Gpr35
entrez
64095
canonical
uniprot
Q9ES90
canonical
ensembl
ENSMUSG00000026271
resolver
ensp
ENSMUSP00000070832
resolver
ensp
ENSMUSP00000126914
resolver
ensp
ENSMUSP00000139648
resolver
ensp
ENSMUSP00000313156
resolver
enst
ENSMUST00000064480
resolver
enst
ENSMUST00000169198
resolver
enst
ENSMUST00000186298
resolver
genesymbol
Gpr35
resolver
uniprot
Q3TBY9
resolver
uniprot
Q3TU48
resolver
uniprot
Q8BS98
resolver
uniprot
Q8CB97
resolver
uniprot_entry
GPR35_MOUSE
resolver
uniprot_entry
Q3TBY9_MOUSE
resolver
uniprot_entry
Q3TU48_MOUSE
resolver
uniprot_entry
Q8BS98_MOUSE
resolver
uniprot_entry
Q8CB97_MOUSE
resolver
amino_acid_sequence
MNSTTCNSTLTWPASVNNFFIIYSALLLVLGLLLNSVALWVFCYRMHQWTETRIYMTNLAVADLCLLCSLPFVLYSLKYSSSDTPVCQLSQGIYLANRYMSISLVTAIAVDRYVAVRHPLRARELRSPRQAAAVCVALWVIVVTSLVVRWRLGMQEGGFCFSSQTRRNFSTTAFSLLGFYLPLAIVVFCSLQVVTVLSRRPAADVGQAEATQKATHMVWANLAVFVICFLPLHVVLTVQVSLNLNTCAARDTFSRALSITGKLSDTNCCLDAICYYYMAREFQEASKPATSSNTPHKSQDSQILSLT
uniprot
proteins
function
FUNCTION: G protein-coupled receptor that binds to several ligands including the tryptophan metabolite kynurenic acid (KYNA), lysophosphatidic acid (LPA) or 5-hydroxyindoleacetic acid (5-HIAA) with high affinity, leading to rapid and transient activation of numerous intracellular signaling pathways (PubMed:16754668, PubMed:29414686, PubMed:32755573). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of downstream effectors, such as adenylate cyclase (By similarity). GPR35 can couple with G(i)/G(o)- or G(12)/G(13) classes of G alpha proteins depending on the context, mediating the inhibition of adenylate cyclase or activation Rho small GTPases, respectively (By similarity). KYNA-binding promotes monocyte adhesion to vascular endothelium under flow conditions, leading to G(i)/GNAI1 activation and inhibition of adenylate cyclase (By similarity). Involved in cardioprotection during ischemia by promoting mitochondrial remodeling: following KYNA-binding and G(i)/GNAI1 activation, GPR35 is internalized to the outer mitochondrial membrane, where it inhibits mitochondrial adenylate cyclase (ADCY10), allowing ATPIF1 to repress ATP synthase activity (PubMed:35926043). Stimulates lipid metabolism, thermogenic and anti-inflammatory gene expression in adipose tissue once activated by KYNA (PubMed:29414686). Plays a role in neutrophil recruitment to sites of inflammation and bacterial clearance through the major serotonin metabolite 5-HIAA that acts as a physiological ligand (By similarity). In macrophages, activation by lysophosphatidic acid promotes GPR35-induced signaling with a distinct transcriptional profile characterized by TNF production associated with ERK and NF-kappa-B activation (PubMed:32755573). In turn, induces chemotaxis of macrophages (PubMed:32755573). {ECO:0000250|UniProtKB:Q9HC97, ECO:0000269|PubMed:16754668, ECO:0000269|PubMed:29414686, ECO:0000269|PubMed:32755573, ECO:0000269|PubMed:35926043}.
uniprot
proteins
mass_dalton
34152
uniprot
proteins
post_translational_modification
PTM: Multiply phosphorylated in clusters of serines and threonines in the C-terminal tail. Phosphorylation of Ser-298 and Ser-301 is mediated by GRK5 and/or GRK6. {ECO:0000250|UniProtKB:Q9HC97}.
uniprot
proteins
protein_family
G protein-coupled receptor 1 family
uniprot
proteins
pubmed
11017071
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16754668
uniprot
proteins
pubmed
29414686
uniprot
proteins
pubmed
32755573
uniprot
proteins
pubmed
35926043
uniprot
proteins
sequence_length
307
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9HC97}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9HC97}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q9HC97}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9HC97}. Note=Internalized to the cytoplasm after exposure to kynurenic acid. Translocates to the outer mitochondrial membrane in response to ischemia. {ECO:0000250|UniProtKB:Q9HC97}.
uniprot
proteins
transmembrane_region
TRANSMEM 15..40; /note="Helical; Name=1"; /evidence="ECO:0000250|UniProtKB:Q9HC97"; TRANSMEM 54..77; /note="Helical; Name=2"; /evidence="ECO:0000250|UniProtKB:Q9HC97"; TRANSMEM 85..110; /note="Helical; Name=3"; /evidence="ECO:0000250|UniProtKB:Q9HC97"; TRANSMEM 132..153; /note="Helical; Name=4"; /evidence="ECO:0000250|UniProtKB:Q9HC97"; TRANSMEM 169..191; /note="Helical; Name=5"; /evidence="ECO:0000250|UniProtKB:Q9HC97"; TRANSMEM 218..241; /note="Helical; Name=6"; /evidence="ECO:0000250|UniProtKB:Q9HC97"; TRANSMEM 256..278; /note="Helical; Name=7"; /evidence="ECO:0000250|UniProtKB:Q9HC97
uniprot
proteins