ID KCNJ1_HUMAN Reviewed; 391 AA. AC P48048; B2RMR4; Q6LD67; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 02-SEP-2026, entry version 221. DE RecName: Full=ATP-sensitive inward rectifier potassium channel 1; DE AltName: Full=ATP-regulated potassium channel ROM-K; DE AltName: Full=Inward rectifier K(+) channel Kir1.1; DE AltName: Full=Potassium channel, inwardly rectifying subfamily J member 1; GN Name=KCNJ1; Synonyms=ROMK1; 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], FUNCTION, ALTERNATIVE SPLICING, AND TRANSPORTER RP ACTIVITY. RC TISSUE=Kidney; RX PubMed=7929082; DOI=10.1016/s0021-9258(19)51076-6; RA Shuck M.E., Bock J.H., Benjamin C.W., Tsai T.-D., Lee K.S., Slightom J.L., RA Bienkowski M.J.; RT "Cloning and characterization of multiple forms of the human kidney ROM-K RT potassium channel."; RL J. Biol. Chem. 269:24261-24270(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING. RC TISSUE=Kidney; RX PubMed=8190102; DOI=10.1016/s0026-895x(25)10199-5; RA Yano H., Philipson L.H., Kugler J.L., Tokuyama Y., Davis E.M., RA le Beau M.M., Nelson D.J., Bell G.I., Takeda J.; RT "Alternative splicing of human inwardly rectifying K+ channel ROMK1 mRNA."; RL Mol. Pharmacol. 45:854-860(1994). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING. RX PubMed=9099852; DOI=10.1016/s0378-1119(96)00759-7; RA Bock J.H., Shuck M.E., Benjamin C.W., Chee M., Bienkowski M.J., RA Slightom J.L.; RT "Nucleotide sequence analysis of the human KCNJ1 potassium channel locus."; RL Gene 188:9-16(1997). 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] (ISOFORM 1). 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 76-177, AND TISSUE SPECIFICITY. RC TISSUE=Brain cortex; RX PubMed=7635463; DOI=10.1007/bf00207372; RA Krishnan S.N., Desai T., Ward D.C., Haddad G.G.; RT "Isolation and chromosomal localization of a human ATP-regulated potassium RT channel."; RL Hum. Genet. 96:155-160(1995). RN [7] RP GLYCOSYLATION AT ASN-117. RX PubMed=10889209; DOI=10.1074/jbc.m005338200; RA Pabon A., Chan K.W., Sui J.L., Wu X., Logothetis D.E., Thornhill W.B.; RT "Glycosylation of GIRK1 at Asn119 and ROMK1 at Asn117 has different RT consequences in potassium channel function."; RL J. Biol. Chem. 275:30677-30682(2000). RN [8] RP INTERACTION WITH SGK1 AND SLC9A3R2/NHERF2. RX PubMed=14623317; DOI=10.1016/j.bbrc.2003.10.037; RA Palmada M., Embark H.M., Yun C., Bohmer C., Lang F.; RT "Molecular requirements for the regulation of the renal outer medullary RT K(+) channel ROMK1 by the serum- and glucocorticoid-inducible kinase RT SGK1."; RL Biochem. Biophys. Res. Commun. 311:629-634(2003). RN [9] RP PHOSPHORYLATION AT SER-44 BY SGK1, AND SUBCELLULAR LOCATION. RX PubMed=12684516; DOI=10.1074/jbc.m212301200; RA Yoo D., Kim B.Y., Campo C., Nance L., King A., Maouyo D., Welling P.A.; RT "Cell surface expression of the ROMK (Kir 1.1) channel is regulated by the RT aldosterone-induced kinase, SGK-1, and protein kinase A."; RL J. Biol. Chem. 278:23066-23075(2003). RN [10] RP ACTIVITY REGULATION, FUNCTION, TRANSPORTER ACTIVITY, AND SUBCELLULAR RP LOCATION. RX PubMed=16357011; DOI=10.1113/jphysiol.2005.102202; RA Leng Q., Kahle K.T., Rinehart J., MacGregor G.G., Wilson F.H., RA Canessa C.M., Lifton R.P., Hebert S.C.; RT "WNK3, a kinase related to genes mutated in hereditary hypertension with RT hyperkalaemia, regulates the K+ channel ROMK1 (Kir1.1)."; RL J. Physiol. (Lond.) 571:275-286(2006). RN [11] RP VARIANTS BARTS2 VAL-214; ARG-219 AND THR-357. RX PubMed=8841184; DOI=10.1038/ng1096-152; RA Simon D.B., Karet F.E., Rodriguez-Soriano J., Hamdan J.H., DiPietro A., RA Trachtman H., Sanjad S.A., Lifton R.P.; RT "Genetic heterogeneity of Bartter's syndrome revealed by mutations in the RT K+ channel, ROMK."; RL Nat. Genet. 