ID   KCJ15_HUMAN             Reviewed;         375 AA.
AC   Q99712; D3DSH5; O00564; Q96L28; Q99446;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 2.
DT   24-JAN-2024, entry version 192.
DE   RecName: Full=ATP-sensitive inward rectifier potassium channel 15;
DE   AltName: Full=Inward rectifier K(+) channel Kir1.3;
DE   AltName: Full=Inward rectifier K(+) channel Kir4.2;
DE   AltName: Full=Potassium channel, inwardly rectifying subfamily J member 15;
GN   Name=KCNJ15; Synonyms=KCNJ14;
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].
RX   PubMed=9299242; DOI=10.1006/geno.1997.4865;
RA   Gosset P., Ghezala G.A., Korn B., Yaspo M.-L., Poutska A., Lehrach H.,
RA   Sinet P.-M., Creau N.;
RT   "A new inward rectifier potassium channel gene (KCNJ15) localized on
RT   chromosome 21 in the Down syndrome chromosome region 1 (DCR1).";
RL   Genomics 44:237-241(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ASP-98.
RC   TISSUE=Kidney;
RX   PubMed=8995301; DOI=10.1074/jbc.272.1.586;
RA   Shuck M.E., Piser T.M., Bock J.H., Slightom J.L., Lee K.S.,
RA   Bienkowski M.J.;
RT   "Cloning and characterization of two K+ inward rectifier (Kir) 1.1
RT   potassium channel homologs from human kidney (Kir1.2 and Kir1.3).";
RL   J. Biol. Chem. 272:586-593(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ASP-98.
RC   TISSUE=Kidney;
RA   Ohira M., Seki N., Nagase T., Suzuki E., Nomura N., Ohara O., Hattori M.,
RA   Sakaki Y., Eki T., Murakami Y., Saito T., Ichikawa H., Ohki M.;
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10830953; DOI=10.1038/35012518;
RA   Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S.,
RA   Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M.,
RA   Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U.,
RA   Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A.,
RA   Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J.,
RA   Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K.,
RA   Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G.,
RA   Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J.,
RA   Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S.,
RA   Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K.,
RA   Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.;
RT   "The DNA sequence of human chromosome 21.";
RL   Nature 405:311-319(2000).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
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   [7]
RP   INTERACTION WITH PATJ.
RX   PubMed=9647694; DOI=10.1006/mcne.1998.0679;
RA   Kurschner C., Mermelstein P.G., Holden W.T., Surmeier D.J.;
RT   "CIPP, a novel multivalent PDZ domain protein, selectively interacts with
RT   Kir4.0 family members, NMDA receptor subunits, neurexins, and
RT   neuroligins.";
RL   Mol. Cell. Neurosci. 11:161-172(1998).
RN   [8]
RP   VARIANT [LARGE SCALE ANALYSIS] THR-71.
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.
CC   -!- SUBUNIT: Interacts with PATJ. {ECO:0000269|PubMed:9647694}.
CC   -!- INTERACTION:
CC       Q99712; P63252: KCNJ2; NbExp=3; IntAct=EBI-7082607, EBI-703457;
CC       Q99712; P48544: KCNJ5; NbExp=3; IntAct=EBI-7082607, EBI-9975563;
CC       Q99712; Q63ZW7: Patj; Xeno; NbExp=4; IntAct=EBI-7082607, EBI-8366894;
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the inward rectifier-type potassium channel
CC       (TC 1.A.2.1) family. KCNJ15 subfamily. {ECO:0000305}.
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DR   EMBL; Y10745; CAA71734.1; -; mRNA.
DR   EMBL; U73191; AAC50922.1; -; mRNA.
DR   EMBL; D87291; BAA13326.1; -; mRNA.
DR   EMBL; AP001434; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471079; EAX09683.1; -; Genomic_DNA.
DR   EMBL; CH471079; EAX09684.1; -; Genomic_DNA.
DR   EMBL; BC013327; AAH13327.1; -; mRNA.
DR   CCDS; CCDS13656.1; -.
DR   RefSeq; NP_001263364.1; NM_001276435.1.
DR   RefSeq; NP_001263365.1; NM_001276436.1.
