G37L1_HUMAN
ID G37L1_HUMAN Reviewed; 481 AA.
AC O60883; B2R7M9; Q5SXP7; Q86VP7;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=G-protein coupled receptor 37-like 1;
DE AltName: Full=Endothelin B receptor-like protein 2;
DE Short=ETBR-LP-2;
DE Flags: Precursor;
GN Name=GPR37L1; Synonyms=ETBRLP2;
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 [MRNA], TISSUE SPECIFICITY, AND VARIANT ASP-90.
RC TISSUE=Brain;
RX PubMed=9539149; DOI=10.1016/s0014-5793(98)00170-7;
RA Valdenaire O., Giller T., Breu V., Ardati A., Schweizer A., Richards J.G.;
RT "A new family of orphan G protein-coupled receptors predominantly expressed
RT in the brain.";
RL FEBS Lett. 424:193-196(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASP-90.
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-91.
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 [6]
RP GLYCOSYLATION AT THR-79; THR-85; SER-86; THR-95 AND THR-107, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=23234360; DOI=10.1021/pr300963h;
RA Halim A., Ruetschi U., Larson G., Nilsson J.;
RT "LC-MS/MS characterization of O-glycosylation sites and glycan structures
RT of human cerebrospinal fluid glycoproteins.";
RL J. Proteome Res. 12:573-584(2013).
RN [7]
RP FUNCTION, AND TISSUE SPECIFICITY.
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 [8]
RP FUNCTION, CLEAVAGE, AND DOMAIN.
RX PubMed=27072655; DOI=10.1126/scisignal.aad1089;
RA Coleman J.L., Ngo T., Schmidt J., Mrad N., Liew C.K., Jones N.M.,
RA Graham R.M., Smith N.J.;
RT "Metalloprotease cleavage of the N terminus of the orphan G protein-coupled
RT receptor GPR37L1 reduces its constitutive activity.";
RL Sci. Signal. 9:RA36-RA36(2016).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, UBIQUITINATION, VARIANT ASN-349, AND
RP CHARACTERIZATION OF VARIANT ASN-349.
RX PubMed=28688853; DOI=10.1016/j.nbd.2017.07.006;
RA Giddens M.M., Wong J.C., Schroeder J.P., Farrow E.G., Smith B.M., Owino S.,
RA Soden S.E., Meyer R.C., Saunders C., LePichon J.B., Weinshenker D.,
RA Escayg A., Hall R.A.;
RT "GPR37L1 modulates seizure susceptibility: Evidence from mouse studies and
RT analyses of a human GPR37L1 variant.";
RL Neurobiol. Dis. 106:181-190(2017).
CC -!- FUNCTION: G-protein coupled receptor (PubMed:27072655). Has been shown
CC to bind the neuroprotective and glioprotective factor prosaposin
CC (PSAP), leading to endocytosis followed by an ERK phosphorylation
CC cascade (PubMed:23690594). However, other studies have shown that
CC prosaposin does not increase activity (PubMed:27072655,
CC PubMed:28688853). It has been suggested that GPR37L1 is a
CC constitutively active receptor which signals through the guanine
CC nucleotide-binding protein G(s) subunit alpha (PubMed:27072655).
CC Participates in the regulation of postnatal cerebellar development by
CC modulating the Shh pathway (By similarity). Regulates baseline blood
CC pressure in females and protects against cardiovascular stress in males
CC (By similarity). Mediates inhibition of astrocyte glutamate
CC transporters and reduction in neuronal N-methyl-D-aspartate receptor
CC activity (By similarity). {ECO:0000250|UniProtKB:Q99JG2,
CC ECO:0000269|PubMed:23690594, ECO:0000269|PubMed:27072655,
CC ECO:0000269|PubMed:28688853}.
CC -!- SUBUNIT: Interacts with the PTCH1 receptor.
CC {ECO:0000250|UniProtKB:Q99JG2}.
