KCNJ4_MOUSE
ID KCNJ4_MOUSE Reviewed; 445 AA.
AC P52189;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 151.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=8013643; DOI=10.1016/0014-5793(94)00483-8;
RA Morishige K., Takahashi N., Jahangir A., Yamada M., Koyama H.,
RA Zanelli J.S., Kurachi Y.;
RT "Molecular cloning and functional expression of a novel brain-specific
RT inward rectifier potassium channel.";
RL FEBS Lett. 346:251-256(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=7926018; DOI=10.1016/0014-5793(94)01007-2;
RA Lesage F., Duprat F., Fink M., Guillemare E., Coppola T., Lazdunski M.,
RA Hugnot J.-P.;
RT "Cloning provides evidence for a family of inward rectifier and G-protein
RT coupled K+ channels in the brain.";
RL FEBS Lett. 353:37-42(1994).
RN [3]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH DLG2 AND
RP DLG4.
RX PubMed=11997254; DOI=10.1152/ajpcell.00615.2001;
RA Inanobe A., Fujita A., Ito M., Tomoike H., Inageda K., Kurachi Y.;
RT "Inward rectifier K+ channel Kir2.3 is localized at the postsynaptic
RT membrane of excitatory synapses.";
RL Am. J. Physiol. 282:C1396-C1403(2002).
RN [4]
RP INTERACTION WITH TAX1BP3 AND LIN7A, SUBCELLULAR LOCATION, AND MUTAGENESIS
RP OF 442-GLU--ARG-444; GLU-442; SER-443 AND ILE-445.
RX PubMed=16855024; DOI=10.1091/mbc.e06-02-0129;
RA Alewine C., Olsen O., Wade J.B., Welling P.A.;
RT "TIP-1 has PDZ scaffold antagonist activity.";
RL Mol. Biol. Cell 17:4200-4211(2006).
CC -!- FUNCTION: Inward rectifier potassium channels are characterized by a
CC greater tendency to allow potassium to flow into the cell rather than
CC out 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 voltages.
CC The inward rectification is mainly due to the blockage of outward
CC current by internal magnesium. Can be blocked by extracellular barium
CC and cesium (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homomultimeric and heteromultimeric association with KCNJ2 and
CC KCNJ12. Association, via its PDZ-recognition domain, with LIN7A, LIN7B,
CC LIN7C, DLG1, DLG2, DLG4, CASK and APBA1 plays a key role in its
CC localization and trafficking (By similarity). Interacts with TAX1BP3.
CC TAX1BP3 competes with LIN7 family members for KCNJ4 binding.
CC {ECO:0000250, ECO:0000269|PubMed:11997254,
CC ECO:0000269|PubMed:16855024}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC Postsynaptic cell membrane; Multi-pass membrane protein. Cytoplasmic
CC vesicle membrane. Note=TAX1BP3 binding promotes dissociation of KCNJ4
CC from LIN7 family members and KCNJ4 internalization.
CC -!- TISSUE SPECIFICITY: Highly expressed in the forebrain, moderately in
CC skeletal muscle. Im olfactory bulb, specifically expressed at the
CC postsynaptic membrane of dendritic spines of granule cells.
CC {ECO:0000269|PubMed:11997254}.
CC -!- DEVELOPMENTAL STAGE: Expression increases between day 2 to 45 and is
CC then stable from day 45 to 120.
CC -!- SIMILARITY: Belongs to the inward rectifier-type potassium channel (TC
CC 1.A.2.1) family. KCNJ4 subfamily. {ECO:0000305}.
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DR EMBL; U11075; AAA53241.1; -; mRNA.
DR EMBL; S71382; AAB31087.1; -; mRNA.
DR CCDS; CCDS27641.1; -.
DR PIR; S45713; S45713.
DR AlphaFoldDB; P52189; -.
DR SMR; P52189; -.
DR IntAct; P52189; 4.
DR MINT; P52189; -.
DR STRING; 10090.ENSMUSP00000094075; -.
DR GuidetoPHARMACOLOGY; 432; -.
