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KCJ10_MOUSE
ID   KCJ10_MOUSE             Reviewed;         379 AA.
AC   Q9JM63;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 166.
DE   RecName: Full=ATP-sensitive inward rectifier potassium channel 10;
DE   AltName: Full=Inward rectifier K(+) channel Kir4.1;
DE   AltName: Full=Potassium channel, inwardly rectifying subfamily J member 10;
GN   Name=Kcnj10;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Inanobe A., Takahashi K., Tanemoto M., Fujita A., Kurachi Y.;
RL   Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=CD-1, and ICR; TISSUE=Brain;
RX   PubMed=11169792;
RX   DOI=10.1002/1098-1136(20010101)33:1<57::aid-glia1006>3.0.co;2-0;
RA   Li L., Head V., Timpe L.C.;
RT   "Identification of an inward rectifier potassium channel gene expressed in
RT   mouse cortical astrocytes.";
RL   Glia 33:57-71(2001).
RN   [3]
RP   INTERACTION WITH PATJ.
RX   PubMed=9647694; DOI=10.1006/mcne.1998.0679;
RA   Kurschner C., Mermelstein P.G., Holden W.T., Surmeier D.J.;
RT   "CIPP, a novel multivalent PDZ domain protein, selectively interacts with
RT   Kir4.0 family members, NMDA receptor subunits, neurexins, and
RT   neuroligins.";
RL   Mol. Cell. Neurosci. 11:161-172(1998).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, and Kidney;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=33811157; DOI=10.1681/asn.2020111587;
RA   Schlingmann K.P., Renigunta A., Hoorn E.J., Forst A.L., Renigunta V.,
RA   Atanasov V., Mahendran S., Barakat T.S., Gillion V., Godefroid N.,
RA   Brooks A.S., Lugtenberg D., Lake J., Debaix H., Rudin C., Knebelmann B.,
RA   Tellier S., Rousset-Rouviere C., Viering D., de Baaij J.H.F., Weber S.,
RA   Palygin O., Staruschenko A., Kleta R., Houillier P., Bockenhauer D.,
RA   Devuyst O., Vargas-Poussou R., Warth R., Zdebik A.A., Konrad M.;
RT   "Defects in KCNJ16 cause a novel tubulopathy with hypokalemia, salt
RT   wasting, disturbed acid-base homeostasis, and sensorineural deafness.";
RL   J. Am. Soc. Nephrol. 32:1498-1512(2021).
CC   -!- FUNCTION: May be responsible for potassium buffering action of glial
CC       cells in the brain. Inward rectifier potassium channels are
CC       characterized by a greater tendency to allow potassium to flow into the
CC       cell rather than out of it. Their voltage dependence is regulated by
CC       the concentration of extracellular potassium; as external potassium is
CC       raised, the voltage range of the channel opening shifts to more
CC       positive voltages. The inward rectification is mainly due to the
CC       blockage of outward current by internal magnesium. Can be blocked by
CC       extracellular barium and cesium (By similarity). In the kidney,
CC       together with KCNJ16, mediates basolateral K(+) recycling in distal
CC       tubules; this process is critical for Na(+) reabsorption at the tubules
CC       (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P78508}.
CC   -!- SUBUNIT: Heterodimer with Kir5.1/KCNJ16; this interaction is required
CC       for KCNJ16 localization to the basolateral membrane in kidney cells.
CC       Interacts with MAGI1, alone and possibly as a heterodimer with KCNJ16;
CC       this interaction may facilitate KCNJ10/KCNJ16 potassium channel
CC       expression at the basolateral membrane in kidney cells (By similarity).
CC       Interacts with PATJ (PubMed:9647694). {ECO:0000250|UniProtKB:P78508,
CC       ECO:0000269|PubMed:9647694}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P78508}; Multi-
CC       pass membrane protein {ECO:0000250|UniProtKB:P78508}. Basolateral cell
CC       membrane {ECO:0000250|UniProtKB:P78508}. Note=In kidney distal
CC       convoluted tubules, located in the basolateral membrane where it
CC       colocalizes with KCNJ16. {ECO:0000250|UniProtKB:P78508}.
CC   -!- TISSUE SPECIFICITY: Widely expressed in adult brain, including in the
CC       neocortex, the stratum pyrimadale of the hippocampus and the piriform
CC       cortex. Expressed by cultured astrocytes and also by cocultured
CC       cortical neurons (at protein level). Expressed in the distal segment of
CC       the nephron (PubMed:33811157). {ECO:0000269|PubMed:11169792,
CC       ECO:0000269|PubMed:33811157}.
CC   -!- SIMILARITY: Belongs to the inward rectifier-type potassium channel (TC
CC       1.A.2.1) family. KCNJ10 subfamily. {ECO:0000305}.
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DR   EMBL; AB039879; BAA92432.1; -; mRNA.
DR   EMBL; AF322631; AAG42845.1; -; mRNA.
DR   CCDS; CCDS15512.1; -.
DR   RefSeq; NP_001034573.1; NM_001039484.1.
DR   RefSeq; XP_006496740.2; XM_006496677.3.
DR   AlphaFoldDB; Q9JM63; -.
DR   SMR; Q9JM63; -.
DR   BioGRID; 200895; 11.
DR   CORUM; Q9JM63; -.
DR   IntAct; Q9JM63; 6.
DR   MINT; Q9JM63; -.
DR   STRING; 10090.ENSMUSP00000054356; -.
DR   iPTMnet; Q9JM63; -.
DR   PhosphoSitePlus; Q9JM63; -.
DR   SwissPalm; Q9JM63; -.
DR   MaxQB; Q9JM63; -.
DR   PaxDb; Q9JM63; -.
DR   PRIDE; Q9JM63; -.
