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G protein-activated inward rectifier potassium channel 4 (GIRK-4) (Cardiac inward rectifier) (CIR) (Heart KATP channel) (Inward rectifier K( ) channel Kir3.4) (IRK-4) (KATP-1) (Potassium channel, inwardly rectifying subfamily J member 5)

 KCNJ5_HUMAN             Reviewed;         419 AA.
P48544; B2R744; Q6DK13; Q6DK14; Q92807;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 2.
27-SEP-2017, entry version 173.
RecName: Full=G protein-activated inward rectifier potassium channel 4;
Short=GIRK-4;
AltName: Full=Cardiac inward rectifier;
Short=CIR;
AltName: Full=Heart KATP channel;
AltName: Full=Inward rectifier K(+) channel Kir3.4;
Short=IRK-4;
AltName: Full=KATP-1;
AltName: Full=Potassium channel, inwardly rectifying subfamily J member 5;
Name=KCNJ5; Synonyms=GIRK4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLU-282.
TISSUE=Pancreas;
Chan K.W., Langan M.N., Sui J., Kozak A., Pabon A., Ladias J.A.A.,
Logothetis D.E.;
Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLU-282.
PubMed=8047164; DOI=10.1038/370456a0;
Ashford M.L.J., Bond C.T., Blair T.A., Adelman J.P.;
"Cloning and functional expression of a rat heart KATP channel.";
Nature 370:456-459(1994).
[3]
ERRATUM, AND RETRACTION.
PubMed=8524415; DOI=10.1038/378792a0;
Ashford M.L.J., Bond C.T., Blair T.A., Adelman J.P.;
Nature 378:792-792(1995).
[4]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLU-282.
PubMed=8558261;
Spauschus A., Lentes K.U., Wischmeyer E., Dissmann E., Karschin C.,
Karschin A.;
"A G-protein-activated inwardly rectifying K+ channel (GIRK4) from
human hippocampus associates with other GIRK channels.";
J. Neurosci. 16:930-938(1996).
[5]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLU-282.
TISSUE=Pituitary;
PubMed=10659995; DOI=10.1016/S0898-6568(99)00059-5;
Schoots O., Wilson J.M., Ethier N., Bigras E., Hebert T.E.,
Van Tol H.H.M.;
"Co-expression of human Kir3 subunits can yield channels with
different functional properties.";
Cell. Signal. 11:871-883(1999).
[6]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLU-282.
TISSUE=Heart;
PubMed=8834003;
Iizuka M., Kubo Y., Tsunenari I., Pan C.X., Akiba I., Kono T.;
"Functional characterization and localization of a cardiac-type
inwardly rectifying K+ channel.";
Recept. Channels 3:299-315(1995).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Thymus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLU-282.
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
TISSUE SPECIFICITY, VARIANTS HALD3 ARG-151 AND ALA-158, VARIANTS
HIS-39; ARG-168 AND ILE-210, CHARACTERIZATION OF VARIANT HALD3
ARG-151, CHARACTERIZATION OF VARIANT ARG-168, AND INVOLVEMENT IN
ALDOSTERONISM ASSOCIATED WITH ADRENAL ADENOMAS.
PubMed=21311022; DOI=10.1126/science.1198785;
Choi M., Scholl U.I., Yue P., Bjorklund P., Zhao B.,
Nelson-Williams C., Ji W., Cho Y., Patel A., Men C.J., Lolis E.,
Wisgerhof M.V., Geller D.S., Mane S., Hellman P., Westin G.,
Akerstrom G., Wang W., Carling T., Lifton R.P.;
"K+ channel mutations in adrenal aldosterone-producing adenomas and
hereditary hypertension.";
Science 331:768-772(2011).
[11]
VARIANT LQT13 ARG-387.
