GPR37
entrez
2861
canonical
uniprot
O15354
canonical
ensembl
ENSG00000170775
resolver
ensp
ENSP00000306449
resolver
enst
ENST00000303921
resolver
genesymbol
GPR37
resolver
hgnc
HGNC:4494
resolver
uniprot
A4D0Y6
resolver
uniprot
O00348
resolver
uniprot
O14768
resolver
uniprot
Q8TD39
resolver
uniprot_entry
GPR37_HUMAN
resolver
uniprot_sec
A4D0Y6
resolver
uniprot_sec
O00348
resolver
uniprot_sec
O14768
resolver
uniprot_sec
Q8TD39
resolver
amino_acid_sequence
MRAPGALLARMSRLLLLLLLKVSASSALGVAPASRNETCLGESCAPTVIQRRGRDAWGPGNSARDVLRARAPREEQGAAFLAGPSWDLPAAPGRDPAAGRGAEASAAGPPGPPTRPPGPWRWKGARGQEPSETLGRGNPTALQLFLQISEEEEKGPRGAGISGRSQEQSVKTVPGASDLFYWPRRAGKLQGSHHKPLSKTANGLAGHEGWTIALPGRALAQNGSLGEGIHEPGGPRRGNSTNRRVRLKNPFYPLTQESYGAYAVMCLSVVIFGTGIIGNLAVMCIVCHNYYMRSISNSLLANLAFWDFLIIFFCLPLVIFHELTKKWLLEDFSCKIVPYIEVASLGVTTFTLCALCIDRFRAATNVQMYYEMIENCSSTTAKLAVIWVGALLLALPEVVLRQLSKEDLGFSGRAPAERCIIKISPDLPDTIYVLALTYDSARLWWYFGCYFCLPTLFTITCSLVTARKIRKAEKACTRGNKRQIQLESQMNCTVVALTILYGFCIIPENICNIVTAYMATGVSQQTMDLLNIISQFLLFFKSCVTPVLLFCLCKPFSRAFMECCCCCCEECIQKSSTVTSDDNDNEYTTELELSPFSTIRREMSTFASVGTHC
uniprot
proteins
function
FUNCTION: G protein-coupled receptor that plays a role in several physiological pathways such as resolution of inflammatory pain and oligodendrocyte differentiation (By similarity). Acts as a receptor for several ligands including prosaposin, osteocalcin or neuroprotectin D1. Ligand binding induces endocytosis, followed by an ERK phosphorylation cascade (PubMed:11439185, PubMed:23690594). Acts as a receptor for osteocalcin (OCN) to regulate oligodendrocyte differentiation and central nervous system myelination. Mechanistically, plays a negative role in oligodendrocyte differentiation and myelination during development via activation of the ERK1/2 signaling pathway. Therefore, regulates the stability of myelin or resistance of myelin itself to demyelination. Upon activation by neuroprotectin D1 (NPD1), promotes the activation of phagocytosis in macrophages as well as the shift in cytokine release toward an anti-inflammatory profile, and thus helps to reverse inflammatory pain. In addition, the increased macrophage phagocytosis mediates protection against sepsis upon pathogen infection. Additionally, extracellular vesicles derived from efferocyte express prosaposin, which binds to macrophage GPR37 to increase expression of the efferocytosis receptor TIM4 via an ERK-AP1-dependent signaling axis, leading to increased macrophage efferocytosis efficiency and accelerated resolution of inflammation (By similarity). May also act as a maturation factor of LRP6, protecting LRP6 from the endoplasmic reticulum (ER)-associated protein degradation (ERAD) and thereby promoting the Wnt/beta-catenin signaling pathway (PubMed:28341812). {ECO:0000250|UniProtKB:Q9QY42, ECO:0000269|PubMed:11439185, ECO:0000269|PubMed:23690594, ECO:0000269|PubMed:25977097, ECO:0000269|PubMed:28341812, ECO:0000269|PubMed:9526070}.
uniprot
proteins
mass_dalton
67114
uniprot
proteins
mutagenesis
MUTAGEN 54; /note="R->A: Strong increase of full-length receptor abundance at the cell surface."; /evidence="ECO:0000269|PubMed:34042202"; MUTAGEN 558; /note="R->Q: Strong loss of interaction with MUPP1 resulting in dendritic alteration."; /evidence="ECO:0000269|PubMed:25977097
uniprot
proteins
post_translational_modification
PTM: The N-terminus is cleaved by ADAM10 metalloproteinase; mediating limited proteolysis leading to the release of receptor ectodomain by shedding (PubMed:26869225, PubMed:34042202). In addition, cleaved by FURIN between Arg-54 and Asp-55 (PubMed:34042202). {ECO:0000269|PubMed:26869225, ECO:0000269|PubMed:34042202}.; PTM: Ubiquitinated by PRKN in the presence of UBE2E1 and UBE2L3 in the endoplasmic reticulum. The unfolded form is specifically ubiquitinated by SYVN1, which promotes its proteasomal degradation and prevents neuronal cell death. {ECO:0000269|PubMed:17059562}.
uniprot
proteins
protein_family
G protein-coupled receptor 1 family
uniprot
proteins
pubmed
11439185
uniprot
proteins
pubmed
12150907
uniprot
proteins
pubmed
12690205
uniprot
proteins
pubmed
12853948
uniprot
proteins
pubmed
14532270
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17059562
uniprot
proteins
pubmed
23690594
uniprot
proteins
pubmed
25977097
uniprot
proteins
pubmed
26869225
uniprot
proteins
pubmed
28341812
uniprot
proteins
pubmed
34042202
uniprot
proteins
pubmed
9144577
uniprot
proteins
pubmed
9339362
uniprot
proteins
pubmed
9526070
uniprot
proteins
sequence_length
613
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell projection, dendrite {ECO:0000269|PubMed:25977097}. Synapse {ECO:0000269|PubMed:25977097}. Cell membrane {ECO:0000269|PubMed:17059562, ECO:0000269|PubMed:25977097, ECO:0000269|PubMed:26869225}; Multi-pass membrane protein {ECO:0000269|PubMed:17059562}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:17059562}; Multi-pass membrane protein {ECO:0000269|PubMed:17059562}.
uniprot
proteins
transmembrane_region
TRANSMEM 266..286; /note="Helical; Name=1"; /evidence="ECO:0000255"; TRANSMEM 300..320; /note="Helical; Name=2"; /evidence="ECO:0000255"; TRANSMEM 336..356; /note="Helical; Name=3"; /evidence="ECO:0000255"; TRANSMEM 380..400; /note="Helical; Name=4"; /evidence="ECO:0000255"; TRANSMEM 444..464; /note="Helical; Name=5"; /evidence="ECO:0000255"; TRANSMEM 494..514; /note="Helical; Name=6"; /evidence="ECO:0000255"; TRANSMEM 532..552; /note="Helical; Name=7"; /evidence="ECO:0000255
uniprot
proteins