GRM1
entrez
2911
canonical
uniprot
Q13255
canonical
ensembl
ENSG00000152822
resolver
ensp
ENSP00000282753
resolver
ensp
ENSP00000347437
resolver
ensp
ENSP00000354896
resolver
ensp
ENSP00000424095
resolver
ensp
ENSP00000425599
resolver
ensp
ENSP00000516579
resolver
ensp
ENSP00000516581
resolver
genesymbol
GRM1
resolver
genesymbol_syn
GPRC1A
resolver
genesymbol_syn
MGLUR1
resolver
hgnc
HGNC:4593
resolver
uniprot
B9EG79
resolver
uniprot
F8W805
resolver
uniprot
Q13256
resolver
uniprot
Q14757
resolver
uniprot
Q14758
resolver
uniprot
Q59HC2
resolver
uniprot
Q5VTF7
resolver
uniprot
Q5VTF8
resolver
uniprot
Q9NU10
resolver
uniprot
Q9UGS9
resolver
uniprot
Q9UGT0
resolver
uniprot_entry
GRM1_HUMAN
resolver
uniprot_entry
Q59HC2_HUMAN
resolver
uniprot_sec
B9EG79
resolver
uniprot_sec
F8W805
resolver
uniprot_sec
Q13256
resolver
uniprot_sec
Q14757
resolver
uniprot_sec
Q14758
resolver
uniprot_sec
Q5VTF7
resolver
uniprot_sec
Q5VTF8
resolver
uniprot_sec
Q9NU10
resolver
uniprot_sec
Q9UGS9
resolver
uniprot_sec
Q9UGT0
resolver
activity_regulation
ACTIVITY REGULATION: Signaling is inhibited by the antagonist LY341495. The LY341495 binding site partially overlaps with the glutamate binding site. Signaling is also inhibited by synthetic allosteric regulators, such as FITM (4-fluoro-N-(4-(6-(isopropylamino)pyrimidin-4-yl)thiazol-2-yl)-N-methylbenzamide) that bind in a pocket between the transmembrane helices. {ECO:0000269|PubMed:24603153}.
uniprot
proteins
amino_acid_sequence
MVGLLLFFFPAIFLEVSLLPRSPGRKVLLAGASSQRSVARMDGDVIIGALFSVHHQPPAEKVPERKCGEIREQYGIQRVEAMFHTLDKINADPVLLPNITLGSEIRDSCWHSSVALEQSIEFIRDSLISIRDEKDGINRCLPDGQSLPPGRTKKPIAGVIGPGSSSVAIQVQNLLQLFDIPQIAYSATSIDLSDKTLYKYFLRVVPSDTLQARAMLDIVKRYNWTYVSAVHTEGNYGESGMDAFKELAAQEGLCIAHSDKIYSNAGEKSFDRLLRKLRERLPKARVVVCFCEGMTVRGLLSAMRRLGVVGEFSLIGSDGWADRDEVIEGYEVEANGGITIKLQSPEVRSFDDYFLKLRLDTNTRNPWFPEFWQHRFQCRLPGHLLENPNFKRICTGNESLEENYVQDSKMGFVINAIYAMAHGLQNMHHALCPGHVGLCDAMKPIDGSKLLDFLIKSSFIGVSGEEVWFDEKGDAPGRYDIMNLQYTEANRYDYVHVGTWHEGVLNIDDYKIQMNKSGVVRSVCSEPCLKGQIKVIRKGEVSCCWICTACKENEYVQDEFTCKACDLGWWPNADLTGCEPIPVRYLEWSNIESIIAIAFSCLGILVTLFVTLIFVLYRDTPVVKSSSRELCYIILAGIFLGYVCPFTLIAKPTTTSCYLQRLLVGLSSAMCYSALVTKTNRIARILAGSKKKICTRKPRFMSAWAQVIIASILISVQLTLVVTLIIMEPPMPILSYPSIKEVYLICNTSNLGVVAPLGYNGLLIMSCTYYAFKTRNVPANFNEAKYIAFTMYTTCIIWLAFVPIYFGSNYKIITTCFAVSLSVTVALGCMFTPKMYIIIAKPERNVRSAFTTSDVVRMHVGDGKLPCRSNTFLNIFRRKKAGAGNANSNGKSVSWSEPGGGQVPKGQHMWHRLSVHVKTNETACNQTAVIKPLTKSYQGSGKSLTFSDTSTKTLYNVEEEEDAQPIRFSPPGSPSMVVHRRVPSAATTPPLPSHLTAEETPLFLAEPALPKGLPPPLQQQQQPPPQQKSLMDQLQGVVSNFSTAIPDFHAVLAGPGGPGNGLRSLYPPPPPPQHLQMLPLQLSTFGEELVSPPADDDDDSERFKLLQEYVYEHEREGNTEEDELEEEEEDLQAASKLTPDDSPALTPPSPFRDSVASGSSVPSSPVSESVLCTPPNVSYASVILRDYKQSSSTL
uniprot
proteins
disease_involvement
