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Inward rectifier potassium channel 4 (BIR11) (Brain inwardly rectifying K( ) channel 2) (Inward rectifier K( ) channel Kir2.3) (IRK-3) (Potassium channel, inwardly rectifying subfamily J member 4)

 KCNJ4_RAT               Reviewed;         446 AA.
P52190; O35752;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
22-NOV-2017, entry version 136.
RecName: Full=Inward rectifier potassium channel 4;
AltName: Full=BIR11;
AltName: Full=Brain inwardly rectifying K(+) channel 2;
AltName: Full=Inward rectifier K(+) channel Kir2.3;
Short=IRK-3;
AltName: Full=Potassium channel, inwardly rectifying subfamily J member 4;
Name=Kcnj4; Synonyms=Irk3;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=GH3/B6;
PubMed=7796907; DOI=10.1016/0014-5793(95)00527-G;
Falk T., Meyerhof W., Corrette B.J., Schaefer J., Bauer C.K.,
Schwarz J.R., Richter D.;
"Cloning, functional expression and mRNA distribution of an inwardly
rectifying potassium channel protein.";
FEBS Lett. 367:127-131(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Brain;
PubMed=7874445;
Bond C.T., Pessia M., Xia X.-M., Lagrutta A., Kavanaugh M.P.,
Adelman J.P.;
"Cloning and expression of a family of inward rectifier potassium
channels.";
Recept. Channels 2:183-191(1994).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7624316; DOI=10.1073/pnas.92.15.6753;
Bredt D.S., Wang T.L., Cohen N.A., Guggino W.B., Snyder S.H.;
"Cloning and expression of two brain-specific inwardly rectifying
potassium channels.";
Proc. Natl. Acad. Sci. U.S.A. 92:6753-6757(1995).
[4]
INTERACTION WITH CASK; LIN7A; LIN7B; LIN7C; APBA1 AND DLG1, AND
FUNCTION.
PubMed=14960569; DOI=10.1074/jbc.M400284200;
Leonoudakis D., Conti L.R., Radeke C.M., McGuire L.M.,
Vandenberg C.A.;
"A multiprotein trafficking complex composed of SAP97, CASK, Veli, and
Mint1 is associated with inward rectifier Kir2 potassium channels.";
J. Biol. Chem. 279:19051-19063(2004).
[5]
TISSUE SPECIFICITY.
PubMed=16855024; DOI=10.1091/mbc.E06-02-0129;
Alewine C., Olsen O., Wade J.B., Welling P.A.;
"TIP-1 has PDZ scaffold antagonist activity.";
Mol. Biol. Cell 17:4200-4211(2006).
-!- FUNCTION: Inward rectifier potassium channels are characterized by
a greater tendency to allow potassium to flow into the cell rather
than out of it. Their voltage dependence is regulated by the
concentration of extracellular potassium; as external potassium is
raised, the voltage range of the channel opening shifts to more
positive voltages. The inward rectification is mainly due to the
blockage of outward current by internal magnesium. Can be blocked
by extracellular barium and cesium (By similarity). {ECO:0000250,
ECO:0000269|PubMed:14960569}.
-!- SUBUNIT: Homomultimeric and heteromultimeric association with
KCNJ2 and KCNJ12. Association, via its PDZ-recognition domain,
with LIN7A, LIN7B, LIN7C, DLG1, CASK and APBA1 plays a key role in
its localization and trafficking. Interacts with TAX1BP3. TAX1BP3
competes with LIN7 family members for KCNJ4 binding.
{ECO:0000269|PubMed:14960569}.
-!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
Cytoplasmic vesicle membrane {ECO:0000250}. Cell junction,
synapse, postsynaptic cell membrane {ECO:0000250}; Multi-pass
membrane protein {ECO:0000250}. Note=TAX1BP3 binding promotes
dissociation of KCNJ4 from LIN7 famaly members and KCNJ4
internalization. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Detected in kidney distal convoluted tubules
(at protein level). Widely expressed throughout the brain. Also
found in some peripheral tissues. {ECO:0000269|PubMed:16855024}.
-!- SIMILARITY: Belongs to the inward rectifier-type potassium channel
(TC 1.A.2.1) family. KCNJ4 subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X87635; CAA60963.1; -; mRNA.
EMBL; X83580; CAA58563.1; -; mRNA.
EMBL; U27582; AAA87812.1; -; mRNA.
PIR; S66268; S66268.
RefSeq; NP_446322.2; NM_053870.2.
UniGene; Rn.10197; -.
ProteinModelPortal; P52190; -.
SMR; P52190; -.
STRING; 10116.ENSRNOP00000053014; -.
iPTMnet; P52190; -.
PhosphoSitePlus; P52190; -.
PaxDb; P52190; -.
