KCNJ5_RAT
ID KCNJ5_RAT Reviewed; 419 AA.
AC P48548;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=G protein-activated inward rectifier potassium channel 4;
DE Short=GIRK-4;
DE AltName: Full=Cardiac inward rectifier;
DE Short=CIR;
DE AltName: Full=Heart KATP channel;
DE AltName: Full=Inward rectifier K(+) channel Kir3.4;
DE AltName: Full=KATP-1;
DE AltName: Full=Potassium channel, inwardly rectifying subfamily J member 5;
GN Name=Kcnj5; Synonyms=Girk4;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Heart;
RX PubMed=8047164; DOI=10.1038/370456a0;
RA Ashford M.L.J., Bond C.T., Blair T.A., Adelman J.P.;
RT "Cloning and functional expression of a rat heart KATP channel.";
RL Nature 370:456-459(1994).
RN [2]
RP ERRATUM OF PUBMED:8047164.
RX PubMed=8524415; DOI=10.1038/378792a0;
RA Ashford M.L.J., Bond C.T., Blair T.A., Adelman J.P.;
RL Nature 378:792-792(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 31-39 AND 333-341,
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Neonatal heart atrium;
RX PubMed=7877685; DOI=10.1038/374135a0;
RA Krapivinsky G.B., Gordon E.A., Wickman K., Velimirovic B.,
RA Krapivinsky L.D., Clapham D.E.;
RT "The G-protein-gated atrial K+ channel IKACh is a heteromultimer of two
RT inwardly rectifying K(+)-channel proteins.";
RL Nature 374:135-141(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBUNIT.
RC TISSUE=Pancreatic islet;
RX PubMed=7592809; DOI=10.1074/jbc.270.44.26086;
RA Ferrer J., Nichols C.G., Makhina E.N., Salkoff L., Bernstein J.,
RA Gerhard D., Wasson J., Ramanadham S., Permutt A.;
RT "Pancreatic islet cells express a family of inwardly rectifying K+ channel
RT subunits which interact to form G-protein-activated channels.";
RL J. Biol. Chem. 270:26086-26091(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Heart;
RX PubMed=8834003;
RA Iizuka M., Kubo Y., Tsunenari I., Pan C.X., Akiba I., Kono T.;
RT "Functional characterization and localization of a cardiac-type inwardly
RT rectifying K+ channel.";
RL Recept. Channels 3:299-315(1995).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
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).
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. Can be blocked by external barium.
CC {ECO:0000269|PubMed:7592809, ECO:0000269|PubMed:7877685,
CC ECO:0000269|PubMed:8834003}.
CC -!- SUBUNIT: Associates with GIRK1 or GIRK2 to form a G-protein-activated
CC heteromultimer pore-forming unit. The resulting inward current is much
CC larger. {ECO:0000269|PubMed:7592809, ECO:0000269|PubMed:7877685}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:7877685}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Most abundant in heart tissue where it is found
CC predominantly in atria. Also found in brain, kidney, liver, spleen,
CC lung and thymus. {ECO:0000269|PubMed:7877685,
CC ECO:0000269|PubMed:8834003}.
CC -!- SIMILARITY: Belongs to the inward rectifier-type potassium channel (TC
CC 1.A.2.1) family. KCNJ5 subfamily. {ECO:0000305}.
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DR EMBL; X83584; CAA58567.1; -; mRNA.
DR EMBL; L35771; AAC42048.1; -; mRNA.
DR EMBL; D50135; BAA08815.1; -; mRNA.
DR EMBL; BC087022; AAH87022.1; -; mRNA.
DR PIR; S48077; S48077.
DR RefSeq; NP_058993.1; NM_017297.2.
DR AlphaFoldDB; P48548; -.
DR SMR; P48548; -.
DR ComplexPortal; CPX-3276; I(KACh) inward rectifier potassium channel complex.
DR STRING; 10116.ENSRNOP00000048134; -.
DR ChEMBL; CHEMBL3714708; -.
