ID   GPR37_HUMAN             Reviewed;         613 AA.
AC   O15354; A4D0Y6; O00348; O14768; Q8TD39;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1999, sequence version 2.
DT   27-MAR-2024, entry version 185.
DE   RecName: Full=Prosaposin receptor GPR37;
DE   AltName: Full=Endothelin B receptor-like protein 1;
DE            Short=ETBR-LP-1;
DE   AltName: Full=G-protein coupled receptor 37;
DE   AltName: Full=Parkin-associated endothelin receptor-like receptor;
DE            Short=PAELR;
DE   Flags: Precursor;
GN   Name=GPR37;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Brain;
RX   PubMed=9339362; DOI=10.1006/geno.1997.4900;
RA   Marazziti D., Golini E., Gallo A., Lombardi M.S., Matteoni R.,
RA   Tocchini-Valentini G.P.;
RT   "Cloning of GPR37, a gene located on chromosome 7 encoding a putative G-
RT   protein-coupled peptide receptor, from a human frontal brain EST library.";
RL   Genomics 45:68-77(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   PubMed=9526070; DOI=10.1016/s0169-328x(97)00336-7;
RA   Donohue P.J., Shapira H., Mantey S.A., Hampton L.L., Jensen R.T.,
RA   Battey J.F.;
RT   "A human gene encodes a putative G protein-coupled receptor highly
RT   expressed in the central nervous system.";
RL   Brain Res. Mol. Brain Res. 54:152-160(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9144577; DOI=10.1006/bbrc.1997.6408;
RA   Zeng Z., Su K., Kyaw H., Li Y.;
RT   "A novel endothelin receptor type-B-like gene enriched in the brain.";
RL   Biochem. Biophys. Res. Commun. 233:559-567(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH PRKN.
RC   TISSUE=Brain;
RX   PubMed=11439185; DOI=10.1016/s0092-8674(01)00407-x;
RA   Imai Y., Soda M., Inoue H., Hattori N., Mizuno Y., Takahashi R.;
RT   "An unfolded putative transmembrane polypeptide, which can lead to
RT   endoplasmic reticulum stress, is a substrate of Parkin.";
RL   Cell 105:891-902(2001).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12853948; DOI=10.1038/nature01782;
RA   Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA   Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA   Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA   Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA   Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA   Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA   Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA   Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA   Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA   Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA   Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA   Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA   Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA   Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA   Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA   Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA   Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA   McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA   Wilson R.K.;
RT   "The DNA sequence of human chromosome 7.";
RL   Nature 424:157-164(2003).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12690205; DOI=10.1126/science.1083423;
RA   Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA   Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA   Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA   Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA   Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA   Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA   Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA   Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA   Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA   Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA   Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA   Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA   Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA   Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA   Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA   Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA   Adams M.D., Tsui L.-C.;
RT   "Human chromosome 7: DNA sequence and biology.";
RL   Science 300:767-772(2003).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [8]
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).
RN   [9]
RP   INTERACTION WITH PRKN; STUB1 AND HSP70.
RX   PubMed=12150907; DOI=10.1016/s1097-2765(02)00583-x;
RA   Imai Y., Soda M., Hatakeyama S., Akagi T., Hashikawa T., Nakayama K.,
RA   Takahashi R.;
RT   "CHIP is associated with Parkin, a gene responsible for familial
RT   Parkinson's disease, and enhances its ubiquitin ligase activity.";
RL   Mol. Cell 10:55-67(2002).
RN   [10]
RP   INTERACTION WITH PACRG.
RX   PubMed=14532270; DOI=10.1074/jbc.m309655200;
RA   Imai Y., Soda M., Murakami T., Shoji M., Abe K., Takahashi R.;
RT   "A product of the human gene adjacent to parkin is a component of Lewy
RT   bodies and suppresses Pael receptor-induced cell death.";
RL   J. Biol. Chem. 278:51901-51910(2003).
RN   [11]
RP   UBIQUITINATION, AND SUBCELLULAR LOCATION.
