Q14BI2 · GRM2_MOUSE
- ProteinMetabotropic glutamate receptor 2
- GeneGrm2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids872 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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 inhibits adenylate cyclase activity. May mediate suppression of neurotransmission or may be involved in synaptogenesis or synaptic stabilization.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 145 | L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 166-168 | L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: AST | ||||||
Binding site | 216 | L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 295 | L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 377 | L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: K |
GO annotations
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMetabotropic glutamate receptor 2
- Short namesmGluR2
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ14BI2
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 19-568 | Extracellular | ||||
Sequence: EGPAKKVLTLEGDLVLGGLFPVHQKGGPAEECGPVNEHRGIQRLEAMLFALDRINRDPHLLPGVRLGAHILDSCSKDTHALEQALDFVRASLSRGADGSRHICPDGSYATLSDAPTAITGVIGGSYSDVSIQVANLLRLFQIPQISYASTSAKLSDKSRYDYFARTVPPDFFQAKAMAEILRFFNWTYVSTVASEGDYGETGIEAFELEARARNICVATSEKVGRAMSRAAFEGVVRALLQKPSARVAVLFTRSEDARELLAATQRLNASFTWVASDGWGALESVVAGSERAAEGAITIELASYPISDFASYFQNLDPWNNSRNPWFREFWEERFRCSFRQRDCAAHSLRAVPFEQESKIMFVVNAVYAMAHALHNMHRALCPNTTRLCDAMRPVNGRRLYKDFVLNVKFDAPFRPADTDDEVRFDRFGDGIGRYNIFTYLRAGNGRYRYQKVGYWAEGLTLDTSIIPWASPSAGTLPASRCSEPCLQNEVKSVQPGEVCCWLCIPCQPYEYRLDEFTCADCGLGYWPNASLTGCFELPQEYIRWGDAWA | ||||||
Transmembrane | 569-589 | Helical; Name=1 | ||||
Sequence: VGPVTIACLGALATLFVLGVF | ||||||
Topological domain | 590-604 | Cytoplasmic | ||||
Sequence: VRHNATPVVKASGRE | ||||||
Transmembrane | 605-625 | Helical; Name=2 | ||||
Sequence: LCYILLGGVFLCYCMTFIFIA | ||||||
Topological domain | 626-633 | Extracellular | ||||
Sequence: KPSTAVCT | ||||||
Transmembrane | 634-651 | Helical; Name=3 | ||||
Sequence: LRRLGLGTAFSVCYSALL | ||||||
Topological domain | 652-679 | Cytoplasmic | ||||
Sequence: TKTNRIARIFGGAREGAQRPRFISPASQ | ||||||
Transmembrane | 680-700 | Helical; Name=4 | ||||
Sequence: VAICLALISGQLLIVAAWLVV | ||||||
Topological domain | 701-726 | Extracellular | ||||
Sequence: EAPGIGKETAPERREVVTLRCNHRDA | ||||||
Transmembrane | 727-747 | Helical; Name=5 | ||||
Sequence: SMLGSLAYNVLLIALCTLYAF | ||||||
Topological domain | 748-760 | Cytoplasmic | ||||
Sequence: KTRKCPENFNEAK | ||||||
Transmembrane | 761-781 | Helical; Name=6 | ||||
Sequence: FIGFTMYTTCIIWLAFLPIFY | ||||||
Topological domain | 782-798 | Extracellular | ||||
Sequence: VTSSDYRVQTTTMCVSV | ||||||
Transmembrane | 799-819 | Helical; Name=7 | ||||
Sequence: SLSGSVVLGCLFAPKLHIILF | ||||||
Topological domain | 820-872 | Cytoplasmic | ||||
Sequence: QPQKNVVSHRAPTSRFGSAAPRASANLGQGSGSQLVPTVCNGREVVDSTTSSL |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-18 | |||||
