ID S12A4_HUMAN Reviewed; 1085 AA. AC Q9UP95; B4DF69; B4DR04; B4DZ82; B7ZAV0; F5H066; F5H0S9; F5H3C0; O60632; AC O75893; Q13953; Q96LD5; DT 13-DEC-2002, integrated into UniProtKB/Swiss-Prot. DT 13-DEC-2002, sequence version 2. DT 27-MAR-2024, entry version 201. DE RecName: Full=Solute carrier family 12 member 4 {ECO:0000305}; DE AltName: Full=Electroneutral potassium-chloride cotransporter 1; DE AltName: Full=Erythroid K-Cl cotransporter 1; DE Short=hKCC1; GN Name=SLC12A4 {ECO:0000312|HGNC:HGNC:10913}; GN Synonyms=KCC1 {ECO:0000303|PubMed:31649201}; 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), AND TISSUE SPECIFICITY. RC TISSUE=Embryonic kidney; RX PubMed=8663127; DOI=10.1074/jbc.271.27.16237; RA Gillen C.M., Brill S., Payne J.A., Forbush B. III; RT "Molecular cloning and functional expression of the K-Cl cotransporter from RT rabbit, rat, and human. A new member of the cation-chloride cotransporter RT family."; RL J. Biol. Chem. 271:16237-16244(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), AND TISSUE SPECIFICITY. RC TISSUE=Erythroleukemia; RX PubMed=9516379; DOI=10.1006/bcmd.1998.0168; RA Pellegrino C.M., Rybicki A.C., Musto S., Nagel R.L., Schwartz R.S.; RT "Molecular identification and expression of erythroid K:Cl cotransporter in RT human and mouse erythroleukemic cells."; RL Blood Cells Mol. Dis. 24:31-40(1998). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5 AND 6), AND NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 25-1087 (ISOFORM 7). RC TISSUE=Cerebellum, and Testis; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., RA Myers R.M., Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Eye; 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 NUCLEOTIDE SEQUENCE [MRNA] OF 280-517. RC TISSUE=Erythroleukemia; RA Golding S., Culliford S.J., Ellory J.C.; RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 684-1085 (ISOFORM 4), SUBUNIT, AND FUNCTION RP (ISOFORM 4). RX PubMed=11551954; DOI=10.1074/jbc.m107155200; RA Casula S., Shmukler B.E., Wilhelm S., Stuart-Tilley A.K., Su W., RA Chernova M.N., Brugnara C., Alper S.L.; RT "A dominant negative mutant of the KCC1 K-Cl cotransporter: both N- and C- RT terminal cytoplasmic domains are required for K-Cl cotransport activity."; RL J. Biol. Chem. 276:41870-41878(2001). RN [8] RP FUNCTION, TRANSPORTER ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND RP SUBCELLULAR LOCATION. RX PubMed=10913127; DOI=10.1074/jbc.m003112200; RA Mercado A., Song L., Vazquez N., Mount D.B., Gamba G.; RT "Functional comparison of the K+-Cl- cotransporters KCC1 and KCC4."; RL J. Biol. Chem. 275:30326-30334(2000). RN [9] RP EXPRESSION IN ERYTHROCYTE MEMBRANES. RX PubMed=10564083; DOI=10.1152/ajpcell.1999.277.5.c899; RA Su W., Shmukler B.E., Chernova M.N., Stuart-Tilley A.K., de Franceschi L., RA Brugnara C., Alper S.L.; RT "Mouse K-Cl cotransporter KCC1: cloning, mapping, pathological expression, RT and functional regulation."; RL Am. J. Physiol. 277:C899-C912(1999). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51 AND SER-967, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-967, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-967, AND IDENTIFICATION BY RP 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 [13] RP ACTIVITY REGULATION. RX PubMed=21613606; DOI=10.1152/ajpcell.00070.2011; RA Cruz-Rangel S., Melo Z., Vazquez N., Meade P., Bobadilla N.A., RA Pasantes-Morales H., Gamba G., Mercado A.; RT "Similar Effects of all WNK3 Variants upon SLC12 Cotransporters."; RL Am. J. Physiol. 301:C601-C608(2011). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-967, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24; SER-51; SER-88; SER-967 RP AND THR-983, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88, AND IDENTIFICATION BY RP 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 [17] {ECO:0007744|PDB:6KKR, ECO:0007744|PDB:6KKT, ECO:0007744|PDB:6KKU} RP STRUCTURE BY ELECTRON MICROSCOPY (2.90 ANGSTROMS) IN COMPLEX WITH CLHORIDE RP AND POTASSIUM, SUBUNIT, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-312 AND RP ASN-361. RX PubMed=31649201; DOI=10.1126/science.aay3129; RA Liu S., Chang S., Han B., Xu L., Zhang M., Zhao C., Yang W., Wang F., RA Li J., Delpire E., Ye S., Bai X.C., Guo J.; RT "Cryo-EM structures of the human cation-chloride cotransporter KCC1."; RL Science 366:505-508(2019). RN [18] {ECO:0007744|PDB:7AIP, ECO:0007744|PDB:7AIQ, ECO:0007744|PDB:7AIR} RP STRUCTURE BY ELECTRON MICROSCOPY (3.12 ANGSTROMS) OF 20-1085 IN COMPLEX RP WITH ATP, FUNCTION, TRANSPORTER ACTIVITY, DISULFIDE BONDS, AND RP PHOSPHORYLATION AT SER-734 AND SER-1050. RX PubMed=34031912; DOI=10.15252/embj.2020107294; RA Chi G., Ebenhoch R., Man H., Tang H., Tremblay L.E., Reggiano G., Qiu X., RA Bohstedt T., Liko I., Almeida F.G., Garneau A.P., Wang D., McKinley G., RA Moreau C.P., Bountra K.D., Abrusci P., Mukhopadhyay S.M.M., RA Fernandez-Cid A., Slimani S., Lavoie J.L., Burgess-Brown N.A., Tehan B., RA DiMaio F., Jazayeri A., Isenring P., Robinson C.V., Duerr K.L.; RT "Phospho-regulation, nucleotide binding and ion access control in RT potassium-chloride cotransporters."; RL EMBO J. 40:e107294-e107294(2021). CC -!- FUNCTION: Mediates electroneutral potassium-chloride cotransport when CC activated by cell swelling. May contribute to cell volume homeostasis CC in single cells (PubMed:10913127, PubMed:34031912). May be involved in CC the regulation of basolateral Cl(-) exit in NaCl absorbing epithelia CC (By similarity). {ECO:0000250|UniProtKB:Q9JIS8, CC ECO:0000269|PubMed:10913127, ECO:0000269|PubMed:34031912}. CC -!- FUNCTION: [Isoform 4]: No transporter activity. CC {ECO:0000269|PubMed:11551954}. CC -!- CATALYTIC ACTIVITY: CC Reaction=chloride(in) + K(+)(in) = chloride(out) + K(+)(out); CC Xref=Rhea:RHEA:72427, ChEBI:CHEBI:17996, ChEBI:CHEBI:29103; CC Evidence={ECO:0000269|PubMed:10913127, ECO:0000269|PubMed:34031912}; CC -!- ACTIVITY REGULATION: Inhibited by WNK3. {ECO:0000269|PubMed:21613606}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=25.5 mM for K(+) {ECO:0000269|PubMed:10913127}; CC -!- SUBUNIT: Homodimer (PubMed:31649201). Heteromultimer with other K-Cl CC cotransporters (PubMed:11551954). {ECO:0000269|PubMed:11551954, CC ECO:0000269|PubMed:31649201}. CC -!- INTERACTION: CC Q9UP95; Q9Y2T2: AP3M1; NbExp=3; IntAct=EBI-7244836, EBI-2371151; CC Q9UP95; Q9BYD5: CNFN; NbExp=3; IntAct=EBI-7244836, EBI-12819063; CC Q9UP95; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-7244836, EBI-3867333; CC Q9UP95; P59991: KRTAP12-2; NbExp=3; IntAct=EBI-7244836, EBI-10176379; CC Q9UP95; Q3LHN2: KRTAP19-2; NbExp=3; IntAct=EBI-7244836, EBI-12196745; CC Q9UP95; Q8IYB1: MB21D2; NbExp=3; IntAct=EBI-7244836, EBI-11323212; CC Q9UP95; Q8N9M5: TMEM102; NbExp=3; IntAct=EBI-7244836, EBI-1050459; CC Q9UP95; Q8N720: ZNF655; NbExp=3; IntAct=EBI-7244836, EBI-625509; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:10913127}; CC Multi-pass membrane protein {ECO:0000269|PubMed:31649201, CC ECO:0000269|PubMed:34031912}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=7; CC Comment=Experimental confirmation may be lacking for some isoforms.; CC Name=1; CC IsoId=Q9UP95-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9UP95-2; Sequence=VSP_006113, VSP_006114; CC Name=3; CC IsoId=Q9UP95-3; Sequence=VSP_006112; CC Name=4; CC IsoId=Q9UP95-4; Sequence=VSP_006108, VSP_006109, VSP_006110, CC VSP_006111; CC Name=5; CC IsoId=Q9UP95-5; Sequence=VSP_044596; CC Name=6; CC IsoId=Q9UP95-6; Sequence=VSP_046146; CC Name=7; CC IsoId=Q9UP95-7; Sequence=VSP_046369; CC -!- TISSUE SPECIFICITY: Ubiquitous (PubMed:8663127, PubMed:9516379). Levels CC are much higher in erythrocytes from patients with Hb SC and Hb SS CC compared to normal AA erythrocytes (PubMed:9516379). This may CC contribute to red blood cell dehydration and to the manifestation of CC sickle cell disease by increasing the intracellular concentration of CC HbS (PubMed:9516379). {ECO:0000269|PubMed:8663127, CC ECO:0000269|PubMed:9516379}. CC -!