KCNJ9_MOUSE
ID KCNJ9_MOUSE Reviewed; 393 AA.
AC P48543; Q9WUE1;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=G protein-activated inward rectifier potassium channel 3;
DE Short=GIRK-3;
DE AltName: Full=Inward rectifier K(+) channel Kir3.3;
DE AltName: Full=Potassium channel, inwardly rectifying subfamily J member 9;
GN Name=Kcnj9; Synonyms=Girk3;
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=Brain;
RX PubMed=7926018; DOI=10.1016/0014-5793(94)01007-2;
RA Lesage F., Duprat F., Fink M., Guillemare E., Coppola T., Lazdunski M.,
RA Hugnot J.-P.;
RT "Cloning provides evidence for a family of inward rectifier and G-protein
RT coupled K+ channels in the brain.";
RL FEBS Lett. 353:37-42(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=10341034; DOI=10.1007/s002329900524;
RA Jelacic T.M., Sims S.M., Clapham D.E.;
RT "Functional expression and characterization of G-protein-gated inwardly
RT rectifying K+ channels containing GIRK3.";
RL J. Membr. Biol. 169:123-129(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: This receptor is controlled by G proteins. Inward rectifier
CC potassium channels are characterized by a greater tendency to allow
CC potassium to flow into the cell rather than out of it. Their voltage
CC dependence is regulated by the concentration of extracellular
CC potassium; as external potassium is raised, the voltage range of the
CC channel opening shifts to more positive voltages. The inward
CC rectification is mainly due to the blockage of outward current by
CC internal magnesium.
CC -!- SUBUNIT: Associates with GIRK1 to form a G-protein-activated
CC heteromultimer pore-forming unit. The resulting inward current is much
CC larger. When alone, fail to give functional channels in Xenopus
CC oocytes. Interacts (via PDZ-binding motif) with SNX27 (via PDZ domain);
CC the interaction is required when endocytosed to prevent degradation in
CC lysosomes and promote recycling to the plasma membrane.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed mainly in the brain, some expression in
CC the skeletal muscle.
CC -!- DOMAIN: The PDZ-binding motif specifically binds the PDZ domain of
CC SNX27: the specificity for SNX27 is provided by the 2 residues located
CC upstream (Glu-388 and Ser-389) of the PDZ-binding motif. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the inward rectifier-type potassium channel (TC
CC 1.A.2.1) family. KCNJ9 subfamily. {ECO:0000305}.
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DR EMBL; U11860; AAA53246.1; -; mRNA.
DR EMBL; AF130860; AAD31016.1; -; mRNA.
DR EMBL; BC065161; AAH65161.1; -; mRNA.
DR CCDS; CCDS35783.1; -.
DR PIR; S48739; S48739.
DR RefSeq; NP_032455.2; NM_008429.2.
DR RefSeq; XP_006496741.1; XM_006496678.3.
DR AlphaFoldDB; P48543; -.
DR SMR; P48543; -.
DR STRING; 10090.ENSMUSP00000060110; -.
DR PhosphoSitePlus; P48543; -.
DR PaxDb; P48543; -.
DR PeptideAtlas; P48543; -.
DR PRIDE; P48543; -.
DR ProteomicsDB; 268961; -.
DR ABCD; P48543; 1 sequenced antibody.
DR Antibodypedia; 34266; 128 antibodies from 29 providers.
DR DNASU; 16524; -.
DR Ensembl; ENSMUST00000062387; ENSMUSP00000060110; ENSMUSG00000038026.
DR Ensembl; ENSMUST00000194204; ENSMUSP00000141633; ENSMUSG00000038026.
DR GeneID; 16524; -.
DR KEGG; mmu:16524; -.
DR UCSC; uc007dqg.1; mouse.
DR CTD; 3765; -.
DR MGI; MGI:108007; Kcnj9.
DR VEuPathDB; HostDB:ENSMUSG00000038026; -.
DR eggNOG; KOG3827; Eukaryota.
DR GeneTree; ENSGT01040000240379; -.
DR HOGENOM; CLU_022738_11_0_1; -.
DR InParanoid; P48543; -.
DR OMA; LRDSHIV; -.
DR OrthoDB; 956263at2759; -.
DR PhylomeDB; P48543; -.
DR TreeFam; TF313676; -.
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; 16524; 2 hits in 71 CRISPR screens.
DR PRO; PR:P48543; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P48543; protein.
DR Bgee; ENSMUSG00000038026; Expressed in cerebellar vermis and 78 other tissues.
DR ExpressionAtlas; P48543; baseline and differential.
DR Genevisible; P48543; MM.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IDA:SynGO.
DR GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; IDA:SynGO.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0015467; F:G-protein activated inward rectifier potassium channel activity; IEA:InterPro.
DR GO; GO:0005242; F:inward rectifier potassium channel activity; IBA:GO_Central.
DR GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
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; IPR003276; K_chnl_inward-rec_Kir3.3.
DR InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR InterPro; IPR040445; Kir_TM.
DR PANTHER; PTHR11767; PTHR11767; 1.
DR PANTHER; PTHR11767:SF17; PTHR11767:SF17; 1.
DR Pfam; PF01007; IRK; 1.
DR Pfam; PF17655; IRK_C; 1.
DR PIRSF; PIRSF005465; GIRK_kir; 1.
DR PRINTS; PR01329; KIR33CHANNEL.
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..393
FT /note="G protein-activated inward rectifier potassium
FT channel 3"
FT /id="PRO_0000154951"
FT TOPO_DOM 1..57
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 58..82
FT /note="Helical; Name=M1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 83..106
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT INTRAMEM 107..118
FT /note="Helical; Pore-forming; Name=H5"
FT /evidence="ECO:0000250"
FT INTRAMEM 119..125
FT /note="Pore-forming"
FT /evidence="ECO:0000250"
FT TOPO_DOM 126..134
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 135..156
FT /note="Helical; Name=M2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 157..393
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 120..125
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT MOTIF 390..393
FT /note="PDZ-binding"
FT SITE 150
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 60
FT /note="S -> R (in Ref. 1; AAA53246)"
FT /evidence="ECO:0000305"
FT CONFLICT 77
FT /note="A -> V (in Ref. 1; AAA53246)"
FT /evidence="ECO:0000305"
FT CONFLICT 370..393
FT /note="AGAGDGADKEHNGCLPPPESESKV -> GRCGRWS (in Ref. 1;
FT AAA53246)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 393 AA; 43974 MW; 9CF749672A865B08 CRC64;
MAQENAAFSP GSEEPPRRRG RQRYVEKDGR CNVQQGNVRE TYRYLTDLFT TLVDLQWRLS
LLFFVLAYAL TWLFFGAIWW LIAYGRGDLE HLEDTAWTPC VNNLNGFVAA FLFSIETETT
IGYGHRVITD QCPEGIVLLL LQAILGSMVN AFMVGCMFVK ISQPNKRAAT LVFSSHAVVS
LRDGRLCLMF RVGDLRSSHI VEASIRAKLI RSRQTLEGEF IPLHQTDLSV GFDTGDDRLF
LVSPLVISHE IDAASPFWEA SRRALERDDF EIVVILEGMV EATGMTCQAR SSYLVDEVLW
GHRFTSVLTL EDGFYEVDYA SFHETFEVPT PSCSARELAE AAARLDAHLY WSIPSRLDEK
VEEEGAGEGA GAGDGADKEH NGCLPPPESE SKV
