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 24-JAN-2024, entry version 184. 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; Q9C0I4: THSD7B; NbExp=3; IntAct=EBI-2927498, EBI-311394; 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}. 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; 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; 55. 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 GlyCosmos; O60883; 7 sites, 2 glycans. 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; 9606-ENSP00000356251; -. DR PeptideAtlas; O60883; -. DR ProteomicsDB; 49649; -. DR Antibodypedia; 20649; 323 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 AGR; HGNC:14923; -. 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; ENSGT01100000263518; -. DR HOGENOM; CLU_029119_0_0_1; -. DR InParanoid; O60883; -. DR OMA; EDWAEYP; -. DR OrthoDB; 4268515at2759; -. 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 1137 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 115 other cell types or tissues. DR GO; GO:0060170; C:ciliary membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C: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:0034614; P:cellular response to reactive oxygen species; ISS:ParkinsonsUK-UCL. DR GO; GO:0048712; P:negative regulation of astrocyte differentiation; IEA:Ensembl. 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 CDD; cd15126; 7tmA_ETBR-LP2; 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:SF4; G-PROTEIN COUPLED RECEPTOR 37-LIKE 1; 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; O60883; HS. 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; uncertain significance; no FT effect on expression levels, cell surface location, FT signaling activity or ubiquitination; 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 //