RX   PubMed=17059562; DOI=10.1111/j.1471-4159.2006.04155.x;
RA   Omura T., Kaneko M., Okuma Y., Orba Y., Nagashima K., Takahashi R.,
RA   Fujitani N., Matsumura S., Hata A., Kubota K., Murahashi K., Uehara T.,
RA   Nomura Y.;
RT   "A ubiquitin ligase HRD1 promotes the degradation of Pael receptor, a
RT   substrate of Parkin.";
RL   J. Neurochem. 99:1456-1469(2006).
RN   [12]
RP   FUNCTION.
RX   PubMed=23690594; DOI=10.1073/pnas.1219004110;
RA   Meyer R.C., Giddens M.M., Schaefer S.A., Hall R.A.;
RT   "GPR37 and GPR37L1 are receptors for the neuroprotective and glioprotective
RT   factors prosaptide and prosaposin.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:9529-9534(2013).
RN   [13]
RP   FUNCTION, INTERACTION WITH CNTNAP2 AND MPDZ, MUTAGENESIS OF ARG-558, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=25977097; DOI=10.1111/jnc.13168;
RA   Tanabe Y., Fujita-Jimbo E., Momoi M.Y., Momoi T.;
RT   "CASPR2 forms a complex with GPR37 via MUPP1 but not with GPR37(R558Q), an
RT   autism spectrum disorder-related mutation.";
RL   J. Neurochem. 134:783-793(2015).
RN   [14]
RP   CLEAVAGE, AND SUBCELLULAR LOCATION.
RX   PubMed=26869225; DOI=10.1242/jcs.176115;
RA   Mattila S.O., Tuusa J.T., Petaejae-Repo U.E.;
RT   "The Parkinson's-disease-associated receptor GPR37 undergoes
RT   metalloproteinase-mediated N-terminal cleavage and ectodomain shedding.";
RL   J. Cell Sci. 129:1366-1377(2016).
RN   [15]
RP   FUNCTION, AND INTERACTION WITH LRP6.
RX   PubMed=28341812; DOI=10.15252/embr.201643585;
RA   Berger B.S., Acebron S.P., Herbst J., Koch S., Niehrs C.;
RT   "Parkinson's disease-associated receptor GPR37 is an ER chaperone for
RT   LRP6.";
RL   EMBO Rep. 18:712-725(2017).
RN   [16]
RP   CLEAVAGE, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-54.
RX   PubMed=34042202; DOI=10.1096/fj.202002385rr;
RA   Mattila S.O., Tuhkanen H.E., Lackman J.J., Konzack A., Morato X.,
RA   Argerich J., Saftig P., Ciruela F., Petaejae-Repo U.E.;
RT   "GPR37 is processed in the N-terminal ectodomain by ADAM10 and furin.";
RL   FASEB J. 35:e21654-e21654(2021).
CC   -!- FUNCTION: G-protein-coupled receptor that plays a role in several
CC       physiological pathways such as resolution of inflammatory pain and
CC       oligodendrocyte differentiation (By similarity). Acts as a receptor for
CC       several ligands including prosaposin, osteocalcin or neuroprotectin D1.
CC       Ligand binding induces endocytosis, followed by an ERK phosphorylation
CC       cascade (PubMed:11439185, PubMed:23690594). Acts as a receptor for
CC       osteocalcin (OCN) to regulate oligodendrocyte differentiation and
CC       central nervous system myelination. Mechanistically, plays a negative
CC       role in oligodendrocyte differentiation and myelination during
CC       development via activation of the ERK1/2 signaling pathway. Therefore,
CC       regulates the stability of myelin or resistance of myelin itself to
CC       demyelination. Upon activation by neuroprotectin D1 (NPD1), promotes
CC       the activation of phagocytosis in macrophages as well as the shift in
CC       cytokine release toward an anti-inflammatory profile, and thus helps to
CC       reverse inflammatory pain. In addition, the increased macrophage
CC       phagocytosis mediates protection against sepsis upon pathogen
CC       infection. Additionally, extracellular vesicles derived from efferocyte
CC       express prosaposin, which binds to macrophage GPR37 to increase
CC       expression of the efferocytosis receptor TIM4 via an ERK-AP1-dependent
CC       signaling axis, leading to increased macrophage efferocytosis
CC       efficiency and accelerated resolution of inflammation (By similarity).