DISEASE: Spinocerebellar ataxia, autosomal recessive, 13 (SCAR13) [MIM:614831]: A form of spinocerebellar ataxia, a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCAR13 is characterized by delayed psychomotor development beginning in infancy. Affected individuals show mild to profound intellectual disability with poor or absent speech as well as gait and stance ataxia and hyperreflexia. {ECO:0000269|PubMed:22901947, ECO:0000269|PubMed:26308914}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Spinocerebellar ataxia 44 (SCA44) [MIM:617691]: A form of spinocerebellar ataxia, a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA44 is a slowly progressive, autosomal dominant form. {ECO:0000269|PubMed:28886343}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: G protein-coupled receptor for glutamate. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Signaling activates a phosphatidylinositol-calcium second messenger system. May participate in the central action of glutamate in the CNS, such as long-term potentiation in the hippocampus and long-term depression in the cerebellum (PubMed:24603153, PubMed:28886343, PubMed:7476890). May function in the light response in the retina (By similarity). Induces GRID1 and GRID2 cation-channel activation via GNAQ-PLC-PKC pathway in dopaminergic neurons and cerebellar Purkinje cell, respectively (PubMed:24357660, PubMed:27276689). {ECO:0000250|UniProtKB:P97772, ECO:0000269|PubMed:24357660, ECO:0000269|PubMed:24603153, ECO:0000269|PubMed:27276689, ECO:0000269|PubMed:28886343, ECO:0000269|PubMed:7476890}.
uniprot
proteins
mass_dalton
132357
uniprot
proteins
protein_family
G protein-coupled receptor 3 family
uniprot
proteins
pubmed
14574404
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16959974
uniprot
proteins
pubmed
22901947
uniprot
proteins
pubmed
24357660
uniprot
proteins
pubmed
24603153
uniprot
proteins
pubmed
26308914
uniprot
proteins
pubmed
27276689
uniprot
proteins
pubmed
28886343
uniprot
proteins
pubmed
7476890
uniprot
proteins
pubmed
9076744
uniprot
proteins
sequence_length
1194
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24603153}; Multi-pass membrane protein {ECO:0000269|PubMed:24603153}. Postsynaptic cell membrane {ECO:0000269|PubMed:27276689}; Multi-pass membrane protein {ECO:0000255}. Cell projection, dendrite {ECO:0000250|UniProtKB:P97772}. Note=Located in dendrioles, small dendrites that makes up a brush structure found as the terminal specialization of a dendrite of a unipolar brush cell. {ECO:0000250|UniProtKB:P97772}.
uniprot
proteins
transmembrane_region
TRANSMEM 593..615; /note="Helical; Name=1"; TRANSMEM 630..650; /note="Helical; Name=2"; TRANSMEM 659..680; /note="Helical; Name=3"; TRANSMEM 704..727; /note="Helical; Name=4"; TRANSMEM 751..772; /note="Helical; Name=5"; TRANSMEM 786..807; /note="Helical; Name=6"; TRANSMEM 816..840; /note="Helical; Name=7
uniprot
proteins