- TISSUE SPECIFICITY: [Isoform 1]: Not detected in circulating CC reticulocytes. {ECO:0000269|PubMed:9516379}. CC -!- PTM: Phosphorylated, phosphorylation may regulate transporter activity. CC {ECO:0000269|PubMed:34031912}. CC -!- SIMILARITY: Belongs to the SLC12A transporter family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC35282.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=BAG57330.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={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; U55054; AAC50563.1; -; mRNA. DR EMBL; AF047338; AAC32815.1; -; mRNA. DR EMBL; AF054505; AAC39684.1; -; mRNA. DR EMBL; AF054506; AAC39685.1; -; mRNA. DR EMBL; AK293956; BAG57330.1; ALT_INIT; mRNA. DR EMBL; AK299042; BAG61116.1; -; mRNA. DR EMBL; AK302790; BAG63994.1; -; mRNA. DR EMBL; AK316415; BAH14786.1; -; mRNA. DR EMBL; AC040162; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC021193; AAH21193.1; -; mRNA. DR EMBL; AF053402; AAC35282.1; ALT_FRAME; mRNA. DR EMBL; AY026038; AAK01946.1; -; mRNA. DR CCDS; CCDS10855.1; -. [Q9UP95-1] DR CCDS; CCDS54030.1; -. [Q9UP95-6] DR CCDS; CCDS54031.1; -. [Q9UP95-5] DR RefSeq; NP_001139433.1; NM_001145961.1. DR RefSeq; NP_001139434.1; NM_001145962.1. [Q9UP95-7] DR RefSeq; NP_001139435.1; NM_001145963.1. [Q9UP95-6] DR RefSeq; NP_001139436.1; NM_001145964.1. [Q9UP95-5] DR RefSeq; NP_005063.1; NM_005072.4. [Q9UP95-1] DR PDB; 6KKR; EM; 2.90 A; A/B=1-1085. DR PDB; 6KKT; EM; 2.90 A; A/B=1-1085. DR PDB; 6KKU; EM; 3.50 A; A/B=1-1085. DR PDB; 7AIP; EM; 3.12 A; A/B=20-1085. DR PDB; 7AIQ; EM; 3.72 A; A/B=20-1085. DR PDB; 7AIR; EM; 3.66 A; A/B=20-1085. DR PDB; 7TTH; EM; 3.25 A; A/B=1-1085. DR PDB; 7TTI; EM; 3.50 A; A/B=1-1085. DR PDBsum; 6KKR; -. DR PDBsum; 6KKT; -. DR PDBsum; 6KKU; -. DR PDBsum; 7AIP; -. DR PDBsum; 7AIQ; -. DR PDBsum; 7AIR; -. DR PDBsum; 7TTH; -. DR PDBsum; 7TTI; -. DR AlphaFoldDB; Q9UP95; -. DR EMDB; EMD-0701; -. DR EMDB; EMD-0702; -. DR EMDB; EMD-0703; -. DR EMDB; EMD-11801; -. DR EMDB; EMD-11802; -. DR EMDB; EMD-11803; -. DR EMDB; EMD-26115; -. DR EMDB; EMD-26116; -. DR SMR; Q9UP95; -. DR BioGRID; 112449; 146. DR IntAct; Q9UP95; 41. DR MINT; Q9UP95; -. DR STRING; 9606.ENSP00000395983; -. DR DrugBank; DB00887; Bumetanide. DR DrugBank; DB00761; Potassium chloride. DR TCDB; 2.A.30.1.17; the cation-chloride cotransporter (ccc) family. DR GlyCosmos; Q9UP95; 5 sites, No reported glycans. DR GlyGen; Q9UP95; 6 sites, 1 O-linked glycan (1 site). DR iPTMnet; Q9UP95; -. DR PhosphoSitePlus; Q9UP95; -. DR BioMuta; SLC12A4; -. DR DMDM; 27151691; -. DR EPD; Q9UP95; -. DR jPOST; Q9UP95; -. DR MassIVE; Q9UP95; -. DR MaxQB; Q9UP95; -. DR PaxDb; 9606-ENSP00000395983; -. DR PeptideAtlas; Q9UP95; -. DR ProteomicsDB; 25245; -. DR ProteomicsDB; 25434; -. DR ProteomicsDB; 26226; -. DR ProteomicsDB; 85360; -. [Q9UP95-1] DR ProteomicsDB; 85361; -. [Q9UP95-2] DR ProteomicsDB; 85362; -. [Q9UP95-3] DR ProteomicsDB; 85363; -. [Q9UP95-4] DR Pumba; Q9UP95; -. DR Antibodypedia; 29685; 199 antibodies from 31 providers. DR DNASU; 6560; -. DR Ensembl; ENST00000316341.8; ENSP00000318557.3; ENSG00000124067.17. [Q9UP95-1] DR Ensembl; ENST00000537830.6; ENSP00000445962.2; ENSG00000124067.17. [Q9UP95-6] DR Ensembl; ENST00000541864.7; ENSP00000438334.2; ENSG00000124067.17. [Q9UP95-5] DR Ensembl; ENST00000576616.5; ENSP00000458902.1; ENSG00000124067.17. [Q9UP95-2] DR GeneID; 6560; -. DR KEGG; hsa:6560; -. DR MANE-Select; ENST00000316341.8; ENSP00000318557.3; NM_005072.5; NP_005063.1. DR UCSC; uc002euz.2; human. [Q9UP95-1] DR AGR; HGNC:10913; -. DR CTD; 6560; -. DR DisGeNET; 6560; -. DR GeneCards; SLC12A4; -. DR HGNC; HGNC:10913; SLC12A4. DR HPA; ENSG00000124067; Low tissue specificity. DR MalaCards; SLC12A4; -. DR MIM; 604119; gene. DR neXtProt; NX_Q9UP95; -. DR OpenTargets; ENSG00000124067; -. DR