14:152-156(1996). RN [12] RP VARIANTS BARTS2 GLU-72; TYR-74; CYS-99; HIS-108; LEU-110; GLU-122; GLU-167; RP THR-198 AND GLY-315. RX PubMed=9002665; DOI=10.1093/hmg/6.1.17; RA Karolyi L., Konrad M., Koeckerling A., Ziegler A., Zimmermann D.K., RA Roth B., Wieg C., Grzeschik K.-H., Koch M.C., Seyberth H.W., Vargas R., RA Forestier L., Jean G., Deschaux M., Rizzoni G.F., Niaudet P., Antignac C., RA Feldmann D., Lorridon F., Cougoureux E., Laroze F., Alessandri J.-L., RA David L., Saunier P., Deschenes G., Hildebrandt F., Vollmer M., RA Proesmans W., Brandis M., van den Heuvel L.P.W.J., Lemmink H.H., RA Nillesen W., Monnens L.A.H., Knoers N.V.A.M., Guay-Woodford L.M., RA Wright C.J., Madrigal G., Hebert S.C.; RT "Mutations in the gene encoding the inwardly-rectifying renal potassium RT channel, ROMK, cause the antenatal variant of Bartter syndrome: evidence RT for genetic heterogeneity."; RL Hum. Mol. Genet. 6:17-26(1997). RN [13] RP VARIANT BARTS2 LYS-124. RX PubMed=9727001; DOI=10.1074/jbc.273.37.23884; RA Derst C., Wischmeyer E., Preisig-Mueller R., Spauschus A., Konrad M., RA Hensen P., Jeck N., Seyberth H.W., Daut J., Karschin A.; RT "A hyperprostaglandin E syndrome mutation in Kir1.1 (renal outer medullary RT potassium) channels reveals a crucial residue for channel function in RT Kir1.3 channels."; RL J. Biol. Chem. 273:23884-23891(1998). RN [14] RP VARIANT [LARGE SCALE ANALYSIS] PHE-115. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: Inward rectifier potassium channels are characterized by a CC greater tendency to allow potassium to flow into the cell rather than CC out of it. Their voltage dependence is regulated by the concentration CC of extracellular potassium; as external potassium is raised, the CC voltage range of the channel opening shifts to more positive voltages. CC The inward rectification is mainly due to the blockage of outward CC current by internal magnesium. This channel is activated by internal CC ATP and can be blocked by external barium. In the kidney, probably CC plays a major role in potassium homeostasis. CC {ECO:0000269|PubMed:16357011, ECO:0000269|PubMed:7929082}. CC -!- CATALYTIC ACTIVITY: CC Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103; CC Evidence={ECO:0000269|PubMed:16357011, ECO:0000269|PubMed:7929082}; CC -!- ACTIVITY REGULATION: Inhibited by WNK3 (PubMed:16357011). Activated by CC phosphatidylinositol 4,5 biphosphate (PtdIns(4,5)P2) (By similarity). CC {ECO:0000250|UniProtKB:P35560, ECO:0000269|PubMed:16357011}. CC -!- SUBUNIT: Interacts with SGK1 and SLC9A3R2/NHERF2. CC {ECO:0000269|PubMed:14623317}. CC -!