DR iPTMnet; P52189; -.
DR PhosphoSitePlus; P52189; -.
DR SwissPalm; P52189; -.
DR PaxDb; P52189; -.
DR PeptideAtlas; P52189; -.
DR PRIDE; P52189; -.
DR ProteomicsDB; 263402; -.
DR MGI; MGI:104743; Kcnj4.
DR eggNOG; KOG3827; Eukaryota.
DR InParanoid; P52189; -.
DR PhylomeDB; P52189; -.
DR Reactome; R-MMU-1296041; Activation of G protein gated Potassium channels.
DR Reactome; R-MMU-1296053; Classical Kir channels.
DR Reactome; R-MMU-5576886; Phase 4 - resting membrane potential.
DR Reactome; R-MMU-997272; Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
DR PRO; PR:P52189; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P52189; protein.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005242; F:inward rectifier potassium channel activity; IBA:GO_Central.
DR GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; IBA:GO_Central.
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; 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 1: Evidence at protein level;
KW Cell membrane; Cytoplasmic vesicle; Ion channel; Ion transport; Membrane;
KW Postsynaptic cell membrane; Potassium; Potassium transport;
KW Reference proteome; Synapse; Transmembrane; Transmembrane helix; Transport;
KW Voltage-gated channel.
FT CHAIN 1..445
FT /note="Inward rectifier potassium channel 4"
FT /id="PRO_0000154932"
FT TOPO_DOM 1..55
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 56..80
FT /note="Helical; Name=M1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 81..119
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT INTRAMEM 120..131
FT /note="Helical; Pore-forming; Name=H5"
FT /evidence="ECO:0000250"
FT INTRAMEM 132..138
FT /note="Pore-forming"
FT /evidence="ECO:0000250"
FT TOPO_DOM 139..147
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 148..169
FT /note="Helical; Name=M2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 170..445
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT MOTIF 133..138
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT MOTIF 443..445
FT /note="PDZ-binding"
FT /evidence="ECO:0000255"
FT SITE 163
FT /note="Role in the control of polyamine-mediated channel
FT gating and in the blocking by intracellular magnesium"
FT /evidence="ECO:0000250"
FT MUTAGEN 442..444
FT /note="ESR->AAA: Abolishes interaction with TAX1BP3."
FT /evidence="ECO:0000269|PubMed:16855024"
FT MUTAGEN 442
FT /note="E->A: Abolishes interaction with TAX1BP3."
FT /evidence="ECO:0000269|PubMed:16855024"
FT MUTAGEN 443
FT /note="S->A,D: Abolishes interaction with TAX1BP3."
FT /evidence="ECO:0000269|PubMed:16855024"
FT MUTAGEN 445
FT /note="I->A: Abolishes interaction with TAX1BP3."
FT /evidence="ECO:0000269|PubMed:16855024"
FT CONFLICT 79
FT /note="W -> C (in Ref. 2; AAA53241)"
FT /evidence="ECO:0000305"
FT CONFLICT 86
FT /note="D -> E (in Ref. 2; AAA53241)"
FT /evidence="ECO:0000305"
FT CONFLICT 96
FT /note="V -> A (in Ref. 2; AAA53241)"
FT /evidence="ECO:0000305"
FT CONFLICT 105
FT /note="E -> A (in Ref. 2; AAA53241)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="R -> G (in Ref. 2; AAA53241)"
FT /evidence="ECO:0000305"
FT CONFLICT 444
FT /note="R -> A (in Ref. 2; AAA53241)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 445 AA; 49899 MW; 09C9E889CC8E0DF3 CRC64;
MHGHNRNGQA HVPRRKRRNR FVKKNGQCNV YFANLSNKSQ RYMADIFTTC VDTRWRYMLM
IFSAAFLVSW LFFGLLFWWI AFFHGDLEAS PSVPAVGGPG GNGGESPNAP 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
PAPPPPPSAF CYENELALMS QEEEEMEEEA AAAAAVAAGL GLEAGSKEEA GIIRMLEFGS
HLDLERMQAA TLPLDNISYR RESRI
