GRM1_HUMAN
ID GRM1_HUMAN Reviewed; 1194 AA.
AC Q13255; B9EG79; F8W805; Q13256; Q14757; Q14758; Q5VTF7; Q5VTF8; Q9NU10;
AC Q9UGS9; Q9UGT0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 3.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Metabotropic glutamate receptor 1;
DE Short=mGluR1;
DE Flags: Precursor;
GN Name=GRM1; Synonyms=GPRC1A, MGLUR1;
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] (ISOFORMS ALPHA AND BETA), FUNCTION, AND
RP VARIANTS PRO-593 AND PRO-993.
RX PubMed=7476890;
RA Desai M.A., Burnett J.P., Mayne N.G., Schoepp D.D.;
RT "Cloning and expression of a human metabotropic glutamate receptor 1 alpha:
RT enhanced coupling on co-transfection with a glutamate transporter.";
RL Mol. Pharmacol. 48:648-657(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA), TISSUE SPECIFICITY,
RP AND VARIANT PRO-993.
RX PubMed=9076744; DOI=10.1016/s0028-3908(96)00108-6;
RA Stephan D., Bon C., Holzwarth J.A., Galvan M., Pruss R.M.;
RT "Human metabotropic glutamate receptor 1: mRNA distribution, chromosome
RT localization and functional expression of two splice variants.";
RL Neuropharmacology 35:1649-1660(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS ALPHA AND 3).
RC TISSUE=Testis;
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 [5]
RP INVOLVEMENT IN SCAR13.
RX PubMed=22901947; DOI=10.1016/j.ajhg.2012.07.019;
RA Guergueltcheva V., Azmanov D.N., Angelicheva D., Smith K.R., Chamova T.,
RA Florez L., Bynevelt M., Nguyen T., Cherninkova S., Bojinova V.,
RA Kaprelyan A., Angelova L., Morar B., Chandler D., Kaneva R., Bahlo M.,
RA Tournev I., Kalaydjieva L.;
RT "Autosomal-recessive congenital cerebellar ataxia is caused by mutations in
RT metabotropic glutamate receptor 1.";
RL Am. J. Hum. Genet. 91:553-564(2012).
RN [6]
RP FUNCTION, INVOLVEMENT IN SCA44, VARIANTS SCA44 CYS-262 AND CYS-792, AND
RP CHARACTERIZATION OF VARIANTS SCA44 CYS-262 AND CYS-792.
RX PubMed=28886343; DOI=10.1016/j.ajhg.2017.08.005;
RA Watson L.M., Bamber E., Schnekenberg R.P., Williams J., Bettencourt C.,
RA Lickiss J., Jayawant S., Fawcett K., Clokie S., Wallis Y., Clouston P.,
RA Sims D., Houlden H., Becker E.B.E., Nemeth A.H.;
RT "Dominant Mutations in GRM1 Cause Spinocerebellar Ataxia Type 44.";
RL Am. J. Hum. Genet. 101:451-458(2017).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 28-518 IN COMPLEX WITH ANTAGONIST
RP LY341495, GLYCOSYLATION AT ASN-223, AND DISULFIDE BONDS.
RG Structural genomics consortium (SGC);
RT "Metabotropic glutamate receptor mGluR1 complexed with LY341495
RT antagonist.";
RL Submitted (JUL-2011) to the PDB data bank.
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 581-860 IN COMPLEX WITH ALLOSTERIC
RP ANTAGONIST, FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, SUBUNIT, DISULFIDE
RP BOND, AND ACTIVITY REGULATION.
RX PubMed=24603153; DOI=10.1126/science.1249489;
RA Wu H., Wang C., Gregory K.J., Han G.W., Cho H.P., Xia Y., Niswender C.M.,
RA Katritch V., Meiler J., Cherezov V., Conn P.J., Stevens R.C.;
RT "Structure of a class C GPCR metabotropic glutamate receptor 1 bound to an
RT allosteric modulator.";
RL Science 344:58-64(2014).
RN [9]
RP VARIANT [LARGE SCALE ANALYSIS] TRP-696.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [10]
RP VARIANT SCAR13 PHE-454.