- INTERACTION: CC P48048; Q02410: APBA1; NbExp=2; IntAct=EBI-66916851, EBI-368690; CC P48048; Q99767: APBA2; NbExp=2; IntAct=EBI-66916851, EBI-81711; CC P48048; Q12959: DLG1; NbExp=3; IntAct=EBI-66916851, EBI-357481; CC P48048; Q15700: DLG2; NbExp=2; IntAct=EBI-66916851, EBI-80426; CC P48048; Q92796: DLG3; NbExp=2; IntAct=EBI-66916851, EBI-80440; CC P48048; P78352: DLG4; NbExp=2; IntAct=EBI-66916851, EBI-80389; CC P48048; Q68DX3: FRMPD2; NbExp=3; IntAct=EBI-66916851, EBI-53993476; CC P48048; A4D2P6: GRID2IP; NbExp=2; IntAct=EBI-66916851, EBI-15893226; CC P48048; Q9Y3R0: GRIP1; NbExp=5; IntAct=EBI-66916851, EBI-5349621; CC P48048; Q9C0E4: GRIP2; NbExp=3; IntAct=EBI-66916851, EBI-949557; CC P48048; Q14005: IL16; NbExp=2; IntAct=EBI-66916851, EBI-2831580; CC P48048; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-66916851, EBI-739832; CC P48048; Q8N448: LNX2; NbExp=2; IntAct=EBI-66916851, EBI-2340947; CC P48048; Q96QZ7: MAGI1; NbExp=2; IntAct=EBI-66916851, EBI-924464; CC P48048; Q86UL8: MAGI2; NbExp=2; IntAct=EBI-66916851, EBI-311035; CC P48048; O75970: MPDZ; NbExp=3; IntAct=EBI-66916851, EBI-821405; CC P48048; Q86UT5: NHERF4; NbExp=2; IntAct=EBI-66916851, EBI-8744528; CC P48048; Q8NI35: PATJ; NbExp=6; IntAct=EBI-66916851, EBI-724390; CC P48048; Q5T2W1: PDZK1; NbExp=2; IntAct=EBI-66916851, EBI-349819; CC P48048; Q07157: TJP1; NbExp=2; IntAct=EBI-66916851, EBI-79553; CC P48048; Q9P202: WHRN; NbExp=2; IntAct=EBI-66916851, EBI-310886; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12684516, CC ECO:0000269|PubMed:16357011}; Multi-pass membrane protein CC {ECO:0000255}. Note=Phosphorylation at Ser-44 by SGK1 is necessary for CC its expression at the cell membrane. {ECO:0000269|PubMed:12684516}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; Synonyms=ROM-K1; CC IsoId=P48048-1; Sequence=Displayed; CC Name=2; Synonyms=2-4-5, ROM-K2, ROM-K4, ROM-K5, ROM-K6; CC IsoId=P48048-2; Sequence=VSP_002797; CC Name=3; Synonyms=ROM-K3; CC IsoId=P48048-3; Sequence=VSP_002798; CC -!- TISSUE SPECIFICITY: In the kidney and pancreatic islets. Lower levels CC in skeletal muscle, pancreas, spleen, brain, heart and liver. CC {ECO:0000269|PubMed:7635463}. CC -!- PTM: Phosphorylation at Ser-44 by SGK1 is necessary for its expression CC at the cell membrane. {ECO:0000269|PubMed:12684516}. CC -!- DISEASE: Bartter syndrome 2, antenatal (BARTS2) [MIM:241200]: A form of CC Bartter syndrome, an autosomal recessive disorder characterized by CC impaired salt reabsorption in the thick ascending loop of Henle with CC pronounced salt wasting, hypokalemic metabolic alkalosis, and varying CC degrees of hypercalciuria. BARTS2 is a life-threatening condition CC beginning in utero, with marked fetal polyuria that leads to CC polyhydramnios and premature delivery. Another hallmark is a marked CC hypercalciuria and, as a secondary consequence, the development of CC nephrocalcinosis and osteopenia. {ECO:0000269|PubMed:8841184, CC ECO:0000269|PubMed:9002665, ECO:0000269|PubMed:9727001}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the inward rectifier-type potassium channel CC (TC 1.A.2.1) family. KCNJ1 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; U12541; AAA61712.1; -; mRNA. DR EMBL; U12542; AAA61713.1; -; mRNA. DR EMBL; U12543; AAA61714.1; -; mRNA. DR EMBL; U12544; AAA61715.1; -; mRNA. DR EMBL; U12545; AAA61716.1; -; mRNA. DR EMBL; U03884; AAA20594.1; -; mRNA. DR EMBL; U65406; AAC51220.1; -; Genomic_DNA. DR EMBL; U65406; AAC51221.1; -; Genomic_DNA. DR