PharmGKB; PA35807; -. DR VEuPathDB; HostDB:ENSG00000124067; -. DR eggNOG; KOG2082; Eukaryota. DR GeneTree; ENSGT00940000157672; -. DR HOGENOM; CLU_001883_1_1_1; -. DR InParanoid; Q9UP95; -. DR OMA; TGQDCPD; -. DR OrthoDB; 5490251at2759; -. DR PhylomeDB; Q9UP95; -. DR TreeFam; TF313657; -. DR PathwayCommons; Q9UP95; -. DR Reactome; R-HSA-426117; Cation-coupled Chloride cotransporters. DR SignaLink; Q9UP95; -. DR SIGNOR; Q9UP95; -. DR BioGRID-ORCS; 6560; 25 hits in 1170 CRISPR screens. DR ChiTaRS; SLC12A4; human. DR GeneWiki; Chloride_potassium_symporter_4; -. DR GenomeRNAi; 6560; -. DR Pharos; Q9UP95; Tbio. DR PRO; PR:Q9UP95; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; Q9UP95; Protein. DR Bgee; ENSG00000124067; Expressed in apex of heart and 145 other cell types or tissues. DR ExpressionAtlas; Q9UP95; baseline and differential. DR GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB. DR GO; GO:0016020; C:membrane; TAS:ProtInc. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:0045202; C:synapse; IEA:GOC. DR GO; GO:0008519; F:ammonium transmembrane transporter activity; ISS:ARUK-UCL. DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB. DR GO; GO:0015379; F:potassium:chloride symporter activity; IDA:UniProtKB. DR GO; GO:0019901; F:protein kinase binding; IPI:ParkinsonsUK-UCL. DR GO; GO:0140157; P:ammonium import across plasma membrane; ISS:ARUK-UCL. DR GO; GO:0006884; P:cell volume homeostasis; IBA:GO_Central. DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central. DR GO; GO:0055064; P:chloride ion homeostasis; ISS:UniProtKB. DR GO; GO:1902476; P:chloride transmembrane transport; IBA:GO_Central. DR GO; GO:0006811; P:monoatomic ion transport; TAS:Reactome. DR GO; GO:0055075; P:potassium ion homeostasis; ISS:UniProtKB. DR GO; GO:1990573; P:potassium ion import across plasma membrane; IBA:GO_Central. DR GO; GO:0071805; P:potassium ion transmembrane transport; ISS:UniProtKB. DR Gene3D; 1.20.1740.10; Amino acid/polyamine transporter I; 1. DR InterPro; IPR004841; AA-permease/SLC12A_dom. DR InterPro; IPR000622; KCC1. DR InterPro; IPR000076; KCL_cotranspt. DR InterPro; IPR018491; SLC12_C. DR InterPro; IPR004842; SLC12A_fam. DR NCBIfam; TIGR00930; 2a30; 1. DR PANTHER; PTHR11827:SF46; SOLUTE CARRIER FAMILY 12 MEMBER 4; 1. DR PANTHER; PTHR11827; SOLUTE CARRIER FAMILY 12, CATION COTRANSPORTERS; 1. DR Pfam; PF00324; AA_permease; 2. DR Pfam; PF03522; SLC12; 2. DR PRINTS; PR01081; KCLTRNSPORT. DR PRINTS; PR01082; KCLTRNSPORT1. DR Genevisible; Q9UP95; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell membrane; Chloride; KW Disulfide bond; Glycoprotein; Ion transport; Membrane; Phosphoprotein; KW Potassium; Potassium transport; Reference proteome; Symport; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1..1085 FT /note="Solute carrier family 12 member 4" FT /id="PRO_0000178030" FT TOPO_DOM 1..119 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:31649201, FT ECO:0000269|PubMed:34031912, ECO:0007744|PDB:6KKR, FT ECO:0007744|PDB:6KKT, ECO:0007744|PDB:6KKU, FT ECO:0007744|PDB:7AIP, ECO:0007744|PDB:7AIQ, FT ECO:0007744|PDB:7AIR" FT TRANSMEM 120..141 FT /note="Discontinuously helical" FT /evidence="ECO:0000269|PubMed:31649201, FT ECO:0000269|PubMed:34031912, ECO:0007744|PDB:6KKR, FT ECO:0007744|PDB:6KKT, ECO:0007744|PDB:6KKU, FT ECO:0007744|PDB:7AIP, ECO:0007744|PDB:7AIQ, FT ECO:0007744|PDB:7AIR" FT TOPO_DOM 142..149 FT /note="Extracellular" FT /evidence="ECO:0000269|PubMed:31649201, FT ECO:0000269|PubMed:34031912, ECO:0007744|PDB:6KKR, FT ECO:0007744|PDB:6KKT, ECO:0007744|PDB:6KKU, FT ECO:0007744|PDB:7AIP, ECO:0007744|PDB:7AIQ, FT ECO:0007744|PDB:7AIR" FT TRANSMEM 150..172 FT /note="Helical" FT /evidence="ECO:0000269|PubMed:31649201, FT ECO:0000269|PubMed:34031912, ECO:0007744|PDB:6KKR, FT ECO:0007744|PDB:6KKT, ECO:0007744|PDB:6KKU, FT ECO:0007744|PDB:7AIP, ECO:0007744|PDB:7AIQ, FT ECO:0007744|PDB:7AIR" FT TOPO_DOM 173..196 