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ATP-sensitive inward rectifier potassium channel 1 (ATP-regulated potassium channel ROM-K) (Inward rectifier K( ) channel Kir1.1) (Potassium channel, inwardly rectifying subfamily J member 1)

 KCNJ1_HUMAN             Reviewed;         391 AA.
P48048; B2RMR4; Q6LD67;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
25-OCT-2017, entry version 174.
RecName: Full=ATP-sensitive inward rectifier potassium channel 1;
AltName: Full=ATP-regulated potassium channel ROM-K;
AltName: Full=Inward rectifier K(+) channel Kir1.1;
AltName: Full=Potassium channel, inwardly rectifying subfamily J member 1;
Name=KCNJ1; Synonyms=ROMK1;
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 ALTERNATIVE SPLICING.
TISSUE=Kidney;
PubMed=7929082;
Shuck M.E., Bock J.H., Benjamin C.W., Tsai T.-D., Lee K.S.,
Slightom J.L., Bienkowski M.J.;
"Cloning and characterization of multiple forms of the human kidney
ROM-K potassium channel.";
J. Biol. Chem. 269:24261-24270(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
TISSUE=Kidney;
PubMed=8190102;
Yano H., Philipson L.H., Kugler J.L., Tokuyama Y., Davis E.M.,
le Beau M.M., Nelson D.J., Bell G.I., Takeda J.;
"Alternative splicing of human inwardly rectifying K+ channel ROMK1
mRNA.";
Mol. Pharmacol. 45:854-860(1994).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
PubMed=9099852; DOI=10.1016/S0378-1119(96)00759-7;
Bock J.H., Shuck M.E., Benjamin C.W., Chee M., Bienkowski M.J.,
Slightom J.L.;
"Nucleotide sequence analysis of the human KCNJ1 potassium channel
locus.";
Gene 188:9-16(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 76-177, AND TISSUE SPECIFICITY.
TISSUE=Brain cortex;
PubMed=7635463; DOI=10.1007/BF00207372;
Krishnan S.N., Desai T., Ward D.C., Haddad G.G.;
"Isolation and chromosomal localization of a human ATP-regulated
potassium channel.";
Hum. Genet. 96:155-160(1995).
[7]
GLYCOSYLATION AT ASN-117.
PubMed=10889209; DOI=10.1074/jbc.M005338200;
Pabon A., Chan K.W., Sui J.L., Wu X., Logothetis D.E., Thornhill W.B.;
"Glycosylation of GIRK1 at Asn119 and ROMK1 at Asn117 has different
consequences in potassium channel function.";
J. Biol. Chem. 275:30677-30682(2000).
[8]
INTERACTION WITH SGK1 AND SLC9A3R2/NHERF2.
PubMed=14623317; DOI=10.1016/j.bbrc.2003.10.037;
Palmada M., Embark H.M., Yun C., Bohmer C., Lang F.;
"Molecular requirements for the regulation of the renal outer
medullary K(+) channel ROMK1 by the serum- and glucocorticoid-
inducible kinase SGK1.";
Biochem. Biophys. Res. Commun. 311:629-634(2003).
[9]
PHOSPHORYLATION AT SER-44 BY SGK1, AND SUBCELLULAR LOCATION.
PubMed=12684516; DOI=10.1074/jbc.M212301200;
Yoo D., Kim B.Y., Campo C., Nance L., King A., Maouyo D.,
Welling P.A.;
"Cell surface expression of the ROMK (Kir 1.1) channel is regulated by
the aldosterone-induced kinase, SGK-1, and protein kinase A.";
J. Biol. Chem. 278:23066-23075(2003).
[10]
ENZYME REGULATION.