CC       May also act as a maturation factor of LRP6, protecting LRP6 from the
CC       endoplasmic reticulum (ER)-associated protein degradation (ERAD) and
CC       thereby promoting the Wnt/beta-catenin signaling pathway
CC       (PubMed:28341812). {ECO:0000250|UniProtKB:Q9QY42,
CC       ECO:0000269|PubMed:11439185, ECO:0000269|PubMed:23690594,
CC       ECO:0000269|PubMed:25977097, ECO:0000269|PubMed:28341812,
CC       ECO:0000269|PubMed:9526070}.
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. Interacts with MPDZ
CC       (PubMed:25977097). Interacts with CNTNAP2 (PubMed:25977097). Interacts
CC       with LRP6; this interaction promotes LRP6 maturation (PubMed:28341812).
CC       {ECO:0000269|PubMed:11439185, ECO:0000269|PubMed:12150907,
CC       ECO:0000269|PubMed:14532270, ECO:0000269|PubMed:25977097,
CC       ECO:0000269|PubMed:28341812}.
CC   -!- INTERACTION:
CC       O15354; P29274: ADORA2A; NbExp=3; IntAct=EBI-15639515, EBI-2902702;
CC       O15354; D3DTF8: APLN; NbExp=3; IntAct=EBI-15639515, EBI-22002556;
CC       O15354; Q02930-3: CREB5; NbExp=3; IntAct=EBI-15639515, EBI-10192698;
CC       O15354; O15540: FABP7; NbExp=3; IntAct=EBI-15639515, EBI-10697159;
CC       O15354; Q5HYJ3-3: FAM76B; NbExp=3; IntAct=EBI-15639515, EBI-11956087;
CC       O15354; Q9UBS5: GABBR1; NbExp=2; IntAct=EBI-15639515, EBI-724156;
CC       O15354; Q13639: HTR4; NbExp=5; IntAct=EBI-15639515, EBI-6656425;
CC       O15354; Q5TA79: LCE2A; NbExp=3; IntAct=EBI-15639515, EBI-10246607;
CC       O15354; Q8IXL7-2: MSRB3; NbExp=3; IntAct=EBI-15639515, EBI-10699187;
CC       O15354; Q14995: NR1D2; NbExp=3; IntAct=EBI-15639515, EBI-6144053;
CC       O15354; Q14671: PUM1; NbExp=3; IntAct=EBI-15639515, EBI-948453;
CC       O15354; Q7Z7K5: PXN; NbExp=3; IntAct=EBI-15639515, EBI-25841978;
CC       O15354; Q969E2: SCAMP4; NbExp=3; IntAct=EBI-15639515, EBI-4403649;
CC       O15354; P34741: SDC2; NbExp=3; IntAct=EBI-15639515, EBI-1172957;
CC       O15354; P08195: SLC3A2; NbExp=3; IntAct=EBI-15639515, EBI-702356;
CC       O15354; Q01959: SLC6A3; NbExp=2; IntAct=EBI-15639515, EBI-6661445;
CC       O15354; A0A024R4B0: SPATA3; NbExp=3; IntAct=EBI-15639515, EBI-14123856;
CC       O15354; Q9NX61: TMEM161A; NbExp=2; IntAct=EBI-15639515, EBI-6138599;
CC       O15354; Q71RG4-4: TMUB2; NbExp=3; IntAct=EBI-15639515, EBI-25831574;
CC       O15354; Q9H313: TTYH1; NbExp=2; IntAct=EBI-15639515, EBI-20793786;
CC       O15354; O95070: YIF1A; NbExp=2; IntAct=EBI-15639515, EBI-2799703;
CC       O15354; Q5BJH7: YIF1B; NbExp=2; IntAct=EBI-15639515, EBI-11288011;
CC       O15354; P25490: YY1; NbExp=3; IntAct=EBI-15639515, EBI-765538;
CC       O15354; Q9C0A1: ZFHX2; NbExp=3; IntAct=EBI-15639515, EBI-25850811;
CC       O15354; Q7L8T7; NbExp=3; IntAct=EBI-15639515, EBI-25831943;
CC   -!- SUBCELLULAR LOCATION: Cell projection, dendrite
CC       {ECO:0000269|PubMed:25977097}. Synapse {ECO:0000269|PubMed:25977097}.
