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ATP-sensitive inward rectifier potassium channel 10 (ATP-dependent inwardly rectifying potassium channel Kir4.1) (Inward rectifier K( ) channel Kir1.2) (Potassium channel, inwardly rectifying subfamily J member 10)

 KCJ10_HUMAN             Reviewed;         379 AA.
P78508; A3KME7; Q5VUT9; Q8N4I7; Q92808;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-MAY-1997, sequence version 1.
25-OCT-2017, entry version 165.
RecName: Full=ATP-sensitive inward rectifier potassium channel 10;
AltName: Full=ATP-dependent inwardly rectifying potassium channel Kir4.1;
AltName: Full=Inward rectifier K(+) channel Kir1.2;
AltName: Full=Potassium channel, inwardly rectifying subfamily J member 10;
Name=KCNJ10;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND NUCLEOTIDE SEQUENCE [MRNA] OF
143-379.
TISSUE=Kidney;
PubMed=8995301; DOI=10.1074/jbc.272.1.586;
Shuck M.E., Piser T.M., Bock J.H., Slightom J.L., Lee K.S.,
Bienkowski M.J.;
"Cloning and characterization of two K+ inward rectifier (Kir) 1.1
potassium channel homologs from human kidney (Kir1.2 and Kir1.3).";
J. Biol. Chem. 272:586-593(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT CYS-271.
TISSUE=Cerebellum;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
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]
FUNCTION, CHARACTERIZATION OF VARIANTS SESAMES PRO-65; ARG-77;
ARG-140; ILE-164; VAL-167 AND CYS-297, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, AND INTERACTION WITH KCNJ16 AND MAGI1.
PubMed=24561201; DOI=10.1016/j.febslet.2014.02.024;
Tanemoto M., Abe T., Uchida S., Kawahara K.;
"Mislocalization of K+ channels causes the renal salt wasting in
EAST/SeSAME syndrome.";
FEBS Lett. 588:899-905(2014).
[7]
VARIANTS SESAMES PRO-65 AND ARG-77.
PubMed=19420365; DOI=10.1056/NEJMoa0810276;
Bockenhauer D., Feather S., Stanescu H.C., Bandulik S., Zdebik A.A.,
Reichold M., Tobin J., Lieberer E., Sterner C., Landoure G., Arora R.,
Sirimanna T., Thompson D., Cross J.H., van't Hoff W., Al Masri O.,
Tullus K., Yeung S., Anikster Y., Klootwijk E., Hubank M.,
Dillon M.J., Heitzmann D., Arcos-Burgos M., Knepper M.A., Dobbie A.,
Gahl W.A., Warth R., Sheridan E., Kleta R.;
"Epilepsy, ataxia, sensorineural deafness, tubulopathy, and KCNJ10
mutations.";
N. Engl. J. Med. 360:1960-1970(2009).
[8]
VARIANTS SESAMES PRO-65; ARG-140; ILE-164; VAL-167 AND CYS-297.
PubMed=19289823; DOI=10.1073/pnas.0901749106;
Scholl U.I., Choi M., Liu T., Ramaekers V.T., Hausler M.G.,
Grimmer J., Tobe S.W., Farhi A., Nelson-Williams C., Lifton R.P.;
"Seizures, sensorineural deafness, ataxia, mental retardation, and
electrolyte imbalance (SeSAME syndrome) caused by mutations in
KCNJ10.";
Proc. Natl. Acad. Sci. U.S.A. 106:5842-5847(2009).
[9]
VARIANTS SESAMES PRO-68 AND VAL-129.
PubMed=22612257; DOI=10.1111/j.1528-1167.2012.03516.x;
Lemke J.R., Riesch E., Scheurenbrand T., Schubach M., Wilhelm C.,
Steiner I., Hansen J., Courage C., Gallati S., Buerki S., Strozzi S.,
Simonetti B.G., Grunt S., Steinlin M., Alber M., Wolff M.,
Klopstock T., Prott E.C., Lorenz R., Spaich C., Rona S.,
Lakshminarasimhan M., Kroell J., Dorn T., Kraemer G., Synofzik M.,
Becker F., Weber Y.G., Lerche H., Boehm D., Biskup S.;
"Targeted next generation sequencing as a diagnostic tool in epileptic
disorders.";
Epilepsia 53:1387-1398(2012).