PubMed=20560207; DOI=10.1016/j.ajhg.2010.04.017;
Yang Y., Yang Y., Liang B., Liu J., Li J., Grunnet M., Olesen S.P.,
Rasmussen H.B., Ellinor P.T., Gao L., Lin X., Li L., Wang L., Xiao J.,
Liu Y., Liu Y., Zhang S., Liang D., Peng L., Jespersen T., Chen Y.H.;
"Identification of a Kir3.4 mutation in congenital long QT syndrome.";
Am. J. Hum. Genet. 86:872-880(2010).
[12]
CHARACTERIZATION OF VARIANT HALD3 ALA-158, FUNCTION, AND SUBCELLULAR
LOCATION.
PubMed=22315453; DOI=10.1210/en.2011-1733;
Oki K., Plonczynski M.W., Luis Lam M., Gomez-Sanchez E.P.,
Gomez-Sanchez C.E.;
"Potassium channel mutant KCNJ5 T158A expression in HAC-15 cells
increases aldosterone synthesis.";
Endocrinology 153:1774-1782(2012).
[13]
VARIANT ARG-168, VARIANTS HALD3 ARG-151; GLU-151 AND ALA-158,
CHARACTERIZATION OF VARIANT HALD3 GLU-151, AND INVOLVEMENT IN
ALDOSTERONISM ASSOCIATED WITH ADRENAL ADENOMAS.
PubMed=22203740; DOI=10.1161/HYPERTENSIONAHA.111.183996;
Mulatero P., Tauber P., Zennaro M.C., Monticone S., Lang K.,
Beuschlein F., Fischer E., Tizzani D., Pallauf A., Viola A., Amar L.,
Williams T.A., Strom T.M., Graf E., Bandulik S., Penton D.,
Plouin P.F., Warth R., Allolio B., Jeunemaitre X., Veglio F.,
Reincke M.;
"KCNJ5 mutations in European families with nonglucocorticoid
remediable familial hyperaldosteronism.";
Hypertension 59:235-240(2012).
[14]
VARIANT HALD3 ARG-151, VARIANT ARG-168, AND INVOLVEMENT IN
ALDOSTERONISM ASSOCIATED WITH ADRENAL ADENOMAS.
PubMed=22275527; DOI=10.1161/HYPERTENSIONAHA.111.186478;
Boulkroun S., Beuschlein F., Rossi G.P., Golib-Dzib J.F., Fischer E.,
Amar L., Mulatero P., Samson-Couterie B., Hahner S., Quinkler M.,
Fallo F., Letizia C., Allolio B., Ceolotto G., Cicala M.V., Lang K.,
Lefebvre H., Lenzini L., Maniero C., Monticone S., Perrocheau M.,
Pilon C., Plouin P.F., Rayes N., Seccia T.M., Veglio F.,
Williams T.A., Zinnamosca L., Mantero F., Benecke A., Jeunemaitre X.,
Reincke M., Zennaro M.C.;
"Prevalence, clinical, and molecular correlates of KCNJ5 mutations in
primary aldosteronism.";
Hypertension 59:592-598(2012).
[15]
VARIANT HALD3 SER-157, CHARACTERIZATION OF VARIANTS HALD3 ARG-151;
SER-157 AND ALA-158, CHARACTERIZATION OF VARIANT ARG-168, AND
FUNCTION.
PubMed=22628607; DOI=10.1210/jc.2012-1334;
Charmandari E., Sertedaki A., Kino T., Merakou C., Hoffman D.A.,
Hatch M.M., Hurt D.E., Lin L., Xekouki P., Stratakis C.A.,
Chrousos G.P.;
"A novel point mutation in the KCNJ5 gene causing primary
hyperaldosteronism and early-onset autosomal dominant hypertension.";
J. Clin. Endocrinol. Metab. 97:E1532-E1539(2012).
[16]
VARIANT HALD3 ARG-151, VARIANTS GLN-145 AND ARG-168, AND INVOLVEMENT
IN ALDOSTERONISM ASSOCIATED WITH ADRENAL ADENOMAS.