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:31649201, FT ECO:0000269|PubMed:34031912, ECO:0007744|PDB:6KKR, FT ECO:0007744|PDB:6KKT, ECO:0007744|PDB:6KKU, FT ECO:0007744|PDB:7AIP, ECO:0007744|PDB:7AIQ, FT ECO:0007744|PDB:7AIR" FT TRANSMEM 197..225 FT /note="Helical" FT /evidence="ECO:0000269|PubMed:31649201, FT ECO:0000269|PubMed:34031912, ECO:0007744|PDB:6KKR, FT ECO:0007744|PDB:6KKT, ECO:0007744|PDB:6KKU, FT ECO:0007744|PDB:7AIP, ECO:0007744|PDB:7AIQ, FT ECO:0007744|PDB:7AIR" FT TOPO_DOM 226..248 FT /note="Extracellular" FT /evidence="ECO:0000269|PubMed:31649201, FT ECO:0000269|PubMed:34031912, ECO:0007744|PDB:6KKR, FT ECO:0007744|PDB:6KKT, ECO:0007744|PDB:6KKU, FT ECO:0007744|PDB:7AIP, ECO:0007744|PDB:7AIQ, FT ECO:0007744|PDB:7AIR" FT TRANSMEM 249..271 FT /note="Helical" FT /evidence="ECO:0000269|PubMed:31649201, FT ECO:0000269|PubMed:34031912, ECO:0007744|PDB:6KKR, FT ECO:0007744|PDB:6KKT, ECO:0007744|PDB:6KKU, FT ECO:0007744|PDB:7AIP, ECO:0007744|PDB:7AIQ, FT ECO:0007744|PDB:7AIR" FT TRANSMEM 272..297 FT /note="Helical" FT /evidence="ECO:0000269|PubMed:31649201, FT ECO:0000269|PubMed:34031912, ECO:0007744|PDB:6KKR, FT ECO:0007744|PDB:6KKT, ECO:0007744|PDB:6KKU, FT ECO:0007744|PDB:7AIP, ECO:0007744|PDB:7AIQ, FT ECO:0007744|PDB:7AIR" FT TOPO_DOM 298..419 FT /note="Extracellular" FT /evidence="ECO:0000269|PubMed:31649201, FT ECO:0000269|PubMed:34031912, ECO:0007744|PDB:6KKR, FT ECO:0007744|PDB:6KKT, ECO:0007744|PDB:6KKU, FT ECO:0007744|PDB:7AIP, ECO:0007744|PDB:7AIQ, FT ECO:0007744|PDB:7AIR" FT TRANSMEM 420..440 FT /note="Helical" FT /evidence="ECO:0000269|PubMed:31649201, FT ECO:0000269|PubMed:34031912, ECO:0007744|PDB:6KKR, FT ECO:0007744|PDB:6KKT, ECO:0007744|PDB:6KKU, FT ECO:0007744|PDB:7AIP, ECO:0007744|PDB:7AIQ, FT ECO:0007744|PDB:7AIR" FT TOPO_DOM 441..450 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:31649201, FT ECO:0000269|PubMed:34031912, ECO:0007744|PDB:6KKR, FT ECO:0007744|PDB:6KKT, ECO:0007744|PDB:6KKU, FT ECO:0007744|PDB:7AIP, ECO:0007744|PDB:7AIQ, FT ECO:0007744|PDB:7AIR" FT TRANSMEM 451..473 FT /note="Helical" FT /evidence="ECO:0000269|PubMed:31649201, FT ECO:0000269|PubMed:34031912, ECO:0007744|PDB:6KKR, FT ECO:0007744|PDB:6KKT, ECO:0007744|PDB:6KKU, FT ECO:0007744|PDB:7AIP, ECO:0007744|PDB:7AIQ, FT ECO:0007744|PDB:7AIR" FT TOPO_DOM 474..504 FT /note="Extracellular" FT /evidence="ECO:0000269|PubMed:31649201, FT ECO:0000269|PubMed:34031912, ECO:0007744|PDB:6KKR, FT ECO:0007744|PDB:6KKT, ECO:0007744|PDB:6KKU, FT ECO:0007744|PDB:7AIP, ECO:0007744|PDB:7AIQ, FT ECO:0007744|PDB:7AIR" FT TRANSMEM 505..531 FT /note="Helical" FT /evidence="ECO:0000269|PubMed:31649201, FT ECO:0000269|PubMed:34031912, ECO:0007744|PDB:6KKR, FT ECO:0007744|PDB:6KKT, ECO:0007744|PDB:6KKU, FT ECO:0007744|PDB:7AIP, ECO:0007744|PDB:7AIQ, FT ECO:0007744|PDB:7AIR" FT TOPO_DOM 532..554 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:31649201, FT ECO:0000269|PubMed:34031912, ECO:0007744|PDB:6KKR, FT ECO:0007744|PDB:6KKT, ECO:0007744|PDB:6KKU, FT ECO:0007744|PDB:7AIP, ECO:0007744|PDB:7AIQ, FT ECO:0007744|PDB:7AIR" FT TRANSMEM 555..575 FT /note="Helical" FT /evidence="ECO:0000269|PubMed:31649201, FT ECO:0000269|PubMed:34031912, ECO:0007744|PDB:6KKR, FT ECO:0007744|PDB:6KKT, ECO:0007744|PDB:6KKU, FT ECO:0007744|PDB:7AIP, ECO:0007744|PDB:7AIQ, FT ECO:0007744|PDB:7AIR" FT TRANSMEM 576..598 FT /note="Helical" FT /evidence="ECO:0000269|PubMed:31649201, FT ECO:0000269|PubMed:34031912, ECO:0007744|PDB:6KKR, FT ECO:0007744|PDB:6KKT, ECO:0007744|PDB:6KKU, FT ECO:0007744|PDB:7AIP, ECO:0007744|PDB:7AIQ, FT ECO:0007744|PDB:7AIR" FT TOPO_DOM 599..612 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:31649201, FT ECO:0000269|PubMed:34031912, ECO:0007744|PDB:6KKR, FT ECO:0007744|PDB:6KKT, ECO:0007744|PDB:6KKU, FT ECO:0007744|PDB:7AIP, ECO:0007744|PDB:7AIQ, FT ECO:0007744|PDB:7AIR" FT TRANSMEM 613..635 FT /note="Helical" FT /evidence="ECO:0000269|PubMed:31649201, FT ECO:0000269|PubMed:34031912, ECO:0007744|PDB:6KKR, FT