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 03-AUG-2022, entry version 112.
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC 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 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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homomultimeric and heteromultimeric association with KCNJ2,
CC resulting in an enhanced G-protein-induced current. Association, via
CC its PDZ-recognition domain, with LIN7A, LIN7B, LIN7C, DLG1, CASK and
CC APBA1 plays a key role in its localization and trafficking (By
CC similarity). May also associate with GIRK1 or GIRK4 to form a G-
CC protein-activated heteromultimer pore-forming unit. The resulting
CC inward current is much larger. Interacts with TAX1BP3. TAX1BP3 competes
CC with LIN7 family members for KCNJ4 binding (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC Cytoplasmic vesicle membrane {ECO:0000250}. Postsynaptic cell membrane
CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=TAX1BP3
CC binding promotes dissociation of KCNJ4 from LIN7 famaly members and
CC KCNJ4 internalization. {ECO:0000250}.
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; S81773; AAB36376.1; -; mRNA.
DR AlphaFoldDB; Q64198; -.
DR SMR; Q64198; -.
DR STRING; 10036.XP_005066905.1; -.
DR eggNOG; KOG3827; Eukaryota.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0070161; C:anchoring 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 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..444
FT /note="Inward rectifier potassium channel 4"
FT /id="PRO_0000154931"
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..444
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT MOTIF 133..138
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT MOTIF 442..444
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"
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