PubMed=22848660; DOI=10.1371/journal.pone.0041926;
Akerstrom T., Crona J., Delgado Verdugo A., Starker L.F., Cupisti K.,
Willenberg H.S., Knoefel W.T., Saeger W., Feller A., Ip J., Soon P.,
Anlauf M., Alesina P.F., Schmid K.W., Decaussin M., Levillain P.,
Wangberg B., Peix J.L., Robinson B., Zedenius J., Backdahl M.,
Caramuta S., Iwen K.A., Botling J., Stalberg P., Kraimps J.L.,
Dralle H., Hellman P., Sidhu S., Westin G., Lehnert H., Walz M.K.,
Akerstrom G., Carling T., Choi M., Lifton R.P., Bjorklund P.;
"Comprehensive re-sequencing of adrenal aldosterone producing lesions
reveal three somatic mutations near the KCNJ5 potassium channel
selectivity filter.";
PLoS ONE 7:E41926-E41926(2012).
[17]
VARIANTS HALD3 ARG-151 AND GLU-151.
PubMed=22308486; DOI=10.1073/pnas.1121407109;
Scholl U.I., Nelson-Williams C., Yue P., Grekin R., Wyatt R.J.,
Dillon M.J., Couch R., Hammer L.K., Harley F.L., Farhi A., Wang W.H.,
Lifton R.P.;
"Hypertension with or without adrenal hyperplasia due to different
inherited mutations in the potassium channel KCNJ5.";
Proc. Natl. Acad. Sci. U.S.A. 109:2533-2538(2012).
[18]
VARIANT HALD3 CYS-152, CHARACTERIZATION OF VARIANTS HALD3 GLU-151 AND
CYS-152, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=24037882; DOI=10.1210/jc.2013-2428;
Monticone S., Hattangady N.G., Penton D., Isales C.M., Edwards M.A.,
Williams T.A., Sterner C., Warth R., Mulatero P., Rainey W.E.;
"a Novel Y152C KCNJ5 mutation responsible for familial
hyperaldosteronism type III.";
J. Clin. Endocrinol. Metab. 98:E1861-E1865(2013).
[19]
VARIANTS MET-259 AND ASN-348, CHARACTERIZATION OF VARIANTS MET-259 AND
ASN-348, INVOLVEMENT IN HYPERTENTION WITH ACTH-DEPENDENT ALDOSTERONE
HYPERSECRETION, AND FUNCTION.
PubMed=27293068; DOI=10.1111/cen.13132;
Sertedaki A., Markou A., Vlachakis D., Kossida S., Campanac E.,
Hoffman D.A., Sierra M.L., Xekouki P., Stratakis C.A., Kaltsas G.,
Piaditis G.P., Chrousos G.P., Charmandari E.;
"Functional characterization of two novel germline mutations of the
KCNJ5 gene in hypertensive patients without primary aldosteronism but
with ACTH-dependent aldosterone hypersecretion.";
Clin. Endocrinol. (Oxf.) 85:845-851(2016).
[20]
CHARACTERIZATION OF VARIANT HALD3 ALA-158, AND FUNCTION.
PubMed=27099398; DOI=10.1530/JME-15-0324;
Hattangady N.G., Karashima S., Yuan L., Ponce-Balbuena D., Jalife J.,
Gomez-Sanchez C.E., Auchus R.J., Rainey W.E., Else T.;
"Mutated KCNJ5 activates the acute and chronic regulatory steps in
aldosterone production.";
J. Mol. Endocrinol. 57:1-11(2016).
-!- FUNCTION: This potassium channel is controlled by G proteins.
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
external barium. {ECO:0000269|PubMed:22315453,
ECO:0000269|PubMed:22628607, ECO:0000269|PubMed:24037882,
ECO:0000269|PubMed:27099398, ECO:0000269|PubMed:27293068}.
-!- SUBUNIT: May associate with GIRK1 and GIRK2 to form a G-protein-
activated heteromultimer pore-forming unit. The resulting inward
current is much larger. {ECO:0000250|UniProtKB:P48548}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:22315453,
ECO:0000269|PubMed:24037882}; Multi-pass membrane protein
{ECO:0000255}.