PubMed=16357011; DOI=10.1113/jphysiol.2005.102202;
Leng Q., Kahle K.T., Rinehart J., MacGregor G.G., Wilson F.H.,
Canessa C.M., Lifton R.P., Hebert S.C.;
"WNK3, a kinase related to genes mutated in hereditary hypertension
with hyperkalaemia, regulates the K+ channel ROMK1 (Kir1.1).";
J. Physiol. (Lond.) 571:275-286(2006).
[11]
VARIANTS BARTS2 VAL-214; ARG-219 AND THR-357.
PubMed=8841184; DOI=10.1038/ng1096-152;
Simon D.B., Karet F.E., Rodriguez-Soriano J., Hamdan J.H.,
DiPietro A., Trachtman H., Sanjad S.A., Lifton R.P.;
"Genetic heterogeneity of Bartter's syndrome revealed by mutations in
the K+ channel, ROMK.";
Nat. Genet. 14:152-156(1996).
[12]
VARIANTS BARTS2 GLU-72; TYR-74; CYS-99; HIS-108; LEU-110; GLU-122;
GLU-167; THR-198 AND GLY-315.
PubMed=9002665;
Karolyi L., Konrad M., Koeckerling A., Ziegler A., Zimmermann D.K.,
Roth B., Wieg C., Grzeschik K.-H., Koch M.C., Seyberth H.W.,
Vargas R., Forestier L., Jean G., Deschaux M., Rizzoni G.F.,
Niaudet P., Antignac C., Feldmann D., Lorridon F., Cougoureux E.,
Laroze F., Alessandri J.-L., David L., Saunier P., Deschenes G.,
Hildebrandt F., Vollmer M., Proesmans W., Brandis M.,
van den Heuvel L.P.W.J., Lemmink H.H., Nillesen W., Monnens L.A.H.,
Knoers N.V.A.M., Guay-Woodford L.M., Wright C.J., Madrigal G.,
Hebert S.C.;
"Mutations in the gene encoding the inwardly-rectifying renal
potassium channel, ROMK, cause the antenatal variant of Bartter
syndrome: evidence for genetic heterogeneity.";
Hum. Mol. Genet. 6:17-26(1997).
[13]
VARIANT BARTS2 LYS-124.
PubMed=9727001; DOI=10.1074/jbc.273.37.23884;
Derst C., Wischmeyer E., Preisig-Mueller R., Spauschus A., Konrad M.,
Hensen P., Jeck N., Seyberth H.W., Daut J., Karschin A.;
"A hyperprostaglandin E syndrome mutation in Kir1.1 (renal outer
medullary potassium) channels reveals a crucial residue for channel
function in Kir1.3 channels.";
J. Biol. Chem. 273:23884-23891(1998).
[14]
VARIANT [LARGE SCALE ANALYSIS] PHE-115.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: In the kidney, probably plays a major role in potassium
homeostasis. 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. This channel is activated by internal ATP and can be
blocked by external barium.
-!- ENZYME REGULATION: Inhibited by WNK3.
{ECO:0000269|PubMed:16357011}.
-!- SUBUNIT: Interacts with SGK1 and SLC9A3R2/NHERF2.
{ECO:0000269|PubMed:14623317}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12684516};
Multi-pass membrane protein {ECO:0000269|PubMed:12684516}.
Note=Phosphorylation at Ser-44 by SGK1 is necessary for its
expression at the cell membrane.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=ROM-K1;
IsoId=P48048-1; Sequence=Displayed;
Name=2; Synonyms=2-4-5, ROM-K2, ROM-K4, ROM-K5, ROM-K6;
IsoId=P48048-2; Sequence=VSP_002797;
Name=3; Synonyms=ROM-K3;
IsoId=P48048-3; Sequence=VSP_002798;
-!- TISSUE SPECIFICITY: In the kidney and pancreatic islets. Lower
levels in skeletal muscle, pancreas, spleen, brain, heart and
liver. {ECO:0000269|PubMed:7635463}.
-!- PTM: Phosphorylation at Ser-44 by SGK1 is necessary for its
expression at the cell membrane. {ECO:0000269|PubMed:12684516}.
