653). Has an essential role in B cell CC development and is required for proper B cell receptor signaling CC (PubMed:30718914). Plays an important role in maintaining intestinal CC epithelial homeostasis and skin dermis development by regulating ER CC function (By similarity). Controls cell signaling pathways involved in CC glucose metabolism in skeletal muscle (By similarity). Has a protective CC role against ER stress in different biological contexts CC (PubMed:29980658, PubMed:30237509). Mediates Zn(2+)-induced ferroptosis CC (PubMed:33608508). {ECO:0000250|UniProtKB:Q31125, CC ECO:0000269|PubMed:14525538, ECO:0000269|PubMed:15705588, CC ECO:0000269|PubMed:22317921, ECO:0000269|PubMed:28205653, CC ECO:0000269|PubMed:29980658, ECO:0000269|PubMed:30237509, CC ECO:0000269|PubMed:30718914, ECO:0000269|PubMed:33608508}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Zn(2+)(in) = Zn(2+)(out); Xref=Rhea:RHEA:29351, CC ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:14525538, CC ECO:0000269|PubMed:15705588, ECO:0000269|PubMed:28205653, CC ECO:0000269|PubMed:29980658}; CC -!- ACTIVITY REGULATION: Phosphorylation activates zinc transport activity. CC {ECO:0000269|PubMed:22317921, ECO:0000269|PubMed:28205653}. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:22317921}. CC -!- INTERACTION: CC Q92504; Q13520: AQP6; NbExp=3; IntAct=EBI-1051105, EBI-13059134; CC Q92504; Q13323: BIK; NbExp=3; IntAct=EBI-1051105, EBI-700794; CC Q92504; Q9UGL9: CRCT1; NbExp=3; IntAct=EBI-1051105, EBI-713677; CC Q92504; P68400: CSNK2A1; NbExp=4; IntAct=EBI-1051105, EBI-347804; CC Q92504; P48165: GJA8; NbExp=3; IntAct=EBI-1051105, EBI-17458373; CC Q92504; Q9H3M0: KCNF1; NbExp=3; IntAct=EBI-1051105, EBI-6918743; CC Q92504; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-1051105, EBI-11749135; CC Q92504; Q6L8G8: KRTAP5-7; NbExp=3; IntAct=EBI-1051105, EBI-11987425; CC Q92504; Q9BYQ4: KRTAP9-2; NbExp=3; IntAct=EBI-1051105, EBI-1044640; CC Q92504; Q5T7P2: LCE1A; NbExp=3; IntAct=EBI-1051105, EBI-11962058; CC Q92504; Q5T751: LCE1C; NbExp=3; IntAct=EBI-1051105, EBI-12224199; CC Q92504; Q5T754: LCE1F; NbExp=3; IntAct=EBI-1051105, EBI-11958008; CC Q92504; Q5TA81: LCE2C; NbExp=3; IntAct=EBI-1051105, EBI-11973993; CC Q92504; Q5TA82: LCE2D; NbExp=3; IntAct=EBI-1051105, EBI-10246750; CC Q92504; Q5TA78: LCE4A; NbExp=3; IntAct=EBI-1051105, EBI-10246358; CC Q92504; Q5TCM9: LCE5A; NbExp=3; IntAct=EBI-1051105, EBI-11955689; CC Q92504; Q5T871: LELP1; NbExp=3; IntAct=EBI-1051105, EBI-18115868; CC Q92504; Q9UGC6: RGS17; NbExp=3; IntAct=EBI-1051105, EBI-3918154; CC Q92504; Q6UXX9-2: RSPO2; NbExp=3; IntAct=EBI-1051105, EBI-12009390; CC Q92504; Q3SXP7: SHISAL1; NbExp=3; IntAct=EBI-1051105, EBI-18037857; CC Q92504; O95436-2: SLC34A2; NbExp=3; IntAct=EBI-1051105, EBI-12811757; CC Q92504; P49901: SMCP; NbExp=3; IntAct=EBI-1051105, EBI-750494; CC Q92504; O43610: SPRY3; NbExp=3; IntAct=EBI-1051105, EBI-12290641; CC Q92504; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-1051105, EBI-8638294; CC Q92504; Q9UBN6: TNFRSF10D; NbExp=3; IntAct=EBI-1051105, EBI-1044859; CC Q92504; Q86WB7-2: UNC93A; NbExp=3; IntAct=EBI-1051105, EBI-13356252; CC Q92504; Q8WWY7: WFDC12; NbExp=3; IntAct=EBI-1051105, EBI-11958577; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:14525538, ECO:0000269|PubMed:29980658, CC ECO:0000269|PubMed:30237509, ECO:0000269|PubMed:30718914}; Multi-pass CC membrane protein {ECO:0000255}. Golgi apparatus, cis-Golgi network CC membrane {ECO:0000269|PubMed:15705588}; Multi-pass membrane protein CC {ECO:0000255}. CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:14525538, CC ECO:0000269|PubMed:15705588}. CC -!