EMBL; U65406; AAC51222.1; -; Genomic_DNA. DR EMBL; CH471065; EAW67724.1; -; Genomic_DNA. DR EMBL; BC074752; AAH74752.1; -; mRNA. DR EMBL; BC136360; AAI36361.1; -; mRNA. DR EMBL; BC136361; AAI36362.1; -; mRNA. DR EMBL; S78737; AAB35012.1; -; mRNA. DR CCDS; CCDS8476.1; -. [P48048-1] DR CCDS; CCDS8477.1; -. [P48048-2] DR PIR; A55119; A55119. DR RefSeq; NP_000211.1; NM_000220.6. [P48048-1] DR RefSeq; NP_722448.1; NM_153764.3. [P48048-2] DR RefSeq; NP_722449.3; NM_153765.3. [P48048-3] DR RefSeq; NP_722450.1; NM_153766.3. [P48048-2] DR RefSeq; NP_722451.1; NM_153767.4. [P48048-2] DR AlphaFoldDB; P48048; -. DR SMR; P48048; -. DR BioGRID; 109960; 4. DR ELM; P48048; -. DR FunCoup; P48048; 150. DR IntAct; P48048; 74. DR STRING; 9606.ENSP00000376432; -. DR BindingDB; P48048; -. DR ChEMBL; CHEMBL1293292; -. DR DrugBank; DB00414; Acetohexamide. DR DrugBank; DB08838; Agmatine. DR DrugBank; DB00217; Bethanidine. DR DrugBank; DB11148; Butamben. DR DrugBank; DB00222; Glimepiride. DR DrugBank; DB01382; Glymidine. DR DrugBank; DB00350; Minoxidil. DR DrugBank; DB00867; Ritodrine. DR DrugBank; DB01124; Tolbutamide. DR DrugBank; DB01392; Yohimbine. DR DrugCentral; P48048; -. DR GuidetoPHARMACOLOGY; 429; -. DR TCDB; 1.A.2.1.1; the inward rectifier k(+) channel (irk-c) family. DR CarbonylDB; P48048; -. DR GlyCosmos; P48048; 1 site, No reported glycans. DR GlyGen; P48048; 2 sites. DR iPTMnet; P48048; -. DR PhosphoSitePlus; P48048; -. DR BioMuta; KCNJ1; -. DR DMDM; 1352479; -. DR jPOST; P48048; -. DR MassIVE; P48048; -. DR PaxDb; 9606-ENSP00000376432; -. DR PeptideAtlas; P48048; -. DR ProteomicsDB; 55838; -. [P48048-1] DR ProteomicsDB; 55839; -. [P48048-2] DR ProteomicsDB; 55840; -. [P48048-3] DR Antibodypedia; 33020; 287 antibodies from 32 providers. DR DNASU; 3758; -. DR Ensembl; ENST00000324036.7; ENSP00000316233.3; ENSG00000151704.17. [P48048-2] DR Ensembl; ENST00000392664.2; ENSP00000376432.2; ENSG00000151704.17. [P48048-1] DR Ensembl; ENST00000392665.6; ENSP00000376433.2; ENSG00000151704.17. [P48048-2] DR Ensembl; ENST00000392666.6; ENSP00000376434.1; ENSG00000151704.17. [P48048-2] DR Ensembl; ENST00000440599.6; ENSP00000406320.2; ENSG00000151704.17. [P48048-2] DR Ensembl; ENST00000857610.1; ENSP00000527669.1; ENSG00000151704.17. [P48048-2] DR Ensembl; ENST00000857611.1; ENSP00000527670.1; ENSG00000151704.17. [P48048-2] DR Ensembl; ENST00000857612.1; ENSP00000527671.1; ENSG00000151704.17. [P48048-2] DR Ensembl; ENST00000857613.1; ENSP00000527672.1; ENSG00000151704.17. [P48048-2] DR Ensembl; ENST00000857614.1; ENSP00000527673.1; ENSG00000151704.17. [P48048-2] DR Ensembl; ENST00000857615.1; ENSP00000527674.1; ENSG00000151704.17. [P48048-2] DR Ensembl; ENST00000923294.1; ENSP00000593353.1; ENSG00000151704.17. [P48048-2] DR Ensembl; ENST00000923295.1; ENSP00000593354.1; ENSG00000151704.17. [P48048-2] DR Ensembl; ENST00000923296.1; ENSP00000593355.1; ENSG00000151704.17. [P48048-2] DR GeneID; 3758; -. DR KEGG; hsa:3758; -. DR MANE-Select; ENST00000392666.6; ENSP00000376434.1; NM_153766.3; NP_722450.1. [P48048-2] DR UCSC; uc001qeo.3; human. [P48048-1] DR AGR; HGNC:6255; -. DR ClinPGx; PA213; -. DR CTD; 3758; -. DR DisGeNET; 3758; -. DR GeneCards; KCNJ1; -. DR HGNC; HGNC:6255; KCNJ1. DR HPA; ENSG00000151704; Tissue enriched (kidney). DR MalaCards; KCNJ1; -. DR MIM; 