GPR35_MOUSE
ID GPR35_MOUSE Reviewed; 307 AA.
AC Q9ES90;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=G-protein coupled receptor 35;
DE AltName: Full=Kynurenic acid receptor;
DE Short=KYNA receptor;
GN Name=Gpr35;
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].
RX PubMed=11017071; DOI=10.1038/79876;
RA Horikawa Y., Oda N., Cox N.J., Li X., Orho-Melander M., Hara M.,
RA Hinokio Y., Lindner T.H., Mashima H., Schwarz P.E.H., del Bosque-Plata L.,
RA Horikawa Y., Oda Y., Yoshiuchi I., Colilla S., Polonsky K.S., Wei S.,
RA Concannon P., Iwasaki N., Schulze J., Baier L.J., Bogardus C., Groop L.,
RA Boerwinkle E., Hanis C.L., Bell G.I.;
RT "Genetic variation in the gene encoding calpain-10 is associated with type
RT 2 diabetes mellitus.";
RL Nat. Genet. 26:163-175(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
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).
RN [3]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=16754668; DOI=10.1074/jbc.m603503200;
RA Wang J., Simonavicius N., Wu X., Swaminath G., Reagan J., Tian H., Ling L.;
RT "Kynurenic acid as a ligand for orphan G protein-coupled receptor GPR35.";
RL J. Biol. Chem. 281:22021-22028(2006).
CC -!- FUNCTION: Acts as a receptor for kynurenic acid, an intermediate in the
CC tryptophan metabolic pathway. The activity of this receptor is mediated
CC by G-proteins that elicit calcium mobilization and inositol phosphate
CC production through G(qi/o) proteins. {ECO:0000269|PubMed:16754668}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in immune and
CC gastrointestinal tissues. {ECO:0000269|PubMed:16754668}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AF200349; AAG18487.1; -; mRNA.
DR EMBL; BC027429; AAH27429.1; -; mRNA.
DR CCDS; CCDS15182.1; -.
DR RefSeq; NP_001097999.1; NM_001104529.1.
DR RefSeq; NP_001258695.1; NM_001271766.1.
DR RefSeq; NP_071715.3; NM_022320.4.
DR RefSeq; XP_006529842.1; XM_006529779.3.
DR RefSeq; XP_006529843.1; XM_006529780.3.
DR RefSeq; XP_006529844.1; XM_006529781.3.
DR RefSeq; XP_011246355.1; XM_011248053.2.
DR AlphaFoldDB; Q9ES90; -.
DR SMR; Q9ES90; -.
DR STRING; 10090.ENSMUSP00000126914; -.
DR BindingDB; Q9ES90; -.
DR ChEMBL; CHEMBL2390813; -.
DR DrugCentral; Q9ES90; -.
DR GuidetoPHARMACOLOGY; 102; -.
DR GlyGen; Q9ES90; 2 sites.
DR PhosphoSitePlus; Q9ES90; -.
DR PaxDb; Q9ES90; -.
DR PRIDE; Q9ES90; -.
DR ProteomicsDB; 271067; -.
DR Antibodypedia; 34526; 234 antibodies from 29 providers.
DR DNASU; 64095; -.
DR Ensembl; ENSMUST00000064480; ENSMUSP00000070832; ENSMUSG00000026271.
DR Ensembl; ENSMUST00000169198; ENSMUSP00000126914; ENSMUSG00000026271.
DR Ensembl; ENSMUST00000186298; ENSMUSP00000139648; ENSMUSG00000026271.
DR GeneID; 64095; -.
DR KEGG; mmu:64095; -.
DR UCSC; uc007cbz.2; mouse.
DR CTD; 2859; -.
DR MGI; MGI:1929509; Gpr35.
DR VEuPathDB; HostDB:ENSMUSG00000026271; -.
DR eggNOG; ENOG502S0QN; Eukaryota.
DR GeneTree; ENSGT01040000240444; -.
DR HOGENOM; CLU_009579_8_2_1; -.
DR InParanoid; Q9ES90; -.
DR OMA; MVWANLV; -.
DR OrthoDB; 966250at2759; -.
DR PhylomeDB; Q9ES90; -.
DR TreeFam; TF335578; -.
DR Reactome; R-MMU-373076; Class A/1 (Rhodopsin-like receptors).
DR BioGRID-ORCS; 64095; 1 hit in 75 CRISPR screens.
DR PRO; PR:Q9ES90; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9ES90; protein.
DR Bgee; ENSMUSG00000026271; Expressed in animal zygote and 66 other tissues.
DR ExpressionAtlas; Q9ES90; baseline and differential.
DR Genevisible; Q9ES90; MM.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0016494; F:C-X-C chemokine receptor activity; ISS:UniProtKB.
DR GO; GO:0004950; F:chemokine receptor activity; ISO:MGI.
DR GO; GO:0004930; F:G protein-coupled receptor activity; ISS:UniProtKB.
DR GO; GO:0070098; P:chemokine-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0007010; P:cytoskeleton organization; IDA:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0048246; P:macrophage chemotaxis; ISO:MGI.
DR GO; GO:1904456; P:negative regulation of neuronal action potential; ISO:MGI.
DR GO; GO:1901386; P:negative regulation of voltage-gated calcium channel activity; ISO:MGI.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISS:UniProtKB.
DR GO; GO:0051482; P:positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G protein-coupled signaling pathway; IBA:GO_Central.
DR GO; GO:0035025; P:positive regulation of Rho protein signal transduction; IBA:GO_Central.
DR CDD; cd15164; 7tmA_GPR35-like; 1.
DR InterPro; IPR044734; 7tmA_GPR35.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
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..307
FT /note="G-protein coupled receptor 35"
FT /id="PRO_0000069564"
FT TOPO_DOM 1..18
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 19..39
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 40..53
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..74
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 75..88
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 89..110
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 111..129
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 130..150
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 151..176
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..197
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 198..217
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..238
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 239..257
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 279..307
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 288..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 2
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 7
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 87..160
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 307 AA; 34152 MW; 0B3D02CECB16710D CRC64;
MNSTTCNSTL TWPASVNNFF IIYSALLLVL GLLLNSVALW VFCYRMHQWT ETRIYMTNLA
VADLCLLCSL PFVLYSLKYS SSDTPVCQLS QGIYLANRYM SISLVTAIAV DRYVAVRHPL
RARELRSPRQ AAAVCVALWV IVVTSLVVRW RLGMQEGGFC FSSQTRRNFS TTAFSLLGFY
LPLAIVVFCS LQVVTVLSRR PAADVGQAEA TQKATHMVWA NLAVFVICFL PLHVVLTVQV
SLNLNTCAAR DTFSRALSIT GKLSDTNCCL DAICYYYMAR EFQEASKPAT SSNTPHKSQD
SQILSLT
