KCJ15_MOUSE
ID KCJ15_MOUSE Reviewed; 375 AA.
AC O88932; Q9JK34;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=ATP-sensitive inward rectifier potassium channel 15;
DE AltName: Full=Inward rectifier K(+) channel Kir4.2;
DE AltName: Full=Potassium channel, inwardly rectifying subfamily J member 15;
GN Name=Kcnj15;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Pearson W.L., Dourado M., Schreiber M., Nichols C.G., Salkoff L.;
RT "Expression of an inward rectifier current from a Kir 4 family K+ channel
RT gene cloned from mouse liver.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ;
RX PubMed=10906485; DOI=10.1016/s0925-4773(00)00364-6;
RA Thiery E., Gosset P., Damotte D., Delezoide A.-L., de Saint-Sauveur N.,
RA Vayssettes C., Creau N.;
RT "Developmentally regulated expression of the murine ortholog of the
RT potassium channel KIR4.2 (KCNJ15).";
RL Mech. Dev. 95:313-316(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; 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 [5]
RP TISSUE SPECIFICITY.
RX PubMed=33811157; DOI=10.1681/asn.2020111587;
RA Schlingmann K.P., Renigunta A., Hoorn E.J., Forst A.L., Renigunta V.,
RA Atanasov V., Mahendran S., Barakat T.S., Gillion V., Godefroid N.,
RA Brooks A.S., Lugtenberg D., Lake J., Debaix H., Rudin C., Knebelmann B.,
RA Tellier S., Rousset-Rouviere C., Viering D., de Baaij J.H.F., Weber S.,
RA Palygin O., Staruschenko A., Kleta R., Houillier P., Bockenhauer D.,
RA Devuyst O., Vargas-Poussou R., Warth R., Zdebik A.A., Konrad M.;
RT "Defects in KCNJ16 cause a novel tubulopathy with hypokalemia, salt
RT wasting, disturbed acid-base homeostasis, and sensorineural deafness.";
RL J. Am. Soc. Nephrol. 32:1498-1512(2021).
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:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in the proximal segment of the nephron.
CC {ECO:0000269|PubMed:33811157}.
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; AF085696; AAC68685.1; -; mRNA.
DR EMBL; AJ012368; CAB89666.1; -; mRNA.
DR EMBL; AK085689; BAC39507.1; -; mRNA.
DR EMBL; BC010794; AAH10794.1; -; mRNA.
DR EMBL; BC057915; AAH57915.1; -; mRNA.
DR CCDS; CCDS37410.1; -.
DR RefSeq; NP_001034145.1; NM_001039056.2.
DR RefSeq; NP_001258618.1; NM_001271689.1.
DR RefSeq; NP_001258620.1; NM_001271691.1.
DR RefSeq; NP_001258622.1; NM_001271693.1.
DR RefSeq; NP_001258624.1; NM_001271695.1.
DR RefSeq; NP_062638.1; NM_019664.5.
DR RefSeq; XP_006523014.1; XM_006522951.3.
DR RefSeq; XP_006523015.1; XM_006522952.3.
DR RefSeq; XP_017172374.1; XM_017316885.1.
DR AlphaFoldDB; O88932; -.
DR SMR; O88932; -.
DR BioGRID; 200898; 2.
DR IntAct; O88932; 1.
DR MINT; O88932; -.
DR STRING; 10090.ENSMUSP00000109493; -.
DR iPTMnet; O88932; -.
DR PhosphoSitePlus; O88932; -.
DR PaxDb; O88932; -.
DR PRIDE; O88932; -.
DR ProteomicsDB; 269188; -.
DR Antibodypedia; 3029; 187 antibodies from 29 providers.
DR DNASU; 16516; -.
DR Ensembl; ENSMUST00000113854; ENSMUSP00000109485; ENSMUSG00000062609.
DR Ensembl; ENSMUST00000113855; ENSMUSP00000109486; ENSMUSG00000062609.
DR Ensembl; ENSMUST00000113856; ENSMUSP00000109487; ENSMUSG00000062609.
DR Ensembl; ENSMUST00000113858; ENSMUSP00000109489; ENSMUSG00000062609.
DR GeneID; 16516; -.
DR KEGG; mmu:16516; -.
DR UCSC; uc008abs.2; mouse.
DR CTD; 3772; -.
DR MGI; MGI:1310000; Kcnj15.
DR VEuPathDB; HostDB:ENSMUSG00000062609; -.
DR eggNOG; KOG3827; Eukaryota.
DR GeneTree; ENSGT00990000203615; -.
DR HOGENOM; CLU_022738_3_3_1; -.
DR InParanoid; O88932; -.
DR OMA; LPMHRST; -.
DR PhylomeDB; O88932; -.
DR Reactome; R-MMU-1296041; Activation of G protein gated Potassium channels.
DR Reactome; R-MMU-997272; Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
DR BioGRID-ORCS; 16516; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Kcnj15; mouse.
DR PRO; PR:O88932; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; O88932; protein.
DR Bgee; ENSMUSG00000062609; Expressed in epithelium of stomach and 141 other tissues.
DR ExpressionAtlas; O88932; baseline and differential.
DR Genevisible; O88932; MM.
DR GO; GO:0016021; C:integral component of membrane; IC:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005242; F:inward rectifier potassium channel activity; ISO:MGI.
DR GO; GO:0005267; F:potassium channel activity; IDA:MGI.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; IBA:GO_Central.
DR GO; GO:0006813; P:potassium ion transport; IDA:MGI.
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 2: Evidence at transcript 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_0000154973"
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 CONFLICT 14
FT /note="V -> W (in Ref. 2; CAB89666)"
FT /evidence="ECO:0000305"
FT CONFLICT 99
FT /note="E -> G (in Ref. 2; CAB89666)"
FT /evidence="ECO:0000305"
FT CONFLICT 262
FT /note="S -> K (in Ref. 2; CAB89666)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 375 AA; 42605 MW; 163277597D4B2C8E CRC64;
MDAIHLGMSS APLVKHTNGV GLKAHRPRVM SKSGHSNVRI DKVDGIYLLY LQDLWTTVID
MKWRYKLTLF AATFVMTWFL FGVVYYAIAF IHGDLQLGES NSNHTPCIMK VDSLTGAFLF
SLESQTTIGY GVRSITEECP HAIFLLVAQL VITTLIEIFI TGTFLAKIAR PKKRAETIKF
SHCAVISKQN GKLCLVIQVA NMRKSLLIQC QLSGKLLQTH VTKEGERILL NQATVKFHVD
SSSESPFLIL PMTFYHVLDE TSPLRDLTPQ NLKEKEFELV VLLNATVEST SAVCQSRTSY
IPEEIYWGFE FVPVVSLSKN GKYVADFSQF EQIRKSPDCT FYCADSEKQK LEEQYRQEDQ
RERELRSLLL QQSNV