-!- FUNCTION: May be responsible for potassium buffering action of
glial cells in the brain. 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). In the kidney, together with KCNJ16, mediates
basolateral K(+) recycling in distal tubules; this process is
critical for Na(+) reabsorption at the tubules. {ECO:0000250,
ECO:0000305|PubMed:24561201}.
-!- SUBUNIT: Heterodimer with Kir5.1/KCNJ16; this interaction is
required for KCNJ16 localization to the basolateral membrane in
kidney cells. Interacts with MAGI1, alone and possibly as a
heterodimer with KCNJ16; this interaction may facilitate
KCNJ10/KCNJ16 potassium channel expression at the basolateral
membrane in kidney cells (PubMed:24561201). Interacts with PATJ
(By similarity). {ECO:0000250|UniProtKB:Q9JM63,
ECO:0000269|PubMed:24561201}.
-!- INTERACTION:
F1PK57:- (xeno); NbExp=2; IntAct=EBI-9117877, EBI-9118227;
Q8IUQ4:SIAH1; NbExp=3; IntAct=EBI-9117877, EBI-747107;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:24561201};
Multi-pass membrane protein. Basolateral cell membrane
{ECO:0000269|PubMed:24561201}. Note=In kidney distal convoluted
tubules, located in the basolateral membrane where it colocalizes
with KCNJ16. {ECO:0000269|PubMed:24561201}.
-!- TISSUE SPECIFICITY: Expressed in kidney (at protein level).
{ECO:0000269|PubMed:24561201}.
-!- DISEASE: Seizures, sensorineural deafness, ataxia, mental
retardation, and electrolyte imbalance (SESAMES) [MIM:612780]: A
complex disorder characterized by generalized seizures with onset
in infancy, delayed psychomotor development, ataxia, sensorineural
hearing loss, hypokalemia, metabolic alkalosis, and
hypomagnesemia. {ECO:0000269|PubMed:19289823,
ECO:0000269|PubMed:19420365, ECO:0000269|PubMed:22612257,
ECO:0000269|PubMed:24561201}. 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. KCNJ10 subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH34036.2; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; U73192; AAC50923.1; -; Genomic_DNA.
EMBL; U73193; AAC50924.1; -; mRNA.
EMBL; U52155; AAB07046.1; -; mRNA.
EMBL; AL513302; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471121; EAW52749.1; -; Genomic_DNA.
EMBL; BC034036; AAH34036.2; ALT_INIT; mRNA.
EMBL; BC131627; AAI31628.1; -; mRNA.
CCDS; CCDS1193.1; -.
RefSeq; NP_002232.2; NM_002241.4.
UniGene; Hs.408960; -.
ProteinModelPortal; P78508; -.
SMR; P78508; -.
BioGrid; 109968; 19.
IntAct; P78508; 5.
STRING; 9606.ENSP00000357068; -.
BindingDB; P78508; -.
ChEMBL; CHEMBL2146348; -.
DrugBank; DB01392; Yohimbine.
GuidetoPHARMACOLOGY; 438; -.
TCDB; 1.A.2.1.16; the inward rectifier k(+) channel (irk-c) family.
iPTMnet; P78508; -.
PhosphoSitePlus; P78508; -.
BioMuta; KCNJ10; -.
DMDM; 2493605; -.
PaxDb; P78508; -.
PeptideAtlas; P78508; -.
PRIDE; P78508; -.
TopDownProteomics; P78508; -.
DNASU; 3766; -.
Ensembl; ENST00000368089; ENSP00000357068; ENSG00000177807.
Ensembl; ENST00000638728; ENSP00000492619; ENSG00000177807.
Ensembl; ENST00000638868; ENSP00000491250; ENSG00000177807.
GeneID; 3766; -.
KEGG; hsa:3766; -.
UCSC; uc001fuw.3; human.
CTD; 3766; -.
DisGeNET; 3766; -.
EuPathDB; HostDB:ENSG00000177807.6; -.
GeneCards; KCNJ10; -.
