ID   Q3ZAT1_MOUSE            Unreviewed;       501 AA.
AC   Q3ZAT1;
DT   27-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2005, sequence version 1.
DT   14-DEC-2022, entry version 147.
DE   RecName: Full=G protein-activated inward rectifier potassium channel 1 {ECO:0000256|ARBA:ARBA00015495};
DE   AltName: Full=Inward rectifier K(+) channel Kir3.1 {ECO:0000256|ARBA:ARBA00032145};
DE   AltName: Full=Potassium channel, inwardly rectifying subfamily J member 3 {ECO:0000256|ARBA:ARBA00031390};
GN   Name=Kcnj3 {ECO:0000313|EMBL:AAI03675.1, ECO:0000313|MGI:MGI:104742};
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 {ECO:0000313|EMBL:AAI03675.1};
RN   [1] {ECO:0000313|EMBL:AAI03675.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6 {ECO:0000313|EMBL:AAH68167.1};
RC   TISSUE=Brain {ECO:0000313|EMBL:AAH68167.1}, and PCR rescued clones
RC   {ECO:0000313|EMBL:AAI03675.1};
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RA   Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
RA   Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M.,
RA   Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.,
RA   Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F.,
RA   Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T.,
RA   Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F.,
RA   Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E.,
RA   Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y.,
RA   Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E.,
RA   Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y.,
RA   Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W.,
RA   Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
RA   Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA   Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J.,
RA   Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W.,
RA   Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J.,
RA   Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I.,
RA   Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U.,
RA   Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A.,
RA   Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.;
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   [2] {ECO:0007829|PubMed:21183079}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 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. {ECO:0000256|ARBA:ARBA00024877}.
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. {ECO:0000256|ARBA:ARBA00025883}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC       ECO:0000256|RuleBase:RU003822}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003822}.
CC   -!- SIMILARITY: Belongs to the inward rectifier-type potassium channel (TC
CC       1.A.2.1) family. KCNJ3 subfamily. {ECO:0000256|ARBA:ARBA00009002}.
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DR   EMBL; BC068167; AAH68167.1; -; mRNA.
DR   EMBL; BC103673; AAI03674.1; -; mRNA.
DR   EMBL; BC103674; AAI03675.1; -; mRNA.
DR   RefSeq; NP_001291739.1; NM_001304810.1.
DR   RefSeq; NP_032452.1; NM_008426.2.
DR   RefSeq; XP_006497793.1; XM_006497730.3.
DR   AlphaFoldDB; Q3ZAT1; -.
DR   SMR; Q3ZAT1; -.
DR   Antibodypedia; 18931; 480 antibodies from 32 providers.
DR   DNASU; 16519; -.
DR   GeneID; 16519; -.
DR   KEGG; mmu:16519; -.
DR   AGR; MGI:104742; -.
DR   CTD; 3760; -.
DR   MGI; MGI:104742; Kcnj3.
DR   VEuPathDB; HostDB:ENSMUSG00000026824; -.
DR   HOGENOM; CLU_022738_13_0_1; -.
DR   OMA; PARMEGN; -.
DR   OrthoDB; 956263at2759; -.
DR   BioGRID-ORCS; 16519; 0 hits in 59 CRISPR screens.
DR   ChiTaRS; Kcnj3; mouse.
DR   ExpressionAtlas; Q3ZAT1; baseline and differential.
DR   GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR   GO; GO:0030315; C:T-tubule; IEA:Ensembl.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:Ensembl.
DR   GO; GO:0015467; F:G-protein activated inward rectifier potassium channel activity; IEA:InterPro.
DR   GO; GO:0099508; F:voltage-gated ion channel activity involved in regulation of presynaptic membrane potential; IEA:Ensembl.
DR   GO; GO:1990573; P:potassium ion import across plasma membrane; IEA:Ensembl.
DR   GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
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; INWARD RECTIFIER POTASSIUM CHANNEL; 1.
DR   Pfam; PF01007; IRK; 1.
DR   Pfam; PF17655; IRK_C; 1.
DR   PRINTS; PR01327; KIR31CHANNEL.
DR   PRINTS; PR01320; KIRCHANNEL.
DR   SUPFAM; SSF81296; E set domains; 1.
PE   1: Evidence at protein level;
KW   Ion channel {ECO:0000256|ARBA:ARBA00023303, ECO:0000256|RuleBase:RU003822};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW   ECO:0000256|RuleBase:RU003822};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|RuleBase:RU003822};
KW   Potassium transport {ECO:0000256|ARBA:ARBA00022538,
KW   ECO:0000256|RuleBase:RU003822};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU003822};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU003822};
KW   Voltage-gated channel {ECO:0000256|ARBA:ARBA00022882,
KW   ECO:0000256|RuleBase:RU003822}.
FT   TRANSMEM        84..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        159..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          47..187
FT                   /note="IRK"
FT                   /evidence="ECO:0000259|Pfam:PF01007"
FT   DOMAIN          194..364
FT                   /note="IRK_C"
FT                   /evidence="ECO:0000259|Pfam:PF17655"
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   COMPBIAS        12..38
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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
//