KCJ13_MOUSE
ID KCJ13_MOUSE Reviewed; 360 AA.
AC P86046;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Inward rectifier potassium channel 13 {ECO:0000250|UniProtKB:O60928};
DE AltName: Full=Inward rectifier K(+) channel Kir7.1 {ECO:0000250|UniProtKB:O60928};
DE AltName: Full=Potassium channel, inwardly rectifying subfamily J member 13 {ECO:0000312|MGI:MGI:3781032};
GN Name=Kcnj13 {ECO:0000312|MGI:MGI:3781032};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
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. KCNJ13 has a very low single channel
CC conductance, low sensitivity to block by external barium and cesium,
CC and no dependence of its inward rectification properties on the
CC internal blocking particle magnesium (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- PTM: Phosphorylation at Ser-287 by PKA increases ionic currents.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the inward rectifier-type potassium channel (TC
CC 1.A.2.1) family. KCNJ13 subfamily. {ECO:0000305}.
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DR EMBL; AC157811; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS35653.1; -.
DR RefSeq; NP_001103697.1; NM_001110227.2.
DR AlphaFoldDB; P86046; -.
DR SMR; P86046; -.
DR STRING; 10090.ENSMUSP00000108838; -.
DR iPTMnet; P86046; -.
DR PhosphoSitePlus; P86046; -.
DR PaxDb; P86046; -.
DR PeptideAtlas; P86046; -.
DR PRIDE; P86046; -.
DR ProteomicsDB; 301768; -.
DR Antibodypedia; 34443; 126 antibodies from 26 providers.
DR Ensembl; ENSMUST00000113212; ENSMUSP00000108838; ENSMUSG00000079436.
DR GeneID; 100040591; -.
DR KEGG; mmu:100040591; -.
DR UCSC; uc007bwu.2; mouse.
DR CTD; 3769; -.
DR MGI; MGI:3781032; Kcnj13.
DR VEuPathDB; HostDB:ENSMUSG00000079436; -.
DR eggNOG; KOG3827; Eukaryota.
DR GeneTree; ENSGT00990000203615; -.
DR HOGENOM; CLU_022738_3_3_1; -.
DR InParanoid; P86046; -.
DR OMA; QGQTCLM; -.
DR OrthoDB; 412069at2759; -.
DR PhylomeDB; P86046; -.
DR TreeFam; TF313676; -.
DR BioGRID-ORCS; 100040591; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Kcnj13; mouse.
DR PRO; PR:P86046; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P86046; protein.
DR Bgee; ENSMUSG00000079436; Expressed in choroid plexus epithelium and 101 other tissues.
DR ExpressionAtlas; P86046; baseline and differential.
DR Genevisible; P86046; MM.
DR GO; GO:0016021; C:integral component of membrane; 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: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; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR InterPro; IPR008062; KCNJ13.
DR InterPro; IPR040445; Kir_TM.
DR PANTHER; PTHR11767; PTHR11767; 1.
DR PANTHER; PTHR11767:SF3; PTHR11767:SF3; 1.
DR Pfam; PF01007; IRK; 1.
DR Pfam; PF17655; IRK_C; 1.
DR PIRSF; PIRSF005465; GIRK_kir; 1.
DR PRINTS; PR01679; KIR7CHANNEL.
DR PRINTS; PR01320; KIRCHANNEL.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 3: Inferred from homology;
KW Ion channel; Ion transport; Membrane; Phosphoprotein; Potassium;
KW Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..360
FT /note="Inward rectifier potassium channel 13"
FT /id="PRO_0000355142"
FT TOPO_DOM 1..53
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O60928"
FT TRANSMEM 54..78
FT /note="Helical; Name=M1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 79..105
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:O60928"
FT INTRAMEM 106..117
FT /note="Helical; Pore-forming; Name=H5"
FT /evidence="ECO:0000250"
FT INTRAMEM 118..124
FT /note="Pore-forming"
FT /evidence="ECO:0000250"
FT TOPO_DOM 125..133
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:O60928"
FT TRANSMEM 134..155
FT /note="Helical; Name=M2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 156..360
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O60928"
FT MOTIF 119..124
FT /note="Selectivity filter"
FT /evidence="ECO:0000250|UniProtKB:O60928"
FT SITE 149
FT /note="Role in the control of polyamine-mediated channel
FT gating and in the blocking by intracellular magnesium"
FT /evidence="ECO:0000250|UniProtKB:O60928"
FT MOD_RES 287
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:O60928"
SQ SEQUENCE 360 AA; 40565 MW; 9D2107FB5C59C11D CRC64;
MDSSNCKVNA PLLSQRHRRM VTKDGHSTLQ MDGAQRGLVY LRDAWGILMD MRWRWMMLVF
SASFVVHWLV FAVLWYAVAE MNGDLEIDHD VPPENHTICV KHITSFTAAF SFSLETQLTI
GYGTMFPSGD CPSAIALLAI QMLLGLMLEA FITGAFVAKI ARPKNRAFSI RFTDLAVVAH
KDGKPNLIFQ VANTRPSPLT NVRVSAVLYQ ERENGELYQT SVDFHLDGIS SEECPFFIFP
LTYYHTISPS SPLATLLQHE TPPHFELVVF LSAMQEGTGE ICQRRTSYLP SEIMLHHRFA
ALMTRGSKGE YQVKMENFDK TVPEHPTPVV SKSPHRTDLD IHINGQSIDN FQIAETGLTE