-!- TISSUE SPECIFICITY: Islets, exocrine pancreas and heart. Expressed
in the adrenal cortex, particularly the zona glomerulosa.
{ECO:0000269|PubMed:21311022}.
-!- DISEASE: Long QT syndrome 13 (LQT13) [MIM:613485]: A heart
disorder characterized by a prolonged QT interval on the ECG and
polymorphic ventricular arrhythmias. They cause syncope and sudden
death in response to exercise or emotional stress, and can present
with a sentinel event of sudden cardiac death in infancy.
{ECO:0000269|PubMed:20560207}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Hyperaldosteronism, familial, 3 (HALD3) [MIM:613677]: A
form of hyperaldosteronism characterized by hypertension secondary
to massive adrenal mineralocorticoid production. HALD3 patients
present with childhood hypertension, elevated aldosteronism
levels, and high levels of the hybrid steroids 18-oxocortisol and
18-hydroxycortisol. Hypertension and aldosteronism are not
reversed by administration of exogenous glucocorticoids and
patients require adrenalectomy to control hypertension.
{ECO:0000269|PubMed:21311022, ECO:0000269|PubMed:22203740,
ECO:0000269|PubMed:22275527, ECO:0000269|PubMed:22308486,
ECO:0000269|PubMed:22315453, ECO:0000269|PubMed:22628607,
ECO:0000269|PubMed:22848660, ECO:0000269|PubMed:24037882,
ECO:0000269|PubMed:27099398}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Note=Somatic mutations in KCNJ5 have been found in
aldosterone-producing adrenal adenomas and can be responsible for
aldosteronism associated with cell autonomous proliferation. APAs
are typically solitary, well circumscribed tumors diagnosed
between ages 30 and 70. They come to medical attention due to new
or worsening hypertension, often with hypokalemia. The precise
role of KCNJ5 mutations in APA is under debate. They produce
increased sodium conductance and cell depolarization, which in
adrenal glomerulosa cells produces calcium entry, the signal for
aldosterone production and cell proliferation. However, they may
not be causative of APA development but may be a consequence of
tumorigenesis, playing only a contributory role toward aldosterone
overproduction and tumor growth (PubMed:22275527). Somatic
mutations in KCNJ5 have not been found in non-aldosterone
secreting adrenal adenomas suggesting that they are specifically
associated with APA (PubMed:22275527 and PubMed:22848660).
{ECO:0000269|PubMed:21311022, ECO:0000269|PubMed:22203740,
ECO:0000269|PubMed:22275527, ECO:0000269|PubMed:22848660}.
-!- DISEASE: Note=Mutations in KCNJ5 are involved in the pathogenesis
of hypertension without primary aldosteronism but with increased
aldosterone response to ACTH stimulation.
{ECO:0000269|PubMed:27293068}.
-!- SIMILARITY: Belongs to the inward rectifier-type potassium channel
(TC 1.A.2.1) family. KCNJ5 subfamily. {ECO:0000305}.
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EMBL; U39195; AAB53093.1; -; mRNA.
EMBL; X83582; CAA58565.1; -; mRNA.
EMBL; L47208; AAB07269.1; -; mRNA.
EMBL; U52154; AAB07045.1; -; mRNA.
EMBL; D50134; BAA08814.1; -; mRNA.
EMBL; AP000920; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AK312837; BAG35691.1; -; mRNA.
EMBL; BC069571; AAH69571.1; -; mRNA.
EMBL; BC074838; AAH74838.2; -; mRNA.
EMBL; BC069386; AAH69386.1; -; mRNA.
EMBL; BC069482; AAH69482.1; -; mRNA.
EMBL; BC069499; AAH69499.1; -; mRNA.
EMBL; BC074839; AAH74839.2; -; mRNA.
CCDS; CCDS8479.1; -.
PIR; G02232; G02232.