-!- DISEASE: Bartter syndrome 2, antenatal (BARTS2) [MIM:241200]: A
form of Bartter syndrome, an autosomal recessive disorder
characterized by impaired salt reabsorption in the thick ascending
loop of Henle with pronounced salt wasting, hypokalemic metabolic
alkalosis, and varying degrees of hypercalciuria. BARTS2 is a
life-threatening condition beginning in utero, with marked fetal
polyuria that leads to polyhydramnios and premature delivery.
Another hallmark is a marked hypercalciuria and, as a secondary
consequence, the development of nephrocalcinosis and osteopenia.
{ECO:0000269|PubMed:8841184, ECO:0000269|PubMed:9002665,
ECO:0000269|PubMed:9727001}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the inward rectifier-type potassium channel
(TC 1.A.2.1) family. KCNJ1 subfamily. {ECO:0000305}.
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EMBL; U12541; AAA61712.1; -; mRNA.
EMBL; U12542; AAA61713.1; -; mRNA.
EMBL; U12543; AAA61714.1; -; mRNA.
EMBL; U12544; AAA61715.1; -; mRNA.
EMBL; U12545; AAA61716.1; -; mRNA.
EMBL; U03884; AAA20594.1; -; mRNA.
EMBL; U65406; AAC51220.1; -; Genomic_DNA.
EMBL; U65406; AAC51221.1; -; Genomic_DNA.
EMBL; U65406; AAC51222.1; -; Genomic_DNA.
EMBL; CH471065; EAW67724.1; -; Genomic_DNA.
EMBL; BC074752; AAH74752.1; -; mRNA.
EMBL; BC136360; AAI36361.1; -; mRNA.
EMBL; BC136361; AAI36362.1; -; mRNA.
EMBL; S78737; AAB35012.1; -; mRNA.
CCDS; CCDS8476.1; -. [P48048-1]
CCDS; CCDS8477.1; -. [P48048-2]
PIR; A55119; A55119.
RefSeq; NP_000211.1; NM_000220.4. [P48048-1]
RefSeq; NP_722448.1; NM_153764.2. [P48048-2]
RefSeq; NP_722449.3; NM_153765.2. [P48048-3]
RefSeq; NP_722450.1; NM_153766.2. [P48048-2]
RefSeq; NP_722451.1; NM_153767.3. [P48048-2]
UniGene; Hs.527830; -.
ProteinModelPortal; P48048; -.
SMR; P48048; -.
BioGrid; 109960; 4.
ELM; P48048; -.
MINT; MINT-90062; -.
STRING; 9606.ENSP00000376432; -.
BindingDB; P48048; -.
ChEMBL; CHEMBL1293292; -.
DrugBank; DB00414; Acetohexamide.
DrugBank; DB08838; Agmatine.
DrugBank; DB00217; Bethanidine.
DrugBank; DB00222; Glimepiride.
DrugBank; DB01382; Glycodiazine.
DrugBank; DB00350; Minoxidil.
DrugBank; DB01124; Tolbutamide.
DrugBank; DB01392; Yohimbine.
GuidetoPHARMACOLOGY; 429; -.
TCDB; 1.A.2.1.1; the inward rectifier k(+) channel (irk-c) family.
iPTMnet; P48048; -.
PhosphoSitePlus; P48048; -.
DMDM; 1352479; -.
PaxDb; P48048; -.
PeptideAtlas; P48048; -.
PRIDE; P48048; -.
Ensembl; ENST00000324036; ENSP00000316233; ENSG00000151704. [P48048-2]
Ensembl; ENST00000392664; ENSP00000376432; ENSG00000151704. [P48048-1]
Ensembl; ENST00000392665; ENSP00000376433; ENSG00000151704. [P48048-2]
Ensembl; ENST00000392666; ENSP00000376434; ENSG00000151704. [P48048-2]
Ensembl; ENST00000440599; ENSP00000406320; ENSG00000151704. [P48048-2]
GeneID; 3758; -.