CC       Cell membrane {ECO:0000269|PubMed:17059562,
CC       ECO:0000269|PubMed:25977097, ECO:0000269|PubMed:26869225}; Multi-pass
CC       membrane protein {ECO:0000269|PubMed:17059562}. Endoplasmic reticulum
CC       membrane {ECO:0000269|PubMed:17059562}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:17059562}.
CC   -!- TISSUE SPECIFICITY: Expressed in brain and spinal cord, and at lower
CC       levels in testis, placenta and liver, but no detectable expression
CC       observed in any other tissue. When overexpressed in cells, tends to
CC       become insoluble and unfolded. Accumulation of the unfolded protein may
CC       lead to dopaminergic neuronal death in juvenile Parkinson disease
CC       (PDJ). {ECO:0000269|PubMed:9526070}.
CC   -!- PTM: The N-terminus is cleaved by ADAM10 metalloproteinase; mediating
CC       limited proteolysis leading to the release of receptor ectodomain by
CC       shedding (PubMed:26869225, PubMed:34042202). In addition, cleaved by
CC       FURIN between Arg-54 and Asp-55 (PubMed:34042202).
CC       {ECO:0000269|PubMed:26869225, ECO:0000269|PubMed:34042202}.
CC   -!- PTM: Ubiquitinated by PRKN in the presence of UBE2E1 and UBE2L3 in the
CC       endoplasmic reticulum. The unfolded form is specifically ubiquitinated
CC       by SYVN1, which promotes its proteasomal degradation and prevents
CC       neuronal cell death. {ECO:0000269|PubMed:17059562}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; Y12476; CAA73080.1; -; Genomic_DNA.
DR   EMBL; Y12477; CAA73080.1; JOINED; Genomic_DNA.
DR   EMBL; AF017262; AAB70008.1; -; mRNA.
DR   EMBL; U87460; AAC51281.1; -; mRNA.
DR   EMBL; AF502281; AAM18625.2; -; mRNA.
DR   EMBL; AC004925; AAD08853.1; -; Genomic_DNA.
DR   EMBL; CH236947; EAL24325.1; -; Genomic_DNA.
DR   EMBL; CH471070; EAW83613.1; -; Genomic_DNA.
DR   EMBL; BC040007; AAH40007.1; -; mRNA.
DR   CCDS; CCDS5792.1; -.
DR   PIR; JC5501; JC5501.
DR   RefSeq; NP_005293.1; NM_005302.3.
DR   AlphaFoldDB; O15354; -.
DR   SMR; O15354; -.
DR   BioGRID; 109119; 93.
DR   DIP; DIP-60954N; -.
DR   IntAct; O15354; 71.
DR   MINT; O15354; -.
DR   STRING; 9606.ENSP00000306449; -.
DR   ChEMBL; CHEMBL4523862; -.
DR   GuidetoPHARMACOLOGY; 103; -.
DR   TCDB; 9.A.14.13.20; the g-protein-coupled receptor (gpcr) family.
DR   GlyCosmos; O15354; 3 sites, No reported glycans.
DR   GlyGen; O15354; 4 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; O15354; -.
DR   PhosphoSitePlus; O15354; -.
DR   BioMuta; GPR37; -.
DR   EPD; O15354; -.
DR   jPOST; O15354; -.
DR   MassIVE; O15354; -.
