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Database: UniProt
Entry: KCNJ2_CAVPO
LinkDB: KCNJ2_CAVPO
Original site: 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   11-DEC-2019, entry version 136.
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}.
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   SMR; P52185; -.
DR   STRING; 10141.ENSCPOP00000016364; -.
DR   PRIDE; P52185; -.
DR   Ensembl; ENSCPOT00000034075; ENSCPOP00000031029; ENSCPOG00000004956.
DR   GeneID; 100135566; -.
DR   CTD; 3759; -.
DR   eggNOG; KOG3827; Eukaryota.
DR   eggNOG; ENOG410XQ62; LUCA.
DR   GeneTree; ENSGT00960000186595; -.
DR   HOGENOM; HOG000237325; -.
DR   InParanoid; P52185; -.
DR   OMA; KVHTRHQ; -.
DR   OrthoDB; 956263at2759; -.
DR   TreeFam; TF313676; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   Bgee; ENSCPOG00000004956; Expressed in 3 organ(s), highest expression level in adult mammalian kidney.
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: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   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
//
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