GPR37_RAT
ID GPR37_RAT Reviewed; 603 AA.
AC Q9QYC6;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Prosaposin receptor GPR37;
DE AltName: Full=G-protein coupled receptor 37;
DE AltName: Full=G-protein coupled receptor CNS1;
DE Flags: Precursor;
GN Name=Gpr37;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Hypothalamus;
RX PubMed=10350639; DOI=10.1016/s0169-328x(99)00092-3;
RA Leng N., Gu G., Simerly R.B., Spindel E.R.;
RT "Molecular cloning and characterization of two putative G protein-coupled
RT receptors which are highly expressed in the central nervous system.";
RL Brain Res. Mol. Brain Res. 69:73-83(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 the neuroprotective and glioprotective factor
CC prosaposin. Ligand binding induces endocytosis, followed by an ERK
CC phosphorylation cascade (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Forms a complex with PRKN, STUB1 and HSP70. The amount of
CC STUB1 in the complex increases during ER stress. STUB1 promotes the
CC dissociation of HSP70 from PRKN, thus facilitating PRKN-mediated GPR37
CC ubiquitination. Interacts with PACRG (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the brain. High levels of
CC expression were seen in fiber tracts such as the corpus callosum,
CC anterior commissure, fornix, internal capsule, cerebral peduncles, and
CC stria terminalis. Additionally, moderate levels of expression were seen
CC in the pyramidal tracts and cerebellar peduncles, as well as in the
CC spinal tract of the trigeminal nerve and the spinal fasciculi.
CC {ECO:0000269|PubMed:10350639}.
CC -!- PTM: Ubiquitinated by PRKN in the presence of ubiquitin-conjugating
CC enzymes in the endoplasmic reticulum. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF087946; AAD54655.1; -; mRNA.
DR EMBL; BC087728; AAH87728.1; -; mRNA.
DR RefSeq; NP_476549.1; NM_057201.1.
DR AlphaFoldDB; Q9QYC6; -.
DR SMR; Q9QYC6; -.
DR STRING; 10116.ENSRNOP00000003593; -.
DR GlyGen; Q9QYC6; 3 sites.
DR PhosphoSitePlus; Q9QYC6; -.
DR PaxDb; Q9QYC6; -.
DR PRIDE; Q9QYC6; -.
DR Ensembl; ENSRNOT00000003593; ENSRNOP00000003593; ENSRNOG00000002524.
DR GeneID; 117549; -.
DR KEGG; rno:117549; -.
DR UCSC; RGD:619848; rat.
DR CTD; 2861; -.
DR RGD; 619848; Gpr37.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01040000240430; -.
DR HOGENOM; CLU_032138_1_0_1; -.
DR InParanoid; Q9QYC6; -.
DR OMA; CLGENCS; -.
DR OrthoDB; 568030at2759; -.
DR PhylomeDB; Q9QYC6; -.
DR TreeFam; TF331292; -.
DR Reactome; R-RNO-375276; Peptide ligand-binding receptors.
DR Reactome; R-RNO-418594; G alpha (i) signalling events.
DR PRO; PR:Q9QYC6; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000002524; Expressed in Ammon's horn and 19 other tissues.
DR Genevisible; Q9QYC6; RN.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0043235; C:receptor complex; ISO:RGD.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0000151; C:ubiquitin ligase complex; ISO:RGD.
DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; ISO:RGD.
DR GO; GO:0031072; F:heat shock protein binding; ISO:RGD.
DR GO; GO:0030544; F:Hsp70 protein binding; ISO:RGD.
DR GO; GO:0042923; F:neuropeptide binding; ISO:RGD.
DR GO; GO:0008188; F:neuropeptide receptor activity; ISO:RGD.
DR GO; GO:0030165; F:PDZ domain binding; ISO:RGD.
DR GO; GO:0042277; F:peptide binding; ISO:RGD.
DR GO; GO:0036505; F:prosaposin receptor activity; ISO:RGD.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; ISO:RGD.
DR GO; GO:0016358; P:dendrite development; ISO:RGD.
DR GO; GO:0042416; P:dopamine biosynthetic process; ISO:RGD.
DR GO; GO:0031987; P:locomotion involved in locomotory behavior; ISO:RGD.
DR GO; GO:1903206; P:negative regulation of hydrogen peroxide-induced cell death; ISO:RGD.
DR GO; GO:0007218; P:neuropeptide signaling pathway; ISO:RGD.
DR GO; GO:0045964; P:positive regulation of dopamine metabolic process; ISO:RGD.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:RGD.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR003909; GPR37_orph.
DR PANTHER; PTHR46216; PTHR46216; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01421; GPR37ORPHANR.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Endoplasmic reticulum;
KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Signal; Transducer; Transmembrane; Transmembrane helix;
KW Ubl conjugation.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..603
FT /note="Prosaposin receptor GPR37"
FT /id="PRO_0000012801"
FT TOPO_DOM 27..255
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 256..276
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 277..289
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 290..310
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 311..325
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 326..346
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 347..369
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 370..390
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 391..433
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 434..454
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 455..483
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 484..504
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 505..521
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 522..542
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 543..603
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 39..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 36
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 324..409
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 603 AA; 66961 MW; 87F3042B8267CEAD CRC64;
MPAPGAPLSR TSRLLLLLLF KVSVSAALSF VPEPRNGTCL GESCSPLIPR RSRDAGGPRN
SARDALRVHV PREKLEAEVR GATSWDLPPP RGGDTGVIEE AAASGPLGPP TKPPGAWRWK
GAQGKEPSGH LGRREPTDSQ LFRQTSERGE MSSKRDEIPQ GSQEHSVKTE PEPRDLFYWP
RKTGQLQGSH YRPSAVHEGR TLAPPGRALP QNGSADDWVP DQGGPRRGNS TNRRVRLKNP
FYPLTQESYG AYAVMCLSVV IFGTGIIGNL AVMCIVCHNY YMRSISNSLL ANLAFWDFLI
IFFCLPLVIF HELTKKWLLE DFSCKIVPYI EVASLGVTTF TLCALCIDRF RAATNVQMYY
EMIENCSSTT AKLAVIWVGA LLLALPEVVL RQLSKEDLGF SGQAPAERCV IKISPDLPDT
IYVLALTYDG ARLWWYFGCY FCLPTLFTIT CSLVTARKIR KAEKASTRGN KRQIHLESQM
NCTVVALTIL YGFCIIPENI CNIVTAYMAT GVSQQTMDLL NIISQFLLFF KSCVTPVLLF
CLCRPFSRAF MECCCCCCEE CIQKSSTVTS DDNDNEYTTE LELSPFSTIR REMSTFASVG
THC