- INDUCTION: Down-regulated by Zn(+2). {ECO:0000269|PubMed:15705588}. CC -!- PTM: Rapidly phosphorylated by CK2 following Zn(2+) treatment. This CC phosphorylation is required for efficient cytosolic Zn(2+) release. CC {ECO:0000269|PubMed:22317921, ECO:0000269|PubMed:28205653}. CC -!- PTM: Methylation at some His residue by METTL9 leads to reduced zinc- CC binding. {ECO:0000269|PubMed:33563959}. CC -!- DISEASE: Agammaglobulinemia 9, autosomal recessive (AGM9) [MIM:619693]: CC A form of agammaglobulinemia, a primary immunodeficiency characterized CC by profoundly low or absent serum antibodies and low or absent CC circulating B-cells due to an early block of B-cell development. CC Affected individuals develop severe infections in the first years of CC life. {ECO:0000269|PubMed:30718914}. Note=The disease is caused by CC variants affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the ZIP transporter (TC 2.A.5) family. CC KE4/Catsup subfamily. {ECO:0000305}. 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; D82060; BAA11528.1; -; mRNA. DR EMBL; AF117221; AAD12305.1; -; Genomic_DNA. DR EMBL; AL031228; CAA20238.1; -; Genomic_DNA. DR EMBL; AL645940; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL662824; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL844527; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR759786; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR936877; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR759733; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR354565; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471081; EAX03680.1; -; Genomic_DNA. DR EMBL; BC000645; AAH00645.1; -; mRNA. DR CCDS; CCDS43453.1; -. DR RefSeq; NP_001070984.1; NM_001077516.1. DR RefSeq; NP_001275706.1; NM_001288777.1. DR RefSeq; NP_008910.2; NM_006979.2. DR PDB; 8GZE; X-ray; 3.40 A; D/E=65-69. DR PDBsum; 8GZE; -. DR AlphaFoldDB; Q92504; -. DR SMR; Q92504; -. DR BioGRID; 113652; 209. DR IntAct; Q92504; 65. DR MINT; Q92504; -. DR STRING; 9606.ENSP00000363809; -. DR DrugBank; DB14533; Zinc chloride. DR DrugBank; DB14548; Zinc sulfate, unspecified form. DR TCDB; 2.A.5.4.3; the zinc (zn(2+))-iron (fe(2+)) permease (zip) family. DR iPTMnet; Q92504; -. DR PhosphoSitePlus; Q92504; -. DR SwissPalm; Q92504; -. DR BioMuta; SLC39A7; -. DR DMDM; 12643344; -. DR EPD; Q92504; -. DR jPOST; Q92504; -. DR MassIVE; Q92504; -. DR MaxQB; Q92504; -. DR PaxDb; 9606-ENSP00000363809; -. DR PeptideAtlas; Q92504; -. DR ProteomicsDB; 75275; -. DR Pumba; Q92504; -. DR Antibodypedia; 28954; 281 antibodies from 33 providers. DR DNASU; 7922; -. DR Ensembl; ENST00000374675.7; ENSP00000363807.3; ENSG00000112473.19. DR Ensembl; ENST00000374677.8; ENSP00000363809.3; ENSG00000112473.19. DR Ensembl; ENST00000383213.8; ENSP00000372700.4; ENSG00000206288.13. DR Ensembl; ENST00000383214.8; ENSP00000372701.4; ENSG00000206288.13. DR Ensembl; ENST00000416369.6; ENSP00000403583.2; ENSG00000229802.11. DR Ensembl; ENST00000418477.6; ENSP00000416439.2; ENSG00000226614.11. DR Ensembl; ENST00000423043.6; ENSP00000389623.2; ENSG00000226614.11. DR Ensembl; ENST00000431735.6; ENSP00000410656.2; ENSG00000224399.11. DR Ensembl; ENST00000441854.6; ENSP00000391735.2; ENSG00000229802.11. DR