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Prosaposin receptor GPR37 (Endothelin B receptor-like protein 1) (ETBR-LP-1) (G-protein coupled receptor 37) (Parkin-associated endothelin receptor-like receptor) (PAELR)

 GPR37_HUMAN             Reviewed;         613 AA.
O15354; A4D0Y6; O00348; O14768; Q8TD39;
11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
01-JAN-1999, sequence version 2.
28-FEB-2018, entry version 150.
RecName: Full=Prosaposin receptor GPR37;
AltName: Full=Endothelin B receptor-like protein 1;
Short=ETBR-LP-1;
AltName: Full=G-protein coupled receptor 37;
AltName: Full=Parkin-associated endothelin receptor-like receptor;
Short=PAELR;
Flags: Precursor;
Name=GPR37;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Brain;
PubMed=9339362; DOI=10.1006/geno.1997.4900;
Marazziti D., Golini E., Gallo A., Lombardi M.S., Matteoni R.,
Tocchini-Valentini G.P.;
"Cloning of GPR37, a gene located on chromosome 7 encoding a putative
G-protein-coupled peptide receptor, from a human frontal brain EST
library.";
Genomics 45:68-77(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
TISSUE=Brain;
PubMed=9526070; DOI=10.1016/S0169-328X(97)00336-7;
Donohue P.J., Shapira H., Mantey S.A., Hampton L.L., Jensen R.T.,
Battey J.F.;
"A human gene encodes a putative G protein-coupled receptor highly
expressed in the central nervous system.";
Brain Res. Mol. Brain Res. 54:152-160(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9144577; DOI=10.1006/bbrc.1997.6408;
Zeng Z., Su K., Kyaw H., Li Y.;
"A novel endothelin receptor type-B-like gene enriched in the brain.";
Biochem. Biophys. Res. Commun. 233:559-567(1997).
[4]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH PRKN.
TISSUE=Brain;
PubMed=11439185; DOI=10.1016/S0092-8674(01)00407-X;
Imai Y., Soda M., Inoue H., Hattori N., Mizuno Y., Takahashi R.;
"An unfolded putative transmembrane polypeptide, which can lead to
endoplasmic reticulum stress, is a substrate of Parkin.";
Cell 105:891-902(2001).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12690205; DOI=10.1126/science.1083423;
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
Mural R.J., Adams M.D., Tsui L.-C.;
"Human chromosome 7: DNA sequence and biology.";
Science 300:767-772(2003).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
INTERACTION WITH PRKN; STUB1 AND HSP70.
PubMed=12150907; DOI=10.1016/S1097-2765(02)00583-X;
Imai Y., Soda M., Hatakeyama S., Akagi T., Hashikawa T., Nakayama K.,
Takahashi R.;
"CHIP is associated with Parkin, a gene responsible for familial
Parkinson's disease, and enhances its ubiquitin ligase activity.";
Mol. Cell 10:55-67(2002).
[10]
INTERACTION WITH PACRG.
PubMed=14532270; DOI=10.1074/jbc.M309655200;
Imai Y., Soda M., Murakami T., Shoji M., Abe K., Takahashi R.;
"A product of the human gene adjacent to parkin is a component of Lewy
bodies and suppresses Pael receptor-induced cell death.";
J. Biol. Chem. 278:51901-51910(2003).
[11]
UBIQUITINATION, AND SUBCELLULAR LOCATION.
PubMed=17059562; DOI=10.1111/j.1471-4159.2006.04155.x;
Omura T., Kaneko M., Okuma Y., Orba Y., Nagashima K., Takahashi R.,
Fujitani N., Matsumura S., Hata A., Kubota K., Murahashi K.,
Uehara T., Nomura Y.;
"A ubiquitin ligase HRD1 promotes the degradation of Pael receptor, a
substrate of Parkin.";
J. Neurochem. 99:1456-1469(2006).
[12]
FUNCTION.
PubMed=23690594; DOI=10.1073/pnas.1219004110;
Meyer R.C., Giddens M.M., Schaefer S.A., Hall R.A.;
"GPR37 and GPR37L1 are receptors for the neuroprotective and
glioprotective factors prosaptide and prosaposin.";
Proc. Natl. Acad. Sci. U.S.A. 110:9529-9534(2013).