RX PubMed=26308914; DOI=10.1371/journal.pone.0129631;
RA Davarniya B., Hu H., Kahrizi K., Musante L., Fattahi Z., Hosseini M.,
RA Maqsoud F., Farajollahi R., Wienker T.F., Ropers H.H., Najmabadi H.;
RT "The role of a novel TRMT1 gene mutation and rare grm1 gene defect in
RT intellectual disability in two azeri families.";
RL PLoS ONE 10:E0129631-E0129631(2015).
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. Signaling activates a phosphatidylinositol-
CC calcium second messenger system. May participate in the central action
CC of glutamate in the CNS, such as long-term potentiation in the
CC hippocampus and long-term depression in the cerebellum
CC (PubMed:24603153, PubMed:28886343, PubMed:7476890). May function in the
CC light response in the retina (By similarity).
CC {ECO:0000250|UniProtKB:P97772, ECO:0000269|PubMed:24603153,
CC ECO:0000269|PubMed:28886343, ECO:0000269|PubMed:7476890}.
CC -!- ACTIVITY REGULATION: Signaling is inhibited by the antagonist LY341495.
CC The LY341495 binding site partially overlaps with the glutamate binding
CC site. Signaling is also inhibited by synthetic allosteric regulators,
CC such as FITM (4-fluoro-N-(4-(6-(isopropylamino)pyrimidin-4-yl)thiazol-
CC 2-yl)-N-methylbenzamide) that bind in a pocket between the
CC transmembrane helices. {ECO:0000269|PubMed:24603153}.
CC -!- SUBUNIT: Homodimer; disulfide-linked (PubMed:24603153). The PPXXF motif
CC binds HOMER1, HOMER2 and HOMER3. Interacts with TAMALIN (By
CC similarity). Interacts with RYR1, RYR2, ITPR1, SHANK1 and SHANK3.
CC Interacts with SIAH1 (By similarity). {ECO:0000250|UniProtKB:P23385,
CC ECO:0000269|PubMed:24603153}.
CC -!- INTERACTION:
CC Q13255; P52294: KPNA1; NbExp=2; IntAct=EBI-8527352, EBI-358383;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24603153};
CC Multi-pass membrane protein {ECO:0000269|PubMed:24603153}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=Alpha;
CC IsoId=Q13255-1; Sequence=Displayed;
CC Name=Beta;
CC IsoId=Q13255-2; Sequence=VSP_002024, VSP_002025;
CC Name=3;
CC IsoId=Q13255-3; Sequence=VSP_055127, VSP_055128;
CC -!- TISSUE SPECIFICITY: Detected in brain. {ECO:0000269|PubMed:9076744}.
CC -!- DISEASE: Spinocerebellar ataxia, autosomal recessive, 13 (SCAR13)
CC [MIM:614831]: A form of spinocerebellar ataxia, a clinically and
CC genetically heterogeneous group of cerebellar disorders. Patients show
CC progressive incoordination of gait and often poor coordination of
CC hands, speech and eye movements, due to degeneration of the cerebellum
CC with variable involvement of the brainstem and spinal cord. SCAR13 is
CC characterized by delayed psychomotor development beginning in infancy.
CC Affected individuals show mild to profound intellectual disability with
CC poor or absent speech as well as gait and stance ataxia and
CC hyperreflexia. {ECO:0000269|PubMed:22901947,
CC ECO:0000269|PubMed:26308914}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Spinocerebellar ataxia 44 (SCA44) [MIM:617691]: A form of
CC spinocerebellar ataxia, a clinically and genetically heterogeneous
CC group of cerebellar disorders. Patients show progressive incoordination
CC of gait and often poor coordination of hands, speech and eye movements,
CC due to degeneration of the cerebellum with variable involvement of the
CC brainstem and spinal cord. SCA44 is a slowly progressive, autosomal
CC dominant form. {ECO:0000269|PubMed:28886343}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family.
CC {ECO:0000305}.
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DR EMBL; U31215; AAA87843.1; -; mRNA.
DR EMBL; U31216; AAA87844.1; -; mRNA.
DR EMBL; L76627; AAB05337.1; -; mRNA.
DR EMBL; L76631; AAB05338.1; -; mRNA.
DR EMBL; AL031769; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL592423; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL096867; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL035698; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC136280; AAI36281.1; -; mRNA.