DR   RefSeq; NP_001263366.1; NM_001276437.1.
DR   RefSeq; NP_001263367.1; NM_001276438.1.
DR   RefSeq; NP_001263368.1; NM_001276439.1.
DR   RefSeq; NP_002234.2; NM_002243.4.
DR   RefSeq; NP_733932.1; NM_170736.2.
DR   RefSeq; NP_733933.1; NM_170737.2.
DR   RefSeq; XP_005261032.1; XM_005260975.2.
DR   RefSeq; XP_006724065.1; XM_006724002.2.
DR   RefSeq; XP_011527862.1; XM_011529560.2.
DR   RefSeq; XP_011527863.1; XM_011529561.2.
DR   RefSeq; XP_016883832.1; XM_017028343.1.
DR   RefSeq; XP_016883833.1; XM_017028344.1.
DR   RefSeq; XP_016883834.1; XM_017028345.1.
DR   AlphaFoldDB; Q99712; -.
DR   SMR; Q99712; -.
DR   BioGRID; 109974; 5.
DR   IntAct; Q99712; 4.
DR   MINT; Q99712; -.
DR   STRING; 9606.ENSP00000381911; -.
DR   DrugBank; DB11148; Butamben.
DR   DrugBank; DB00867; Ritodrine.
DR   DrugBank; DB01392; Yohimbine.
DR   iPTMnet; Q99712; -.
DR   PhosphoSitePlus; Q99712; -.
DR   BioMuta; KCNJ15; -.
DR   DMDM; 77416869; -.
DR   MassIVE; Q99712; -.
DR   PaxDb; 9606-ENSP00000331698; -.
DR   PeptideAtlas; Q99712; -.
DR   ProteomicsDB; 78426; -.
DR   Antibodypedia; 3029; 211 antibodies from 29 providers.
DR   DNASU; 3772; -.
DR   Ensembl; ENST00000328656.8; ENSP00000331698.3; ENSG00000157551.19.
DR   Ensembl; ENST00000398930.5; ENSP00000381904.1; ENSG00000157551.19.
DR   Ensembl; ENST00000398932.5; ENSP00000381905.1; ENSG00000157551.19.
DR   Ensembl; ENST00000398934.5; ENSP00000381907.1; ENSG00000157551.19.
DR   Ensembl; ENST00000398938.7; ENSP00000381911.2; ENSG00000157551.19.
DR   Ensembl; ENST00000612702.4; ENSP00000484960.1; ENSG00000157551.19.
DR   Ensembl; ENST00000613499.4; ENSP00000479100.1; ENSG00000157551.19.
DR   GeneID; 3772; -.
DR   KEGG; hsa:3772; -.
DR   MANE-Select; ENST00000398938.7; ENSP00000381911.2; NM_170736.3; NP_733932.1.
DR   UCSC; uc002ywv.5; human.
DR   AGR; HGNC:6261; -.
DR   CTD; 3772; -.
DR   DisGeNET; 3772; -.
DR   GeneCards; KCNJ15; -.
DR   HGNC; HGNC:6261; KCNJ15.
DR   HPA; ENSG00000157551; Tissue enhanced (kidney, thyroid gland).
DR   MIM; 602106; gene.
DR   neXtProt; NX_Q99712; -.
DR   OpenTargets; ENSG00000157551; -.
DR   PharmGKB; PA30046; -.
DR   VEuPathDB; HostDB:ENSG00000157551; -.
DR   eggNOG; KOG3827; Eukaryota.
DR   GeneTree; ENSGT00990000203615; -.
DR   HOGENOM; CLU_022738_3_3_1; -.
DR   InParanoid; Q99712; -.
DR   OMA; LPMHRST; -.
DR   OrthoDB; 4126787at2759; -.
DR   PhylomeDB; Q99712; -.
DR   TreeFam; TF313676; -.
DR   PathwayCommons; Q99712; -.
DR   Reactome; R-HSA-1296041; Activation of G protein gated Potassium channels.
DR   Reactome; R-HSA-997272; Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
DR   SignaLink; Q99712; -.
DR   BioGRID-ORCS; 3772; 17 hits in 1151 CRISPR screens.