ECO:0007744|PDB:6KKT, ECO:0007744|PDB:6KKU, FT ECO:0007744|PDB:7AIP, ECO:0007744|PDB:7AIQ, FT ECO:0007744|PDB:7AIR" FT TRANSMEM 636..651 FT /note="Helical" FT /evidence="ECO:0000269|PubMed:31649201, FT ECO:0000269|PubMed:34031912, ECO:0007744|PDB:6KKR, FT ECO:0007744|PDB:6KKT, ECO:0007744|PDB:6KKU, FT ECO:0007744|PDB:7AIP, ECO:0007744|PDB:7AIQ, FT ECO:0007744|PDB:7AIR" FT TOPO_DOM 652..1085 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:31649201, FT ECO:0000269|PubMed:34031912, ECO:0007744|PDB:6KKR, FT ECO:0007744|PDB:6KKT, ECO:0007744|PDB:6KKU, FT ECO:0007744|PDB:7AIP, ECO:0007744|PDB:7AIQ, FT ECO:0007744|PDB:7AIR" FT BINDING 131 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000269|PubMed:31649201, FT ECO:0007744|PDB:6KKR, ECO:0007744|PDB:6KKT" FT BINDING 132 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000269|PubMed:31649201, FT ECO:0007744|PDB:6KKR, ECO:0007744|PDB:6KKT" FT BINDING 216 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000269|PubMed:31649201, FT ECO:0007744|PDB:6KKR" FT BINDING 429 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000269|PubMed:31649201, FT ECO:0007744|PDB:6KKR, ECO:0007744|PDB:6KKT" FT BINDING 432 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000269|PubMed:31649201, FT ECO:0007744|PDB:6KKR, ECO:0007744|PDB:6KKT" FT BINDING 433 FT /ligand="chloride" FT /ligand_id="ChEBI:CHEBI:17996" FT /ligand_label="1" FT /evidence="ECO:0000305|PubMed:31649201" FT BINDING 434 FT /ligand="chloride" FT /ligand_id="ChEBI:CHEBI:17996" FT /ligand_label="1" FT /evidence="ECO:0000305|PubMed:31649201" FT BINDING 435 FT /ligand="chloride" FT /ligand_id="ChEBI:CHEBI:17996" FT /ligand_label="1" FT /evidence="ECO:0000305|PubMed:31649201" FT BINDING 589 FT /ligand="chloride" FT /ligand_id="ChEBI:CHEBI:17996" FT /ligand_label="1" FT /evidence="ECO:0000305|PubMed:31649201" FT BINDING 589 FT /ligand="chloride" FT /ligand_id="ChEBI:CHEBI:17996" FT /ligand_label="2" FT /evidence="ECO:0000305|PubMed:31649201" FT BINDING 697 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:34031912, FT ECO:0007744|PDB:7AIP" FT BINDING 699 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:34031912, FT ECO:0007744|PDB:7AIP, ECO:0007744|PDB:7AIQ" FT BINDING 707 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:34031912, FT ECO:0007744|PDB:7AIR" FT BINDING 708 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:34031912, FT ECO:0007744|PDB:7AIP, ECO:0007744|PDB:7AIQ" FT BINDING 730 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:34031912, FT ECO:0007744|PDB:7AIP" FT BINDING 794 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:34031912, FT ECO:0007744|PDB:7AIQ, ECO:0007744|PDB:7AIR" FT BINDING 795 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:34031912, FT ECO:0007744|PDB:7AIR" FT BINDING 797 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:34031912, FT ECO:0007744|PDB:7AIR" FT MOD_RES 24 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 47 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9JIS8" FT MOD_RES 51 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 81 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9UHW9" FT MOD_RES 88 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 734 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:34031912" FT MOD_RES 967 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 983 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1050 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:34031912" FT CARBOHYD 245 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 312 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:31649201, FT ECO:0007744|PDB:6KKR, ECO:0007744|PDB:6KKT, FT ECO:0007744|PDB:6KKU" FT CARBOHYD 331 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 347 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 361 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:31649201" FT DISULFID 308..323 FT /evidence="ECO:0000269|PubMed:31649201, FT ECO:0000269|PubMed:34031912, ECO:0007744|PDB:6KKR, FT ECO:0007744|PDB:6KKT, ECO:0007744|PDB:6KKU, FT ECO:0007744|PDB:7AIP, ECO:0007744|PDB:7AIQ, FT ECO:0007744|PDB:7AIR, ECO:0007744|PDB:7TTH, FT ECO:0007744|PDB:7TTI" FT DISULFID 343..353 FT /evidence="ECO:0000269|PubMed:31649201, FT ECO:0000269|PubMed:34031912, ECO:0007744|PDB:6KKR, FT ECO:0007744|PDB:6KKT, ECO:0007744|PDB:6KKU, FT ECO:0007744|PDB:7AIP, ECO:0007744|PDB:7AIQ, FT ECO:0007744|PDB:7AIR, ECO:0007744|PDB:7TTH, FT ECO:0007744|PDB:7TTI" FT VAR_SEQ 1..70 FT /note="MPHFTVVPVDGPRRGDYDNLEGLSWVDYGERAELDDSDGHGNHRESSPFLSP FT LEASRGIDYYDRNLALFE -> MRAGGACRPGAAGTAAGTAAGGWDGGCGGAEPARCLT FT SPWCQWTGRGAATMTTSRGSVGWTTGSAPSWMTRT (in isoform 7)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_046369" FT VAR_SEQ 1..38 FT /note="MPHFTVVPVDGPRRGDYDNLEGLSWVDYGERAELDDSD -> MGDTLSP FT (in isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_044596" FT VAR_SEQ 1..38 FT /note="MPHFTVVPVDGPRRGDYDNLEGLSWVDYGERAELDDSD -> MAAEGAVCGF FT VYLEGTAWAVPEDTEPLASCTL (in isoform 6)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_046146" FT VAR_SEQ 749..955 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:11551954" FT /id="VSP_006108" FT VAR_SEQ 956..958 FT /note="RHS -> PCA (in isoform 4)" FT /evidence="ECO:0000303|PubMed:11551954" FT /id="VSP_006109" FT VAR_SEQ 963..987 FT /note="ESLYSDEEDESAVGADKIQMTWTRD -> PTWPCSCPRTSPSTPATTSATWR FT AT (in isoform 4)" FT /evidence="ECO:0000303|PubMed:11551954" FT /id="VSP_006110" FT VAR_SEQ 988..1085 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:11551954" FT /id="VSP_006111" FT VAR_SEQ 1012..1085 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:9516379" FT /id="VSP_006112" FT VAR_SEQ 1056..1068 FT /note="YMEFLEVLTEGLE -> CIPLWRGRQLGGG (in isoform 2)" FT /evidence="ECO:0000303|PubMed:9516379" FT /id="VSP_006113" FT VAR_SEQ 1069..1085 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:9516379" FT /id="VSP_006114" FT CONFLICT 42 FT /note="N -> D (in Ref. 3; BAG61116)" FT /evidence="ECO:0000305" FT CONFLICT 211 FT /note="F -> L (in Ref. 3; BAG63994)" FT /evidence="ECO:0000305" FT CONFLICT 288 FT /note="I -> N (in Ref. 3; BAG63994)" FT /evidence="ECO:0000305" FT CONFLICT 370 FT /note="G -> R (in Ref. 3; BAG57330)" FT /evidence="ECO:0000305" FT CONFLICT 697 FT /note="L -> P (in Ref. 3; BAG63994)" FT /evidence="ECO:0000305" FT CONFLICT 1016 FT /note="V -> A (in Ref. 3; BAG57330)" FT /evidence="ECO:0000305" FT CONFLICT 1055 FT /note="N -> D (in Ref. 3; BAG57330)" FT /evidence="ECO:0000305" FT HELIX 120..123 FT /evidence="ECO:0007829|PDB:6KKR" FT HELIX 125..132 FT /evidence="ECO:0007829|PDB:6KKR" FT HELIX 136..139 FT /evidence="ECO:0007829|PDB:6KKR" FT HELIX 141..175 FT /evidence="ECO:0007829|PDB:6KKR" FT HELIX 186..193 FT /evidence="ECO:0007829|PDB:6KKR" FT HELIX 195..226 FT /evidence="ECO:0007829|PDB:6KKR" FT TURN 230..232 FT /evidence="ECO:0007829|PDB:7TTI" FT HELIX 233..235 FT /evidence="ECO:0007829|PDB:7TTI" FT STRAND 239..241 FT /evidence="ECO:0007829|PDB:6KKR" FT HELIX 245..268 FT /evidence="ECO:0007829|PDB:6KKR" FT HELIX 270..275 FT /evidence="ECO:0007829|PDB:6KKR" FT TURN 276..278 FT /evidence="ECO:0007829|PDB:6KKR" FT HELIX 279..300 FT /evidence="ECO:0007829|PDB:6KKR" FT STRAND 306..310 FT /evidence="ECO:0007829|PDB:6KKR" FT STRAND 313..315 FT /evidence="ECO:0007829|PDB:7AIP" FT TURN 317..319 FT /evidence="ECO:0007829|PDB:6KKR" FT STRAND 325..329 FT /evidence="ECO:0007829|PDB:6KKR" FT STRAND 332..335 FT /evidence="ECO:0007829|PDB:6KKR" FT HELIX 337..343 FT /evidence="ECO:0007829|PDB:6KKR" FT STRAND 344..346 FT /evidence="ECO:0007829|PDB:6KKR" FT STRAND 347..349 FT /evidence="ECO:0007829|PDB:7TTI" FT HELIX 355..359 FT /evidence="ECO:0007829|PDB:6KKR" FT STRAND 362..367 FT /evidence="ECO:0007829|PDB:6KKR" FT HELIX 373..378 FT /evidence="ECO:0007829|PDB:6KKR" FT STRAND 394..396 FT /evidence="ECO:0007829|PDB:6KKR" FT HELIX 405..407 