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Database: UniProt
Entry: KCNJ4_MESAU
LinkDB: KCNJ4_MESAU
Original site: KCNJ4_MESAU 
ID   KCNJ4_MESAU             Reviewed;         444 AA.
AC   Q64198;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   13-NOV-2019, entry version 106.
DE   RecName: Full=Inward rectifier potassium channel 4;
DE   AltName: Full=Inward rectifier K(+) channel Kir2.3;
DE            Short=IRK-3;
DE   AltName: Full=Potassium channel, inwardly rectifying subfamily J member 4;
GN   Name=KCNJ4; Synonyms=IRK3;
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Insulinoma;
RX   PubMed=8613774; DOI=10.1523/jneurosci.16-01-00001.1996;
RA   Collins A., German M.S., Jan Y.N., Jan L.Y., Zhao B.;
RT   "A strongly inwardly rectifying K+ channel that is sensitive to ATP.";
RL   J. Neurosci. 16:1-9(1996).
CC   -!- FUNCTION: Inward rectifier potassium channels are characterized by
CC       a greater tendency to allow potassium to flow into the cell rather
CC       than out of it. Their voltage dependence is regulated by the
CC       concentration of extracellular potassium; as external potassium is
CC       raised, the voltage range of the channel opening shifts to more
CC       positive voltages. The inward rectification is mainly due to the
CC       blockage of outward current by internal magnesium (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homomultimeric and heteromultimeric association with
CC       KCNJ2, resulting in an enhanced G-protein-induced current.
CC       Association, via its PDZ-recognition domain, with LIN7A, LIN7B,
CC       LIN7C, DLG1, CASK and APBA1 plays a key role in its localization
CC       and trafficking (By similarity). May also associate with GIRK1 or
CC       GIRK4 to form a G-protein-activated heteromultimer pore-forming
CC       unit. The resulting inward current is much larger. Interacts with
CC       TAX1BP3. TAX1BP3 competes with LIN7 family members for KCNJ4
CC       binding (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC       Cytoplasmic vesicle membrane {ECO:0000250}. Cell junction,
CC       synapse, postsynaptic cell membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}. Note=TAX1BP3 binding promotes
CC       dissociation of KCNJ4 from LIN7 famaly members and KCNJ4
CC       internalization. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the inward rectifier-type potassium channel
CC       (TC 1.A.2.1) family. KCNJ4 subfamily. {ECO:0000305}.
DR   EMBL; S81773; AAB36376.1; -; mRNA.
DR   SMR; Q64198; -.
DR   STRING; 10036.XP_005066905.1; -.
DR   Proteomes; UP000189706; Genome assembly.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005242; F:inward rectifier potassium channel activity; IEA:InterPro.
DR   GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
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; IPR003273; K_chnl_inward-rec_Kir2.3.
DR   InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR   InterPro; IPR040445; Kir_TM.
DR   PANTHER; PTHR11767; PTHR11767; 1.
DR   PANTHER; PTHR11767:SF53; PTHR11767:SF53; 1.
DR   Pfam; PF01007; IRK; 1.
DR   Pfam; PF17655; IRK_C; 1.
DR   PIRSF; PIRSF005465; GIRK_kir; 1.
DR   PRINTS; PR01326; KIR23CHANNEL.
DR   PRINTS; PR01320; KIRCHANNEL.
DR   SUPFAM; SSF81296; SSF81296; 1.
PE   2: Evidence at transcript level;
KW   Cell junction; Cell membrane; Complete proteome; Cytoplasmic vesicle;
KW   Ion channel; Ion transport; Membrane; Postsynaptic cell membrane;
KW   Potassium; Potassium transport; Reference proteome; Synapse;
KW   Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN         1    444       Inward rectifier potassium channel 4.
FT                                /FTId=PRO_0000154931.
FT   TOPO_DOM      1     55       Cytoplasmic. {ECO:0000250}.
FT   TRANSMEM     56     80       Helical; Name=M1. {ECO:0000250}.
FT   TOPO_DOM     81    119       Extracellular. {ECO:0000250}.
FT   INTRAMEM    120    131       Helical; Pore-forming; Name=H5.
FT                                {ECO:0000250}.
FT   INTRAMEM    132    138       Pore-forming. {ECO:0000250}.
FT   TOPO_DOM    139    147       Extracellular. {ECO:0000250}.
FT   TRANSMEM    148    169       Helical; Name=M2. {ECO:0000250}.
FT   TOPO_DOM    170    444       Cytoplasmic. {ECO:0000250}.
FT   MOTIF       133    138       Selectivity filter. {ECO:0000250}.
FT   MOTIF       442    444       PDZ-binding. {ECO:0000255}.
FT   COMPBIAS    361    366       Poly-Pro.
FT   COMPBIAS    382    389       Poly-Glu.
FT   COMPBIAS    390    398       Poly-Ala.
FT   SITE        163    163       Role in the control of polyamine-mediated
FT                                channel gating and in the blocking by
FT                                intracellular magnesium. {ECO:0000250}.
SQ   SEQUENCE   444 AA;  49584 MW;  14B0DAD4AC2A3DD8 CRC64;
     MHGHNRNGQA HVPRRKRRNR FVKKNGQCNV YFANLSNKSQ RYMADIFTTC VDTRWRYMLM
     LFSAAFLVSW LFFGLLFWCI AFFHGDLEAS PSVPAAGAPG GNGGAAPAAP KPCIMHVNGF
     LGAFLFSVET QTTIGYGFRC VTEECPLAVI AVVVQSIVGC VIDSFMIGTI MAKMARPKKR
     AQTLLFSHHA VISVRDGKLC LMWRVGNLRK SHIVEAHVRA QLIKPYMTQE GEYLPLDQRD
     LNVGYDIGLD RIFLVSPIII VHEIDEDSPL YGMGKEELES EDFEIVVILE GMVEATAMTT
     QARSSYLASE ILWGHRFEPV VFEEKSHYKV DYSRFHKTYE VAGTPCCSAR ELQESKITVL
     PAPPPPRSAF CYENELALMS QEEEEMEEEA AAAAAVAAGL GLEAGPKEEA GIIRMLEFGS
     HLDLERMQGT LPLDNISYRR ESAI
//
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