KCNJ3_BOVIN
ID KCNJ3_BOVIN Reviewed; 501 AA.
AC E1BNE9;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 67.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
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 -!- INTERACTION:
CC E1BNE9; F1MYR9: KCNJ5; NbExp=2; IntAct=EBI-9973959, EBI-9973944;
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; DAAA02004538; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02004539; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02004540; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02004541; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02004542; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02004543; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001179553.1; NM_001192624.1.
DR AlphaFoldDB; E1BNE9; -.
DR SMR; E1BNE9; -.
DR ComplexPortal; CPX-3275; I(KACh) inward rectifier potassium channel complex.
DR IntAct; E1BNE9; 1.
DR STRING; 9913.ENSBTAP00000008100; -.
DR PaxDb; E1BNE9; -.
DR PRIDE; E1BNE9; -.
DR Ensembl; ENSBTAT00000008100; ENSBTAP00000008100; ENSBTAG00000006159.
DR GeneID; 526088; -.
DR KEGG; bta:526088; -.
DR CTD; 3760; -.
DR VEuPathDB; HostDB:ENSBTAG00000006159; -.
DR VGNC; VGNC:30461; KCNJ3.
DR eggNOG; KOG3827; Eukaryota.
DR GeneTree; ENSGT01040000240379; -.
DR HOGENOM; CLU_022738_13_0_1; -.
DR InParanoid; E1BNE9; -.
DR OMA; PARMEGN; -.
DR OrthoDB; 956263at2759; -.
DR TreeFam; TF313676; -.
DR Proteomes; UP000009136; Chromosome 2.
DR Bgee; ENSBTAG00000006159; Expressed in cardiac atrium and 37 other tissues.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IEA:Ensembl.
DR GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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: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 1: Evidence at protein level;
KW Glycoprotein; Ion channel; Ion transport; Membrane; Phosphoprotein;
KW Potassium; Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..501
FT /note="G protein-activated inward rectifier potassium
FT channel 1"
FT /id="PRO_0000431727"
FT TOPO_DOM 1..80
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
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 /evidence="ECO:0000250"
FT REGION 1..40
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:0000250|UniProtKB:P63250"
FT MOD_RES 424
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P63250"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P48549"
SQ SEQUENCE 501 AA; 56547 MW; E388B6FF8187CABE 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 YDLSQRSMQS EQFEIVVILE
GIVETTGMTC QARTSYTEDE VLWGHRFFPV ISLEEGFFKV DYSQFHATFE VPTPPYSVKE
QEEMLLMSSP LIAPAITNSK ERHNSVECLD GLDDISTKLP SKLQKITGRE DFPKKLLRMS
STTSEKAYSL GDLPMKLQRI SSVPGNSEEK LVSKTTKMLS DPMSQSVADL PPKLQKMAGG
ATRMEGNLPA KLRKMNSDRF T