DR EMBL; BC143779; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS47497.1; -. [Q13255-2]
DR CCDS; CCDS5209.1; -. [Q13255-1]
DR CCDS; CCDS64548.1; -. [Q13255-3]
DR RefSeq; NP_001264993.1; NM_001278064.1. [Q13255-1]
DR RefSeq; NP_001264994.1; NM_001278065.1. [Q13255-2]
DR RefSeq; NP_001264995.1; NM_001278066.1. [Q13255-2]
DR RefSeq; NP_001264996.1; NM_001278067.1. [Q13255-3]
DR RefSeq; XP_011534084.1; XM_011535782.1. [Q13255-1]
DR RefSeq; XP_016866272.1; XM_017010783.1. [Q13255-1]
DR RefSeq; XP_016866273.1; XM_017010784.1. [Q13255-1]
DR RefSeq; XP_016866274.1; XM_017010785.1. [Q13255-2]
DR RefSeq; XP_016866275.1; XM_017010786.1. [Q13255-2]
DR RefSeq; XP_016866276.1; XM_017010787.1. [Q13255-2]
DR PDB; 3KS9; X-ray; 1.90 A; A/B=28-518.
DR PDB; 4OR2; X-ray; 2.80 A; A/B=581-860.
DR PDB; 7DGD; EM; 3.96 A; A/B=31-863.
DR PDB; 7DGE; EM; 3.65 A; A/B=31-863.
DR PDBsum; 3KS9; -.
DR PDBsum; 4OR2; -.
DR PDBsum; 7DGD; -.
DR PDBsum; 7DGE; -.
DR AlphaFoldDB; Q13255; -.
DR SMR; Q13255; -.
DR BioGRID; 109168; 44.
DR CORUM; Q13255; -.
DR DIP; DIP-57522N; -.
DR ELM; Q13255; -.
DR IntAct; Q13255; 5.
DR MINT; Q13255; -.
DR STRING; 9606.ENSP00000354896; -.
DR BindingDB; Q13255; -.
DR ChEMBL; CHEMBL3772; -.
DR DrugBank; DB04256; (S)-alpha-methyl-4-carboxyphenylglycine.
DR DrugBank; DB00142; Glutamic acid.
DR DrugCentral; Q13255; -.
DR GuidetoPHARMACOLOGY; 289; -.
DR TCDB; 9.A.14.7.1; the g-protein-coupled receptor (gpcr) family.
DR GlyGen; Q13255; 4 sites.
DR iPTMnet; Q13255; -.
DR PhosphoSitePlus; Q13255; -.
DR BioMuta; GRM1; -.
DR DMDM; 311033443; -.
DR jPOST; Q13255; -.
DR MassIVE; Q13255; -.
DR MaxQB; Q13255; -.
DR PaxDb; Q13255; -.
DR PeptideAtlas; Q13255; -.
DR PRIDE; Q13255; -.
DR ProteomicsDB; 30048; -.
DR ProteomicsDB; 59254; -. [Q13255-1]
DR ProteomicsDB; 59255; -. [Q13255-2]
DR Antibodypedia; 2943; 712 antibodies from 43 providers.
DR DNASU; 2911; -.
DR Ensembl; ENST00000282753.6; ENSP00000282753.1; ENSG00000152822.14. [Q13255-1]
DR Ensembl; ENST00000355289.8; ENSP00000347437.4; ENSG00000152822.14. [Q13255-3]
DR Ensembl; ENST00000361719.6; ENSP00000354896.2; ENSG00000152822.14. [Q13255-1]
DR Ensembl; ENST00000492807.6; ENSP00000424095.1; ENSG00000152822.14. [Q13255-2]
DR Ensembl; ENST00000507907.1; ENSP00000425599.1; ENSG00000152822.14. [Q13255-2]
DR GeneID; 2911; -.
DR KEGG; hsa:2911; -.
DR MANE-Select; ENST00000282753.6; ENSP00000282753.1; NM_001278064.2; NP_001264993.1.
DR UCSC; uc003qll.4; human. [Q13255-1]
DR CTD; 2911; -.
DR DisGeNET; 2911; -.
DR GeneCards; GRM1; -.
DR HGNC; HGNC:4593; GRM1.
DR HPA; ENSG00000152822; Tissue enriched (brain).
DR MalaCards; GRM1; -.
DR MIM; 604473; gene.
DR MIM; 614831; phenotype.
DR MIM; 617691; phenotype.