GeneReviews; KCNJ10; -.
HGNC; HGNC:6256; KCNJ10.
MalaCards; KCNJ10; -.
MIM; 602208; gene.
MIM; 612780; phenotype.
neXtProt; NX_P78508; -.
OpenTargets; ENSG00000177807; -.
Orphanet; 199343; EAST syndrome.
Orphanet; 705; Pendred syndrome.
PharmGKB; PA30043; -.
eggNOG; KOG3827; Eukaryota.
eggNOG; ENOG410XQ62; LUCA.
GeneTree; ENSGT00900000140895; -.
HOGENOM; HOG000237326; -.
HOVERGEN; HBG006178; -.
InParanoid; P78508; -.
KO; K05003; -.
OMA; HTPCVME; -.
OrthoDB; EOG091G08HC; -.
PhylomeDB; P78508; -.
TreeFam; TF313676; -.
Reactome; R-HSA-1296041; Activation of G protein gated Potassium channels.
Reactome; R-HSA-1296067; Potassium transport channels.
Reactome; R-HSA-997272; Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
ChiTaRS; KCNJ10; human.
GeneWiki; KCNJ10; -.
GenomeRNAi; 3766; -.
PRO; PR:P78508; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000177807; -.
CleanEx; HS_KCNJ10; -.
ExpressionAtlas; P78508; baseline and differential.
Genevisible; P78508; HS.
GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0098793; C:presynapse; IEA:GOC.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0015272; F:ATP-activated inward rectifier potassium channel activity; TAS:ProtInc.
GO; GO:0015467; F:G-protein activated inward rectifier potassium channel activity; TAS:Reactome.
GO; GO:0005242; F:inward rectifier potassium channel activity; TAS:Reactome.
GO; GO:0007628; P:adult walking behavior; IEA:Ensembl.
GO; GO:0022010; P:central nervous system myelination; IEA:Ensembl.
GO; GO:0051935; P:glutamate reuptake; IEA:Ensembl.
GO; GO:0055075; P:potassium ion homeostasis; IEA:Ensembl.
GO; GO:0010107; P:potassium ion import; IBA:GO_Central.
GO; GO:0006813; P:potassium ion transport; TAS:ProtInc.
GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IEA:Ensembl.
GO; GO:0060075; P:regulation of resting membrane potential; IEA:Ensembl.
GO; GO:0007601; P:visual perception; IEA:Ensembl.
Gene3D; 2.60.40.1400; -; 1.
InterPro; IPR014756; Ig_E-set.
InterPro; IPR016449; K_chnl_inward-rec_Kir.
InterPro; IPR003269; K_chnl_inward-rec_Kir1.2.
InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
PANTHER; PTHR11767; PTHR11767; 1.
PANTHER; PTHR11767:SF21; PTHR11767:SF21; 1.
Pfam; PF01007; IRK; 1.
PIRSF; PIRSF005465; GIRK_kir; 1.
PRINTS; PR01322; KIR12CHANNEL.
PRINTS; PR01320; KIRCHANNEL.
SUPFAM; SSF81296; SSF81296; 1.
1: Evidence at protein level;
ATP-binding; Cell membrane; Complete proteome; Deafness;
Disease mutation; Epilepsy; Ion channel; Ion transport; Membrane;
Mental retardation; Nucleotide-binding; Polymorphism; Potassium;
Potassium transport; Reference proteome; Transmembrane;
Transmembrane helix; Transport; Voltage-gated channel.
CHAIN 1 379 ATP-sensitive inward rectifier potassium
channel 10.
/FTId=PRO_0000154953.
TOPO_DOM 1 64 Cytoplasmic. {ECO:0000250}.
TRANSMEM 65 89 Helical; Name=M1. {ECO:0000250}.
TOPO_DOM 90 114 Extracellular. {ECO:0000250}.
INTRAMEM 115 126 Helical; Pore-forming; Name=H5.
{ECO:0000250}.
INTRAMEM 127 133 Pore-forming. {ECO:0000250}.
TOPO_DOM 134 142 Extracellular. {ECO:0000250}.
TRANSMEM 143 164 Helical; Name=M2. {ECO:0000250}.