RefSeq; NP_000881.3; NM_000890.3.
RefSeq; XP_011541111.1; XM_011542809.2.
RefSeq; XP_011541112.1; XM_011542810.2.
UniGene; Hs.444595; -.
UniGene; Hs.632109; -.
ProteinModelPortal; P48544; -.
SMR; P48544; -.
BioGrid; 109964; 17.
MINT; MINT-90031; -.
STRING; 9606.ENSP00000339960; -.
BindingDB; P48544; -.
ChEMBL; CHEMBL3038488; -.
DrugBank; DB00898; Ethanol.
DrugBank; DB01016; Glyburide.
GuidetoPHARMACOLOGY; 437; -.
TCDB; 1.A.2.1.3; the inward rectifier k(+) channel (irk-c) family.
iPTMnet; P48544; -.
PhosphoSitePlus; P48544; -.
BioMuta; KCNJ5; -.
DMDM; 296434543; -.
EPD; P48544; -.
PaxDb; P48544; -.
PeptideAtlas; P48544; -.
PRIDE; P48544; -.
DNASU; 3762; -.
Ensembl; ENST00000338350; ENSP00000339960; ENSG00000120457.
Ensembl; ENST00000529694; ENSP00000433295; ENSG00000120457.
Ensembl; ENST00000533599; ENSP00000434266; ENSG00000120457.
GeneID; 3762; -.
KEGG; hsa:3762; -.
UCSC; uc001qet.4; human.
CTD; 3762; -.
DisGeNET; 3762; -.
EuPathDB; HostDB:ENSG00000120457.11; -.
GeneCards; KCNJ5; -.
GeneReviews; KCNJ5; -.
HGNC; HGNC:6266; KCNJ5.
HPA; CAB022569; -.
HPA; HPA014722; -.
HPA; HPA017353; -.
MalaCards; KCNJ5; -.
MIM; 600734; gene.
MIM; 613485; phenotype.
MIM; 613677; phenotype.
neXtProt; NX_P48544; -.
OpenTargets; ENSG00000120457; -.
Orphanet; 85142; Aldosterone-producing adenoma.
Orphanet; 37553; Cardiodysrhythmic potassium-sensitive periodic paralysis.
Orphanet; 251274; Familial hyperaldosteronism type III.
Orphanet; 101016; Romano-Ward syndrome.
PharmGKB; PA216; -.
eggNOG; KOG3827; Eukaryota.
eggNOG; ENOG410XQ62; LUCA.
GeneTree; ENSGT00760000118842; -.
HOGENOM; HOG000237325; -.
HOVERGEN; HBG006178; -.
InParanoid; P48544; -.
KO; K04999; -.
OMA; MEKSGKC; -.
OrthoDB; EOG091G08HC; -.
PhylomeDB; P48544; -.
TreeFam; TF313676; -.
Reactome; R-HSA-1296041; Activation of G protein gated Potassium channels.
Reactome; R-HSA-997272; Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
SIGNOR; P48544; -.
GeneWiki; KCNJ5; -.
GenomeRNAi; 3762; -.
PRO; PR:P48544; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000120457; -.
CleanEx; HS_KCNJ5; -.
Genevisible; P48544; HS.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0030315; C:T-tubule; IEA:Ensembl.
GO; GO:0008076; C:voltage-gated potassium channel complex; IDA:BHF-UCL.
GO; GO:0015467; F:G-protein activated inward rectifier potassium channel activity; TAS:UniProtKB.
GO; GO:0086089; F:voltage-gated potassium channel activity involved in atrial cardiac muscle cell action potential repolarization; IMP:BHF-UCL.
GO; GO:1902282; F:voltage-gated potassium channel activity involved in ventricular cardiac muscle cell action potential repolarization; IC:BHF-UCL.
GO; GO:0098914; P:membrane repolarization during atrial cardiac muscle cell action potential; IMP:BHF-UCL.
GO; GO:0010107; P:potassium ion import; IDA:BHF-UCL.