CC -!- INTERACTION:
CC O60883; O60242: ADGRB3; NbExp=3; IntAct=EBI-2927498, EBI-2682765;
CC O60883; P29972: AQP1; NbExp=3; IntAct=EBI-2927498, EBI-745213;
CC O60883; Q96PS8: AQP10; NbExp=3; IntAct=EBI-2927498, EBI-12820279;
CC O60883; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-2927498, EBI-11343438;
CC O60883; P15529-3: CD46; NbExp=3; IntAct=EBI-2927498, EBI-13046140;
CC O60883; Q8N5K1: CISD2; NbExp=3; IntAct=EBI-2927498, EBI-1045797;
CC O60883; O95471: CLDN7; NbExp=3; IntAct=EBI-2927498, EBI-740744;
CC O60883; Q8NHS1: CLDND2; NbExp=3; IntAct=EBI-2927498, EBI-11959453;
CC O60883; Q6UVW9: CLEC2A; NbExp=3; IntAct=EBI-2927498, EBI-15839595;
CC O60883; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-2927498, EBI-6942903;
CC O60883; Q8NBI2: CYB561A3; NbExp=3; IntAct=EBI-2927498, EBI-10269179;
CC O60883; Q9GZR5: ELOVL4; NbExp=3; IntAct=EBI-2927498, EBI-18535450;
CC O60883; Q9UKR5: ERG28; NbExp=3; IntAct=EBI-2927498, EBI-711490;
CC O60883; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-2927498, EBI-18304435;
CC O60883; O15552: FFAR2; NbExp=3; IntAct=EBI-2927498, EBI-2833872;
CC O60883; Q14802-3: FXYD3; NbExp=3; IntAct=EBI-2927498, EBI-12175685;
CC O60883; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-2927498, EBI-13345167;
CC O60883; O15529: GPR42; NbExp=3; IntAct=EBI-2927498, EBI-18076404;
CC O60883; Q8TED1: GPX8; NbExp=3; IntAct=EBI-2927498, EBI-11721746;
CC O60883; P24593: IGFBP5; NbExp=3; IntAct=EBI-2927498, EBI-720480;
CC O60883; Q9Y5U4: INSIG2; NbExp=3; IntAct=EBI-2927498, EBI-8503746;
CC O60883; Q8N5M9: JAGN1; NbExp=3; IntAct=EBI-2927498, EBI-10266796;
CC O60883; Q8TAF8: LHFPL5; NbExp=3; IntAct=EBI-2927498, EBI-2820517;
CC O60883; Q9BQ51: PDCD1LG2; NbExp=3; IntAct=EBI-2927498, EBI-16427978;
CC O60883; P26678: PLN; NbExp=3; IntAct=EBI-2927498, EBI-692836;
CC O60883; P42785: PRCP; NbExp=2; IntAct=EBI-2927498, EBI-2803892;
CC O60883; Q9H9V4: RNF122; NbExp=3; IntAct=EBI-2927498, EBI-2129998;
CC O60883; Q9NS64: RPRM; NbExp=3; IntAct=EBI-2927498, EBI-1052363;
CC O60883; Q14108: SCARB2; NbExp=3; IntAct=EBI-2927498, EBI-1564650;
CC O60883; Q14162: SCARF1; NbExp=3; IntAct=EBI-2927498, EBI-12056025;
CC O60883; Q96IW7: SEC22A; NbExp=3; IntAct=EBI-2927498, EBI-8652744;
CC O60883; Q9Y6X1: SERP1; NbExp=3; IntAct=EBI-2927498, EBI-10329948;
CC O60883; Q8IWU4: SLC30A8; NbExp=3; IntAct=EBI-2927498, EBI-10262251;
CC O60883; P27105: STOM; NbExp=3; IntAct=EBI-2927498, EBI-1211440;
CC O60883; Q8TBG9: SYNPR; NbExp=3; IntAct=EBI-2927498, EBI-10273251;
CC O60883; Q8WY91: THAP4; NbExp=3; IntAct=EBI-2927498, EBI-726691;
CC O60883; C9JKN6: THSD7B; NbExp=3; IntAct=EBI-2927498, EBI-17192156;
CC O60883; P48230: TM4SF4; NbExp=3; IntAct=EBI-2927498, EBI-8650934;
CC O60883; Q9BVK8: TMEM147; NbExp=3; IntAct=EBI-2927498, EBI-348587;
CC O60883; Q9BU79: TMEM243; NbExp=3; IntAct=EBI-2927498, EBI-12887458;
CC O60883; Q9NWD8: TMEM248; NbExp=3; IntAct=EBI-2927498, EBI-10314986;
CC O60883; Q4KMG9: TMEM52B; NbExp=3; IntAct=EBI-2927498, EBI-18178701;
CC O60883; Q969K7: TMEM54; NbExp=3; IntAct=EBI-2927498, EBI-3922833;
CC O60883; Q96HE8: TMEM80; NbExp=3; IntAct=EBI-2927498, EBI-11742770;
CC O60883; Q8N2M4: TMEM86A; NbExp=3; IntAct=EBI-2927498, EBI-12015604;
CC O60883; Q8N661: TMEM86B; NbExp=3; IntAct=EBI-2927498, EBI-2548832;
CC O60883; Q5BJF2: TMEM97; NbExp=3; IntAct=EBI-2927498, EBI-12111910;
CC O60883; O14798: TNFRSF10C; NbExp=3; IntAct=EBI-2927498, EBI-717441;
CC O60883; O95859: TSPAN12; NbExp=3; IntAct=EBI-2927498, EBI-2466403;
CC O60883; Q9H1C4: UNC93B1; NbExp=3; IntAct=EBI-2927498, EBI-4401271;
CC O60883; O75841: UPK1B; NbExp=3; IntAct=EBI-2927498, EBI-12237619;
CC O60883; A0A087WZY1; NbExp=3; IntAct=EBI-2927498, EBI-13387614;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:28688853};
CC Multi-pass membrane protein {ECO:0000255}. Cell projection, cilium
CC membrane {ECO:0000250|UniProtKB:Q99JG2}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Associates with the basal membrane of Bergmann glia
CC cell primary cilia. {ECO:0000250|UniProtKB:Q99JG2}.
