GPR37_MOUSE
ID GPR37_MOUSE Reviewed; 600 AA.
AC Q9QY42; Q8BKF8; Q8BXP9; Q8C022; Q9Z0G3;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Prosaposin receptor GPR37;
DE AltName: Full=G-protein coupled receptor 37;
DE Flags: Precursor;
GN Name=Gpr37;
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 [GENOMIC DNA / MRNA] (ISOFORM 1).
RC STRAIN=BALB/cJ; TISSUE=Brain, and Liver;
RX PubMed=9799598; DOI=10.1006/geno.1998.5433;
RA Marazziti D., Gallo A., Golini E., Matteoni R., Tocchini-Valentini G.P.;
RT "Molecular cloning and chromosomal localization of the mouse Gpr37 gene
RT encoding an orphan G-protein-coupled peptide receptor expressed in brain
RT and testis.";
RL Genomics 53:315-324(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Platzer M., Zhao W., Herman G.E., Rosenthal A.;
RT "Genomic structure of the murine G protein-coupled receptor 37 on
RT chromosome 6.";
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Eye, Olfactory bulb, and Retina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye;
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9QY42-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9QY42-2; Sequence=VSP_011762;
CC Name=3;
CC IsoId=Q9QY42-3; Sequence=VSP_011763, VSP_011764;
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}.
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DR EMBL; AJ223305; CAA11247.1; -; mRNA.
DR EMBL; AJ223834; CAA11579.1; -; Genomic_DNA.
DR EMBL; AJ223835; CAA11579.1; JOINED; Genomic_DNA.
DR EMBL; AF132039; AAF22144.1; -; Genomic_DNA.
DR EMBL; AK032525; BAC27911.1; -; mRNA.
DR EMBL; AK044508; BAC31956.1; -; mRNA.
DR EMBL; AK053287; BAC35333.1; -; mRNA.
DR EMBL; BC031918; AAH31918.1; -; mRNA.
DR CCDS; CCDS19949.1; -. [Q9QY42-1]
DR RefSeq; NP_034468.2; NM_010338.2. [Q9QY42-1]
DR AlphaFoldDB; Q9QY42; -.
DR SMR; Q9QY42; -.
DR BioGRID; 200028; 4.
DR STRING; 10090.ENSMUSP00000052185; -.
DR GlyGen; Q9QY42; 3 sites.
DR iPTMnet; Q9QY42; -.
DR PhosphoSitePlus; Q9QY42; -.
DR SwissPalm; Q9QY42; -.
DR PaxDb; Q9QY42; -.
DR PeptideAtlas; Q9QY42; -.
DR PRIDE; Q9QY42; -.
DR ProteomicsDB; 271453; -. [Q9QY42-1]
DR ProteomicsDB; 271454; -. [Q9QY42-2]
DR ProteomicsDB; 271455; -. [Q9QY42-3]
DR Antibodypedia; 17671; 312 antibodies from 35 providers.
DR DNASU; 14763; -.
DR Ensembl; ENSMUST00000054867; ENSMUSP00000052185; ENSMUSG00000039904. [Q9QY42-1]
DR Ensembl; ENSMUST00000200812; ENSMUSP00000144683; ENSMUSG00000039904. [Q9QY42-3]
DR GeneID; 14763; -.
DR KEGG; mmu:14763; -.
DR UCSC; uc009bcd.2; mouse. [Q9QY42-1]
DR CTD; 2861; -.
DR MGI; MGI:1313297; Gpr37.
DR VEuPathDB; HostDB:ENSMUSG00000039904; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01040000240430; -.
DR HOGENOM; CLU_032138_1_0_1; -.
DR InParanoid; Q9QY42; -.
DR OMA; CLGENCS; -.
DR OrthoDB; 568030at2759; -.
DR PhylomeDB; Q9QY42; -.
DR TreeFam; TF331292; -.
DR Reactome; R-MMU-375276; Peptide ligand-binding receptors.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR BioGRID-ORCS; 14763; 3 hits in 75 CRISPR screens.
DR PRO; PR:Q9QY42; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9QY42; protein.
DR Bgee; ENSMUSG00000039904; Expressed in cerebellar nuclear complex and 139 other tissues.
DR Genevisible; Q9QY42; MM.
DR GO; GO:0009986; C:cell surface; IMP:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
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:MGI.