241200; phenotype. DR MIM; 600359; gene. DR OpenTargets; ENSG00000151704; -. DR Orphanet; 620220; Bartter syndrome type 2. DR VEuPathDB; HostDB:ENSG00000151704; -. DR eggNOG; KOG3827; Eukaryota. DR GeneTree; ENSGT01140000282491; -. DR HOGENOM; CLU_022738_3_0_1; -. DR InParanoid; P48048; -. DR PAN-GO; P48048; 2 GO annotations based on evolutionary models. DR PhylomeDB; P48048; -. DR PathwayCommons; P48048; -. DR Reactome; R-HSA-1296067; Potassium transport channels. DR SignaLink; P48048; -. DR SIGNOR; P48048; -. DR Agora; ENSG00000151704; -. DR BioGRID-ORCS; 3758; 13 hits in 1161 CRISPR screens. DR GeneWiki; ROMK; -. DR GenomeRNAi; 3758; -. DR Pharos; P48048; Tchem. DR PRO; PR:P48048; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; P48048; protein. DR Bgee; ENSG00000151704; Expressed in renal medulla and 94 other cell types or tissues. DR GO; GO:0009986; C:cell surface; IDA:MGI. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; ISS:ARUK-UCL. DR GO; GO:0005242; F:inward rectifier potassium channel activity; IDA:UniProtKB. DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:BHF-UCL. DR GO; GO:0005267; F:potassium channel activity; IDA:UniProtKB. DR GO; GO:0010467; P:gene expression; IDA:MGI. DR GO; GO:0006811; P:monoatomic ion transport; IDA:MGI. DR GO; GO:1990573; P:potassium ion import across plasma membrane; ISS:UniProtKB. DR GO; GO:0034765; P:regulation of monoatomic ion transmembrane transport; IEA:InterPro. DR FunFam; 1.10.287.70:FF:000036; ATP-sensitive inward rectifier potassium channel 1; 1. DR FunFam; 2.60.40.1400:FF:000002; ATP-sensitive inward rectifier potassium channel 1; 1. DR Gene3D; 1.10.287.70; -; 1. DR Gene3D; 2.60.40.1400; G protein-activated inward rectifier potassium channel 1; 1. DR InterPro; IPR014756; Ig_E-set. DR InterPro; IPR041647; IRK_C. DR InterPro; IPR016449; K_chnl_inward-rec_Kir. DR InterPro; IPR003268; K_chnl_inward-rec_Kir1.1. DR InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto. DR InterPro; IPR040445; Kir_TM. DR PANTHER; PTHR11767:SF6; ATP-SENSITIVE INWARD RECTIFIER POTASSIUM CHANNEL 1; 1. DR PANTHER; PTHR11767; INWARD RECTIFIER POTASSIUM CHANNEL; 1. DR Pfam; PF01007; IRK; 1. DR Pfam; PF17655; IRK_C; 1. DR PIRSF; PIRSF005465; GIRK_kir; 1. DR PRINTS; PR01321; KIR11CHANNEL. DR PRINTS; PR01320; KIRCHANNEL. DR SUPFAM; SSF81296; E set domains; 1. DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1. PE 1: Evidence at protein level; KW Alternative splicing; ATP-binding; Bartter syndrome; Cell membrane; KW Disease variant; Glycoprotein; Ion channel; Ion transport; Membrane; KW Nucleotide-binding; Phosphoprotein; Potassium; Potassium transport; KW Proteomics identification; Reference proteome; Transmembrane; KW Transmembrane helix; Transport; Voltage-gated channel. FT CHAIN 1..391 FT /note="ATP-sensitive inward rectifier potassium channel 1" FT /id="PRO_0000154917" FT TOPO_DOM 1..77 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:O00180" FT TRANSMEM 78..102 FT /note="Helical; Name=M1" FT /evidence="ECO:0000250" FT TOPO_DOM 103..127 FT /note="Extracellular" FT /evidence="ECO:0000250|UniProtKB:O00180" FT INTRAMEM 128..139 FT /note="Helical; Pore-forming; Name=H5" FT /evidence="ECO:0000250" FT INTRAMEM 140..146 FT /note="Pore-forming" FT /evidence="ECO:0000250" FT TOPO_DOM 