DR   PaxDb; 9606-ENSP00000306449; -.
DR   PeptideAtlas; O15354; -.
DR   ProteomicsDB; 48607; -.
DR   Antibodypedia; 17671; 346 antibodies from 35 providers.
DR   DNASU; 2861; -.
DR   Ensembl; ENST00000303921.3; ENSP00000306449.2; ENSG00000170775.3.
DR   GeneID; 2861; -.
DR   KEGG; hsa:2861; -.
DR   MANE-Select; ENST00000303921.3; ENSP00000306449.2; NM_005302.5; NP_005293.1.
DR   UCSC; uc003vli.5; human.
DR   AGR; HGNC:4494; -.
DR   CTD; 2861; -.
DR   DisGeNET; 2861; -.
DR   GeneCards; GPR37; -.
DR   HGNC; HGNC:4494; GPR37.
DR   HPA; ENSG00000170775; Group enriched (brain, retina).
DR   MIM; 602583; gene.
DR   neXtProt; NX_O15354; -.
DR   OpenTargets; ENSG00000170775; -.
DR   PharmGKB; PA28882; -.
DR   VEuPathDB; HostDB:ENSG00000170775; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT01100000263518; -.
DR   HOGENOM; CLU_032138_1_0_1; -.
DR   InParanoid; O15354; -.
DR   OMA; HSRRWRT; -.
DR   OrthoDB; 4268515at2759; -.
DR   PhylomeDB; O15354; -.
DR   TreeFam; TF331292; -.
DR   PathwayCommons; O15354; -.
DR   Reactome; R-HSA-375276; Peptide ligand-binding receptors.
DR   Reactome; R-HSA-418594; G alpha (i) signalling events.
DR   SignaLink; O15354; -.
DR   SIGNOR; O15354; -.
DR   BioGRID-ORCS; 2861; 13 hits in 1149 CRISPR screens.
DR   ChiTaRS; GPR37; human.
DR   GeneWiki; GPR37; -.
DR   GenomeRNAi; 2861; -.
DR   Pharos; O15354; Tbio.
DR   PRO; PR:O15354; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   RNAct; O15354; Protein.
DR   Bgee; ENSG00000170775; Expressed in secondary oocyte and 132 other cell types or tissues.
DR   GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0043235; C:receptor complex; IDA:MGI.
DR   GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR   GO; GO:0000151; C:ubiquitin ligase complex; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0008528; F:G protein-coupled peptide receptor activity; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; TAS:ProtInc.
DR   GO; GO:0031072; F:heat shock protein binding; IPI:ParkinsonsUK-UCL.
DR   GO; GO:0030544; F:Hsp70 protein binding; IPI:ParkinsonsUK-UCL.
DR   GO; GO:0042923; F:neuropeptide binding; IPI:UniProtKB.
DR   GO; GO:0008188; F:neuropeptide receptor activity; IDA:UniProtKB.
DR   GO; GO:0030165; F:PDZ domain binding; IEA:Ensembl.
DR   GO; GO:0042277; F:peptide binding; IPI:ParkinsonsUK-UCL.
DR   GO; GO:0036505; F:prosaposin receptor activity; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL.
DR   GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0034614; P:cellular response to reactive oxygen species; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0016358; P:dendrite development; IEA:Ensembl.
DR   GO; GO:0042416; P:dopamine biosynthetic process; IEA:Ensembl.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR   GO; GO:0031987; P:locomotion involved in locomotory behavior; IEA:Ensembl.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IDA:UniProtKB.
DR   GO; GO:0045964; P:positive regulation of dopamine metabolic process; IEA:Ensembl.
DR   GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:ParkinsonsUK-UCL.
DR   CDD; cd15127; 7tmA_GPR37; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   InterPro; IPR003909; GPR37_orph.
DR   PANTHER; PTHR46216:SF3; PROSAPOSIN RECEPTOR GPR37; 1.
DR   PANTHER; PTHR46216; PROSAPOSIN RECEPTOR GPR37 FAMILY MEMBER; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR01421; GPR37ORPHANR.
