GRM1_CAEEL
ID GRM1_CAEEL Reviewed; 999 AA.
AC Q09630;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Probable metabotropic glutamate receptor mgl-1;
GN Name=mgl-1; ORFNames=ZC506.4;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: G-protein coupled receptor for glutamate. Ligand binding
CC causes a conformation change that triggers signaling via guanine
CC nucleotide-binding proteins (G proteins) and modulates the activity of
CC down-stream effectors (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family.
CC {ECO:0000305}.
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DR EMBL; Z47073; CAA87374.1; -; Genomic_DNA.
DR PIR; T27628; T27628.
DR RefSeq; NP_509674.2; NM_077273.2.
DR AlphaFoldDB; Q09630; -.
DR SMR; Q09630; -.
DR BioGRID; 56204; 3.
DR STRING; 6239.ZC506.4a; -.
DR EPD; Q09630; -.
DR PaxDb; Q09630; -.
DR EnsemblMetazoa; ZC506.4a.1; ZC506.4a.1; WBGene00003232.
DR GeneID; 191707; -.
DR UCSC; ZC506.4b; c. elegans.
DR CTD; 191707; -.
DR WormBase; ZC506.4a; CE50434; WBGene00003232; mgl-1.
DR eggNOG; KOG1056; Eukaryota.
DR GeneTree; ENSGT01030000234595; -.
DR InParanoid; Q09630; -.
DR PhylomeDB; Q09630; -.
DR Reactome; R-CEL-418594; G alpha (i) signalling events.
DR Reactome; R-CEL-420499; Class C/3 (Metabotropic glutamate/pheromone receptors).
DR PRO; PR:Q09630; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00003232; Expressed in anatomical system and 4 other tissues.
DR ExpressionAtlas; Q09630; baseline and differential.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0001640; F:adenylate cyclase inhibiting G protein-coupled glutamate receptor activity; IBA:GO_Central.
DR GO; GO:0001641; F:group II metabotropic glutamate receptor activity; IBA:GO_Central.
DR GO; GO:0007216; P:G protein-coupled glutamate receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0010884; P:positive regulation of lipid storage; IGI:WormBase.
DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IBA:GO_Central.
DR Gene3D; 2.10.50.30; -; 1.
DR InterPro; IPR001828; ANF_lig-bd_rcpt.
DR InterPro; IPR000337; GPCR_3.
DR InterPro; IPR011500; GPCR_3_9-Cys_dom.
DR InterPro; IPR038550; GPCR_3_9-Cys_sf.
DR InterPro; IPR017978; GPCR_3_C.
DR InterPro; IPR017979; GPCR_3_CS.
DR InterPro; IPR000162; GPCR_3_mtglu_rcpt.
DR InterPro; IPR028082; Peripla_BP_I.
DR Pfam; PF00003; 7tm_3; 1.
DR Pfam; PF01094; ANF_receptor; 1.
DR Pfam; PF07562; NCD3G; 1.
DR PRINTS; PR00248; GPCRMGR.
DR PRINTS; PR00593; MTABOTROPICR.
DR SUPFAM; SSF53822; SSF53822; 1.
DR PROSITE; PS00979; G_PROTEIN_RECEP_F3_1; 1.
DR PROSITE; PS00980; G_PROTEIN_RECEP_F3_2; 1.
DR PROSITE; PS00981; G_PROTEIN_RECEP_F3_3; 1.
DR PROSITE; PS50259; G_PROTEIN_RECEP_F3_4; 1.
PE 3: Inferred from homology;
KW Cell membrane; G-protein coupled receptor; Glycoprotein; Membrane;
KW Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..999
FT /note="Probable metabotropic glutamate receptor mgl-1"
FT /id="PRO_0000206893"
FT TRANSMEM 682..704
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 719..739
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 751..769
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 792..812
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 836..857
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 871..893
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 904..929
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 975..999
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 983..999
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 202
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 223..225
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 273
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 363
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 455
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT CARBOHYD 518
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 999 AA; 113276 MW; AB22AF2A28D9A0CF CRC64;
MDKKWSLEQR WLHLLNQQFL DCLNHLFNHY RRLSTFQKPP SIIRHMFSVL ALAIQILANV
NVVAQTTEAV DLAPPPKVRQ IRIPGDILIG GVFPVHSKSL NGDEPCGEIA ETRGVHRVEA
MLYALDQINS QNDFLRGYKL GALILDSCSN PAYALNQSLD FVRDMIGSSE ASDYVCLDGS
DPNLKKQSQK KNVAAVVGGS YSSVSVQLAN LLRLFRIAQV SPASTNADLS DKNRFEYFAR
TVPSDDYQAM AMVEIAVKFK WSYVSLVYSA DEYGELGADA FKKEARKKGI CIALEERIQN
KKESFTESIN NLVQKLQPEK NVGATVVVLF VGTEYIPDIL RYTAERMKLT SGAKKRIIWL
ASESWDRNND KYTAGDNRLA AQGAIVLMLA SQKVPSFEEY FMSLHPGTEA FERNKWLREL
WQVKYKCEFD TPPGSTASRC EDIKQSTEGF NADDKVQFVI DAVYAIAHGL QSMKQAICPD
DAIENHWISR YSKQPEICHA MQNIDGSDFY QNYLLKVNFT GKTISIFSSF RLSPFSDIVG
KRFRFSPQGD GPASYTILTY KPKSMDKKRR MTDDESSPSD YVEIGHWSEN NLTIYEKNLW
WDPDHTPVSV CSLPCKIGFR KQLIKDEQCC WACSKCEDYE YLINETHCVG CEQGWWPTKD
RKGCFDLSLS QLKYMRWRSM YSLVPTILAV FGIIATLFVI VVYVIYNETP VVKASGRELS
YILLISMIMC YCMTFVLLSK PSAIVCAIKR TGIGFAFSCL YSAMFVKTNR IFRIFSTRSA
QRPRFISPIS QVVMTAMLAG VQLIGSLIWL SVVPPGWRHH YPTRDQVVLT CNVPDHHFLY
SLAYDGFLIV LCTTYAVKTR KVPENFNETK FIGFSMYTTC VVWLSWIFFF FGTGSDFQIQ
TSSLCISISM SANVALACIF SPKLWIILFE KHKNVRKQEG ESMLNKSSRS LGNCSSRLCA
NSIDEPNQYT ALLTDSTRRR SSRKTSQPTS TSSAHDTFL
