G37L1_RAT
ID G37L1_RAT Reviewed; 481 AA.
AC Q9QYC5;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 106.
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 AltName: Full=G-protein coupled receptor CNS2;
DE Flags: Precursor;
GN Name=Gpr37l1; Synonyms=Etbrlp2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Hypothalamus;
RX PubMed=10350639; DOI=10.1016/s0169-328x(99)00092-3;
RA Leng N., Gu G., Simerly R.B., Spindel E.R.;
RT "Molecular cloning and characterization of two putative G protein-coupled
RT receptors which are highly expressed in the central nervous system.";
RL Brain Res. Mol. Brain Res. 69:73-83(1999).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-471, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [3]
RP CLEAVAGE.
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).
CC -!- FUNCTION: G-protein coupled receptor (By similarity). Has been shown to
CC bind the neuroprotective and glioprotective factor prosaposin (PSAP),
CC leading to endocytosis followed by an ERK phosphorylation cascade (By
CC similarity). However, other studies have shown that prosaposin does not
CC increase activity (By similarity). It has been suggested that GPR37L1
CC is a constitutively active receptor which signals through the guanine
CC nucleotide-binding protein G(s) subunit alpha (By similarity).
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:O60883,
CC ECO:0000250|UniProtKB:Q99JG2}.
CC -!- SUBUNIT: Interacts with the PTCH1 receptor.
CC {ECO:0000250|UniProtKB:Q99JG2}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O60883};
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: Highly expressed in brain.
CC {ECO:0000269|PubMed:10350639}.
CC -!- DOMAIN: The N-terminal region is required for constitutive signal
CC transduction. {ECO:0000250|UniProtKB:O60883}.
CC -!- PTM: Undergoes metalloprotease-mediated cleavage which reduces its
CC constitutive activity. {ECO:0000269|PubMed:27072655}.
CC -!- PTM: Ubiquitinated. {ECO:0000250|UniProtKB:O60883}.
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 However, it has also been shown that prosaposin does not increase
CC activity. It has been suggested that GPR37L1 is a constitutively active
CC receptor. {ECO:0000250|UniProtKB:O60883}.
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DR EMBL; AF087947; AAD54656.1; -; mRNA.
DR AlphaFoldDB; Q9QYC5; -.
DR SMR; Q9QYC5; -.
DR IntAct; Q9QYC5; 1.
DR MINT; Q9QYC5; -.
DR STRING; 10116.ENSRNOP00000008282; -.
DR GlyGen; Q9QYC5; 1 site.
DR iPTMnet; Q9QYC5; -.
DR PhosphoSitePlus; Q9QYC5; -.
DR PaxDb; Q9QYC5; -.
DR PRIDE; Q9QYC5; -.
DR UCSC; RGD:628835; rat.
DR RGD; 628835; Gpr37l1.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; Q9QYC5; -.
DR PhylomeDB; Q9QYC5; -.
DR Reactome; R-RNO-375276; Peptide ligand-binding receptors.
DR Reactome; R-RNO-418594; G alpha (i) signalling events.
DR PRO; PR:Q9QYC5; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0060170; C:ciliary membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0043235; C:receptor complex; ISO:RGD.
DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; ISO:RGD.
DR GO; GO:0004930; F:G protein-coupled receptor activity; ISS:UniProtKB.
DR GO; GO:0042277; F:peptide binding; ISO:RGD.
DR GO; GO:0036505; F:prosaposin receptor activity; ISS:UniProtKB.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; ISO:RGD.
DR GO; GO:0048712; P:negative regulation of astrocyte differentiation; ISO:RGD.
DR GO; GO:1903206; P:negative regulation of hydrogen peroxide-induced cell death; ISO:RGD.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; ISO:RGD.
DR GO; GO:0045879; P:negative regulation of smoothened signaling pathway; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:RGD.
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..24
FT /evidence="ECO:0000255"
FT CHAIN 25..481
FT /note="G-protein coupled receptor 37-like 1"
FT /id="PRO_0000012798"
FT TOPO_DOM 25..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..360
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 361..381
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 382..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 30..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 76..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..55
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 471
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 479
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q99JG2"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 203..286
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 481 AA; 52860 MW; 0AD20D1C346FFF68 CRC64;
MRWLWPLAVS LAVVLAVGPS EVSGAATLSL GGHRAKVQEQ QSRPRRGTKD EGPKEVQHYV
PEEWAEYPKP IHPAGLQPTK PLVATSPNPD KDGATSESGQ ELRTNLTGTP SQRLQIQNPL
YPVTESSYSA YAVMLLALVV FAVGIVGNLS VMCIVWHSYY LKSAWNSILA SLALWDFLVL
FFCLPIVIFN EITKQRLLGD VSCRAVPFME VSSLGVTTFS LCALGIDRFH VATSTLPKVR
PIERCQSILA KLAVIWVGSM MLAVPELLLW QLAQEPTPTM GTVDSCIMKP SADLPESLYS
LVMTYQNARM WWYFGCYFCL PILFTVTCQL VTWRVRGPPG RKPECRAGRH EQCESQLNST
VVGLTVVYAF CTLPENICNI VVAYLSTELT RQTLDLLGLI NQFSTFFKGA ITPVLLLCIC
RPLGQAFLDC CCCCCCEECG GASDSSATVS ADSKLKAEVS SSIYFHKPRE SPPLLPLGTP
C
