KCNJ4_RAT
ID KCNJ4_RAT Reviewed; 446 AA.
AC P52190; O35752;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Inward rectifier potassium channel 4;
DE AltName: Full=BIR11;
DE AltName: Full=Brain inwardly rectifying K(+) channel 2;
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 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].
RC STRAIN=GH3/B6;
RX PubMed=7796907; DOI=10.1016/0014-5793(95)00527-g;
RA Falk T., Meyerhof W., Corrette B.J., Schaefer J., Bauer C.K., Schwarz J.R.,
RA Richter D.;
RT "Cloning, functional expression and mRNA distribution of an inwardly
RT rectifying potassium channel protein.";
RL FEBS Lett. 367:127-131(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=7874445;
RA Bond C.T., Pessia M., Xia X.-M., Lagrutta A., Kavanaugh M.P., Adelman J.P.;
RT "Cloning and expression of a family of inward rectifier potassium
RT channels.";
RL Recept. Channels 2:183-191(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7624316; DOI=10.1073/pnas.92.15.6753;
RA Bredt D.S., Wang T.L., Cohen N.A., Guggino W.B., Snyder S.H.;
RT "Cloning and expression of two brain-specific inwardly rectifying potassium
RT channels.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:6753-6757(1995).
RN [4]
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).
RN [5]
RP TISSUE SPECIFICITY.
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, ECO:0000269|PubMed:14960569}.
CC -!- SUBUNIT: Homomultimeric and heteromultimeric association with KCNJ2 and
CC KCNJ12. Association, via its PDZ-recognition domain, with LIN7A, LIN7B,
CC LIN7C, DLG1, CASK and APBA1 plays a key role in its localization and
CC trafficking. Interacts with TAX1BP3. TAX1BP3 competes with LIN7 family
CC members for KCNJ4 binding. {ECO:0000269|PubMed:14960569}.
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 -!- TISSUE SPECIFICITY: Detected in kidney distal convoluted tubules (at
CC protein level). Widely expressed throughout the brain. Also found in
CC some peripheral tissues. {ECO:0000269|PubMed:16855024}.
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; X87635; CAA60963.1; -; mRNA.
DR EMBL; X83580; CAA58563.1; -; mRNA.
DR EMBL; U27582; AAA87812.1; -; mRNA.
DR PIR; S66268; S66268.
DR RefSeq; NP_446322.2; NM_053870.2.
DR AlphaFoldDB; P52190; -.
DR SMR; P52190; -.
DR STRING; 10116.ENSRNOP00000053014; -.
DR iPTMnet; P52190; -.
DR PhosphoSitePlus; P52190; -.
DR PaxDb; P52190; -.
DR PRIDE; P52190; -.
DR GeneID; 116649; -.
DR KEGG; rno:116649; -.
DR UCSC; RGD:621436; rat.
DR CTD; 3761; -.
DR RGD; 621436; Kcnj4.
DR eggNOG; KOG3827; Eukaryota.
DR InParanoid; P52190; -.
DR PhylomeDB; P52190; -.
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:P52190; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:RGD.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; 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: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:RGD.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:RGD.
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..446
FT /note="Inward rectifier potassium channel 4"
FT /id="PRO_0000154933"
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..120
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT INTRAMEM 121..132
FT /note="Helical; Pore-forming; Name=H5"
FT /evidence="ECO:0000250"
FT INTRAMEM 133..139
FT /note="Pore-forming"
FT /evidence="ECO:0000250"
FT TOPO_DOM 140..148
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 149..170
FT /note="Helical; Name=M2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 171..446
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 91..111
FT /note="Val/Gly/Ala/Pro stretch"
FT MOTIF 134..139
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT MOTIF 444..446
FT /note="PDZ-binding"
FT /evidence="ECO:0000255"
FT SITE 164
FT /note="Role in the control of polyamine-mediated channel
FT gating and in the blocking by intracellular magnesium"
FT /evidence="ECO:0000250"
FT CONFLICT 53..54
FT /note="Missing (in Ref. 3; AAA87812)"
FT /evidence="ECO:0000305"
FT CONFLICT 91..98
FT /note="PSGPTAGG -> LRAHGGS (in Ref. 3; AAA87812)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="T -> R (in Ref. 3; AAA87812)"
FT /evidence="ECO:0000305"
FT CONFLICT 115..122
FT /note="IMHVNGFL -> YHACKRLFW (in Ref. 3; AAA87812)"
FT /evidence="ECO:0000305"
FT CONFLICT 130..131
FT /note="ET -> GA (in Ref. 3; AAA87812)"
FT /evidence="ECO:0000305"
FT CONFLICT 135
FT /note="I -> Y (in Ref. 3; AAA87812)"
FT /evidence="ECO:0000305"
FT CONFLICT 155
FT /note="Missing (in Ref. 3; AAA87812)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="P -> A (in Ref. 3; AAA87812)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="P -> G (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 178
FT /note="P -> S (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 197..198
FT /note="DG -> T (in Ref. 3; AAA87812)"
FT /evidence="ECO:0000305"
FT CONFLICT 205..207
FT /note="RVG -> GWV (in Ref. 3; AAA87812)"
FT /evidence="ECO:0000305"
FT CONFLICT 294
FT /note="V -> A (in Ref. 3; AAA87812)"
FT /evidence="ECO:0000305"
FT CONFLICT 298
FT /note="A -> V (in Ref. 2; CAA60963)"
FT /evidence="ECO:0000305"
FT CONFLICT 308
FT /note="L -> Q (in Ref. 3; AAA87812)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 446 AA; 49690 MW; A86073996861D20C CRC64;
MHGHSRNGQA HVPRRKRRNR FVKKNGQCNV YFANLSNKSQ RYMADIFTTC VDTRWRYMLM
IFSAAFLVSW LFFGLLFWCI AFFHGDLEPS PSGPTAGGPG GNGGGAAPTA AKPCIMHVNG
FLGAFLFSVE TQTTIGYGFR CVTEECPLAV IAVVVQSIVG CVIDSFMIGT IMAKMPRPKK
RAQTLLFSHH AVISVRDGKL CLMWRVGNLR KSHIVEAHVR AQLIKPYMTQ EGEYLPLDQR
DLNVGYDIGL DRIFLVSPII IVHEIDEDSP LYGMGKEELE SEDFEIVVIL EGMVEATAMT
TQARSSYLAS EILWGHRFEP VVFEEKSHYK VDYSRFHKTY EVAGTPCCSA RELQESKITV
LPAPPPPPSA FCYENELALM SQEEEEMEEE AAAAAAVAAG LGLEAGSKEE TGIIRMLEFG
SHLDLERMQA ATLPLDNISY RRESAI