DR neXtProt; NX_Q13255; -.
DR OpenTargets; ENSG00000152822; -.
DR Orphanet; 324262; Autosomal recessive congenital cerebellar ataxia due to MGLUR1 deficiency.
DR Orphanet; 404507; Chondromyxoid fibroma.
DR PharmGKB; PA28990; -.
DR VEuPathDB; HostDB:ENSG00000152822; -.
DR eggNOG; KOG1056; Eukaryota.
DR GeneTree; ENSGT01030000234595; -.
DR HOGENOM; CLU_005389_0_1_1; -.
DR InParanoid; Q13255; -.
DR OMA; RVCSGNE; -.
DR OrthoDB; 107675at2759; -.
DR PhylomeDB; Q13255; -.
DR TreeFam; TF313240; -.
DR PathwayCommons; Q13255; -.
DR Reactome; R-HSA-416476; G alpha (q) signalling events.
DR Reactome; R-HSA-420499; Class C/3 (Metabotropic glutamate/pheromone receptors).
DR Reactome; R-HSA-6794361; Neurexins and neuroligins.
DR Reactome; R-HSA-9717207; Sensory perception of sweet, bitter, and umami (glutamate) taste.
DR SignaLink; Q13255; -.
DR SIGNOR; Q13255; -.
DR BioGRID-ORCS; 2911; 10 hits in 1068 CRISPR screens.
DR ChiTaRS; GRM1; human.
DR EvolutionaryTrace; Q13255; -.
DR GeneWiki; Metabotropic_glutamate_receptor_1; -.
DR GenomeRNAi; 2911; -.
DR Pharos; Q13255; Tchem.
DR PRO; PR:Q13255; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q13255; protein.
DR Bgee; ENSG00000152822; Expressed in lateral nuclear group of thalamus and 73 other tissues.
DR Genevisible; Q13255; HS.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0038037; C:G protein-coupled receptor dimeric complex; IDA:UniProtKB.
DR GO; GO:0038038; C:G protein-coupled receptor homodimeric complex; IPI:FlyBase.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; IMP:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0098839; C:postsynaptic density membrane; IBA:GO_Central.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR GO; GO:0001640; F:adenylate cyclase inhibiting G protein-coupled glutamate receptor activity; IBA:GO_Central.
DR GO; GO:0098872; F:G protein-coupled neurotransmitter receptor activity involved in regulation of postsynaptic cytosolic calcium ion concentration; IEA:Ensembl.
DR GO; GO:0004930; F:G protein-coupled receptor activity; TAS:UniProtKB.
DR GO; GO:0099530; F:G protein-coupled receptor activity involved in regulation of postsynaptic membrane potential; IBA:GO_Central.
DR GO; GO:0008066; F:glutamate receptor activity; IDA:UniProtKB.
DR GO; GO:0099583; F:neurotransmitter receptor activity involved in regulation of postsynaptic cytosolic calcium ion concentration; IBA:GO_Central.
DR GO; GO:0071257; P:cellular response to electrical stimulus; IEA:Ensembl.
DR GO; GO:0007268; P:chemical synaptic transmission; TAS:ProtInc.
DR GO; GO:0007216; P:G protein-coupled glutamate receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0098712; P:L-glutamate import across plasma membrane; IEA:Ensembl.
DR GO; GO:0007626; P:locomotory behavior; IEA:Ensembl.
DR GO; GO:0051482; P:positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G protein-coupled signaling pathway; IMP:UniProtKB.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl.
DR GO; GO:0051930; P:regulation of sensory perception of pain; IEA:Ensembl.
DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IBA:GO_Central.
DR GO; GO:0019233; P:sensory perception of pain; IEA:Ensembl.
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; IPR001256; GPCR_3_mGluR1.
DR InterPro; IPR000162; GPCR_3_mtglu_rcpt.
DR InterPro; IPR019588; Metabotropic_Glu_rcpt_Homer-bd.
DR InterPro; IPR028082; Peripla_BP_I.
DR Pfam; PF00003; 7tm_3; 1.
DR Pfam; PF01094; ANF_receptor; 1.
DR Pfam; PF10606; GluR_Homer-bdg; 1.
DR Pfam; PF07562; NCD3G; 1.
DR PRINTS; PR00248; GPCRMGR.