147..155 FT /note="Extracellular" FT /evidence="ECO:0000250|UniProtKB:O00180" FT TRANSMEM 156..177 FT /note="Helical; Name=M2" FT /evidence="ECO:0000250" FT TOPO_DOM 178..391 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:O00180" FT REGION 180..207 FT /note="Polyphosphoinositide (PIP2)-binding" FT /evidence="ECO:0000250|UniProtKB:P35560" FT MOTIF 141..146 FT /note="Selectivity filter" FT /evidence="ECO:0000250|UniProtKB:Q63472" FT BINDING 223..230 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255" FT SITE 171 FT /note="Role in the control of polyamine-mediated channel FT gating and in the blocking by intracellular magnesium" FT /evidence="ECO:0000250" FT MOD_RES 44 FT /note="Phosphoserine; by SGK1" FT /evidence="ECO:0000269|PubMed:12684516" FT CARBOHYD 117 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:10889209" FT VAR_SEQ 1..19 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_002797" FT VAR_SEQ 1..12 FT /note="MNASSRNVFDTL -> MPTVYLCSEQ (in isoform 3)" FT /evidence="ECO:0000305" FT /id="VSP_002798" FT VARIANT 6 FT /note="R -> W (in dbSNP:rs34191956)" FT /id="VAR_049668" FT VARIANT 72 FT /note="V -> E (in BARTS2)" FT /evidence="ECO:0000269|PubMed:9002665" FT /id="VAR_001548" FT VARIANT 74 FT /note="D -> Y (in BARTS2)" FT /evidence="ECO:0000269|PubMed:9002665" FT /id="VAR_001549" FT VARIANT 99 FT /note="W -> C (in BARTS2; dbSNP:rs1213764655)" FT /evidence="ECO:0000269|PubMed:9002665" FT /id="VAR_001550" FT VARIANT 108 FT /note="D -> H (in BARTS2; dbSNP:rs104894250)" FT /evidence="ECO:0000269|PubMed:9002665" FT /id="VAR_001551" FT VARIANT 110 FT /note="P -> L (in BARTS2; dbSNP:rs373745258)" FT /evidence="ECO:0000269|PubMed:9002665" FT /id="VAR_001552" FT VARIANT 115 FT /note="S -> F (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036426" FT VARIANT 122 FT /note="V -> E (in BARTS2; dbSNP:rs766131330)" FT /evidence="ECO:0000269|PubMed:9002665" FT /id="VAR_001553" FT VARIANT 124 FT /note="N -> K (in BARTS2; dbSNP:rs104894251)" FT /evidence="ECO:0000269|PubMed:9727001" FT /id="VAR_019724" FT VARIANT 167 FT /note="G -> E (in BARTS2; dbSNP:rs104894254)" FT /evidence="ECO:0000269|PubMed:9002665" FT /id="VAR_001554" FT VARIANT 198 FT /note="A -> T (in BARTS2; dbSNP:rs104894253)" FT /evidence="ECO:0000269|PubMed:9002665" FT /id="VAR_001555" FT VARIANT 214 FT /note="A -> V (in BARTS2; dbSNP:rs104894246)" FT /evidence="ECO:0000269|PubMed:8841184" FT /id="VAR_019725" FT VARIANT 219 FT /note="S -> R (in BARTS2; dbSNP:rs104894245)" FT /evidence="ECO:0000269|PubMed:8841184" FT /id="VAR_019726" FT VARIANT 315 FT /note="V -> G (in BARTS2; dbSNP:rs753949204)" FT /evidence="ECO:0000269|PubMed:9002665" FT /id="VAR_001556" FT VARIANT 357 FT /note="M -> T (in BARTS2; dbSNP:rs59172778)" FT /evidence="ECO:0000269|PubMed:8841184" FT /id="VAR_019727" SQ SEQUENCE 391 AA; 44795 MW; DF01C89B16BE6205 CRC64; MNASSRNVFD TLIRVLTESM FKHLRKWVVT RFFGHSRQRA RLVSKDGRCN IEFGNVEAQS RFIFFVDIWT TVLDLKWRYK MTIFITAFLG SWFFFGLLWY AVAYIHKDLP EFHPSANHTP CVENINGLTS AFLFSLETQV TIGYGFRCVT EQCATAIFLL IFQSILGVII NSFMCGAILA KISRPKKRAK TITFSKNAVI SKRGGKLCLL IRVANLRKSL LIGSHIYGKL LKTTVTPEGE TIILDQININ FVVDAGNENL FFISPLTIYH VIDHNSPFFH MAAETLLQQD FELVVFLDGT VESTSATCQV RTSYVPEEVL WGYRFAPIVS KTKEGKYRVD FHNFSKTVEV ETPHCAMCLY NEKDVRARMK RGYDNPNFIL SEVNETDDTK M //