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 03-AUG-2022, entry version 183. 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, SUBCELLULAR LOCATION, AND TISSUE 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, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, 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, AND MUTAGENESIS OF RP SER-275 AND SER-276. 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 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). CC -!- FUNCTION: Zinc transporter, that transports Zn(2+) from the endoplasmic CC reticulum/Golgi apparatus to the cytosol. Transport is stimulated by CC growth factors, such as EGF, and Ca(2+), as well as by exogenous CC Zn(2+). {ECO:0000269|PubMed:14525538, ECO:0000269|PubMed:15705588, CC 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}; Multi-pass membrane protein CC {ECO:0000255}. Golgi apparatus, cis-Golgi network membrane CC {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}. CC -!- PTM: Methylation at some His residue by METTL9 leads to reduced zinc- CC binding. {ECO:0000269|PubMed:33563959}. 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 AlphaFoldDB; Q92504; -. DR SMR; Q92504; -. DR BioGRID; 113652; 183. DR IntAct; Q92504; 56. 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; Q92504; -. DR PeptideAtlas; Q92504; -. DR PRIDE; Q92504; -. DR ProteomicsDB; 75275; -. DR Antibodypedia; 28954; 258 antibodies from 33 providers. DR DNASU; 7922; -. DR Ensembl; ENST00000374675.7; ENSP00000363807.3; ENSG00000112473.18. DR Ensembl; ENST00000374677.8; ENSP00000363809.3; ENSG00000112473.18. 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 CTD; 7922; -. DR DisGeNET; 7922; -. DR GeneCards; SLC39A7; -. DR HGNC; HGNC:4927; SLC39A7. DR HPA; ENSG00000112473; Low tissue specificity. DR MIM; 601416; gene. DR neXtProt; NX_Q92504; -. DR OpenTargets; ENSG00000112473; -. 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; 657777at2759; -. 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; 635 hits in 1082 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 95 other tissues. DR ExpressionAtlas; Q92504; baseline and differential. DR Genevisible; Q92504; HS. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA. DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. 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; IBA:GO_Central. DR GO; GO:0006882; P:cellular zinc ion homeostasis; IBA:GO_Central. DR GO; GO:0071577; P:zinc ion transmembrane transport; IBA:GO_Central. DR InterPro; IPR003689; ZIP. DR Pfam; PF02535; Zip; 1. PE 1: Evidence at protein level; KW Endoplasmic reticulum; Golgi apparatus; Ion transport; Membrane; KW Methylation; Phosphoprotein; Reference proteome; Transmembrane; KW 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 275 FT /note="Phosphoserine; by CK2" FT /evidence="ECO:0000269|PubMed:22317921, FT ECO:0007744|PubMed:20068231" FT MOD_RES 276 FT /note="Phosphoserine; by CK2" FT /evidence="ECO:0000269|PubMed:22317921, FT 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 280 FT /note="E -> G (in dbSNP:rs1048778)" FT /evidence="ECO:0000269|PubMed:8812499, ECO:0000269|Ref.2" FT /id="VAR_050036" 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 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 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 //