DR GO; GO:0043235; C:receptor complex; ISO:MGI.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0000151; C:ubiquitin ligase complex; ISO:MGI.
DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; ISO:MGI.
DR GO; GO:0031072; F:heat shock protein binding; ISO:MGI.
DR GO; GO:0030544; F:Hsp70 protein binding; ISO:MGI.
DR GO; GO:0042923; F:neuropeptide binding; ISO:MGI.
DR GO; GO:0008188; F:neuropeptide receptor activity; ISO:MGI.
DR GO; GO:0030165; F:PDZ domain binding; IPI:MGI.
DR GO; GO:0042277; F:peptide binding; ISO:MGI.
DR GO; GO:0036505; F:prosaposin receptor activity; ISO:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0016358; P:dendrite development; IMP:MGI.
DR GO; GO:0042416; P:dopamine biosynthetic process; IMP:MGI.
DR GO; GO:0031987; P:locomotion involved in locomotory behavior; IMP:MGI.
DR GO; GO:1903206; P:negative regulation of hydrogen peroxide-induced cell death; IMP:ParkinsonsUK-UCL.
DR GO; GO:0007218; P:neuropeptide signaling pathway; ISO:MGI.
DR GO; GO:0045964; P:positive regulation of dopamine metabolic process; IMP:MGI.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IMP:ParkinsonsUK-UCL.
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 Alternative splicing; 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..600
FT /note="Prosaposin receptor GPR37"
FT /id="PRO_0000012800"
FT TOPO_DOM 27..252
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 253..273
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 274..286
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..307
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 308..322
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 323..343
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 344..366
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 367..387
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 388..430
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 431..451
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 452..480
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 481..501
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 502..518
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 519..539
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 540..600
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 103..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..175
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 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 227
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 321..406
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VAR_SEQ 1..251
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_011762"
FT VAR_SEQ 418..440
FT /note="IYVLALTYDGARLWWYFGCYFCL -> VQVERDCFIKIRTRNHWIRLSHL
FT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_011763"
FT VAR_SEQ 441..600
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_011764"
FT CONFLICT 205
FT /note="R -> M (in Ref. 3; BAC27911)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="R -> P (in Ref. 1; CAA11247/CAA11579)"
FT /evidence="ECO:0000305"
FT CONFLICT 228
FT /note="T -> P (in Ref. 1; CAA11247/CAA11579)"
FT /evidence="ECO:0000305"
FT CONFLICT 326
FT /note="Y -> N (in Ref. 3; BAC27911)"
FT /evidence="ECO:0000305"
FT CONFLICT 399
FT /note="G -> V (in Ref. 3; BAC31956)"
FT /evidence="ECO:0000305"
FT CONFLICT 551
FT /note="C -> Y (in Ref. 3; BAC27911)"
FT /evidence="ECO:0000305"
FT CONFLICT 598
FT /note="T -> N (in Ref. 3; BAC27911)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 600 AA; 66775 MW; 5F92E65984746B30 CRC64;
MPARGAPLSR TSRLLLLLLF KVSVSAALSF VPEPRNGTCL GESCSPLIQR RSRDARGPGN
SAKDALRVHV PREKLEAEVR GATSWDLPPP RGGDTGVIEE AAAAGPLGPP TKPPSAWRWK
SAQGKEPSGH LRRRDPTDPQ LFFPTSEGGE MSSKRDGIPQ SRQEHSVKTE PRDLFYWPRR
TGQLQDSQHR PSAVHEGRTL APPGRALPQN GSADDWVPDQ GGPRRGNTTR RVRLKNPFYP
LTQESYGAYA VMCLSVVIFG TGIIGNLAVM CIVCHNYYMR SISNSLLANL AFWDFLIIFF
CLPLVIFHEL TKKWLLEDFS CKIVPYIEVA SLGVTTFTLC ALCIDRFRAA TNVQMYYEMI
ENCSSTTAKL AVIWVGALLL ALPEVVLRQL SKEDLGFSGQ APAERCVIKI SPDLPDTIYV
LALTYDGARL WWYFGCYFCL PTLFTITCSL VTARKIRKAE KASTRGNKRQ IHLESQMNCT
VVALTILYGF CIIPENICNI VTAYMATGVS QQTMDLLNII SQFLLFFKSC VTPVLLFCLC
RPFSRAFMEC CCCCCEECIQ KSSTVTSDDN DNEYTTELEL SPFSTIRREM STFASVGTHC
