KCJ15_HUMAN
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 03-AUG-2022, entry version 184.
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 (TC
CC 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.ENSP00000331698; -.
DR DrugBank; DB11148; Butamben.
DR DrugBank; DB01392; Yohimbine.
DR iPTMnet; Q99712; -.
DR PhosphoSitePlus; Q99712; -.
DR BioMuta; KCNJ15; -.
DR DMDM; 77416869; -.
DR MassIVE; Q99712; -.
DR PaxDb; Q99712; -.
DR PeptideAtlas; Q99712; -.
DR PRIDE; Q99712; -.
DR ProteomicsDB; 78426; -.
DR Antibodypedia; 3029; 187 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 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; 956263at2759; -.
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; 16 hits in 1071 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 159 other tissues.
DR ExpressionAtlas; Q99712; baseline and differential.
DR Genevisible; Q99712; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
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 ion transmembrane transport; IBA:GO_Central.
DR Gene3D; 2.60.40.1400; -; 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; PTHR11767; 1.
DR PANTHER; PTHR11767:SF20; PTHR11767:SF20; 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; SSF81296; 1.
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