DR   ChiTaRS; KCNJ15; human.
DR   GeneWiki; KCNJ15; -.
DR   GenomeRNAi; 3772; -.
DR   Pharos; Q99712; Tbio.
DR   PRO; PR:Q99712; -.
DR   Proteomes; UP000005640; Chromosome 21.
DR   RNAct; Q99712; Protein.
DR   Bgee; ENSG00000157551; Expressed in nephron tubule and 161 other cell types or tissues.
DR   ExpressionAtlas; Q99712; baseline and differential.
DR   GO; GO:0034702; C:monoatomic ion channel complex; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005242; F:inward rectifier potassium channel activity; IBA:GO_Central.
DR   GO; GO:1990573; P:potassium ion import across plasma membrane; IBA:GO_Central.
DR   GO; GO:0006813; P:potassium ion transport; TAS:ProtInc.
DR   GO; GO:0034765; P:regulation of monoatomic ion transmembrane transport; IBA:GO_Central.
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; IPR003270; K_chnl_inward-rec_Kir1.3.
DR   InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR   InterPro; IPR040445; Kir_TM.
DR   PANTHER; PTHR11767:SF20; ATP-SENSITIVE INWARD RECTIFIER POTASSIUM CHANNEL 15; 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; PR01323; KIR13CHANNEL.
DR   PRINTS; PR01320; KIRCHANNEL.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
DR   Genevisible; Q99712; HS.
PE   1: Evidence at protein level;
KW   Ion channel; Ion transport; Membrane; Potassium; Potassium transport;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport;
KW   Voltage-gated channel.
FT   CHAIN           1..375
FT                   /note="ATP-sensitive inward rectifier potassium channel 15"
FT                   /id="PRO_0000154972"
FT   TOPO_DOM        1..63
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        64..88
FT                   /note="Helical; Name=M1"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        89..113
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   INTRAMEM        114..125
FT                   /note="Helical; Pore-forming; Name=H5"
FT                   /evidence="ECO:0000250"
FT   INTRAMEM        126..132
FT                   /note="Pore-forming"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        133..141
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        142..163
FT                   /note="Helical; Name=M2"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        164..375
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   MOTIF           127..132
FT                   /note="Selectivity filter"
FT                   /evidence="ECO:0000250"
FT   SITE            157
FT                   /note="Role in the control of polyamine-mediated channel
FT                   gating and in the blocking by intracellular magnesium"
FT                   /evidence="ECO:0000250"
FT   VARIANT         30
FT                   /note="M -> L (in dbSNP:rs3746875)"
FT                   /id="VAR_025523"
FT   VARIANT         71
FT                   /note="A -> T (in a breast cancer sample; somatic mutation;
FT                   dbSNP:rs199857043)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036427"
FT   VARIANT         98
FT                   /note="G -> D (in dbSNP:rs2230033)"
FT                   /evidence="ECO:0000269|PubMed:8995301, ECO:0000269|Ref.3"
FT                   /id="VAR_019728"
FT   CONFLICT        235
FT                   /note="V -> A (in Ref. 1; CAA71734)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        245
FT                   /note="S -> G (in Ref. 3; BAA13326)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   375 AA;  42577 MW;  CECCB4EDF827B24D CRC64;
     MDAIHIGMSS TPLVKHTAGA GLKANRPRVM SKSGHSNVRI DKVDGIYLLY LQDLWTTVID
     MKWRYKLTLF AATFVMTWFL FGVIYYAIAF IHGDLEPGEP ISNHTPCIMK VDSLTGAFLF
     SLESQTTIGY GVRSITEECP HAIFLLVAQL VITTLIEIFI TGTFLAKIAR PKKRAETIKF
     SHCAVITKQN GKLCLVIQVA NMRKSLLIQC QLSGKLLQTH VTKEGERILL NQATVKFHVD
     SSSESPFLIL PMTFYHVLDE TSPLRDLTPQ NLKEKEFELV VLLNATVEST SAVCQSRTSY
     IPEEIYWGFE FVPVVSLSKN GKYVADFSQF EQIRKSPDCT FYCADSEKQQ LEEKYRQEDQ
     RERELRTLLL QQSNV
//