位置:首页 > 蛋白库 > KCJ12_BOVIN
KCJ12_BOVIN
ID   KCJ12_BOVIN             Reviewed;         427 AA.
AC   Q4TZY1;
DT   11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=ATP-sensitive inward rectifier potassium channel 12;
DE   AltName: Full=Potassium channel, inwardly rectifying subfamily J member 12;
GN   Name=KCNJ12;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Corneal endothelium;
RA   Rae J.L.;
RT   "Ion channels in ocular epithelia.";
RL   Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}. Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
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 (TC
CC       1.A.2.1) family. KCNJ12 subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DQ023214; AAY53910.1; -; mRNA.
DR   RefSeq; XP_005220652.1; XM_005220595.3.
DR   AlphaFoldDB; Q4TZY1; -.
DR   SMR; Q4TZY1; -.
DR   STRING; 9913.ENSBTAP00000056563; -.
DR   PaxDb; Q4TZY1; -.
DR   Ensembl; ENSBTAT00000026726; ENSBTAP00000056563; ENSBTAG00000020061.
DR   GeneID; 538479; -.
DR   CTD; 3768; -.
DR   VEuPathDB; HostDB:ENSBTAG00000020061; -.
DR   eggNOG; KOG3827; Eukaryota.
DR   GeneTree; ENSGT01030000234586; -.
DR   InParanoid; Q4TZY1; -.
DR   OMA; MHGMNGF; -.
DR   Proteomes; UP000009136; Chromosome 19.
DR   Bgee; ENSBTAG00000020061; Expressed in choroid plexus and 64 other tissues.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031224; C:intrinsic component of membrane; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005242; F:inward rectifier potassium channel activity; ISS:UniProtKB.
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 ion transmembrane transport; IBA:GO_Central.
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; 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; PTHR11767; 1.
DR   PANTHER; PTHR11767:SF14; PTHR11767:SF14; 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; SSF81296; 1.
PE   2: Evidence at transcript 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_0000154961"
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   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;  48442 MW;  B41DC759912A088F CRC64;
     MTASGRTNPY SIVSSEEDGL HLVTMSGANG FGNGKVHTRR RCRNRFVKKN GQCNIEFANM
     DEKSQRYLAD MFTTCVDIRW RYMLLIFSLA FLASWLLFGV IFWVIAVAHG DLEPAEAHGR
     TPCVLQVHGF MAAFLFSIET QTTIGYGLRC VTEECPVAVF MVVAQSIVGC IIDSFMIGAI
     MAKMARPKKR AQTLLFSHNA VVALRDGKLC LMWRVGNLRK SHIVEAHVRA QLIKPRVTEE
     GEYIPLDQID IDVGFDKGLD RIFLVSPITI LHEIDEASPL FGISRQDLET DDFEIVVILE
     GMVEATAMTT QARSSYLANE ILWGHRFEPV LFEEKNQYKI DYSHFHKTYE VPSTPRCSAK
     DLVENKFLLP STNSFCYENE LAFLSRDEED EVDGEQDSLG PQARRDFDRP QAGTALEQRP
     YRRESEI
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024