DR PRINTS; PR01051; MTABOTROPC1R.
DR PRINTS; PR00593; MTABOTROPICR.
DR SMART; SM01229; GluR_Homer-bdg; 1.
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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Disease variant;
KW Disulfide bond; G-protein coupled receptor; Glycoprotein; Membrane;
KW Neurodegeneration; Phosphoprotein; Receptor; Reference proteome; Signal;
KW Spinocerebellar ataxia; Transducer; Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..1194
FT /note="Metabotropic glutamate receptor 1"
FT /id="PRO_0000012922"
FT TOPO_DOM 19..592
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:24603153"
FT TRANSMEM 593..615
FT /note="Helical; Name=1"
FT TOPO_DOM 616..629
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:24603153"
FT TRANSMEM 630..650
FT /note="Helical; Name=2"
FT TOPO_DOM 651..658
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:24603153"
FT TRANSMEM 659..680
FT /note="Helical; Name=3"
FT TOPO_DOM 681..703
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:24603153"
FT TRANSMEM 704..727
FT /note="Helical; Name=4"
FT TOPO_DOM 728..750
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:24603153"
FT TRANSMEM 751..772
FT /note="Helical; Name=5"
FT TOPO_DOM 773..785
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:24603153"
FT TRANSMEM 786..807
FT /note="Helical; Name=6"
FT TOPO_DOM 808..815
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:24603153"
FT TRANSMEM 816..840
FT /note="Helical; Name=7"
FT TOPO_DOM 841..1194
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:24603153"
FT REGION 883..905
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1007..1030
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1113..1173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1008..1022
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1152..1173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 74
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000305"
FT BINDING 165
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000305"
FT BINDING 186..188
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000305"
FT BINDING 236
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 318
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 409
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT MOD_RES 853
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97772"
FT MOD_RES 871
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P97772"
FT MOD_RES 894
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P23385"
FT MOD_RES 969
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97772"
FT MOD_RES 1091
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97772"
FT MOD_RES 1142
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97772"
FT MOD_RES 1146
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P23385"
FT MOD_RES 1149
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97772"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 223
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|Ref.7"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 515
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 67..109
FT DISULFID 140
FT /note="Interchain"
FT DISULFID 289..291
FT /evidence="ECO:0000250"
FT DISULFID 378..394