GO; GO:1990573; P:potassium ion import across plasma membrane; IDA:BHF-UCL.
GO; GO:0006813; P:potassium ion transport; TAS:ProtInc.
GO; GO:0086091; P:regulation of heart rate by cardiac conduction; IMP:BHF-UCL.
GO; GO:0099625; P:ventricular cardiac muscle cell membrane repolarization; IC:BHF-UCL.
Gene3D; 2.60.40.1400; -; 1.
InterPro; IPR014756; Ig_E-set.
InterPro; IPR016449; K_chnl_inward-rec_Kir.
InterPro; IPR003277; K_chnl_inward-rec_Kir3.4.
InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
PANTHER; PTHR11767; PTHR11767; 1.
Pfam; PF01007; IRK; 1.
PIRSF; PIRSF005465; GIRK_kir; 1.
PRINTS; PR01330; KIR34CHANNEL.
PRINTS; PR01320; KIRCHANNEL.
SUPFAM; SSF81296; SSF81296; 1.
1: Evidence at protein level;
Complete proteome; Disease mutation; Ion channel; Ion transport;
Long QT syndrome; Membrane; Phosphoprotein; Polymorphism; Potassium;
Potassium transport; Reference proteome; Transmembrane;
Transmembrane helix; Transport; Voltage-gated channel.
CHAIN 1 419 G protein-activated inward rectifier
potassium channel 4.
/FTId=PRO_0000154934.
TOPO_DOM 1 86 Cytoplasmic. {ECO:0000250}.
TRANSMEM 87 111 Helical; Name=M1. {ECO:0000250}.
TOPO_DOM 112 135 Extracellular. {ECO:0000250}.
INTRAMEM 136 147 Helical; Pore-forming; Name=H5.
{ECO:0000250}.
INTRAMEM 148 154 Pore-forming. {ECO:0000250}.
TOPO_DOM 155 163 Extracellular. {ECO:0000250}.
TRANSMEM 164 185 Helical; Name=M2. {ECO:0000250}.
TOPO_DOM 186 419 Cytoplasmic. {ECO:0000250}.
MOTIF 149 154 Selectivity filter. {ECO:0000250}.
SITE 179 179 Role in the control of polyamine-mediated
channel gating and in the blocking by
intracellular magnesium. {ECO:0000250}.
MOD_RES 5 5 Phosphoserine.
{ECO:0000250|UniProtKB:P48542}.
VARIANT 39 39 R -> H (in dbSNP:rs560269341).
{ECO:0000269|PubMed:21311022}.
/FTId=VAR_065929.
VARIANT 145 145 E -> Q (found in aldosterone-producing
adrenal adenoma samples; somatic
mutation). {ECO:0000269|PubMed:22848660}.
/FTId=VAR_069182.
VARIANT 151 151 G -> E (in HALD3; results in a profound
alteration of channel function with loss
of channel selectivity and membrane
depolarization; dbSNP:rs587777437).
{ECO:0000269|PubMed:22203740,
ECO:0000269|PubMed:22308486,
ECO:0000269|PubMed:24037882}.
/FTId=VAR_067090.
VARIANT 151 151 G -> R (in HALD3; detected as germline
mutation in a kindred with severe primary
aldosteronism and adrenocortical
hyperplasia; also found as somatic
mutation in aldosterone-producing adrenal
adenoma samples; results in loss of
channel selectivity and membrane
depolarization; dbSNP:rs386352319).
{ECO:0000269|PubMed:21311022,
ECO:0000269|PubMed:22203740,
ECO:0000269|PubMed:22275527,
ECO:0000269|PubMed:22308486,
ECO:0000269|PubMed:22628607,
ECO:0000269|PubMed:22848660}.
/FTId=VAR_065930.
VARIANT 152 152 Y -> C (in HALD3; results in alteration
of channel function with reduced channel
selectivity and membrane depolarization;
increases expression of CYP11B2 and its
transcriptional regulator NR4A2).
{ECO:0000269|PubMed:24037882}.
