P21279 · GNAQ_MOUSE
- ProteinGuanine nucleotide-binding protein G(q) subunit alpha
- GeneGnaq
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids359 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Guanine nucleotide-binding proteins (G proteins) function as transducers downstream of G protein-coupled receptors (GPCRs) in numerous signaling cascades (PubMed:20966218, PubMed:9687499).
The alpha chain contains the guanine nucleotide binding site and alternates between an active, GTP-bound state and an inactive, GDP-bound state (PubMed:20966218).
Signaling by an activated GPCR promotes GDP release and GTP binding (PubMed:20966218).
The alpha subunit has a low GTPase activity that converts bound GTP to GDP, thereby terminating the signal (PubMed:20966218).
Both GDP release and GTP hydrolysis are modulated by numerous regulatory proteins (PubMed:20966218).
Signaling is mediated via phospholipase C-beta-dependent inositol lipid hydrolysis for signal propagation: activates phospholipase C-beta: following GPCR activation, GNAQ activates PLC-beta (PLCB1, PLCB2, PLCB3 or PLCB4), leading to production of diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) (PubMed:20966218).
Required for platelet activation (PubMed:9296496).
Regulates B-cell selection and survival and is required to prevent B-cell-dependent autoimmunity (PubMed:20624888).
Regulates chemotaxis of BM-derived neutrophils and dendritic cells (in vitro) (PubMed:17938235).
Transduces FFAR4 signaling in response to long-chain fatty acids (LCFAs) (By similarity).
Together with GNA11, required for heart development (PubMed:9687499).
The alpha chain contains the guanine nucleotide binding site and alternates between an active, GTP-bound state and an inactive, GDP-bound state (PubMed:20966218).
Signaling by an activated GPCR promotes GDP release and GTP binding (PubMed:20966218).
The alpha subunit has a low GTPase activity that converts bound GTP to GDP, thereby terminating the signal (PubMed:20966218).
Both GDP release and GTP hydrolysis are modulated by numerous regulatory proteins (PubMed:20966218).
Signaling is mediated via phospholipase C-beta-dependent inositol lipid hydrolysis for signal propagation: activates phospholipase C-beta: following GPCR activation, GNAQ activates PLC-beta (PLCB1, PLCB2, PLCB3 or PLCB4), leading to production of diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) (PubMed:20966218).
Required for platelet activation (PubMed:9296496).
Regulates B-cell selection and survival and is required to prevent B-cell-dependent autoimmunity (PubMed:20624888).
Regulates chemotaxis of BM-derived neutrophils and dendritic cells (in vitro) (PubMed:17938235).
Transduces FFAR4 signaling in response to long-chain fatty acids (LCFAs) (By similarity).
Together with GNA11, required for heart development (PubMed:9687499).
Catalytic activity
- GTP + H2O = GDP + H+ + phosphateThis reaction proceeds in the forward direction.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 50 | GTP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 51 | GTP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 52 | GTP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 53 | GTP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 53 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 54 | GTP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 156 | GTP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 180 | GTP (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 181 | GTP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 183 | GTP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 186 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 274 | GTP (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 275 | GTP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 277 | GTP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 331 | GTP (UniProtKB | ChEBI) | ||||
Sequence: A |
GO annotations
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGuanine nucleotide-binding protein G(q) subunit alpha
- EC number
- Alternative names
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 accessionP21279
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Lipid-anchor
Note: Colocalizes with the adrenergic receptors, ADREN1A and ADREN1B, at the nuclear membrane of cardiac myocytes.
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Mice are viable but suffer from cerebellar ataxia and display deficiencies in primary hemostasis due to a defect in platelet activation (PubMed:9296496, PubMed:9391157).
Mice lacking Gnaq and Gna11 are embryonic lethal due to cardiomyocyte hypoplasia (PubMed:9687499).
Mice lacking Gnaq and with one single intact copy of Gna11, as well as mice lacking Gna11 and with one single intact copy of Gnaq die shortly after birth; lethality is caused by heart malformations (PubMed:9687499).
Newborns display craniofacial defects (PubMed:9687499).
Mice lacking Gnaq and Gna11 are embryonic lethal due to cardiomyocyte hypoplasia (PubMed:9687499).
Mice lacking Gnaq and with one single intact copy of Gna11, as well as mice lacking Gna11 and with one single intact copy of Gnaq die shortly after birth; lethality is caused by heart malformations (PubMed:9687499).
Newborns display craniofacial defects (PubMed:9687499).
