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Database: UniProt
Entry: KCNJ2_CANLF
LinkDB: KCNJ2_CANLF
Original site: KCNJ2_CANLF 
ID   KCNJ2_CANLF             Reviewed;         427 AA.
AC   Q9MYY9;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   16-OCT-2019, entry version 130.
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   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
OC   Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Cocker spaniel; TISSUE=Kidney;
RA   Schueler T.M., Wegmann M., Derst C.;
RT   "Cloning and sequencing of Canis familiaris Kir2.1.";
RL   Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
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
CC       tendency to allow potassium to flow into the cell rather than out
CC       of it. Their voltage dependence is regulated by the concentration
CC       of extracellular potassium; as external potassium is raised, the
CC       voltage range of the channel opening shifts to more positive
CC       voltages. The inward rectification is mainly due to the blockage
CC       of outward current by internal magnesium. Blocked by external
CC       barium or cesium (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homomultimeric and heteromultimeric association with
CC       KCNJ4/Kir2.3. Association, via its PDZ-recognition domain, with
CC       LIN7A, LIN7B, LIN7C, DLG1, CASK and APBA1 plays a key role in its
CC       localization and trafficking (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC       Membrane; 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
CC       (TC 1.A.2.1) family. KCNJ2 subfamily. {ECO:0000305}.
DR   EMBL; AF277647; AAF79214.1; -; mRNA.
DR   RefSeq; NP_001003120.1; NM_001003120.3.
DR   SMR; Q9MYY9; -.
DR   STRING; 9612.ENSCAFP00000015804; -.
DR   PaxDb; Q9MYY9; -.
DR   PRIDE; Q9MYY9; -.
DR   Ensembl; ENSCAFT00000017080; ENSCAFP00000015804; ENSCAFG00000010736.
DR   GeneID; 403717; -.
DR   KEGG; cfa:403717; -.
DR   CTD; 3759; -.
DR   VGNC; VGNC:42263; KCNJ2.
DR   eggNOG; KOG3827; Eukaryota.
DR   eggNOG; ENOG410XQ62; LUCA.
DR   GeneTree; ENSGT00960000186595; -.
DR   HOGENOM; HOG000237325; -.
DR   InParanoid; Q9MYY9; -.
DR   KO; K04996; -.
DR   OMA; KVHTRHQ; -.
DR   OrthoDB; 956263at2759; -.
DR   TreeFam; TF313676; -.
DR   Reactome; R-CFA-1296041; Activation of G protein gated Potassium channels.
DR   Reactome; R-CFA-1296053; Classical Kir channels.
DR   Reactome; R-CFA-5576886; Phase 4 - resting membrane potential.
DR   Reactome; R-CFA-997272; Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
DR   Proteomes; UP000002254; Chromosome 9.
DR   Bgee; ENSCAFG00000010736; Expressed in 3 organ(s), highest expression level in liver.
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; IBA:GO_Central.
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: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   Complete proteome; Ion channel; Ion transport; Lipoprotein; Membrane;
KW   Myristate; Potassium; Potassium transport; Reference proteome;
KW   S-nitrosylation; Transmembrane; Transmembrane helix; Transport;
KW   Voltage-gated channel.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    427       Inward rectifier potassium channel 2.
FT                                /FTId=PRO_0000154921.
FT   TOPO_DOM      2     81       Cytoplasmic. {ECO:0000250}.
FT   TRANSMEM     82    106       Helical; Name=M1. {ECO:0000250}.
FT   TOPO_DOM    107    128       Extracellular. {ECO:0000250}.
FT   INTRAMEM    129    140       Helical; Pore-forming; Name=H5.
FT                                {ECO:0000250}.
FT   INTRAMEM    141    147       Pore-forming. {ECO:0000250}.
FT   TOPO_DOM    148    156       Extracellular. {ECO:0000250}.
FT   TRANSMEM    157    178       Helical; Name=M2. {ECO:0000250}.
FT   TOPO_DOM    179    427       Cytoplasmic. {ECO:0000250}.
FT   MOTIF       142    147       Selectivity filter. {ECO:0000250}.
FT   MOTIF       425    427       PDZ-binding. {ECO:0000255}.
FT   SITE        172    172       Role in the control of polyamine-mediated
FT                                channel gating and in the blocking by
FT                                intracellular magnesium. {ECO:0000250}.
FT   MOD_RES      76     76       S-nitrosocysteine.
FT                                {ECO:0000250|UniProtKB:P63252}.
FT   LIPID         2      2       N-myristoyl glycine.
FT                                {ECO:0000250|UniProtKB:P63252}.
SQ   SEQUENCE   427 AA;  48304 MW;  C7519AD5EBC9ED8D CRC64;
     MGSVRTNRYS IVSSEEDGMK LATMAVANGF GNGKSKVHTR QQCRSRFVKK DGHCNVQFIN
     VGEKGQRYLA DIFTTCVDIR WRWMLVIFCL AFVLSWLFFG CVFWLIALLH GDLDASKESK
     ACVSEVNSFT AAFLFSIETQ TTIGYGFRCV TDECPVAVFM VVFQSIVGCI IDAFIIGAVM
     AKMAKPKKRN ETLVFSHNAV IAMRDGKLCL MWRVGNLRKS HLVEAHVRAQ LLKSRITSEG
     EYIPLDQIDI NVGFDSGIDR IFLVSPITIV HEIDEDSPLY DLSKQDIDNA DFEIVVILEG
     MVEATAMTTQ CRSSYLANEI LWGHRYEPVL FEEKHYYKVD YSRFHKTYEV PNTPLCSARD
     LAEKKYILSN ANSFCYENEV ALTSKEEDDS ENGVPESTST DTPPDLDLHN QASVPLEPRP
     LRRESEI
//
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