CC -!- TISSUE SPECIFICITY: Expressed in primary cortical astrocytes (at
CC protein level) (PubMed:23690594). Expressed in the central nervous
CC system (PubMed:9539149). {ECO:0000269|PubMed:23690594,
CC ECO:0000269|PubMed:9539149}.
CC -!- DOMAIN: The N-terminal region is required for constitutive signal
CC transduction. {ECO:0000269|PubMed:27072655}.
CC -!- PTM: O-glycosylated. {ECO:0000269|PubMed:23234360}.
CC -!- PTM: Undergoes metalloprotease-mediated cleavage which reduces its
CC constitutive activity. {ECO:0000269|PubMed:27072655}.
CC -!- PTM: Ubiquitinated. {ECO:0000269|PubMed:28688853}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- CAUTION: Has been reported to act as a receptor for prosaposin (PSAP)
CC (PubMed:23690594). However, it has also been shown that prosaposin does
CC not increase activity (PubMed:27072655, PubMed:28688853). It has been
CC suggested that GPR37L1 is a constitutively active receptor
CC (PubMed:27072655). {ECO:0000269|PubMed:23690594,
CC ECO:0000269|PubMed:27072655, ECO:0000269|PubMed:28688853}.
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DR EMBL; Y16280; CAA76153.1; -; mRNA.
DR EMBL; AK313044; BAG35876.1; -; mRNA.
DR EMBL; AK222639; BAD96359.1; -; mRNA.
DR EMBL; AL592300; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC050334; AAH50334.1; -; mRNA.
DR CCDS; CCDS1420.1; -.
DR RefSeq; NP_004758.3; NM_004767.3.
DR AlphaFoldDB; O60883; -.
DR SMR; O60883; -.
DR BioGRID; 114700; 54.
DR IntAct; O60883; 54.
DR MINT; O60883; -.
DR STRING; 9606.ENSP00000356251; -.
DR BindingDB; O60883; -.
DR ChEMBL; CHEMBL5892; -.
DR GuidetoPHARMACOLOGY; 104; -.
DR GlyConnect; 661; 1 O-Linked glycan (6 sites).
DR GlyGen; O60883; 7 sites, 2 O-linked glycans (6 sites).
DR iPTMnet; O60883; -.
DR PhosphoSitePlus; O60883; -.
DR BioMuta; GPR37L1; -.
DR MassIVE; O60883; -.
DR PaxDb; O60883; -.
DR PeptideAtlas; O60883; -.
DR PRIDE; O60883; -.
DR ProteomicsDB; 49649; -.
DR Antibodypedia; 20649; 300 antibodies from 32 providers.
DR DNASU; 9283; -.
DR Ensembl; ENST00000367282.6; ENSP00000356251.4; ENSG00000170075.10.
DR GeneID; 9283; -.
DR KEGG; hsa:9283; -.
DR MANE-Select; ENST00000367282.6; ENSP00000356251.4; NM_004767.5; NP_004758.3.
DR UCSC; uc001gxj.4; human.
DR CTD; 9283; -.
DR DisGeNET; 9283; -.
DR GeneCards; GPR37L1; -.
DR HGNC; HGNC:14923; GPR37L1.
DR HPA; ENSG00000170075; Tissue enriched (brain).
DR MIM; 617630; gene.
DR neXtProt; NX_O60883; -.
DR OpenTargets; ENSG00000170075; -.
DR PharmGKB; PA28883; -.
DR VEuPathDB; HostDB:ENSG00000170075; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01040000240430; -.
DR HOGENOM; CLU_029119_0_0_1; -.
DR InParanoid; O60883; -.
DR OMA; QCERQLN; -.
DR OrthoDB; 568030at2759; -.
DR PhylomeDB; O60883; -.
DR TreeFam; TF331292; -.
DR PathwayCommons; O60883; -.
DR Reactome; R-HSA-375276; Peptide ligand-binding receptors.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR SignaLink; O60883; -.