-!- FUNCTION: Receptor for the neuroprotective and glioprotective
factor prosaposin. Ligand binding induces endocytosis, followed by
an ERK phosphorylation cascade. {ECO:0000269|PubMed:11439185,
ECO:0000269|PubMed:23690594, ECO:0000269|PubMed:9526070}.
-!- SUBUNIT: Forms a complex with PRKN, STUB1 and HSP70. The amount of
STUB1 in the complex increases during ER stress. STUB1 promotes
the dissociation of HSP70 from PRKN, thus facilitating PRKN-
mediated GPR37 ubiquitination. Interacts with PACRG.
{ECO:0000269|PubMed:11439185, ECO:0000269|PubMed:12150907,
ECO:0000269|PubMed:14532270}.
-!- INTERACTION:
Q01959:SLC6A3; NbExp=2; IntAct=EBI-15639515, EBI-6661445;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17059562};
Multi-pass membrane protein {ECO:0000269|PubMed:17059562}.
Endoplasmic reticulum membrane {ECO:0000269|PubMed:17059562};
Multi-pass membrane protein {ECO:0000269|PubMed:17059562}.
-!- TISSUE SPECIFICITY: Expressed in brain and spinal cord, and at
lower levels in testis, placenta and liver, but no detectable
expression observed in any other tissue. When overexpressed in
cells, tends to become insoluble and unfolded. Accumulation of the
unfolded protein may lead to dopaminergic neuronal death in
juvenile Parkinson disease (PDJ). {ECO:0000269|PubMed:9526070}.
-!- 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}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
{ECO:0000255|PROSITE-ProRule:PRU00521}.
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EMBL; Y12476; CAA73080.1; -; Genomic_DNA.
EMBL; Y12477; CAA73080.1; JOINED; Genomic_DNA.
EMBL; AF017262; AAB70008.1; -; mRNA.
EMBL; U87460; AAC51281.1; -; mRNA.
EMBL; AF502281; AAM18625.2; -; mRNA.
EMBL; AC004925; AAD08853.1; -; Genomic_DNA.
EMBL; CH236947; EAL24325.1; -; Genomic_DNA.
EMBL; CH471070; EAW83613.1; -; Genomic_DNA.
EMBL; BC040007; AAH40007.1; -; mRNA.
CCDS; CCDS5792.1; -.
PIR; JC5501; JC5501.
RefSeq; NP_005293.1; NM_005302.3.
UniGene; Hs.406094; -.
UniGene; Hs.731392; -.
ProteinModelPortal; O15354; -.
BioGrid; 109119; 27.
DIP; DIP-60954N; -.
IntAct; O15354; 1.
STRING; 9606.ENSP00000306449; -.
GuidetoPHARMACOLOGY; 103; -.
TCDB; 9.A.14.13.20; the g-protein-coupled receptor (gpcr) family.
iPTMnet; O15354; -.
PhosphoSitePlus; O15354; -.
EPD; O15354; -.
PaxDb; O15354; -.
PeptideAtlas; O15354; -.
PRIDE; O15354; -.
DNASU; 2861; -.
Ensembl; ENST00000303921; ENSP00000306449; ENSG00000170775.
GeneID; 2861; -.
KEGG; hsa:2861; -.
UCSC; uc003vli.5; human.
CTD; 2861; -.
DisGeNET; 2861; -.
EuPathDB; HostDB:ENSG00000170775.2; -.
GeneCards; GPR37; -.
HGNC; HGNC:4494; GPR37.
HPA; HPA042903; -.
HPA; HPA068009; -.
MIM; 602583; gene.
neXtProt; NX_O15354; -.
OpenTargets; ENSG00000170775; -.
PharmGKB; PA28882; -.
eggNOG; KOG3656; Eukaryota.
eggNOG; ENOG410XRW9; LUCA.
GeneTree; ENSGT00760000119177; -.
HOGENOM; HOG000252922; -.
HOVERGEN; HBG051808; -.
InParanoid; O15354; -.
KO; K04243; -.
OMA; AERCVIK; -.
OrthoDB; EOG091G04SU; -.
PhylomeDB; O15354; -.
TreeFam; TF331292; -.
Reactome; R-HSA-375276; Peptide ligand-binding receptors.
Reactome; R-HSA-418594; G alpha (i) signalling events.
SIGNOR; O15354; -.
GeneWiki; GPR37; -.
GenomeRNAi; 2861; -.
PRO; PR:O15354; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000170775; -.
CleanEx; HS_GPR37; -.
Genevisible; O15354; HS.