Ensembl; ENST00000441953.6; ENSP00000413027.2; ENSG00000224399.11. DR Ensembl; ENST00000443773.6; ENSP00000407093.2; ENSG00000227402.11. DR Ensembl; ENST00000456261.6; ENSP00000414145.2; ENSG00000227402.11. DR GeneID; 7922; -. DR KEGG; hsa:7922; -. DR MANE-Select; ENST00000374677.8; ENSP00000363809.3; NM_006979.3; NP_008910.2. DR UCSC; uc003odf.4; human. DR AGR; HGNC:4927; -. DR CTD; 7922; -. DR DisGeNET; 7922; -. DR GeneCards; SLC39A7; -. DR HGNC; HGNC:4927; SLC39A7. DR HPA; ENSG00000112473; Low tissue specificity. DR MalaCards; SLC39A7; -. DR MIM; 601416; gene. DR MIM; 619693; phenotype. DR neXtProt; NX_Q92504; -. DR OpenTargets; ENSG00000112473; -. DR Orphanet; 33110; Autosomal agammaglobulinemia. DR PharmGKB; PA29305; -. DR VEuPathDB; HostDB:ENSG00000112473; -. DR eggNOG; KOG2693; Eukaryota. DR GeneTree; ENSGT00940000160076; -. DR HOGENOM; CLU_015114_0_1_1; -. DR InParanoid; Q92504; -. DR OMA; IWLHSIG; -. DR OrthoDB; 5488029at2759; -. DR PhylomeDB; Q92504; -. DR TreeFam; TF318470; -. DR PathwayCommons; Q92504; -. DR Reactome; R-HSA-442380; Zinc influx into cells by the SLC39 gene family. DR SignaLink; Q92504; -. DR BioGRID-ORCS; 7922; 646 hits in 1160 CRISPR screens. DR ChiTaRS; SLC39A7; human. DR GeneWiki; SLC39A7; -. DR GenomeRNAi; 7922; -. DR Pharos; Q92504; Tbio. DR PRO; PR:Q92504; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; Q92504; Protein. DR Bgee; ENSG00000112473; Expressed in stromal cell of endometrium and 97 other cell types or tissues. DR ExpressionAtlas; Q92504; baseline and differential. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB. DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; TAS:ProtInc. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005385; F:zinc ion transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:0030183; P:B cell differentiation; IMP:UniProtKB. DR GO; GO:0006882; P:intracellular zinc ion homeostasis; IMP:UniProtKB. DR GO; GO:0110075; P:regulation of ferroptosis; IMP:UniProtKB. DR GO; GO:0098773; P:skin epidermis development; IEA:Ensembl. DR GO; GO:0071577; P:zinc ion transmembrane transport; IDA:UniProtKB. DR InterPro; IPR003689; ZIP. DR PANTHER; PTHR16950:SF25; ZINC TRANSPORTER SLC39A7; 1. DR PANTHER; PTHR16950; ZINC TRANSPORTER SLC39A7 HISTIDINE-RICH MEMBRANE PROTEIN KE4; 1. DR Pfam; PF02535; Zip; 1. DR Genevisible; Q92504; HS. PE 1: Evidence at protein level; KW 3D-structure; Disease variant; Endoplasmic reticulum; Golgi apparatus; KW Ion transport; Membrane; Methylation; Phosphoprotein; Reference proteome; KW Transmembrane; Transmembrane helix; Transport; Zinc; Zinc transport. FT CHAIN 1..469 FT /note="Zinc transporter SLC39A7" FT /id="PRO_0000213688" FT TRANSMEM 10..30 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 138..158 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 169..189 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 214..234 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 381..401 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 417..436 FT /note="Helical" FT /evidence="ECO:0000255" FT REGION 42..121 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 242..310 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 56..116 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 242..259 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 260..288 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 66 FT /note="Pros-methylhistidine" FT /evidence="ECO:0000250|UniProtKB:Q31125" FT MOD_RES 275 FT /note="Phosphoserine; by CK2" FT /evidence="ECO:0000269|PubMed:22317921, FT ECO:0000269|PubMed:28205653, ECO:0007744|PubMed:20068231" FT MOD_RES 276 FT /note="Phosphoserine; by CK2" FT /evidence="ECO:0000269|PubMed:22317921, FT ECO:0000269|PubMed:28205653, ECO:0007744|PubMed:20068231" FT VARIANT 87 FT /note="D -> N (in dbSNP:rs34211188)" FT /id="VAR_050034" FT VARIANT 124 FT /note="G -> R (in dbSNP:rs35690712)" FT /id="VAR_050035" FT VARIANT 190 FT /note="P -> A (in AGM9; decreased zinc ion transporter FT activity; does not affect localization to endoplasmic FT reticulum)" FT /evidence="ECO:0000269|PubMed:30718914" FT /id="VAR_086723" FT VARIANT 217 FT /note="L -> P (in AGM9)" FT /evidence="ECO:0000269|PubMed:30718914" FT /id="VAR_086724" FT VARIANT 280 FT /note="E -> G (in dbSNP:rs1048778)" FT /evidence="ECO:0000269|PubMed:8812499, ECO:0000269|Ref.2" FT /id="VAR_050036" FT VARIANT 363 FT /note="E -> K (in AGM9; decreased zinc ion transporter FT activity; does not affect localization to endoplasmic FT reticulum)" FT /evidence="ECO:0000269|PubMed:30718914" FT /id="VAR_086725" FT VARIANT 372..469 FT /note="Missing (in AGM9)" FT /evidence="ECO:0000269|PubMed:30718914" FT /id="VAR_086726" FT VARIANT 395 FT /note="T -> I (in AGM9; uncertain significance)" FT /evidence="ECO:0000269|PubMed:30718914" FT /id="VAR_086727" FT VARIANT 451..469 FT /note="Missing (in AGM9; uncertain significance)" FT /evidence="ECO:0000269|PubMed:30718914" FT /id="VAR_086728" FT VARIANT 458 FT /note="G -> A (in AGM9; uncertain significance)" FT /evidence="ECO:0000269|PubMed:30718914" FT /id="VAR_086729" FT MUTAGEN 275 FT /note="S->A: Loss of phosphorylation in response to Zn(2+) FT treatment and of cytosolic Zn(2+) release; when associated FT with A-276." FT /evidence="ECO:0000269|PubMed:22317921, FT ECO:0000269|PubMed:28205653" FT MUTAGEN 276 FT /note="S->A: Loss of phosphorylation in response to Zn(2+) FT treatment and of cytosolic Zn(2+) release; when associated FT with A-275." FT /evidence="ECO:0000269|PubMed:22317921, FT ECO:0000269|PubMed:28205653" FT MUTAGEN 293 FT /note="S->A: Loss of phosphorylation in response to Zn(2+) FT treatment and of cytosolic Zn(2+) release." FT /evidence="ECO:0000269|PubMed:28205653" FT MUTAGEN 294 FT /note="T->A: Loss of phosphorylation in response to Zn(2+) FT treatment and of cytosolic Zn(2+) release." FT /evidence="ECO:0000269|PubMed:28205653" FT CONFLICT 7 FT /note="A -> G (in Ref. 1; BAA11528 and 2; AAD12305)" FT /evidence="ECO:0000305" FT CONFLICT 376 FT /note="S -> T (in Ref. 1; BAA11528 and 2; AAD12305)" FT /evidence="ECO:0000305" FT CONFLICT 397..469 FT /note="CALLTEGGAVGSEIAGGAGPGWVLPFTAGGFIYVATVSVLPELLREASPLQS FT LLEVLGLLGGVIMMVLIAHLE -> VPFSLKEEQWTVKLQVVQVLAGSCHLLQVALST FT (in Ref. 1; BAA11528 and 2; AAD12305)" FT /evidence="ECO:0000305" SQ SEQUENCE 469 AA; 50118 MW; 6504A1EF5AA6A5B9 CRC64; MARGLGAPHW VAVGLLTWAT LGLLVAGLGG HDDLHDDLQE DFHGHSHRHS HEDFHHGHSH AHGHGHTHES IWHGHTHDHD HGHSHEDLHH GHSHGYSHES LYHRGHGHDH EHSHGGYGES GAPGIKQDLD AVTLWAYALG ATVLISAAPF FVLFLIPVES NSPRHRSLLQ ILLSFASGGL LGDAFLHLIP HALEPHSHHT LEQPGHGHSH SGQGPILSVG LWVLSGIVAF LVVEKFVRHV KGGHGHSHGH GHAHSHTRGS HGHGRQERST KEKQSSEEEE KETRGVQKRR GGSTVPKDGP VRPQNAEEEK RGLDLRVSGY LNLAADLAHN FTDGLAIGAS FRGGRGLGIL TTMTVLLHEV PHEVGDFAIL VQSGCSKKQA MRLQLLTAVG ALAGTACALL TEGGAVGSEI AGGAGPGWVL PFTAGGFIYV ATVSVLPELL REASPLQSLL EVLGLLGGVI MMVLIAHLE //