Sequence: MESLLRFLALLLLRGAVA | ||||||
Chain | PRO_0000306249 | 19-872 | Metabotropic glutamate receptor 2 | |||
Sequence: EGPAKKVLTLEGDLVLGGLFPVHQKGGPAEECGPVNEHRGIQRLEAMLFALDRINRDPHLLPGVRLGAHILDSCSKDTHALEQALDFVRASLSRGADGSRHICPDGSYATLSDAPTAITGVIGGSYSDVSIQVANLLRLFQIPQISYASTSAKLSDKSRYDYFARTVPPDFFQAKAMAEILRFFNWTYVSTVASEGDYGETGIEAFELEARARNICVATSEKVGRAMSRAAFEGVVRALLQKPSARVAVLFTRSEDARELLAATQRLNASFTWVASDGWGALESVVAGSERAAEGAITIELASYPISDFASYFQNLDPWNNSRNPWFREFWEERFRCSFRQRDCAAHSLRAVPFEQESKIMFVVNAVYAMAHALHNMHRALCPNTTRLCDAMRPVNGRRLYKDFVLNVKFDAPFRPADTDDEVRFDRFGDGIGRYNIFTYLRAGNGRYRYQKVGYWAEGLTLDTSIIPWASPSAGTLPASRCSEPCLQNEVKSVQPGEVCCWLCIPCQPYEYRLDEFTCADCGLGYWPNASLTGCFELPQEYIRWGDAWAVGPVTIACLGALATLFVLGVFVRHNATPVVKASGRELCYILLGGVFLCYCMTFIFIAKPSTAVCTLRRLGLGTAFSVCYSALLTKTNRIARIFGGAREGAQRPRFISPASQVAICLALISGQLLIVAAWLVVEAPGIGKETAPERREVVTLRCNHRDASMLGSLAYNVLLIALCTLYAFKTRKCPENFNEAKFIGFTMYTTCIIWLAFLPIFYVTSSDYRVQTTTMCVSVSLSGSVVLGCLFAPKLHIILFQPQKNVVSHRAPTSRFGSAAPRASANLGQGSGSQLVPTVCNGREVVDSTTSSL | ||||||
Disulfide bond | 50↔92 | |||||
Sequence: CGPVNEHRGIQRLEAMLFALDRINRDPHLLPGVRLGAHILDSC | ||||||
Glycosylation | 203 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 234↔518 | |||||
Sequence: CVATSEKVGRAMSRAAFEGVVRALLQKPSARVAVLFTRSEDARELLAATQRLNASFTWVASDGWGALESVVAGSERAAEGAITIELASYPISDFASYFQNLDPWNNSRNPWFREFWEERFRCSFRQRDCAAHSLRAVPFEQESKIMFVVNAVYAMAHALHNMHRALCPNTTRLCDAMRPVNGRRLYKDFVLNVKFDAPFRPADTDDEVRFDRFGDGIGRYNIFTYLRAGNGRYRYQKVGYWAEGLTLDTSIIPWASPSAGTLPASRCSEPCLQNEVKSVQPGEVC | ||||||
Glycosylation | 286 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 338 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 355↔362 | |||||
Sequence: CSFRQRDC | ||||||
Disulfide bond | 400↔407 | |||||
Sequence: CPNTTRLC | ||||||
Glycosylation | 402 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 500↔519 | |||||
Sequence: CSEPCLQNEVKSVQPGEVCC | ||||||
Disulfide bond | 504↔522 | |||||
Sequence: CLQNEVKSVQPGEVCCWLC | ||||||
Disulfide bond | 525↔537 | |||||
Sequence: CQPYEYRLDEFTC | ||||||
Disulfide bond | 540↔553 | |||||
Sequence: CGLGYWPNASLTGC | ||||||
Glycosylation | 547 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Detected in neurons in brain cortex (at protein level).
Gene expression databases
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 677-685 | Important for interaction with HTR2A | ||||
Sequence: ASQVAICLA |
Sequence similarities
Belongs to the G-protein coupled receptor 3 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Protein family/group databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length872
- Mass (Da)95,887
- Last updated2007-10-02 v2
- ChecksumFE1726B0684E256D
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0J9YVF0 | A0A0J9YVF0_MOUSE | Grm2 | 594 | ||
A0A0J9YU95 | A0A0J9YU95_MOUSE | Grm2 | 381 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC152452 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC115866 EMBL· GenBank· DDBJ | AAI15867.1 EMBL· GenBank· DDBJ | mRNA |