GO; GO:0005783; C:endoplasmic reticulum; IDA:ParkinsonsUK-UCL.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0005886; C:plasma membrane; IDA:ParkinsonsUK-UCL.
GO; GO:0043235; C:receptor complex; IDA:MGI.
GO; GO:0000151; C:ubiquitin ligase complex; IDA:ParkinsonsUK-UCL.
GO; GO:0008528; F:G-protein coupled peptide receptor activity; IDA:ParkinsonsUK-UCL.
GO; GO:0004930; F:G-protein coupled receptor activity; TAS:ProtInc.
GO; GO:0031072; F:heat shock protein binding; IPI:ParkinsonsUK-UCL.
GO; GO:0030544; F:Hsp70 protein binding; IPI:ParkinsonsUK-UCL.
GO; GO:0042277; F:peptide binding; IPI:ParkinsonsUK-UCL.
GO; GO:0036505; F:prosaposin receptor activity; IDA:ParkinsonsUK-UCL.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL.
GO; GO:0007193; P:adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway; IDA:ParkinsonsUK-UCL.
GO; GO:0042416; P:dopamine biosynthetic process; IEA:Ensembl.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; TAS:Reactome.
GO; GO:0031987; P:locomotion involved in locomotory behavior; IEA:Ensembl.
GO; GO:1903206; P:negative regulation of hydrogen peroxide-induced cell death; ISS:ParkinsonsUK-UCL.
GO; GO:0045964; P:positive regulation of dopamine metabolic process; IEA:Ensembl.
GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:ParkinsonsUK-UCL.
InterPro; IPR000276; GPCR_Rhodpsn.
InterPro; IPR017452; GPCR_Rhodpsn_7TM.
InterPro; IPR003909; GPR37_orph.
Pfam; PF00001; 7tm_1; 1.
PRINTS; PR00237; GPCRRHODOPSN.
PRINTS; PR01421; GPR37ORPHANR.
PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Disulfide bond;
Endoplasmic reticulum; G-protein coupled receptor; Glycoprotein;
Membrane; Receptor; Reference proteome; Signal; Transducer;
Transmembrane; Transmembrane helix; Ubl conjugation.
SIGNAL 1 26 {ECO:0000255}.
CHAIN 27 613 Prosaposin receptor GPR37.
/FTId=PRO_0000012799.
TOPO_DOM 27 265 Extracellular. {ECO:0000255}.
TRANSMEM 266 286 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 287 299 Cytoplasmic. {ECO:0000255}.
TRANSMEM 300 320 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 321 335 Extracellular. {ECO:0000255}.
TRANSMEM 336 356 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 357 379 Cytoplasmic. {ECO:0000255}.
TRANSMEM 380 400 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 401 443 Extracellular. {ECO:0000255}.
TRANSMEM 444 464 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 465 493 Cytoplasmic. {ECO:0000255}.
TRANSMEM 494 514 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 515 531 Extracellular. {ECO:0000255}.
TRANSMEM 532 552 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 553 613 Cytoplasmic. {ECO:0000255}.
COMPBIAS 563 568 Poly-Cys.
CARBOHYD 36 36 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 222 222 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 239 239 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 334 419 {ECO:0000255|PROSITE-ProRule:PRU00521}.
CONFLICT 93 93 G -> D (in Ref. 3; AAC51281).
{ECO:0000305}.
CONFLICT 106 106 A -> T (in Ref. 3; AAC51281).
{ECO:0000305}.
CONFLICT 118 118 G -> V (in Ref. 3; AAC51281).
{ECO:0000305}.
CONFLICT 160 160 G -> V (in Ref. 3; AAC51281).
{ECO:0000305}.
CONFLICT 182 182 W -> C (in Ref. 3; AAC51281).
{ECO:0000305}.
CONFLICT 231 231 E -> D (in Ref. 3; AAC51281).
{ECO:0000305}.
CONFLICT 284 284 C -> S (in Ref. 2; AAB70008).
{ECO:0000305}.
CONFLICT 304 304 A -> V (in Ref. 3; AAC51281).
{ECO:0000305}.
CONFLICT 329 329 L -> V (in Ref. 3; AAC51281).
{ECO:0000305}.
CONFLICT 503 504 FC -> LG (in Ref. 3; AAC51281).
{ECO:0000305}.
CONFLICT 598 598 T -> A (in Ref. 3; AAC51281).
{ECO:0000305}.
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


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