KCNJ2_CAVPO
ID KCNJ2_CAVPO Reviewed; 427 AA.
AC P52185;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Inward rectifier potassium channel 2;
DE AltName: Full=Cardiac inward rectifier potassium channel;
DE AltName: Full=Inward rectifier K(+) channel Kir2.1;
DE Short=IRK-1;
DE AltName: Full=Potassium channel, inwardly rectifying subfamily J member 2;
GN Name=KCNJ2; Synonyms=IRK1;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Hartley; TISSUE=Heart;
RX PubMed=8534918; DOI=10.1091/mbc.6.9.1231;
RA Tang W., Ruknudin A., Yang W.-P., Shaw S.-Y., Knickerbocker A., Kurtz S.;
RT "Functional expression of a vertebrate inwardly rectifying K+ channel in
RT yeast.";
RL Mol. Biol. Cell 6:1231-1240(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Lens epithelium;
RX PubMed=9533862; DOI=10.1006/exer.1997.0432;
RA Rae J.L., Shepard A.R.;
RT "Inwardly rectifying potassium channels in lens epithelium are from the
RT IRK1 (Kir 2.1) family.";
RL Exp. Eye Res. 66:347-359(1998).
CC -!- FUNCTION: Probably participates in establishing action potential
CC waveform and excitability of neuronal and muscle tissues. 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. Blocked by external barium or cesium.
CC -!- SUBUNIT: Homomultimeric and heteromultimeric association with
CC KCNJ4/Kir2.3. Association, via its PDZ-recognition domain, with LIN7A,
CC LIN7B, LIN7C, DLG1, CASK and APBA1 plays a key role in its localization
CC and trafficking (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. Membrane;
CC Lipid-anchor {ECO:0000250|UniProtKB:P63252}.
CC -!- PTM: S-nitrosylation increases the open probability and inward
CC rectifying currents. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the inward rectifier-type potassium channel (TC
CC 1.A.2.1) family. KCNJ2 subfamily. {ECO:0000305}.
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DR EMBL; Z48971; CAA88835.1; -; Genomic_DNA.
DR EMBL; AF021142; AAB88800.1; -; mRNA.
DR PIR; S52846; S52846.
DR RefSeq; NP_001166446.1; NM_001172975.1.
DR RefSeq; XP_012997745.1; XM_013142291.1.
DR AlphaFoldDB; P52185; -.
DR SMR; P52185; -.
DR STRING; 10141.ENSCPOP00000016364; -.
DR Ensembl; ENSCPOT00000034075; ENSCPOP00000031029; ENSCPOG00000004956.
DR GeneID; 100135566; -.
DR KEGG; cpoc:100135566; -.
DR CTD; 3759; -.
DR eggNOG; KOG3827; Eukaryota.
DR GeneTree; ENSGT01030000234586; -.
DR HOGENOM; CLU_022738_3_0_1; -.
DR InParanoid; P52185; -.
DR OMA; NISETEH; -.
DR OrthoDB; 956263at2759; -.
DR TreeFam; TF313676; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000004956; Expressed in heart left ventricle and 9 other tissues.
DR GO; GO:0031224; C:intrinsic component of membrane; ISS:UniProtKB.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0005242; F:inward rectifier potassium channel activity; ISS:UniProtKB.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IEA:Ensembl.
DR GO; GO:0086008; F:voltage-gated potassium channel activity involved in cardiac muscle cell action potential repolarization; IEA:Ensembl.
DR GO; GO:0086002; P:cardiac muscle cell action potential involved in contraction; IEA:Ensembl.
DR GO; GO:0015693; P:magnesium ion transport; IEA:Ensembl.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; IEA:Ensembl.
DR GO; GO:0006813; P:potassium ion transport; ISS:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR GO; GO:0086091; P:regulation of heart rate by cardiac conduction; IEA:Ensembl.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0060306; P:regulation of membrane repolarization; IEA:Ensembl.
DR GO; GO:0014861; P:regulation of skeletal muscle contraction via regulation of action potential; IEA:Ensembl.
DR GO; GO:0055119; P:relaxation of cardiac muscle; IEA:Ensembl.
DR GO; GO:0090076; P:relaxation of skeletal muscle; 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; IPR003271; K_chnl_inward-rec_Kir2.1.
DR InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR InterPro; IPR013673; K_chnl_inward-rec_Kir_N.
DR InterPro; IPR040445; Kir_TM.
DR PANTHER; PTHR11767; PTHR11767; 1.
DR PANTHER; PTHR11767:SF43; PTHR11767:SF43; 1.
DR Pfam; PF01007; IRK; 1.
DR Pfam; PF17655; IRK_C; 1.
DR Pfam; PF08466; IRK_N; 1.
DR PIRSF; PIRSF005465; GIRK_kir; 1.
DR PRINTS; PR01324; KIR21CHANNEL.
DR PRINTS; PR01320; KIRCHANNEL.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 2: Evidence at transcript level;
KW Ion channel; Ion transport; Lipoprotein; Membrane; Myristate; Potassium;
KW Potassium transport; Reference proteome; S-nitrosylation; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..427
FT /note="Inward rectifier potassium channel 2"
FT /id="PRO_0000154922"
FT TOPO_DOM 2..81
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 82..106
FT /note="Helical; Name=M1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 107..128
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT INTRAMEM 129..140
FT /note="Helical; Pore-forming; Name=H5"
FT /evidence="ECO:0000250"
FT INTRAMEM 141..147
FT /note="Pore-forming"
FT /evidence="ECO:0000250"
FT TOPO_DOM 148..156
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 157..178
FT /note="Helical; Name=M2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 179..427
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 384..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 142..147
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT MOTIF 425..427
FT /note="PDZ-binding"
FT /evidence="ECO:0000255"
FT SITE 172
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 76
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:P63252"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:P63252"
SQ SEQUENCE 427 AA; 48318 MW; B3BA0ADD76F05B3B CRC64;
MGSVRTNRYS IVSSEEDGMK LATMAVANGF GNGKSKVHTR QQCRSRFVKK DGHCNVQFIN
VGEKGQRYLA DIFTTCVDIR WRWMLVIFCL AFVLSWLFFG CVFWLIALLH GDLDASKESK
ACVSEVNSFT AAFLFSIETQ TTIGYGFRCV TDECPIAVFM VVFQSIVGCI IDAFIIGAVM
AKMAKPKKRN ETLVFSHNAV IAMRDGKLCL MWRVGNLRKS HLVEAHVRAQ LLKSRITSEG
EYIPLDQIDI NVGFDSGIDR IFLVSPITIV HEIDEDSPLY DLSKQDIDNA DFEIVVILEG
MVEATAMTTQ CRSSYLANEI LWGHRYEPVL FEEKHYYKVD YSRFHKTYEV PNTPLCSARD
LAEKKYILSN ANSFCYENEV ALTSKEEDDS ENGVPESTST DTPPDIDLHN QASVPLEPRP
LRRESEI
