KCNJ3_MOUSE
ID KCNJ3_MOUSE Reviewed; 501 AA.
AC P63250; P35562;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=G protein-activated inward rectifier potassium channel 1;
DE Short=GIRK-1;
DE AltName: Full=Inward rectifier K(+) channel Kir3.1;
DE AltName: Full=Potassium channel, inwardly rectifying subfamily J member 3;
GN Name=Kcnj3; Synonyms=Girk1;
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 STRAIN=C57BL/6J;
RX PubMed=7702616; DOI=10.1006/bbrc.1995.1456;
RA Kobayashi T., Ikeda K., Ichikawa T., Abe S., Togashi S., Kumanishi T.;
RT "Molecular cloning of a mouse G-protein-activated K+ channel (mGIRK1) and
RT distinct distributions of three GIRK (GIRK1, 2 and 3) mRNAs in mouse
RT brain.";
RL Biochem. Biophys. Res. Commun. 208:1166-1173(1995).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-385 AND SER-424, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, and Lung;
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).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 43-63 AND 190-370.
RX PubMed=12507423; DOI=10.1016/s0092-8674(02)01227-8;
RA Nishida M., MacKinnon R.;
RT "Structural basis of inward rectification: cytoplasmic pore of the G
RT protein-gated inward rectifier GIRK1 at 1.8 A resolution.";
RL Cell 111:957-965(2002).
CC -!- FUNCTION: This potassium channel is controlled by G proteins. Inward
CC rectifier potassium channels are characterized by a greater tendency to
CC allow potassium to flow into the cell rather than out of it. Their
CC voltage 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. This receptor plays a crucial role in regulating
CC the heartbeat.
CC -!- SUBUNIT: Associates with GIRK2, GIRK3 or GIRK4 to form a G-protein
CC activated heteromultimer pore-forming unit. The resulting inward
CC current is much larger (By similarity). {ECO:0000250}.
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. KCNJ3 subfamily. {ECO:0000305}.
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DR EMBL; D45022; BAA08079.1; -; mRNA.
DR CCDS; CCDS16042.1; -.
DR PIR; JC4139; JC4139.
DR RefSeq; NP_032452.1; NM_008426.2.
DR RefSeq; XP_006497793.1; XM_006497730.3.
DR PDB; 1N9P; X-ray; 1.80 A; A=41-371.
DR PDB; 1U4E; X-ray; 2.09 A; A=41-63, A=189-371.
DR PDB; 2QKS; X-ray; 2.20 A; A/B=41-82, A/B=178-371.
DR PDB; 3K6N; X-ray; 2.00 A; A=41-63, A=190-371.
DR PDB; 5UM4; X-ray; 2.50 A; A=201-370.
DR PDBsum; 1N9P; -.
DR PDBsum; 1U4E; -.
DR PDBsum; 2QKS; -.
DR PDBsum; 3K6N; -.
DR PDBsum; 5UM4; -.
DR AlphaFoldDB; P63250; -.
DR SMR; P63250; -.
DR ComplexPortal; CPX-3277; I(KACh) inward rectifier potassium channel complex.
DR CORUM; P63250; -.
DR DIP; DIP-48585N; -.
DR STRING; 10090.ENSMUSP00000063329; -.
DR GlyGen; P63250; 1 site.
DR iPTMnet; P63250; -.
DR PhosphoSitePlus; P63250; -.
DR PaxDb; P63250; -.
DR PeptideAtlas; P63250; -.
DR PRIDE; P63250; -.
DR ProteomicsDB; 263401; -.
DR Antibodypedia; 18931; 483 antibodies from 33 providers.
DR DNASU; 16519; -.
DR Ensembl; ENSMUST00000067101; ENSMUSP00000063329; ENSMUSG00000026824.
DR Ensembl; ENSMUST00000112633; ENSMUSP00000108252; ENSMUSG00000026824.
DR GeneID; 16519; -.
DR KEGG; mmu:16519; -.
DR UCSC; uc008jru.2; mouse.
DR CTD; 3760; -.
DR MGI; MGI:104742; Kcnj3.
DR VEuPathDB; HostDB:ENSMUSG00000026824; -.
DR eggNOG; KOG3827; Eukaryota.
DR GeneTree; ENSGT01040000240379; -.
DR HOGENOM; CLU_022738_13_0_1; -.
DR InParanoid; P63250; -.
DR OMA; PARMEGN; -.
DR OrthoDB; 956263at2759; -.
DR PhylomeDB; P63250; -.
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; 16519; 0 hits in 59 CRISPR screens.
DR ChiTaRS; Kcnj3; mouse.
DR EvolutionaryTrace; P63250; -.
DR PRO; PR:P63250; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P63250; protein.
DR Bgee; ENSMUSG00000026824; Expressed in retrosplenial region and 116 other tissues.
DR ExpressionAtlas; P63250; baseline and differential.
DR Genevisible; P63250; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:MGI.
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; IBA:GO_Central.
DR GO; GO:0030315; C:T-tubule; ISO:MGI.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; ISO:MGI.