FT /evidence="ECO:0007829|PDB:6KKR" FT HELIX 408..410 FT /evidence="ECO:0007829|PDB:7AIP" FT HELIX 420..427 FT /evidence="ECO:0007829|PDB:6KKR" FT HELIX 428..430 FT /evidence="ECO:0007829|PDB:6KKR" FT HELIX 435..437 FT /evidence="ECO:0007829|PDB:6KKR" FT TURN 439..443 FT /evidence="ECO:0007829|PDB:6KKR" FT HELIX 447..476 FT /evidence="ECO:0007829|PDB:6KKR" FT HELIX 479..482 FT /evidence="ECO:0007829|PDB:6KKR" FT HELIX 485..487 FT /evidence="ECO:0007829|PDB:6KKR" FT TURN 488..492 FT /evidence="ECO:0007829|PDB:6KKR" FT HELIX 497..499 FT /evidence="ECO:0007829|PDB:6KKR" FT STRAND 500..502 FT /evidence="ECO:0007829|PDB:7TTI" FT HELIX 505..535 FT /evidence="ECO:0007829|PDB:6KKR" FT TURN 536..538 FT /evidence="ECO:0007829|PDB:7TTI" FT HELIX 540..546 FT /evidence="ECO:0007829|PDB:6KKR" FT STRAND 550..552 FT /evidence="ECO:0007829|PDB:6KKR" FT HELIX 556..569 FT /evidence="ECO:0007829|PDB:6KKR" FT HELIX 574..601 FT /evidence="ECO:0007829|PDB:6KKR" FT HELIX 616..633 FT /evidence="ECO:0007829|PDB:6KKR" FT HELIX 635..651 FT /evidence="ECO:0007829|PDB:6KKR" FT STRAND 661..664 FT /evidence="ECO:0007829|PDB:7TTH" FT HELIX 665..681 FT /evidence="ECO:0007829|PDB:7AIP" FT STRAND 694..697 FT /evidence="ECO:0007829|PDB:7AIP" FT HELIX 710..719 FT /evidence="ECO:0007829|PDB:7AIP" FT STRAND 725..733 FT /evidence="ECO:0007829|PDB:7AIP" FT HELIX 735..737 FT /evidence="ECO:0007829|PDB:7AIP" FT HELIX 740..755 FT /evidence="ECO:0007829|PDB:7AIP" FT STRAND 761..769 FT /evidence="ECO:0007829|PDB:7AIP" FT HELIX 770..779 FT /evidence="ECO:0007829|PDB:7AIP" FT STRAND 790..792 FT /evidence="ECO:0007829|PDB:7AIP" FT TURN 797..801 FT /evidence="ECO:0007829|PDB:7AIP" FT HELIX 806..819 FT /evidence="ECO:0007829|PDB:7AIP" FT TURN 820..822 FT /evidence="ECO:0007829|PDB:7AIP" FT STRAND 824..830 FT /evidence="ECO:0007829|PDB:7AIP" FT HELIX 831..833 FT /evidence="ECO:0007829|PDB:7AIP" FT STRAND 845..848 FT /evidence="ECO:0007829|PDB:7AIP" FT HELIX 855..866 FT /evidence="ECO:0007829|PDB:7AIP" FT HELIX 869..871 FT /evidence="ECO:0007829|PDB:7AIP" FT STRAND 875..880 FT /evidence="ECO:0007829|PDB:7AIP" FT HELIX 888..902 FT /evidence="ECO:0007829|PDB:7AIP" FT STRAND 907..910 FT /evidence="ECO:0007829|PDB:7AIP" FT TURN 915..918 FT /evidence="ECO:0007829|PDB:7AIP" FT HELIX 919..925 FT /evidence="ECO:0007829|PDB:7AIP" FT HELIX 1015..1032 FT /evidence="ECO:0007829|PDB:7AIP" FT STRAND 1039..1042 FT /evidence="ECO:0007829|PDB:7AIP" FT TURN 1050..1052 FT /evidence="ECO:0007829|PDB:7AIP" FT HELIX 1053..1063 FT /evidence="ECO:0007829|PDB:7AIP" FT STRAND 1068..1074 FT /evidence="ECO:0007829|PDB:7AIP" FT CONFLICT Q9UP95-6:4 FT /note="E -> G (in Ref. 3; BAH14786)" FT /evidence="ECO:0000305" SQ SEQUENCE 1085 AA; 120650 MW; 42B590EC3D94EA4D CRC64; MPHFTVVPVD GPRRGDYDNL EGLSWVDYGE RAELDDSDGH GNHRESSPFL SPLEASRGID YYDRNLALFE EELDIRPKVS SLLGKLVSYT NLTQGAKEHE EAESGEGTRR RAAEAPSMGT LMGVYLPCLQ NIFGVILFLR LTWMVGTAGV LQALLIVLIC CCCTLLTAIS MSAIATNGVV PAGGSYFMIS RSLGPEFGGA VGLCFYLGTT FAAAMYILGA IEILLTYIAP PAAIFYPSGA HDTSNATLNN MRVYGTIFLT FMTLVVFVGV KYVNKFASLF LACVIISILS IYAGGIKSIF DPPVFPVCML GNRTLSRDQF DICAKTAVVD NETVATQLWS FFCHSPNLTT DSCDPYFMLN NVTEIPGIPG AAAGVLQENL WSAYLEKGDI VEKHGLPSAD APSLKESLPL YVVADIATSF TVLVGIFFPS VTGIMAGSNR SGDLRDAQKS IPVGTILAII TTSLVYFSSV VLFGACIEGV VLRDKYGDGV SRNLVVGTLA WPSPWVIVIG SFFSTCGAGL QSLTGAPRLL QAIAKDNIIP FLRVFGHGKV NGEPTWALLL TALIAELGIL IASLDMVAPI LSMFFLMCYL FVNLACAVQT LLRTPNWRPR FKYYHWALSF LGMSLCLALM FVSSWYYALV AMLIAGMIYK YIEYQGAEKE WGDGIRGLSL SAARYALLRL EEGPPHTKNW RPQLLVLLKL DEDLHVKYPR LLTFASQLKA GKGLTIVGSV IQGSFLESYG EAQAAEQTIK NMMEIEKVKG FCQVVVASKV REGLAHLIQS CGLGGMRHNS VVLGWPYGWR QSEDPRAWKT FIDTVRCTTA AHLALLVPKN IAFYPSNHER YLEGHIDVWW IVHDGGMLML LPFLLRQHKV WRKCRMRIFT VAQMDDNSIQ MKKDLAVFLY HLRLEAEVEV VEMHNSDISA YTYERTLMME QRSQMLRQMR LTKTEREREA QLVKDRHSAL RLESLYSDEE DESAVGADKI QMTWTRDKYM TETWDPSHAP DNFRELVHIK PDQSNVRRMH TAVKLNEVIV TRSHDARLVL LNMPGPPRNS EGDENYMEFL EVLTEGLERV LLVRGGGREV ITIYS //