KCNJ3_CHICK
ID KCNJ3_CHICK Reviewed; 492 AA.
AC Q90854;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 123.
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 Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=8626438; DOI=10.1074/jbc.271.11.6398;
RA Gadbut A.P., Riccardi D., Wu L.Y., Hebert S.C., Galper J.B.;
RT "Specificity of coupling of muscarinic receptor isoforms to a novel chick
RT inward-rectifying acetylcholine-sensitive K+ channel.";
RL J. Biol. Chem. 271:6398-6402(1996).
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 (By similarity). {ECO:0000250}.
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; L35555; AAA64786.1; -; mRNA.
DR PIR; I50235; I50235.
DR RefSeq; NP_990735.1; NM_205404.1.
DR AlphaFoldDB; Q90854; -.
DR SMR; Q90854; -.
DR STRING; 9031.ENSGALP00000020449; -.
DR PaxDb; Q90854; -.
DR PRIDE; Q90854; -.
DR GeneID; 396369; -.
DR KEGG; gga:396369; -.
DR CTD; 3760; -.
DR VEuPathDB; HostDB:geneid_396369; -.
DR eggNOG; KOG3827; Eukaryota.
DR InParanoid; Q90854; -.
DR OrthoDB; 956263at2759; -.
DR PhylomeDB; Q90854; -.
DR PRO; PR:Q90854; -.
DR Proteomes; UP000000539; Unplaced.
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: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: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; 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 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..492
FT /note="G protein-activated inward rectifier potassium
FT channel 1"
FT /id="PRO_0000154941"
FT TOPO_DOM 1..72
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 73..97
FT /note="Helical; Name=M1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 98..121
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT INTRAMEM 122..133
FT /note="Helical; Pore-forming; Name=H5"
FT /evidence="ECO:0000250"
FT INTRAMEM 134..140
FT /note="Pore-forming"
FT /evidence="ECO:0000250"
FT TOPO_DOM 141..149
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 150..171
FT /note="Helical; Name=M2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 172..492
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 16..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 135..140
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT SITE 165
FT /note="Role in the control of polyamine-mediated channel
FT gating and in the blocking by intracellular magnesium"
FT /evidence="ECO:0000250"
SQ SEQUENCE 492 AA; 55417 MW; 77E924317413B15B CRC64;
MSALRRKLGD EYQVVSTSAS GGGLPPPRAA PRGKRQRFVD KNGRCNVQHG NLGGETSRYL
SDLFTTLVDL KWRWNLFIFV LTYTVAWLFM ASMWWVIAYM RGDLNKAHDD SYTPCVANVY
NFPSAFLFFI ETEATIGYGY RYITDKCPEG IILFLFQSIL GSIVDAFLIG CMFIKMSQPK
KRAETLMFSE HAAISMRDGK LTLMFRVGNL RNSHMVSAQI RCKLLKSRQT PEGEFLPLDQ
LELDVGFSTG ADQLFLVSPL TICHVIDAKS PFYDLSQRTM QTEQFEIVVI LEGIVETTGM
TCQARTSYTE DEVLWGHRFF PVISLEEGFF KVDYSQFHAT FEVPTPPYSV KEQEEMLLMS
SPLIAPAVSN SKERNNSVEC LDGLDEVGIK LPSKLQKITG RDDFPKKLLR ISSTTSEKAY
SMGDLPMKLQ RISSVPGNSE EKLVSKATKM MSDPMSQSVA DLPPKLQKLS GGGRMEGNLP
PKLRKMNSDR FT
