G37L1_BOVIN
ID G37L1_BOVIN Reviewed; 482 AA.
AC Q17QD8;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 101.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal pons;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:0000250|UniProtKB:O60883}.
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}.
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; BC118418; AAI18419.1; -; mRNA.
DR RefSeq; NP_001069367.1; NM_001075899.2.
DR AlphaFoldDB; Q17QD8; -.
DR SMR; Q17QD8; -.
DR STRING; 9913.ENSBTAP00000019957; -.
DR PaxDb; Q17QD8; -.
DR GeneID; 527572; -.
DR KEGG; bta:527572; -.
DR CTD; 9283; -.
DR eggNOG; KOG3656; Eukaryota.
DR HOGENOM; CLU_029119_0_0_1; -.
DR InParanoid; Q17QD8; -.
DR OrthoDB; 568030at2759; -.
DR TreeFam; TF331292; -.
DR Proteomes; UP000009136; 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; IBA:GO_Central.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; ISS:UniProtKB.
DR GO; GO:0036505; F:prosaposin receptor activity; ISS:UniProtKB.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0003085; P:negative regulation of systemic arterial blood pressure; ISS:UniProtKB.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IBA:GO_Central.
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 2: Evidence at transcript 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..482
FT /note="G-protein coupled receptor 37-like 1"
FT /id="PRO_0000307928"
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..482
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 25..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 480
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 482 AA; 51930 MW; 9792F2310AB4A33C CRC64;
MRWLWPLGVS LAVALAAGPE RAPRGVWLQQ GGHQPVAQEQ PDRSRRGAER EDAKGLQQYV
PEGWAEYPRP IRPAALQPTQ PWVAASPSPD RARATGGSGQ EPQGNVTGPP GQRPQVQNPL
YPVTERSYGA YAVLLLALLL FAVGIVGSLA VMCIVWHSYY LKSAWNSVLA SLALWDFLVL
FFCLPVVTFH EITKQRLLGA VSCRAVPFVE VSSLGVTTFS LCALGIDRFH VATSTLPKAR
PIEPCPSILA KLAVIWVGSM TLAAPELLLW QLVREPSPAA GTVDTCIMKP SAHLPESLYS
LVLTYQNARM WWSFGCYFCL PVLFTVTCQL VTWRVRGTPG RKPESRPGPQ EPRGARPSST
VAGLAAVHAL CALPENVCNV VAAYLSAALT RQTLELLGLV TQFSTFFKAA LTPLLLLCVS
RPLGRAFLDC CCCCCGEGCG EGCGGRAAPA GPRAKLHTEL SASGYFHKPR EAPPLLALGT
PC