DR GuidetoPHARMACOLOGY; 437; -.
DR iPTMnet; P48548; -.
DR PhosphoSitePlus; P48548; -.
DR PaxDb; P48548; -.
DR DNASU; 29713; -.
DR Ensembl; ENSRNOT00000041038; ENSRNOP00000048134; ENSRNOG00000033796.
DR GeneID; 29713; -.
DR KEGG; rno:29713; -.
DR UCSC; RGD:61971; rat.
DR CTD; 3762; -.
DR RGD; 61971; Kcnj5.
DR eggNOG; KOG3827; Eukaryota.
DR GeneTree; ENSGT01040000240379; -.
DR HOGENOM; CLU_022738_11_0_1; -.
DR InParanoid; P48548; -.
DR OMA; FMNQDME; -.
DR OrthoDB; 956263at2759; -.
DR PhylomeDB; P48548; -.
DR Reactome; R-RNO-1296041; Activation of G protein gated Potassium channels.
DR Reactome; R-RNO-997272; Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
DR PRO; PR:P48548; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000033796; Expressed in heart and 12 other tissues.
DR Genevisible; P48548; RN.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0030315; C:T-tubule; IDA:RGD.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; ISO:RGD.
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:0086089; F:voltage-gated potassium channel activity involved in atrial cardiac muscle cell action potential repolarization; ISO:RGD.
DR GO; GO:0098914; P:membrane repolarization during atrial cardiac muscle cell action potential; ISO:RGD.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; ISO:RGD.
DR GO; GO:0086091; P:regulation of heart rate by cardiac conduction; ISO:RGD.
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; IPR003277; K_chnl_inward-rec_Kir3.4.
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 PIRSF; PIRSF005465; GIRK_kir; 1.
DR PRINTS; PR01330; KIR34CHANNEL.
DR PRINTS; PR01320; KIRCHANNEL.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Ion channel; Ion transport; Membrane;
KW Phosphoprotein; Potassium; Potassium transport; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..419
FT /note="G protein-activated inward rectifier potassium
FT channel 4"
FT /id="PRO_0000154937"
FT TOPO_DOM 1..86
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 87..111
FT /note="Helical; Name=M1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 112..135
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT INTRAMEM 136..147
FT /note="Helical; Pore-forming; Name=H5"
FT /evidence="ECO:0000250"
FT INTRAMEM 148..154
FT /note="Pore-forming"
FT /evidence="ECO:0000250"
FT TOPO_DOM 155..163
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 164..185
FT /note="Helical; Name=M2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 186..419
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 380..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 149..154
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT SITE 179
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 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48542"
FT CONFLICT 188
FT /note="V -> I (in Ref. 1; CAA58567)"
FT /evidence="ECO:0000305"
FT CONFLICT 375
FT /note="Q -> E (in Ref. 1; CAA58567)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 419 AA; 47783 MW; DFF537CD79A7370D CRC64;
MAGDSRNAMN QDMEIGVTSQ DHKKIPKQAR DYIPIATDRT RLLPEGKKPR QRYMEKTGKC
NVHHGNVQET YRYLSDLFTT LVDLKWRFNL LVFTMVYTIT WLFFGFIWWL IAYVRGDLDH
VGDQEWIPCV ENLSGFVSAF LFSIETETTI GYGFRVITEK CPEGIILLLV QAILGSIVNA
FMVGCMFVKI SQPKKRAETL MFSNNAVISM RDEKLCLMFR VGDLRNSHIV EASIRAKLIK
SRQTKEGEFI PLNQTDINVG FDTGDDRLFL VSPLIISHEI NEKSPFWEMS RAQLEQEEFE
VVVILEGMVE ATGMTCQARS SYMDTEVLWG HRFTPVLTLE KGFYEVDYNT FHDTYETNTP
SCCAKELAEM KRNGQLLQSL PSPPLLGGCA EAEKEAEAEH DEEEEPNGLS VSRATRGSM