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 9 | Abolishes palmitoylation. | ||||
Sequence: C → S | ||||||
Mutagenesis | 10 | Abolishes palmitoylation. | ||||
Sequence: C → S | ||||||
Mutagenesis | 218 | Reduced ability to activate phospholipase PLCB3. | ||||
Sequence: H → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 12 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, lipidation, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000203761 | 1-359 | Guanine nucleotide-binding protein G(q) subunit alpha | |||
Sequence: MTLESIMACCLSEEAKEARRINDEIERQLRRDKRDARRELKLLLLGTGESGKSTFIKQMRIIHGSGYSDEDKRGFTKLVYQNIFTAMQAMIRAMDTLKIPYKYEHNKAHAQLVREVDVEKVSAFENPYVDAIKSLWNDPGIQECYDRRREYQLSDSTKYYLNDLDRVADPSYLPTQQDVLRVRVPTTGIIEYPFDLQSVIFRMVDVGGQRSERRKWIHCFENVTSIMFLVALSEYDQVLVESDNENRMEESKALFRTIITYPWFQNSSVILFLNKKDLLEEKIMYSHLVDYFPEYDGPQRDAQAAREFILKMFVDLNPDSDKIIYSHFTCATDTENIRFVFAAVKDTILQLNLKEYNLV | ||||||
Lipidation | 9 | S-palmitoyl cysteine | ||||
Sequence: C | ||||||
Lipidation | 10 | S-palmitoyl cysteine | ||||
Sequence: C | ||||||
Modified residue | 209 | 5-glutamyl histamine | ||||
Sequence: Q |
Post-translational modification
Palmitoylated by ZDHHC3 and ZDHHC7 (PubMed:19001095).
Palmitoylation occurs in the Golgi and participates in the localization of GNAQ to the plasma membrane (PubMed:19001095).
Palmitoylation occurs in the Golgi and participates in the localization of GNAQ to the plasma membrane (PubMed:19001095).
Histaminylated at Gln-209 residues by TGM2.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
G proteins are composed of 3 units; alpha, beta and gamma (By similarity).
The alpha chain contains the guanine nucleotide binding site (By similarity).
Binds NHERF1 (By similarity).
Forms a complex with PECAM1 and BDKRB2 (By similarity).
Interacts with GAS2L2 (PubMed:23994616).
The alpha chain contains the guanine nucleotide binding site (By similarity).
Binds NHERF1 (By similarity).
Forms a complex with PECAM1 and BDKRB2 (By similarity).
Interacts with GAS2L2 (PubMed:23994616).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P21279 | Aip O08915 | 2 | EBI-771975, EBI-6935014 | |
XENO | P21279 | PLCB3 Q01970 | 6 | EBI-771975, EBI-4289548 | |
XENO | P21279 | RGS2 P41220-1 | 3 | EBI-771975, EBI-16037474 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 38-359 | G-alpha | ||||
Sequence: RELKLLLLGTGESGKSTFIKQMRIIHGSGYSDEDKRGFTKLVYQNIFTAMQAMIRAMDTLKIPYKYEHNKAHAQLVREVDVEKVSAFENPYVDAIKSLWNDPGIQECYDRRREYQLSDSTKYYLNDLDRVADPSYLPTQQDVLRVRVPTTGIIEYPFDLQSVIFRMVDVGGQRSERRKWIHCFENVTSIMFLVALSEYDQVLVESDNENRMEESKALFRTIITYPWFQNSSVILFLNKKDLLEEKIMYSHLVDYFPEYDGPQRDAQAAREFILKMFVDLNPDSDKIIYSHFTCATDTENIRFVFAAVKDTILQLNLKEYNLV | ||||||
Region | 41-54 | G1 motif | ||||
Sequence: KLLLLGTGESGKST | ||||||
Region | 178-186 | G2 motif | ||||
Sequence: DVLRVRVPT | ||||||
Region | 201-210 | G3 motif | ||||
Sequence: FRMVDVGGQR | ||||||
Region | 270-277 | G4 motif | ||||
Sequence: ILFLNKKD | ||||||
Region | 329-334 | G5 motif | ||||
Sequence: TCATDT |
Sequence similarities
Belongs to the G-alpha family. G(q) subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length359
- Mass (Da)42,158
- Last updated2009-07-07 v4
- Checksum3BCBA4EE7DADADBF
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 28-29 | in Ref. 1; AAA63306 | ||||
Sequence: QL → HV | ||||||
Sequence conflict | 62 | in Ref. 2; AAH57583 | ||||
Sequence: Missing |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M55412 EMBL· GenBank· DDBJ | AAA63306.1 EMBL· GenBank· DDBJ | mRNA | ||
BC057583 EMBL· GenBank· DDBJ | AAH57583.1 EMBL· GenBank· DDBJ | mRNA |