FT DISULFID 432..439
FT DISULFID 657..746
FT VAR_SEQ 887..908
FT /note="NSNGKSVSWSEPGGGQVPKGQH -> KWRTGAQGTAYVAPPLCAREDQ (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055127"
FT VAR_SEQ 887..906
FT /note="NSNGKSVSWSEPGGGQVPKG -> KKRQPEFSPTSQCPSAHVQL (in
FT isoform Beta)"
FT /evidence="ECO:0000303|PubMed:7476890,
FT ECO:0000303|PubMed:9076744"
FT /id="VSP_002024"
FT VAR_SEQ 907..1194
FT /note="Missing (in isoform Beta)"
FT /evidence="ECO:0000303|PubMed:7476890,
FT ECO:0000303|PubMed:9076744"
FT /id="VSP_002025"
FT VAR_SEQ 909..1194
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055128"
FT VARIANT 34
FT /note="S -> Y (in dbSNP:rs12190109)"
FT /id="VAR_028184"
FT VARIANT 262
FT /note="Y -> C (in SCA44; enhances G-protein coupled
FT glutamate receptor signaling pathway; dbSNP:rs1554274719)"
FT /evidence="ECO:0000269|PubMed:28886343"
FT /id="VAR_080186"
FT VARIANT 285
FT /note="R -> K (in dbSNP:rs7760248)"
FT /id="VAR_028185"
FT VARIANT 454
FT /note="L -> F (in SCAR13)"
FT /evidence="ECO:0000269|PubMed:26308914"
FT /id="VAR_081782"
FT VARIANT 593
FT /note="S -> P (in dbSNP:rs1047005)"
FT /evidence="ECO:0000269|PubMed:7476890"
FT /id="VAR_055875"
FT VARIANT 696
FT /note="R -> W (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs1450433570)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036194"
FT VARIANT 741
FT /note="E -> D (in dbSNP:rs3025919)"
FT /id="VAR_028186"
FT VARIANT 792
FT /note="Y -> C (in SCA44; enhances G-protein coupled
FT glutamate receptor signaling pathway; dbSNP:rs1554308513)"
FT /evidence="ECO:0000269|PubMed:28886343"
FT /id="VAR_080187"
FT VARIANT 884
FT /note="G -> E (in dbSNP:rs362936)"
FT /id="VAR_028187"
FT VARIANT 929
FT /note="V -> I (in dbSNP:rs2941)"
FT /id="VAR_024482"
FT VARIANT 993
FT /note="S -> P (in dbSNP:rs6923492)"
FT /evidence="ECO:0000269|PubMed:7476890,
FT ECO:0000269|PubMed:9076744"
FT /id="VAR_028188"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:3KS9"
FT STRAND 44..51
FT /evidence="ECO:0007829|PDB:3KS9"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:3KS9"
FT TURN 62..65
FT /evidence="ECO:0007829|PDB:3KS9"
FT TURN 72..75
FT /evidence="ECO:0007829|PDB:3KS9"
FT HELIX 76..90
FT /evidence="ECO:0007829|PDB:3KS9"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:3KS9"
FT STRAND 101..107
FT /evidence="ECO:0007829|PDB:3KS9"
FT HELIX 112..123
FT /evidence="ECO:0007829|PDB:3KS9"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:3KS9"
FT HELIX 165..175
FT /evidence="ECO:0007829|PDB:3KS9"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:3KS9"
FT STRAND 182..186
FT /evidence="ECO:0007829|PDB:3KS9"
FT HELIX 190..193
FT /evidence="ECO:0007829|PDB:3KS9"
FT TURN 195..197
FT /evidence="ECO:0007829|PDB:3KS9"
FT STRAND 201..205
FT /evidence="ECO:0007829|PDB:3KS9"
FT HELIX 209..221
FT /evidence="ECO:0007829|PDB:3KS9"
FT STRAND 226..234
FT /evidence="ECO:0007829|PDB:3KS9"
FT HELIX 235..250
FT /evidence="ECO:0007829|PDB:3KS9"
FT STRAND 254..261
FT /evidence="ECO:0007829|PDB:3KS9"
FT HELIX 267..278
FT /evidence="ECO:0007829|PDB:3KS9"
FT TURN 279..284
FT /evidence="ECO:0007829|PDB:3KS9"
FT STRAND 286..290
FT /evidence="ECO:0007829|PDB:3KS9"
FT HELIX 293..306
FT /evidence="ECO:0007829|PDB:3KS9"
FT STRAND 313..316
FT /evidence="ECO:0007829|PDB:3KS9"