DR   ProteomicsDB; 301767; -.
DR   Antibodypedia; 1679; 288 antibodies from 27 providers.
DR   DNASU; 16513; -.
DR   Ensembl; ENSMUST00000056136; ENSMUSP00000054356; ENSMUSG00000044708.
DR   GeneID; 16513; -.
DR   KEGG; mmu:16513; -.
DR   UCSC; uc007dqj.1; mouse.
DR   CTD; 3766; -.
DR   MGI; MGI:1194504; Kcnj10.
DR   VEuPathDB; HostDB:ENSMUSG00000044708; -.
DR   eggNOG; KOG3827; Eukaryota.
DR   GeneTree; ENSGT00990000203615; -.
DR   HOGENOM; CLU_022738_3_3_1; -.
DR   InParanoid; Q9JM63; -.
DR   OMA; QVNVAFQ; -.
DR   OrthoDB; 956263at2759; -.
DR   PhylomeDB; Q9JM63; -.
DR   TreeFam; TF313676; -.
DR   Reactome; R-MMU-1296041; Activation of G protein gated Potassium channels.
DR   Reactome; R-MMU-1296067; Potassium transport channels.
DR   Reactome; R-MMU-997272; Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
DR   BioGRID-ORCS; 16513; 3 hits in 73 CRISPR screens.
DR   ChiTaRS; Kcnj10; mouse.
DR   PRO; PR:Q9JM63; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; Q9JM63; protein.
DR   Bgee; ENSMUSG00000044708; Expressed in cerebellar nuclear complex and 108 other tissues.
DR   ExpressionAtlas; Q9JM63; baseline and differential.
DR   Genevisible; Q9JM63; MM.
DR   GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR   GO; GO:0097449; C:astrocyte projection; IDA:ARUK-UCL.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR   GO; GO:0044297; C:cell body; IDA:ARUK-UCL.
DR   GO; GO:0097546; C:ciliary base; IDA:MGI.
DR   GO; GO:0005887; C:integral component of plasma membrane; IC:MGI.
DR   GO; GO:0005902; C:microvillus; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0098793; C:presynapse; IEA:GOC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0005242; F:inward rectifier potassium channel activity; IMP:MGI.
DR   GO; GO:0005267; F:potassium channel activity; IDA:MGI.
DR   GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR   GO; GO:0007628; P:adult walking behavior; IMP:MGI.
DR   GO; GO:0035865; P:cellular response to potassium ion; IMP:MGI.
DR   GO; GO:0022010; P:central nervous system myelination; IMP:MGI.
DR   GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR   GO; GO:0051935; P:glutamate reuptake; IMP:MGI.
DR   GO; GO:0051938; P:L-glutamate import; ISO:MGI.
DR   GO; GO:0060081; P:membrane hyperpolarization; ISO:MGI.
DR   GO; GO:1905515; P:non-motile cilium assembly; IMP:MGI.
DR   GO; GO:0014003; P:oligodendrocyte development; IMP:MGI.
DR   GO; GO:0055075; P:potassium ion homeostasis; IMP:MGI.
DR   GO; GO:1990573; P:potassium ion import across plasma membrane; ISO:MGI.
DR   GO; GO:0071805; P:potassium ion transmembrane transport; IMP:MGI.
DR   GO; GO:0006813; P:potassium ion transport; IDA:MGI.
DR   GO; GO:0034765; P:regulation of ion transmembrane transport; IBA:GO_Central.
DR   GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IMP:MGI.
DR   GO; GO:0042391; P:regulation of membrane potential; IMP:MGI.
DR   GO; GO:0060075; P:regulation of resting membrane potential; IMP:MGI.
DR   GO; GO:0051930; P:regulation of sensory perception of pain; ISO:MGI.
DR   GO; GO:0007601; P:visual perception; IMP:MGI.
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; IPR003269; K_chnl_inward-rec_Kir1.2.
DR   InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR   InterPro; IPR040445; Kir_TM.
DR   PANTHER; PTHR11767; PTHR11767; 1.
DR   PANTHER; PTHR11767:SF21; PTHR11767:SF21; 1.
DR   Pfam; PF01007; IRK; 1.
DR   Pfam; PF17655; IRK_C; 1.
DR   PIRSF; PIRSF005465; GIRK_kir; 1.
DR   PRINTS; PR01322; KIR12CHANNEL.
DR   PRINTS; PR01320; KIRCHANNEL.
DR   SUPFAM; SSF81296; SSF81296; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell membrane; Ion channel; Ion transport; Membrane;
KW   Nucleotide-binding; Potassium; Potassium transport; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN           1..379
FT                   /note="ATP-sensitive inward rectifier potassium channel 10"
FT                   /id="PRO_0000154954"
FT   TOPO_DOM        1..64
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        65..89
FT                   /note="Helical; Name=M1"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        90..114
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   INTRAMEM        115..126
FT                   /note="Helical; Pore-forming; Name=H5"
FT                   /evidence="ECO:0000250"
FT   INTRAMEM        127..133
FT                   /note="Pore-forming"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        134..142
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        143..164
FT                   /note="Helical; Name=M2"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        165..379
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   MOTIF           128..133
FT                   /note="Selectivity filter"
FT                   /evidence="ECO:0000250"
FT   BINDING         210..217
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   SITE            158
FT                   /note="Role in the control of polyamine-mediated channel
FT                   gating and in the blocking by intracellular magnesium"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   379 AA;  42432 MW;  7FF08446B7F43453 CRC64;
     MTSVAKVYYS QTTQTESRPL VAPGIRRRRV LTKDGRSNVR MEHIADKRFL YLKDLWTTFI
     DMQWRYKLLL FSATFAGTWF LFGVVWYLVA VAHGDLLELG 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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