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KCNJ1_MOUSE
ID   KCNJ1_MOUSE             Reviewed;         372 AA.
AC   O88335;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 177.
DE   RecName: Full=ATP-sensitive inward rectifier potassium channel 1;
DE   AltName: Full=ATP-regulated potassium channel ROM-K;
DE   AltName: Full=Inward rectifier K(+) channel Kir1.1;
DE   AltName: Full=Potassium channel, inwardly rectifying subfamily J member 1;
GN   Name=Kcnj1;
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].
RC   STRAIN=CD-1; TISSUE=Kidney;
RA   Xu J.Z., Mount D.B., Hebert S.C.;
RT   "Cloning and characterization of alternatively spliced isoforms of mouse
RT   ROMK.";
RL   Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: In the kidney, probably plays a major role in potassium
CC       homeostasis. Inward rectifier potassium channels are characterized by a
CC       greater tendency to allow potassium to flow into the cell rather than
CC       out of it. Their voltage dependence is regulated by the concentration
CC       of extracellular potassium; as external potassium is raised, the
CC       voltage range of the channel opening shifts to more positive voltages.
CC       The inward rectification is mainly due to the blockage of outward
CC       current by internal magnesium. This channel is activated by internal
CC       ATP and can be blocked by external barium (By similarity).
CC       {ECO:0000250|UniProtKB:P48048}.
CC   -!- ACTIVITY REGULATION: Inhibited by WNK3. {ECO:0000250|UniProtKB:P48048}.
CC   -!- SUBUNIT: Interacts with SGK1 and SLC9A3R2/NHERF2.
CC       {ECO:0000250|UniProtKB:P48048}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P48048};
CC       Multi-pass membrane protein {ECO:0000250|UniProtKB:P48048}.
CC       Note=Phosphorylation at Ser-44 by SGK1 is necessary for its expression
CC       at the cell membrane. {ECO:0000250|UniProtKB:P48048}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced.;
CC       Name=1;
CC         IsoId=O88335-1; Sequence=Displayed;
CC   -!- PTM: Phosphorylation at Ser-25 by SGK1 is necessary for its expression
CC       at the cell membrane. {ECO:0000250|UniProtKB:P48048}.
CC   -!- SIMILARITY: Belongs to the inward rectifier-type potassium channel (TC
CC       1.A.2.1) family. KCNJ1 subfamily. {ECO:0000305}.
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DR   EMBL; AF012834; AAC24973.1; -; mRNA.
DR   EMBL; BC020525; AAH20525.1; -; mRNA.
DR   CCDS; CCDS22953.1; -. [O88335-1]
DR   RefSeq; NP_062633.1; NM_019659.3. [O88335-1]
DR   AlphaFoldDB; O88335; -.
DR   SMR; O88335; -.
DR   BioGRID; 207940; 5.
DR   IntAct; O88335; 3.
DR   STRING; 10090.ENSMUSP00000131625; -.
DR   GlyGen; O88335; 1 site.
DR   iPTMnet; O88335; -.
DR   PhosphoSitePlus; O88335; -.
DR   PaxDb; O88335; -.
DR   PRIDE; O88335; -.
DR   ProteomicsDB; 269202; -. [O88335-1]
DR   Antibodypedia; 33020; 289 antibodies from 31 providers.
DR   DNASU; 56379; -.
DR   Ensembl; ENSMUST00000047334; ENSMUSP00000046793; ENSMUSG00000041248. [O88335-1]
DR   Ensembl; ENSMUST00000213393; ENSMUSP00000150540; ENSMUSG00000041248. [O88335-1]
DR   GeneID; 56379; -.
DR   KEGG; mmu:56379; -.
DR   UCSC; uc009orx.2; mouse. [O88335-1]
DR   CTD; 3758; -.
DR   MGI; MGI:1927248; Kcnj1.
DR   VEuPathDB; HostDB:ENSMUSG00000041248; -.
DR   eggNOG; KOG3827; Eukaryota.
DR   GeneTree; ENSGT00990000203615; -.
DR   HOGENOM; CLU_022738_3_0_1; -.
DR   InParanoid; O88335; -.
DR   OMA; LTGHCAG; -.
DR   PhylomeDB; O88335; -.
DR   Reactome; R-MMU-1296067; Potassium transport channels.
DR   BioGRID-ORCS; 56379; 1 hit in 72 CRISPR screens.
DR   ChiTaRS; Kcnj1; mouse.
DR   PRO; PR:O88335; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; O88335; protein.