KEGG; hsa:3758; -.
UCSC; uc001qeo.3; human. [P48048-1]
CTD; 3758; -.
DisGeNET; 3758; -.
EuPathDB; HostDB:ENSG00000151704.15; -.
GeneCards; KCNJ1; -.
HGNC; HGNC:6255; KCNJ1.
HPA; HPA026962; -.
MalaCards; KCNJ1; -.
MIM; 241200; phenotype.
MIM; 600359; gene.
neXtProt; NX_P48048; -.
OpenTargets; ENSG00000151704; -.
Orphanet; 93604; Antenatal Bartter syndrome.
PharmGKB; PA213; -.
eggNOG; KOG3827; Eukaryota.
eggNOG; ENOG410XQ62; LUCA.
GeneTree; ENSGT00900000140895; -.
HOGENOM; HOG000237326; -.
HOVERGEN; HBG006178; -.
InParanoid; P48048; -.
KO; K04995; -.
OMA; WYAVAYI; -.
OrthoDB; EOG091G08HC; -.
PhylomeDB; P48048; -.
TreeFam; TF313676; -.
Reactome; R-HSA-1296067; Potassium transport channels.
SIGNOR; P48048; -.
GeneWiki; ROMK; -.
GenomeRNAi; 3758; -.
PRO; PR:P48048; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000151704; -.
CleanEx; HS_KCNJ1; -.
ExpressionAtlas; P48048; baseline and differential.
Genevisible; P48048; HS.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0008076; C:voltage-gated potassium channel complex; TAS:ProtInc.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0015272; F:ATP-activated inward rectifier potassium channel activity; IBA:GO_Central.
GO; GO:0005242; F:inward rectifier potassium channel activity; TAS:Reactome.
GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:BHF-UCL.
GO; GO:0007588; P:excretion; TAS:ProtInc.
GO; GO:0010107; P:potassium ion import; IBA:GO_Central.
GO; GO:0006813; P:potassium ion transport; TAS:ProtInc.
Gene3D; 2.60.40.1400; -; 1.
InterPro; IPR014756; Ig_E-set.
InterPro; IPR016449; K_chnl_inward-rec_Kir.
InterPro; IPR003268; K_chnl_inward-rec_Kir1.1.
InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
PANTHER; PTHR11767; PTHR11767; 1.
PANTHER; PTHR11767:SF6; PTHR11767:SF6; 1.
Pfam; PF01007; IRK; 1.
PIRSF; PIRSF005465; GIRK_kir; 1.
PRINTS; PR01321; KIR11CHANNEL.
PRINTS; PR01320; KIRCHANNEL.
SUPFAM; SSF81296; SSF81296; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Bartter syndrome; Cell membrane;
Complete proteome; Disease mutation; Glycoprotein; Ion channel;
Ion transport; Membrane; Nucleotide-binding; Phosphoprotein;
Polymorphism; Potassium; Potassium transport; Reference proteome;
Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
CHAIN 1 391 ATP-sensitive inward rectifier potassium
channel 1.
/FTId=PRO_0000154917.
TOPO_DOM 1 77 Cytoplasmic. {ECO:0000250}.
TRANSMEM 78 102 Helical; Name=M1. {ECO:0000250}.
TOPO_DOM 103 127 Extracellular. {ECO:0000250}.
INTRAMEM 128 139 Helical; Pore-forming; Name=H5.
{ECO:0000250}.
INTRAMEM 140 146 Pore-forming. {ECO:0000250}.
TOPO_DOM 147 155 Extracellular. {ECO:0000250}.
TRANSMEM 156 177 Helical; Name=M2. {ECO:0000250}.
TOPO_DOM 178 391 Cytoplasmic. {ECO:0000250}.
NP_BIND 223 230 ATP. {ECO:0000255}.