TOPO_DOM 165 379 Cytoplasmic. {ECO:0000250}.
NP_BIND 210 217 ATP. {ECO:0000255}.
MOTIF 128 133 Selectivity filter. {ECO:0000250}.
SITE 158 158 Role in the control of polyamine-mediated
channel gating and in the blocking by
intracellular magnesium. {ECO:0000250}.
VARIANT 65 65 R -> P (in SESAMES; no effect on
localization to the basolateral membrane
in kidney cells; dbSNP:rs137853066).
{ECO:0000269|PubMed:19289823,
ECO:0000269|PubMed:19420365,
ECO:0000269|PubMed:24561201}.
/FTId=VAR_063059.
VARIANT 68 68 L -> P (in SESAMES).
{ECO:0000269|PubMed:22612257}.
/FTId=VAR_072746.
VARIANT 77 77 G -> R (in SESAMES; important loss of
localization to the basolateral membrane
in kidney cells; in non-tubular cells,
does not form functional channels;
dbSNP:rs137853072).
{ECO:0000269|PubMed:19420365,
ECO:0000269|PubMed:24561201}.
/FTId=VAR_063060.
VARIANT 129 129 I -> V (in SESAMES).
{ECO:0000269|PubMed:22612257}.
/FTId=VAR_072747.
VARIANT 140 140 C -> R (in SESAMES; loss of localization
to the basolateral membrane in kidney
cells; in non-tubular cells, does not
form functional channels;
dbSNP:rs137853068).
{ECO:0000269|PubMed:19289823,
ECO:0000269|PubMed:24561201}.
/FTId=VAR_063061.
VARIANT 164 164 T -> I (in SESAMES; no effect on
localization to the basolateral membrane
in kidney cells; dbSNP:rs137853069).
{ECO:0000269|PubMed:19289823,
ECO:0000269|PubMed:24561201}.
/FTId=VAR_063062.
VARIANT 167 167 A -> V (in SESAMES; loss of localization
to the basolateral membrane in kidney
cells; in non-tubular cells, forms
functional channels; important loss of
MAGI1-binding when transfected in tubular
MDCKII cells, but not in non-tubular
HEK293T cells; dbSNP:rs137853070).
{ECO:0000269|PubMed:19289823,
ECO:0000269|PubMed:24561201}.
/FTId=VAR_063063.
VARIANT 271 271 R -> C (in dbSNP:rs1130183).
{ECO:0000269|PubMed:10659995}.
/FTId=VAR_034018.
VARIANT 271 271 R -> H (in dbSNP:rs3795339).
/FTId=VAR_020339.
VARIANT 297 297 R -> C (in SESAMES; no effect on
localization to the basolateral membrane
in kidney cells; dbSNP:rs137853071).
{ECO:0000269|PubMed:19289823,
ECO:0000269|PubMed:24561201}.
/FTId=VAR_063064.
CONFLICT 50 50 L -> P (in Ref. 2; AAB07046).
{ECO:0000305}.
CONFLICT 83 83 G -> V (in Ref. 5; AAH34036).
{ECO:0000305}.
CONFLICT 166 166 L -> Q (in Ref. 2; AAB07046).
{ECO:0000305}.
SEQUENCE 379 AA; 42508 MW; D9DA013FF4003533 CRC64;
MTSVAKVYYS QTTQTESRPL MGPGIRRRRV LTKDGRSNVR MEHIADKRFL YLKDLWTTFI
DMQWRYKLLL FSATFAGTWF LFGVVWYLVA VAHGDLLELD PPANHTPCVV QVHTLTGAFL
FSLESQTTIG YGFRYISEEC PLAIVLLIAQ LVLTTILEIF ITGTFLAKIA RPKKRAETIR
FSQHAVVASH NGKPCLMIRV ANMRKSLLIG CQVTGKLLQT HQTKEGENIR LNQVNVTFQV
DTASDSPFLI LPLTFYHVVD ETSPLKDLPL RSGEGDFELV LILSGTVEST SATCQVRTSY
LPEEILWGYE FTPAISLSAS GKYIADFSLF DQVVKVASPS GLRDSTVRYG DPEKLKLEES
LREQAEKEGS ALSVRISNV


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