KCNJ2_RAT
ID KCNJ2_RAT Reviewed; 427 AA.
AC Q64273;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Inward rectifier potassium channel 2;
DE AltName: Full=Inward rectifier K(+) channel Kir2.1;
DE Short=IRK-1;
DE Short=RBL-IRK1;
DE AltName: Full=Potassium channel, inwardly rectifying subfamily J member 2;
GN Name=Kcnj2; Synonyms=Irk1;
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].
RX PubMed=7603835; DOI=10.1007/bf00374805;
RA Wischmeyer E., Lentes K.U., Karschin A.;
RT "Physiological and molecular characterization of an IRK-type inward
RT rectifier K+ channel in a tumour mast cell line.";
RL Pflugers Arch. 429:809-819(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; 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).
RN [3]
RP INTERACTION WITH CASK; LIN7A; LIN7B; LIN7C; APBA1 AND DLG1, AND FUNCTION.
RX PubMed=14960569; DOI=10.1074/jbc.m400284200;
RA Leonoudakis D., Conti L.R., Radeke C.M., McGuire L.M., Vandenberg C.A.;
RT "A multiprotein trafficking complex composed of SAP97, CASK, Veli, and
RT Mint1 is associated with inward rectifier Kir2 potassium channels.";
RL J. Biol. Chem. 279:19051-19063(2004).
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. Can be blocked by extracellular barium and cesium
CC (By similarity). {ECO:0000250, ECO:0000269|PubMed:14960569}.
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.
CC -!- INTERACTION:
CC Q64273; Q62696: Dlg1; NbExp=3; IntAct=EBI-703577, EBI-389325;
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. Membrane;
CC Lipid-anchor {ECO:0000250|UniProtKB:P63252}.
CC -!- TISSUE SPECIFICITY: Prominently expressed in the central nervous
CC system. Also found in other excitable tissues such as heart and
CC skeletal muscle.
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; L48490; AAB03890.1; -; mRNA.
DR EMBL; AF021137; AAB88795.1; -; mRNA.
DR RefSeq; NP_058992.1; NM_017296.1.
DR RefSeq; XP_006247629.1; XM_006247567.3.
DR AlphaFoldDB; Q64273; -.
DR SMR; Q64273; -.
DR BioGRID; 248329; 2.
DR DIP; DIP-33299N; -.
DR IntAct; Q64273; 3.
DR STRING; 10116.ENSRNOP00000006254; -.
DR PaxDb; Q64273; -.
DR ABCD; Q64273; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000102334; ENSRNOP00000079758; ENSRNOG00000064933.
DR GeneID; 29712; -.
DR KEGG; rno:29712; -.
DR CTD; 3759; -.
DR RGD; 61968; Kcnj2.
DR eggNOG; KOG3827; Eukaryota.
DR GeneTree; ENSGT01030000234586; -.
DR HOGENOM; CLU_022738_3_0_1; -.
DR InParanoid; Q64273; -.
DR OMA; NISETEH; -.
DR OrthoDB; 956263at2759; -.
DR PhylomeDB; Q64273; -.
DR TreeFam; TF313676; -.
DR Reactome; R-RNO-1296041; Activation of G protein gated Potassium channels.
DR Reactome; R-RNO-1296053; Classical Kir channels.
DR Reactome; R-RNO-5576886; Phase 4 - resting membrane potential.
DR Reactome; R-RNO-997272; Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
DR PRO; PR:Q64273; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000004720; Expressed in skeletal muscle tissue and 17 other tissues.
DR Genevisible; Q64273; RN.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0043197; C:dendritic spine; IDA:RGD.
DR GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
DR GO; GO:0014704; C:intercalated disc; IDA:RGD.
DR GO; GO:0031224; C:intrinsic component of membrane; ISS:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IDA:RGD.
DR GO; GO:0005790; C:smooth endoplasmic reticulum; IDA:RGD.
DR GO; GO:0030315; C:T-tubule; IDA:RGD.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0005242; F:inward rectifier potassium channel activity; ISS:UniProtKB.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISO:RGD.
DR GO; GO:0086008; F:voltage-gated potassium channel activity involved in cardiac muscle cell action potential repolarization; ISO:RGD.
DR GO; GO:0086001; P:cardiac muscle cell action potential; ISO:RGD.
DR GO; GO:0086002; P:cardiac muscle cell action potential involved in contraction; ISO:RGD.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:RGD.
DR GO; GO:0015693; P:magnesium ion transport; ISO:RGD.
DR GO; GO:0086011; P:membrane repolarization during action potential; ISO:RGD.
DR GO; GO:0086013; P:membrane repolarization during cardiac muscle cell action potential; ISO:RGD.
DR GO; GO:1901381; P:positive regulation of potassium ion transmembrane transport; IMP:RGD.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; ISO:RGD.
DR GO; GO:0071805; P:potassium ion transmembrane transport; ISO:RGD.
DR GO; GO:0006813; P:potassium ion transport; ISS:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR GO; GO:0086004; P:regulation of cardiac muscle cell contraction; IMP: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 GO; GO:0060306; P:regulation of membrane repolarization; ISO:RGD.
DR GO; GO:0014861; P:regulation of skeletal muscle contraction via regulation of action potential; ISO:RGD.
DR GO; GO:0055119; P:relaxation of cardiac muscle; ISO:RGD.
DR GO; GO:0090076; P:relaxation of skeletal muscle; ISO:RGD.
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 1: Evidence at protein 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_0000154928"
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 383..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; 48200 MW; 85538FB1CCEBF8ED 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 FEEKHCYKVD YSRFHKTYEV PNTPLCSARD
LAEKKYILSN ANSFCYENEV ALTSKEEEDS ENGVPESTST DSPPGIDLHN QASVPLEPRP
LRRESEI