DR GO; GO:0015467; F:G-protein activated inward rectifier potassium channel activity; TAS:MGI.
DR GO; GO:0005242; F:inward rectifier potassium channel activity; ISO:MGI.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; ISO:MGI.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0051602; P:response to electrical stimulus; IEA:Ensembl.
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; IPR003274; K_chnl_inward-rec_Kir3.1.
DR InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR InterPro; IPR040445; Kir_TM.
DR PANTHER; PTHR11767; PTHR11767; 1.
DR Pfam; PF01007; IRK; 1.
DR Pfam; PF17655; IRK_C; 1.
DR PRINTS; PR01327; KIR31CHANNEL.
DR PRINTS; PR01320; KIRCHANNEL.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glycoprotein; Ion channel; Ion transport; Membrane;
KW Phosphoprotein; Potassium; Potassium transport; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..501
FT /note="G protein-activated inward rectifier potassium
FT channel 1"
FT /id="PRO_0000154939"
FT TOPO_DOM 1..80
FT /note="Cytoplasmic"
FT TRANSMEM 81..105
FT /note="Helical; Name=M1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 106..129
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT INTRAMEM 130..141
FT /note="Helical; Pore-forming; Name=H5"
FT /evidence="ECO:0000250"
FT INTRAMEM 142..148
FT /note="Pore-forming"
FT /evidence="ECO:0000250"
FT TOPO_DOM 149..157
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 158..179
FT /note="Helical; Name=M2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 180..501
FT /note="Cytoplasmic"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 456..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 143..148
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT COMPBIAS 12..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 173
FT /note="Role in the control of polyamine-mediated channel
FT gating and in the blocking by intracellular magnesium"
FT /evidence="ECO:0000250"
FT MOD_RES 385
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 424
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT HELIX 69..77
FT /evidence="ECO:0007829|PDB:2QKS"
FT HELIX 179..185
FT /evidence="ECO:0007829|PDB:2QKS"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:2QKS"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:1N9P"
FT STRAND 200..205
FT /evidence="ECO:0007829|PDB:1N9P"
FT STRAND 208..215
FT /evidence="ECO:0007829|PDB:1N9P"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:1N9P"
FT STRAND 223..237
FT /evidence="ECO:0007829|PDB:1N9P"
FT STRAND 243..250
FT /evidence="ECO:0007829|PDB:1N9P"
FT TURN 255..257
FT /evidence="ECO:0007829|PDB:1N9P"
FT TURN 258..260
FT /evidence="ECO:0007829|PDB:5UM4"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:1N9P"
FT STRAND 268..273
FT /evidence="ECO:0007829|PDB:1N9P"
FT TURN 279..282
FT /evidence="ECO:0007829|PDB:1N9P"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:1N9P"
FT STRAND 294..303
FT /evidence="ECO:0007829|PDB:1N9P"
FT TURN 304..306
FT /evidence="ECO:0007829|PDB:1N9P"
FT STRAND 312..317
FT /evidence="ECO:0007829|PDB:1N9P"
FT HELIX 318..320
FT /evidence="ECO:0007829|PDB:1N9P"
FT STRAND 321..323
FT /evidence="ECO:0007829|PDB:1N9P"
FT STRAND 325..327
FT /evidence="ECO:0007829|PDB:1N9P"
FT STRAND 331..336
FT /evidence="ECO:0007829|PDB:1N9P"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:1N9P"
FT HELIX 342..344
FT /evidence="ECO:0007829|PDB:1N9P"
FT STRAND 348..350
FT /evidence="ECO:0007829|PDB:1N9P"
FT HELIX 358..368
FT /evidence="ECO:0007829|PDB:1N9P"
SQ SEQUENCE 501 AA; 56573 MW; AB8910E9CC08FFEC CRC64;
MSALRRKFGD DYQVVTTSSS GSGLQPQGPG QGPQQQLVPK KKRQRFVDKN GRCNVQHGNL
GSETSRYLSD LFTTLVDLKW RWNLFIFILT YTVAWLFMAS MWWVIAYTRG DLNKAHVGNY
TPCVANVYNF PSAFLFFIET EATIGYGYRY ITDKCPEGII LFLFQSILGS IVDAFLIGCM
FIKMSQPKKR AETLMFSEHA VISMRDGKLT LMFRVGNLRN SHMVSAQIRC KLLKSRQTPE
GEFLPLDQLE LDVGFSTGAD QLFLVSPLTI CHVIDAKSPF YDLSQRSMQT EQFEVVVILE
GIVETTGMTC QARTSYTEDE VLWGHRFFPV ISLEEGFFKV DYSQFHATFE VPTPPYSVKE
QEEMLLMSSP LIAPAITNSK ERHNSVECLD GLDDISTKLP SKLQKITGRE DFPKKLLRMS
STTSEKAYSL GDLPMKLQRI SSVPGNSEEK LVSKTTKMLS DPMSQSVADL PPKLQKMAGG
PTRMEGNLPA KLRKMNSDRF T