FT TURN 318..322
FT /evidence="ECO:0007829|PDB:3KS9"
FT HELIX 324..327
FT /evidence="ECO:0007829|PDB:3KS9"
FT HELIX 331..334
FT /evidence="ECO:0007829|PDB:3KS9"
FT STRAND 338..342
FT /evidence="ECO:0007829|PDB:3KS9"
FT HELIX 348..354
FT /evidence="ECO:0007829|PDB:3KS9"
FT TURN 359..361
FT /evidence="ECO:0007829|PDB:3KS9"
FT HELIX 368..375
FT /evidence="ECO:0007829|PDB:3KS9"
FT STRAND 391..393
FT /evidence="ECO:0007829|PDB:3KS9"
FT TURN 400..403
FT /evidence="ECO:0007829|PDB:3KS9"
FT HELIX 410..431
FT /evidence="ECO:0007829|PDB:3KS9"
FT HELIX 440..442
FT /evidence="ECO:0007829|PDB:3KS9"
FT HELIX 447..455
FT /evidence="ECO:0007829|PDB:3KS9"
FT STRAND 458..460
FT /evidence="ECO:0007829|PDB:3KS9"
FT STRAND 466..468
FT /evidence="ECO:0007829|PDB:3KS9"
FT STRAND 478..486
FT /evidence="ECO:0007829|PDB:3KS9"
FT STRAND 492..501
FT /evidence="ECO:0007829|PDB:3KS9"
FT STRAND 504..507
FT /evidence="ECO:0007829|PDB:3KS9"
FT TURN 509..511
FT /evidence="ECO:0007829|PDB:3KS9"
FT HELIX 591..616
FT /evidence="ECO:0007829|PDB:4OR2"
FT STRAND 618..620
FT /evidence="ECO:0007829|PDB:4OR2"
FT HELIX 621..624
FT /evidence="ECO:0007829|PDB:4OR2"
FT HELIX 628..649
FT /evidence="ECO:0007829|PDB:4OR2"
FT HELIX 654..685
FT /evidence="ECO:0007829|PDB:4OR2"
FT HELIX 703..727
FT /evidence="ECO:0007829|PDB:4OR2"
FT STRAND 732..735
FT /evidence="ECO:0007829|PDB:4OR2"
FT STRAND 738..740
FT /evidence="ECO:0007829|PDB:4OR2"
FT STRAND 742..746
FT /evidence="ECO:0007829|PDB:4OR2"
FT HELIX 750..773
FT /evidence="ECO:0007829|PDB:4OR2"
FT TURN 774..776
FT /evidence="ECO:0007829|PDB:4OR2"
FT HELIX 779..807
FT /evidence="ECO:0007829|PDB:4OR2"
FT HELIX 811..839
FT /evidence="ECO:0007829|PDB:4OR2"
FT CONFLICT Q13255-2:896
FT /note="T -> S (in Ref. 1; AAA87844)"
FT /evidence="ECO:0000305"
FT CONFLICT Q13255-2:904
FT /note="V -> A (in Ref. 1; AAA87844)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1194 AA; 132357 MW; 0A633505F6D51909 CRC64;
MVGLLLFFFP AIFLEVSLLP RSPGRKVLLA GASSQRSVAR MDGDVIIGAL FSVHHQPPAE
KVPERKCGEI REQYGIQRVE AMFHTLDKIN ADPVLLPNIT LGSEIRDSCW HSSVALEQSI
EFIRDSLISI RDEKDGINRC LPDGQSLPPG RTKKPIAGVI GPGSSSVAIQ VQNLLQLFDI
PQIAYSATSI DLSDKTLYKY FLRVVPSDTL QARAMLDIVK RYNWTYVSAV HTEGNYGESG
MDAFKELAAQ EGLCIAHSDK IYSNAGEKSF DRLLRKLRER LPKARVVVCF CEGMTVRGLL
SAMRRLGVVG EFSLIGSDGW ADRDEVIEGY EVEANGGITI KLQSPEVRSF DDYFLKLRLD
TNTRNPWFPE FWQHRFQCRL PGHLLENPNF KRICTGNESL EENYVQDSKM GFVINAIYAM
AHGLQNMHHA LCPGHVGLCD AMKPIDGSKL LDFLIKSSFI GVSGEEVWFD EKGDAPGRYD
IMNLQYTEAN RYDYVHVGTW HEGVLNIDDY KIQMNKSGVV RSVCSEPCLK GQIKVIRKGE
VSCCWICTAC KENEYVQDEF TCKACDLGWW PNADLTGCEP IPVRYLEWSN IESIIAIAFS
CLGILVTLFV TLIFVLYRDT PVVKSSSREL CYIILAGIFL GYVCPFTLIA KPTTTSCYLQ
RLLVGLSSAM CYSALVTKTN RIARILAGSK KKICTRKPRF MSAWAQVIIA SILISVQLTL
VVTLIIMEPP MPILSYPSIK EVYLICNTSN LGVVAPLGYN GLLIMSCTYY AFKTRNVPAN
FNEAKYIAFT MYTTCIIWLA FVPIYFGSNY KIITTCFAVS LSVTVALGCM FTPKMYIIIA
KPERNVRSAF TTSDVVRMHV GDGKLPCRSN TFLNIFRRKK AGAGNANSNG KSVSWSEPGG
GQVPKGQHMW HRLSVHVKTN ETACNQTAVI KPLTKSYQGS GKSLTFSDTS TKTLYNVEEE
EDAQPIRFSP PGSPSMVVHR RVPSAATTPP LPSHLTAEET PLFLAEPALP KGLPPPLQQQ
QQPPPQQKSL MDQLQGVVSN FSTAIPDFHA VLAGPGGPGN GLRSLYPPPP PPQHLQMLPL
QLSTFGEELV SPPADDDDDS ERFKLLQEYV YEHEREGNTE EDELEEEEED LQAASKLTPD
DSPALTPPSP FRDSVASGSS VPSSPVSESV LCTPPNVSYA SVILRDYKQS SSTL