/FTId=VAR_077577.
VARIANT 157 157 I -> S (in HALD3; loss of channel
selectivity; dbSNP:rs587777438).
{ECO:0000269|PubMed:22628607}.
/FTId=VAR_077578.
VARIANT 158 158 T -> A (in HALD3; also found in
aldosterone-producing adrenal adenoma
samples; results in loss of channel
selectivity and membrane depolarization;
increases expression of CYP11B2 and its
transcriptional regulators NR4A2 and
ATF2; increases aldosterone and hybrid
steroids 18-oxocortisol and 18-
hydroxycortisol synthesis; increases STAR
expression and phosphorylation;
dbSNP:rs387906778).
{ECO:0000269|PubMed:21311022,
ECO:0000269|PubMed:22203740,
ECO:0000269|PubMed:22315453,
ECO:0000269|PubMed:22628607,
ECO:0000269|PubMed:27099398}.
/FTId=VAR_065931.
VARIANT 168 168 L -> R (found in aldosterone-producing
adrenal adenoma samples; somatic
mutation; results in loss of channel
selectivity and membrane depolarization;
dbSNP:rs386352318).
{ECO:0000269|PubMed:21311022,
ECO:0000269|PubMed:22203740,
ECO:0000269|PubMed:22275527,
ECO:0000269|PubMed:22628607,
ECO:0000269|PubMed:22848660}.
/FTId=VAR_065932.
VARIANT 210 210 M -> I (in dbSNP:rs138295501).
{ECO:0000269|PubMed:21311022}.
/FTId=VAR_065933.
VARIANT 259 259 V -> M (found in patients with
hypertension with ACTH-dependent
aldosterone hypersecretion; unknown
pathological significance; no effect on
channel funciton; dbSNP:rs759363415).
{ECO:0000269|PubMed:27293068}.
/FTId=VAR_077579.
VARIANT 282 282 Q -> E (in dbSNP:rs7102584).
{ECO:0000269|PubMed:10659995,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:8047164,
ECO:0000269|PubMed:8558261,
ECO:0000269|PubMed:8834003,
ECO:0000269|Ref.1}.
/FTId=VAR_063107.
VARIANT 348 348 Y -> N (probable disease-associated
mutation found in patients with
hypertension with ACTH-dependent
aldosterone hypersecretion; loss of
channel selectivity).
{ECO:0000269|PubMed:27293068}.
/FTId=VAR_077580.
VARIANT 387 387 G -> R (in LQT13; dbSNP:rs199830292).
{ECO:0000269|PubMed:20560207}.
/FTId=VAR_063766.
CONFLICT 35 35 I -> T (in Ref. 5; AAB07045).
{ECO:0000305}.
CONFLICT 388 388 G -> R (in Ref. 2; CAA58565).
{ECO:0000305}.
SEQUENCE 419 AA; 47668 MW; 7C14A6B0B7EA0FD4 CRC64;
MAGDSRNAMN QDMEIGVTPW DPKKIPKQAR DYVPIATDRT RLLAEGKKPR QRYMEKSGKC
NVHHGNVQET YRYLSDLFTT LVDLKWRFNL LVFTMVYTVT WLFFGFIWWL IAYIRGDLDH
VGDQEWIPCV ENLSGFVSAF LFSIETETTI GYGFRVITEK CPEGIILLLV QAILGSIVNA
FMVGCMFVKI SQPKKRAETL MFSNNAVISM RDEKLCLMFR VGDLRNSHIV EASIRAKLIK
SRQTKEGEFI PLNQTDINVG FDTGDDRLFL VSPLIISHEI NQKSPFWEMS QAQLHQEEFE
VVVILEGMVE ATGMTCQARS SYMDTEVLWG HRFTPVLTLE KGFYEVDYNT FHDTYETNTP
SCCAKELAEM KREGRLLQYL PSPPLLGGCA EAGLDAEAEQ NEEDEPKGLG GSREARGSV


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