PRIDE; P52190; -.
GeneID; 116649; -.
KEGG; rno:116649; -.
UCSC; RGD:621436; rat.
CTD; 3761; -.
RGD; 621436; Kcnj4.
eggNOG; KOG3827; Eukaryota.
eggNOG; ENOG410XQ62; LUCA.
HOGENOM; HOG000237325; -.
HOVERGEN; HBG006178; -.
InParanoid; P52190; -.
KO; K04998; -.
PhylomeDB; P52190; -.
PRO; PR:P52190; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0016323; C:basolateral plasma membrane; ISO:RGD.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0030425; C:dendrite; IDA:RGD.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
GO; GO:0005242; F:inward rectifier potassium channel activity; IBA:GO_Central.
GO; GO:0030165; F:PDZ domain binding; ISO:RGD.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:RGD.
GO; GO:0010107; P:potassium ion import; IBA:GO_Central.
Gene3D; 2.60.40.1400; -; 1.
InterPro; IPR014756; Ig_E-set.
InterPro; IPR016449; K_chnl_inward-rec_Kir.
InterPro; IPR003273; K_chnl_inward-rec_Kir2.3.
InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
PANTHER; PTHR11767; PTHR11767; 1.
PANTHER; PTHR11767:SF53; PTHR11767:SF53; 1.
Pfam; PF01007; IRK; 1.
PIRSF; PIRSF005465; GIRK_kir; 1.
PRINTS; PR01326; KIR23CHANNEL.
PRINTS; PR01320; KIRCHANNEL.
SUPFAM; SSF81296; SSF81296; 1.
1: Evidence at protein level;
Cell junction; Cell membrane; Complete proteome; Cytoplasmic vesicle;
Ion channel; Ion transport; Membrane; Postsynaptic cell membrane;
Potassium; Potassium transport; Reference proteome; Synapse;
Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
CHAIN 1 446 Inward rectifier potassium channel 4.
/FTId=PRO_0000154933.
TOPO_DOM 1 55 Cytoplasmic. {ECO:0000250}.
TRANSMEM 56 80 Helical; Name=M1. {ECO:0000250}.
TOPO_DOM 81 120 Extracellular. {ECO:0000250}.
INTRAMEM 121 132 Helical; Pore-forming; Name=H5.
{ECO:0000250}.
INTRAMEM 133 139 Pore-forming. {ECO:0000250}.
TOPO_DOM 140 148 Extracellular. {ECO:0000250}.
TRANSMEM 149 170 Helical; Name=M2. {ECO:0000250}.
TOPO_DOM 171 446 Cytoplasmic. {ECO:0000250}.
REGION 91 111 Val/Gly/Ala/Pro stretch.
MOTIF 134 139 Selectivity filter. {ECO:0000250}.
MOTIF 444 446 PDZ-binding. {ECO:0000255}.
COMPBIAS 362 368 Poly-Pro.
COMPBIAS 383 390 Poly-Glu.
COMPBIAS 391 399 Poly-Ala.
SITE 164 164 Role in the control of polyamine-mediated
channel gating and in the blocking by
intracellular magnesium. {ECO:0000250}.
CONFLICT 53 54 Missing (in Ref. 3; AAA87812).
{ECO:0000305}.
CONFLICT 91 98 PSGPTAGG -> LRAHGGS (in Ref. 3;
AAA87812). {ECO:0000305}.
CONFLICT 109 109 T -> R (in Ref. 3; AAA87812).
{ECO:0000305}.
CONFLICT 115 122 IMHVNGFL -> YHACKRLFW (in Ref. 3;
AAA87812). {ECO:0000305}.
CONFLICT 130 131 ET -> GA (in Ref. 3; AAA87812).
{ECO:0000305}.
CONFLICT 135 135 I -> Y (in Ref. 3; AAA87812).
{ECO:0000305}.
CONFLICT 155 155 Missing (in Ref. 3; AAA87812).
{ECO:0000305}.
CONFLICT 176 176 P -> A (in Ref. 3; AAA87812).
{ECO:0000305}.
CONFLICT 176 176 P -> G (in Ref. 2). {ECO:0000305}.
CONFLICT 178 178 P -> S (in Ref. 2). {ECO:0000305}.
CONFLICT 197 198 DG -> T (in Ref. 3; AAA87812).
{ECO:0000305}.
CONFLICT 205 207 RVG -> GWV (in Ref. 3; AAA87812).
{ECO:0000305}.
CONFLICT 294 294 V -> A (in Ref. 3; AAA87812).
{ECO:0000305}.
CONFLICT 298 298 A -> V (in Ref. 2; CAA60963).
{ECO:0000305}.
CONFLICT 308 308 L -> Q (in Ref. 3; AAA87812).
{ECO:0000305}.
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


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