MOTIF 141 146 Selectivity filter. {ECO:0000250}.
SITE 171 171 Role in the control of polyamine-mediated
channel gating and in the blocking by
intracellular magnesium. {ECO:0000250}.
MOD_RES 44 44 Phosphoserine; by SGK1.
{ECO:0000269|PubMed:12684516}.
CARBOHYD 117 117 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:10889209}.
VAR_SEQ 1 19 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_002797.
VAR_SEQ 1 12 MNASSRNVFDTL -> MPTVYLCSEQ (in isoform
3). {ECO:0000305}.
/FTId=VSP_002798.
VARIANT 6 6 R -> W (in dbSNP:rs34191956).
/FTId=VAR_049668.
VARIANT 72 72 V -> E (in BARTS2).
{ECO:0000269|PubMed:9002665}.
/FTId=VAR_001548.
VARIANT 74 74 D -> Y (in BARTS2).
{ECO:0000269|PubMed:9002665}.
/FTId=VAR_001549.
VARIANT 99 99 W -> C (in BARTS2).
{ECO:0000269|PubMed:9002665}.
/FTId=VAR_001550.
VARIANT 108 108 D -> H (in BARTS2; dbSNP:rs104894250).
{ECO:0000269|PubMed:9002665}.
/FTId=VAR_001551.
VARIANT 110 110 P -> L (in BARTS2; dbSNP:rs373745258).
{ECO:0000269|PubMed:9002665}.
/FTId=VAR_001552.
VARIANT 115 115 S -> F (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036426.
VARIANT 122 122 V -> E (in BARTS2).
{ECO:0000269|PubMed:9002665}.
/FTId=VAR_001553.
VARIANT 124 124 N -> K (in BARTS2; dbSNP:rs104894251).
{ECO:0000269|PubMed:9727001}.
/FTId=VAR_019724.
VARIANT 167 167 G -> E (in BARTS2; dbSNP:rs104894254).
{ECO:0000269|PubMed:9002665}.
/FTId=VAR_001554.
VARIANT 198 198 A -> T (in BARTS2; dbSNP:rs104894253).
{ECO:0000269|PubMed:9002665}.
/FTId=VAR_001555.
VARIANT 214 214 A -> V (in BARTS2; dbSNP:rs104894246).
{ECO:0000269|PubMed:8841184}.
/FTId=VAR_019725.
VARIANT 219 219 S -> R (in BARTS2; dbSNP:rs104894245).
{ECO:0000269|PubMed:8841184}.
/FTId=VAR_019726.
VARIANT 315 315 V -> G (in BARTS2; dbSNP:rs753949204).
{ECO:0000269|PubMed:9002665}.
/FTId=VAR_001556.
VARIANT 357 357 M -> T (in BARTS2; dbSNP:rs59172778).
{ECO:0000269|PubMed:8841184}.
/FTId=VAR_019727.
SEQUENCE 391 AA; 44795 MW; DF01C89B16BE6205 CRC64;
MNASSRNVFD TLIRVLTESM FKHLRKWVVT RFFGHSRQRA RLVSKDGRCN IEFGNVEAQS
RFIFFVDIWT TVLDLKWRYK MTIFITAFLG SWFFFGLLWY AVAYIHKDLP EFHPSANHTP
CVENINGLTS AFLFSLETQV TIGYGFRCVT EQCATAIFLL IFQSILGVII NSFMCGAILA
KISRPKKRAK TITFSKNAVI SKRGGKLCLL IRVANLRKSL LIGSHIYGKL LKTTVTPEGE
TIILDQININ FVVDAGNENL FFISPLTIYH VIDHNSPFFH MAAETLLQQD FELVVFLDGT
VESTSATCQV RTSYVPEEVL WGYRFAPIVS KTKEGKYRVD FHNFSKTVEV ETPHCAMCLY
NEKDVRARMK RGYDNPNFIL SEVNETDDTK M


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