DR   Bgee; ENSMUSG00000041248; Expressed in right kidney and 51 other tissues.
DR   ExpressionAtlas; O88335; baseline and differential.
DR   Genevisible; O88335; MM.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0005524; F:ATP binding; ISO:MGI.
DR   GO; GO:0015272; F:ATP-activated inward rectifier potassium channel activity; ISO:MGI.
DR   GO; GO:0005242; F:inward rectifier potassium channel activity; ISS:UniProtKB.
DR   GO; GO:0042277; F:peptide binding; ISO:MGI.
DR   GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISO:MGI.
DR   GO; GO:0030955; F:potassium ion binding; ISO:MGI.
DR   GO; GO:0071286; P:cellular response to magnesium ion; ISO:MGI.
DR   GO; GO:0072359; P:circulatory system development; IMP:MGI.
DR   GO; GO:0010467; P:gene expression; IMP:MGI.
DR   GO; GO:0001822; P:kidney development; IMP:MGI.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR   GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR   GO; GO:1990573; P:potassium ion import across plasma membrane; ISS:UniProtKB.
DR   GO; GO:0006813; P:potassium ion transport; ISO:MGI.
DR   GO; GO:1900128; P:regulation of G-protein activated inward rectifier potassium channel activity; IMP:MGI.
DR   GO; GO:0034765; P:regulation of ion transmembrane transport; IBA:GO_Central.
DR   GO; GO:0070294; P:renal sodium ion absorption; IMP:MGI.
DR   GO; GO:0001894; P:tissue homeostasis; 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; IPR003268; K_chnl_inward-rec_Kir1.1.
DR   InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR   InterPro; IPR040445; Kir_TM.
DR   PANTHER; PTHR11767; PTHR11767; 1.
DR   PANTHER; PTHR11767:SF6; PTHR11767:SF6; 1.
DR   Pfam; PF01007; IRK; 1.
DR   Pfam; PF17655; IRK_C; 1.
DR   PIRSF; PIRSF005465; GIRK_kir; 1.
DR   PRINTS; PR01320; KIRCHANNEL.
DR   SUPFAM; SSF81296; SSF81296; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; ATP-binding; Cell membrane; Glycoprotein;
KW   Ion channel; Ion transport; Membrane; Nucleotide-binding; Phosphoprotein;
KW   Potassium; Potassium transport; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN           1..372
FT                   /note="ATP-sensitive inward rectifier potassium channel 1"
FT                   /id="PRO_0000154918"
FT   TOPO_DOM        1..58
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:O00180"
FT   TRANSMEM        59..83
FT                   /note="Helical; Name=M1"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        84..108
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:O00180"
FT   INTRAMEM        109..120
FT                   /note="Helical; Pore-forming; Name=H5"
FT                   /evidence="ECO:0000250"
FT   INTRAMEM        121..127
FT                   /note="Pore-forming"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        128..136
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:O00180"
FT   TRANSMEM        137..158
FT                   /note="Helical; Name=M2"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        159..372
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:O00180"
FT   MOTIF           122..127
FT                   /note="Selectivity filter"
FT                   /evidence="ECO:0000250|UniProtKB:Q63472"
FT   BINDING         204..211
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   SITE            152
FT                   /note="Role in the control of polyamine-mediated channel
FT                   gating and in the blocking by intracellular magnesium"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         25
FT                   /note="Phosphoserine; by SGK1"
FT                   /evidence="ECO:0000250|UniProtKB:P48048"
FT   CARBOHYD        98
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   372 AA;  42776 MW;  EA95D896622232D6 CRC64;
     MFKHLRRWFV THIFGRSRQR ARLVSKDGRC NIEFGNVDAQ SRFIFFVDIW TTVLDLKWRY
     KMTVFITAFL GSWFLFGLLW YVVAYVHKDL PEFYPPDNRT PCVENINGMT SAFLFSLETQ
     VTIGYGFRFV TEQCATAIFL LIFQSILGVI INSFMCGAIL AKISRPKKRA KTITFSKNAV
     ISKRGGKLCL LIRVANLRKS LLIGSHIYGK LLKTTITPEG ETIILDQTNI NFVVDAGNEN
     LFFISPLTIY HIIDHNSPFF HMAAETLSQQ DFELVVFLDG TVESTSATCQ VRTSYIPEEV
     LWGYRFVPIV SKTKEGKYRV DFHNFGKTVE VETPHCAMCL YNEKDARARM KRGYDNPNFV
     LSEVDETDDT QM
 
 
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