ID   KCJ12_RAT               Reviewed;         427 AA.
AC   P52188;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   24-JAN-2024, entry version 162.
DE   RecName: Full=ATP-sensitive inward rectifier potassium channel 12;
DE   AltName: Full=Inward rectifier K(+) channel Kir2.2;
DE            Short=IRK-2;
DE   AltName: Full=Potassium channel, inwardly rectifying subfamily J member 12;
GN   Name=Kcnj12; Synonyms=Irk2;
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], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Brain;
RX   PubMed=8137958; DOI=10.1016/0014-5793(94)80478-8;
RA   Koyama H., Morishige K., Takahashi N., Zanelli J.S., Fass D.N., Kurachi Y.;
RT   "Molecular cloning, functional expression and localization of a novel
RT   inward rectifier potassium channel in the rat brain.";
RL   FEBS Lett. 341:303-307(1994).
RN   [2]
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: Inward rectifying potassium channel that is activated by
CC       phosphatidylinositol 4,5-bisphosphate and that probably participates in
CC       controlling the resting membrane potential in electrically excitable
CC       cells. Probably participates in establishing action potential waveform
CC       and excitability of neuronal and muscle tissues. Inward rectifier
CC       potassium channels are characterized by a greater tendency to allow
CC       potassium to flow into the cell rather than out of it. Their voltage
CC       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. {ECO:0000269|PubMed:14960569,
CC       ECO:0000269|PubMed:8137958}.
CC   -!- SUBUNIT: Homotetramer. Forms heteromer with KCNJ4. Association, via its
CC       PDZ-recognition domain, with LIN7A, LIN7B, LIN7C, DLG1, CASK and APBA1
CC       plays a key role in its localization and trafficking.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:8137958}; Multi-pass
CC       membrane protein {ECO:0000269|PubMed:8137958}. Cell membrane
CC       {ECO:0000269|PubMed:8137958}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:8137958}.
CC   -!- TISSUE SPECIFICITY: Highest level in cerebellum. Moderately found in
CC       kidney, forebrain and skeletal muscle. Not detected in uterus, liver
CC       and pancreas. {ECO:0000269|PubMed:8137958}.
CC   -!- DOMAIN: Phosphatidylinositol 4,5-bisphosphate binding to the
CC       cytoplasmic side of the channel triggers a conformation change leading
CC       to channel opening. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the inward rectifier-type potassium channel
CC       (TC 1.A.2.1) family. KCNJ12 subfamily. {ECO:0000305}.
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DR   EMBL; X78461; CAA55216.1; -; mRNA.
DR   PIR; S43667; S43667.
DR   AlphaFoldDB; P52188; -.
DR   SMR; P52188; -.
DR   CORUM; P52188; -.
DR   IntAct; P52188; 8.
DR   MINT; P52188; -.
DR   STRING; 10116.ENSRNOP00000054762; -.
DR   GuidetoPHARMACOLOGY; 431; -.
DR   iPTMnet; P52188; -.
DR   PhosphoSitePlus; P52188; -.
DR   PaxDb; 10116-ENSRNOP00000054762; -.
DR   ABCD; P52188; 1 sequenced antibody.
DR   UCSC; RGD:621660; rat.
DR   AGR; RGD:621660; -.
DR   RGD; 621660; Kcnj12.
DR   eggNOG; KOG3827; Eukaryota.
DR   InParanoid; P52188; -.
DR   PhylomeDB; P52188; -.
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:P52188; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0030425; C:dendrite; IDA:RGD.
DR   GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR   GO; GO:0034702; C:monoatomic ion channel complex; IEA:UniProtKB-KW.
DR   GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0030315; C:T-tubule; IDA:RGD.
DR   GO; GO:0005242; F:inward rectifier potassium channel activity; ISS:UniProtKB.
DR   GO; GO:0030165; F:PDZ domain binding; IPI:RGD.
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:0034765; P:regulation of monoatomic ion transmembrane transport; IBA:GO_Central.
DR   Gene3D; 1.10.287.70; -; 1.
DR   Gene3D; 2.60.40.1400; G protein-activated inward rectifier potassium channel 1; 1.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR041647; IRK_C.
DR   InterPro; IPR016449; K_chnl_inward-rec_Kir.
DR   InterPro; IPR003272; K_chnl_inward-rec_Kir2.2.
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:SF14; ATP-SENSITIVE INWARD RECTIFIER POTASSIUM CHANNEL 12-RELATED; 1.
DR   PANTHER; PTHR11767; INWARD RECTIFIER POTASSIUM CHANNEL; 1.
DR   Pfam; PF01007; IRK; 1.
DR   Pfam; PF17655; IRK_C; 1.
DR   Pfam; PF08466; IRK_N; 1.
DR   PRINTS; PR01325; KIR22CHANNEL.
DR   PRINTS; PR01320; KIRCHANNEL.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Disulfide bond; Ion channel; Ion transport; Membrane;
KW   Potassium; Potassium transport; Reference proteome; S-nitrosylation;
KW   Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN           1..427
FT                   /note="ATP-sensitive inward rectifier potassium channel 12"
FT                   /id="PRO_0000154964"
FT   TOPO_DOM        1..82
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        83..107
FT                   /note="Helical; Name=M1"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        108..123
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   INTRAMEM        124..128
FT                   /evidence="ECO:0000250"
FT   INTRAMEM        129..141
FT                   /note="Helical; Pore-forming; Name=H5"
FT                   /evidence="ECO:0000250"
FT   INTRAMEM        142..151
FT                   /note="Pore-forming"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        152..156
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        157..181
FT                   /note="Helical; Name=M2"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        182..427
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   REGION          387..427
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           79..81
FT                   /note="Interaction with phosphatidylinositides"
FT                   /evidence="ECO:0000250"
FT   MOTIF           143..148
FT                   /note="Selectivity filter"
FT                   /evidence="ECO:0000250"
FT   MOTIF           183..190
FT                   /note="Interaction with phosphatidylinositides"
FT                   /evidence="ECO:0000250"
FT   MOTIF           425..427
FT                   /note="PDZ-binding"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        387..406
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            173
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         75
FT                   /note="S-nitrosocysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P63252"
FT   DISULFID        155
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   427 AA;  48399 MW;  6FA100FEB6066677 CRC64;
     MTAASRANPY SIVSSEEDGL HLVTMSGANG FGNGKVHTRR RCRNRFVKKN GQCNIEFANM
     DEKSQRYLAD MFTTCVDIRW RYMLLIFSLA FLASWLLFGI IFWVIAVAHG DLEPAEGRGR
     TPCVLQVHGF MAAFLFSIET QTTIGYGLRC VTEECPVAVF MVVAQSIVGC IIDSFMIGAI
     MAKMGRPKKR AQTLLFSHNA VVALRDGKLC LMWRVGNLRK SHIVEAHVRA QLIKPRVTEE
     GEYIPLDQID IDVGFDKGLD RIFLVSPITI LHEIDEASPL FGISRQDLET DDFEIVVILE
     GMVEATAMTT QARSSYLANE ILWGHRFEPV LFEEKNQYKI DYSHFHKTYE VPSTPRCSAK
     DLVENKFLLP SANSFCYENE LAFLSRDEED EVATDRDGRS PQPEHDFDRL QASSGALERP
     YRRESEI
//