DR   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR   Genevisible; O15354; HS.
PE   1: Evidence at protein level;
KW   Cell membrane; Cell projection; Disulfide bond; Endoplasmic reticulum;
KW   G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW   Reference proteome; Signal; Synapse; Transducer; Transmembrane;
KW   Transmembrane helix; Ubl conjugation.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..613
FT                   /note="Prosaposin receptor GPR37"
FT                   /id="PRO_0000012799"
FT   TOPO_DOM        27..265
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        266..286
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        287..299
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        300..320
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        321..335
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        336..356
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        357..379
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        380..400
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        401..443
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        444..464
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        465..493
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        494..514
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        515..531
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        532..552
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        553..613
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          80..138
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          152..172
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            54..55
FT                   /note="Cleavage; by FURIN"
FT                   /evidence="ECO:0000269|PubMed:34042202"
FT   SITE            167..168
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000269|PubMed:26869225,
FT                   ECO:0000269|PubMed:34042202"
FT   CARBOHYD        36
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        222
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        239
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        334..419
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   MUTAGEN         54
FT                   /note="R->A: Strong increase of full-length receptor
FT                   abundance at the cell surface."
FT                   /evidence="ECO:0000269|PubMed:34042202"
FT   MUTAGEN         558
FT                   /note="R->Q: Strong loss of interaction with MUPP1
FT                   resulting in dendritic alteration."
FT                   /evidence="ECO:0000269|PubMed:25977097"
FT   CONFLICT        93
FT                   /note="G -> D (in Ref. 3; AAC51281)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        106
FT                   /note="A -> T (in Ref. 3; AAC51281)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        118
FT                   /note="G -> V (in Ref. 3; AAC51281)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        160
FT                   /note="G -> V (in Ref. 3; AAC51281)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        182
FT                   /note="W -> C (in Ref. 3; AAC51281)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        231
FT                   /note="E -> D (in Ref. 3; AAC51281)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        284
FT                   /note="C -> S (in Ref. 2; AAB70008)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        304
FT                   /note="A -> V (in Ref. 3; AAC51281)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        329
FT                   /note="L -> V (in Ref. 3; AAC51281)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        503..504
FT                   /note="FC -> LG (in Ref. 3; AAC51281)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        598
FT                   /note="T -> A (in Ref. 3; AAC51281)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   613 AA;  67114 MW;  5A1AB269ED63E765 CRC64;
     MRAPGALLAR MSRLLLLLLL KVSASSALGV APASRNETCL GESCAPTVIQ RRGRDAWGPG
     NSARDVLRAR APREEQGAAF LAGPSWDLPA APGRDPAAGR GAEASAAGPP GPPTRPPGPW
     RWKGARGQEP SETLGRGNPT ALQLFLQISE EEEKGPRGAG ISGRSQEQSV KTVPGASDLF
     YWPRRAGKLQ GSHHKPLSKT ANGLAGHEGW TIALPGRALA QNGSLGEGIH EPGGPRRGNS
     TNRRVRLKNP FYPLTQESYG AYAVMCLSVV IFGTGIIGNL AVMCIVCHNY YMRSISNSLL
     ANLAFWDFLI IFFCLPLVIF HELTKKWLLE DFSCKIVPYI EVASLGVTTF TLCALCIDRF
     RAATNVQMYY EMIENCSSTT AKLAVIWVGA LLLALPEVVL RQLSKEDLGF SGRAPAERCI
     IKISPDLPDT IYVLALTYDS ARLWWYFGCY FCLPTLFTIT CSLVTARKIR KAEKACTRGN
     KRQIQLESQM NCTVVALTIL YGFCIIPENI CNIVTAYMAT GVSQQTMDLL NIISQFLLFF
     KSCVTPVLLF CLCKPFSRAF MECCCCCCEE CIQKSSTVTS DDNDNEYTTE LELSPFSTIR
     REMSTFASVG THC
//