DR BioGRID-ORCS; 9283; 14 hits in 1061 CRISPR screens.
DR ChiTaRS; GPR37L1; human.
DR GeneWiki; GPR37L1; -.
DR GenomeRNAi; 9283; -.
DR Pharos; O60883; Tbio.
DR PRO; PR:O60883; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O60883; protein.
DR Bgee; ENSG00000170075; Expressed in buccal mucosa cell and 116 other tissues.
DR Genevisible; O60883; HS.
DR GO; GO:0060170; C:ciliary membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0043235; C:receptor complex; IDA:MGI.
DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IDA:UniProtKB.
DR GO; GO:0042277; F:peptide binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0036505; F:prosaposin receptor activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IDA:ParkinsonsUK-UCL.
DR GO; GO:0060020; P:Bergmann glial cell differentiation; IEA:Ensembl.
DR GO; GO:0048712; P:negative regulation of astrocyte differentiation; IEA:Ensembl.
DR GO; GO:1903206; P:negative regulation of hydrogen peroxide-induced cell death; ISS:ParkinsonsUK-UCL.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; IEA:Ensembl.
DR GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IEA:Ensembl.
DR GO; GO:0003085; P:negative regulation of systemic arterial blood pressure; ISS:UniProtKB.
DR GO; GO:0021940; P:positive regulation of cerebellar granule cell precursor proliferation; IEA:Ensembl.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:ParkinsonsUK-UCL.
DR GO; GO:0007224; P:smoothened signaling pathway; IEA:Ensembl.
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 1: Evidence at protein level;
KW Cell membrane; Cell projection; Disulfide bond; G-protein coupled receptor;
KW Glycoprotein; Membrane; Phosphoprotein; Receptor; Reference proteome;
KW Signal; Transducer; Transmembrane; Transmembrane helix; Ubl conjugation.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..481
FT /note="G-protein coupled receptor 37-like 1"
FT /id="PRO_0000012796"
FT TOPO_DOM 26..134
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 135..155
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 156..167
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 189..205
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..226
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 227..251
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..272
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 273..310
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 311..331
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 332..361
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 362..382
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 383..398
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 399..419
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 420..481
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 26..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 70..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 471
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99JG2"
FT MOD_RES 479
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q99JG2"
FT CARBOHYD 79
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:23234360"
FT CARBOHYD 85
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:23234360"
FT CARBOHYD 86
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:23234360"
FT CARBOHYD 95
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:23234360"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 107
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:23234360"
FT DISULFID 203..286
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VARIANT 81
FT /note="P -> A (in dbSNP:rs3795594)"
FT /id="VAR_047455"
FT VARIANT 90
FT /note="G -> D (in dbSNP:rs3795595)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:9539149"
FT /id="VAR_047456"
FT VARIANT 91
FT /note="K -> R (in dbSNP:rs17854616)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_047457"
FT VARIANT 349
FT /note="K -> N (found in siblings with a novel form of
FT progressive myoclonus epilepsy; unknown pathological
FT significance; no effect on expression levels, cell surface
FT location, signaling activity or ubiquitination;
FT dbSNP:rs372386575)"
FT /evidence="ECO:0000269|PubMed:28688853"
FT /id="VAR_080868"
FT CONFLICT 204
FT /note="R -> S (in Ref. 2; BAG35876)"
FT /evidence="ECO:0000305"
FT CONFLICT 433
FT /note="C -> F (in Ref. 2; BAG35876)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 481 AA; 52771 MW; EE9DFE0446E3AF24 CRC64;
MRWLWPLAVS LAVILAVGLS RVSGGAPLHL GRHRAETQEQ QSRSKRGTED EEAKGVQQYV
PEEWAEYPRP IHPAGLQPTK PLVATSPNPG KDGGTPDSGQ ELRGNLTGAP GQRLQIQNPL
YPVTESSYSA YAIMLLALVV FAVGIVGNLS VMCIVWHSYY LKSAWNSILA SLALWDFLVL
FFCLPIVIFN EITKQRLLGD VSCRAVPFME VSSLGVTTFS LCALGIDRFH VATSTLPKVR
PIERCQSILA KLAVIWVGSM TLAVPELLLW QLAQEPAPTM GTLDSCIMKP SASLPESLYS
LVMTYQNARM WWYFGCYFCL PILFTVTCQL VTWRVRGPPG RKSECRASKH EQCESQLNST
VVGLTVVYAF CTLPENVCNI VVAYLSTELT RQTLDLLGLI NQFSTFFKGA ITPVLLLCIC
RPLGQAFLDC CCCCCCEECG GASEASAANG SDNKLKTEVS SSIYFHKPRE SPPLLPLGTP
C
