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CLTR2_MOUSE
ID   CLTR2_MOUSE             Reviewed;         309 AA.
AC   Q920A1; A2RT90;
DT   11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=Cysteinyl leukotriene receptor 2;
DE            Short=CysLTR2;
GN   Name=Cysltr2; Synonyms=Cyslt2;
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   TISSUE=Heart;
RX   PubMed=11591709; DOI=10.1074/jbc.m107556200;
RA   Hui Y., Yang G., Galczenski H., Figueroa D.J., Austin C.P., Copeland N.G.,
RA   Gilbert D.J., Jenkins N.A., Funk C.D.;
RT   "The murine cysteinyl leukotriene 2 (CysLT2) receptor. cDNA and genomic
RT   cloning, alternative splicing, and in vitro characterization.";
RL   J. Biol. Chem. 276:47489-47495(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung;
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: Receptor for cysteinyl leukotrienes. The response is mediated
CC       via a G-protein that activates a phosphatidylinositol-calcium second
CC       messenger system. The rank order of affinities for the leukotrienes is
CC       LTC4 = LTD4 >> LTE4.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Widely expressed at low levels, with highest
CC       expression in the spleen, thymus and adrenal gland, and lower in the
CC       kidney, brain and peripheral blood leukocytes.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; AF331658; AAK97354.1; -; mRNA.
DR   EMBL; CH466535; EDL35864.1; -; Genomic_DNA.
DR   EMBL; CH466535; EDL35865.1; -; Genomic_DNA.
DR   EMBL; BC132414; AAI32415.1; -; mRNA.
DR   EMBL; BC132418; AAI32419.1; -; mRNA.
DR   CCDS; CCDS27265.1; -.
DR   RefSeq; NP_001155884.1; NM_001162412.1.
DR   RefSeq; NP_598481.2; NM_133720.3.
DR   RefSeq; XP_011243480.1; XM_011245178.2.
DR   AlphaFoldDB; Q920A1; -.
DR   SMR; Q920A1; -.
DR   STRING; 10090.ENSMUSP00000040715; -.
DR   GlyGen; Q920A1; 1 site.
DR   PhosphoSitePlus; Q920A1; -.
DR   MaxQB; Q920A1; -.
DR   PaxDb; Q920A1; -.
DR   PRIDE; Q920A1; -.
DR   ProteomicsDB; 285498; -.
DR   DNASU; 70086; -.
DR   Ensembl; ENSMUST00000044664; ENSMUSP00000040715; ENSMUSG00000033470.
DR   Ensembl; ENSMUST00000169168; ENSMUSP00000125958; ENSMUSG00000033470.
DR   GeneID; 70086; -.
DR   KEGG; mmu:70086; -.
DR   UCSC; uc007upi.2; mouse.
DR   CTD; 57105; -.
DR   MGI; MGI:1917336; Cysltr2.
DR   VEuPathDB; HostDB:ENSMUSG00000033470; -.
DR   eggNOG; ENOG502RX8K; Eukaryota.
DR   GeneTree; ENSGT00990000203619; -.
DR   HOGENOM; CLU_009579_8_2_1; -.
DR   InParanoid; Q920A1; -.
DR   OMA; CMLSICY; -.
DR   OrthoDB; 930634at2759; -.
DR   PhylomeDB; Q920A1; -.
DR   TreeFam; TF350009; -.
DR   Reactome; R-MMU-163359; Glucagon signaling in metabolic regulation.
DR   Reactome; R-MMU-391906; Leukotriene receptors.
DR   Reactome; R-MMU-416476; G alpha (q) signalling events.
DR   Reactome; R-MMU-418555; G alpha (s) signalling events.
DR   Reactome; R-MMU-420092; Glucagon-type ligand receptors.
DR   BioGRID-ORCS; 70086; 1 hit in 73 CRISPR screens.
DR   PRO; PR:Q920A1; -.
DR   Proteomes; UP000000589; Chromosome 14.
DR   RNAct; Q920A1; protein.
DR   Bgee; ENSMUSG00000033470; Expressed in secondary oocyte and 46 other tissues.
DR   Genevisible; Q920A1; MM.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IDA:MGI.
DR   GO; GO:0001631; F:cysteinyl leukotriene receptor activity; IDA:MGI.
DR   GO; GO:0008528; F:G protein-coupled peptide receptor activity; IBA:GO_Central.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; ISO:MGI.
DR   GO; GO:0010942; P:positive regulation of cell death; ISO:MGI.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR   InterPro; IPR013311; CLT2_recept.
DR   InterPro; IPR004071; Cyst_leuk_rcpt.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR01903; CYSLT2RECPTR.
DR   PRINTS; PR01533; CYSLTRECPTR.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW   Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..309
FT                   /note="Cysteinyl leukotriene receptor 2"
FT                   /id="PRO_0000069304"
FT   TOPO_DOM        1..26
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        27..47
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        48..56
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        57..77
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        78..98
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        99..119
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        120..138
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        139..159
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        160..187
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        188..208
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        209..229
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        230..250
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        251..271
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        272..292
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        293..309
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        14
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        95..171
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   CONFLICT        122
FT                   /note="L -> Q (in Ref. 1; AAK97354)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   309 AA;  35213 MW;  BA8B055A00D1CBFE CRC64;
     MEVTGTPSSY SNRNCTIENF KKEFYPIIYL IIFFWGALGN GFSIYVFLQT CKKSTSVNVF
     MLNLATSDFL FISTLPFRAD YYFRGSNWIF GDLACRVMSY SLYVNMYTSI YFLTVLSVVR
     FLATVHPFRM FHVTSVRSAW ILCGIIWVFI MASSALLLVN GQEEKDNIIS CLELSPQKFK
     SLLIMNHIAV AVGFLLPFLT LTVCYLLIIR ILLKAEIPES GPRAAHRKAL TTIVIAMITF
     LLCFLPYHAL RTLHLVTWDK DSCGDVLHKA TVITLTMAAA NSCFNPFLYY FAGENFKARL
     RAIFSKVHL
 
 
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