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P21279 (GNAQ_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 155. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Guanine nucleotide-binding protein G(q) subunit alpha
Alternative name(s):
Guanine nucleotide-binding protein alpha-q
Gene names
Name:Gnaq
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length359 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Regulates B-cell selection and survival and is required to prevent B-cell-dependent autoimmunity. Regulates chemotaxis of BM-derived neutrophils and dendritic cells (in vitro). Ref.5 Ref.7

Subunit structure

G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site. Binds SLC9A3R1. Forms a complex with PECAM1 and BDKRB2. Interacts with PECAM1 By similarity.

Subcellular location

Nucleus. Membrane. Nucleus membrane. Note: Colocalizes with the adrenergic receptors, ADREN1A and ADREN1B, at the nuclear membrane of cardiac myocytes. Ref.6

Sequence similarities

Belongs to the G-alpha family. G(q) subfamily.

Ontologies

Keywords
   Cellular componentMembrane
Nucleus
   LigandGTP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionTransducer
   PTMLipoprotein
Palmitate
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled receptor signaling pathway

Inferred from mutant phenotype PubMed 9687499. Source: MGI

action potential

Inferred from mutant phenotype PubMed 10818132. Source: MGI

adenylate cyclase-activating G-protein coupled receptor signaling pathway

Inferred from direct assay PubMed 10481072. Source: MGI

developmental pigmentation

Inferred from mutant phenotype PubMed 15322542. Source: MGI

embryonic digit morphogenesis

Inferred from genetic interaction PubMed 12077299. Source: MGI

forebrain neuron development

Inferred from mutant phenotype PubMed 15340067. Source: MGI

glutamate receptor signaling pathway

Inferred from mutant phenotype PubMed 11438569. Source: MGI

heart development

Inferred from mutant phenotype PubMed 9687499. Source: MGI

maternal behavior

Inferred from mutant phenotype PubMed 15340067. Source: MGI

negative regulation of protein kinase activity

Inferred from electronic annotation. Source: Ensembl

neuron remodeling

Inferred from mutant phenotype PubMed 9391157. Source: MGI

phospholipase C-activating dopamine receptor signaling pathway

Inferred from genetic interaction PubMed 17194762. Source: MGI

post-embryonic development

Inferred from mutant phenotype PubMed 15340067. Source: MGI

protein stabilization

Inferred from electronic annotation. Source: Ensembl

regulation of catenin import into nucleus

Inferred from electronic annotation. Source: Ensembl

regulation of melanocyte differentiation

Inferred from mutant phenotype PubMed 15322542. Source: MGI

skeletal system development

Inferred from mutant phenotype PubMed 9687499. Source: MGI

   Cellular_componentextrinsic component of cytoplasmic side of plasma membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

heterotrimeric G-protein complex

Inferred from Biological aspect of Ancestor. Source: RefGenome

lysosomal membrane

Inferred from electronic annotation. Source: Ensembl

membrane

Inferred from direct assay PubMed 9016340. Source: MGI

nuclear membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionG-protein beta/gamma-subunit complex binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

G-protein coupled receptor binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

GTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GTPase activator activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

GTPase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 16354929. Source: UniProtKB

signal transducer activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

AipO089152EBI-771975,EBI-6935014

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 359359Guanine nucleotide-binding protein G(q) subunit alpha
PRO_0000203761

Regions

Nucleotide binding46 – 538GTP By similarity
Nucleotide binding180 – 1867GTP By similarity
Nucleotide binding205 – 2095GTP By similarity
Nucleotide binding274 – 2774GTP By similarity

Sites

Metal binding531Magnesium By similarity
Metal binding1861Magnesium By similarity
Binding site3311GTP; via amide nitrogen By similarity

Amino acid modifications

Lipidation91S-palmitoyl cysteine Ref.4
Lipidation101S-palmitoyl cysteine Ref.4

Experimental info

Mutagenesis91C → S: Abolishes palmitoylation. Ref.4
Mutagenesis101C → S: Abolishes palmitoylation. Ref.4
Sequence conflict28 – 292QL → HV in AAA63306. Ref.1
Sequence conflict621Missing in AAH57583. Ref.2

Secondary structure

........................................................ 359
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P21279 [UniParc].

Last modified July 7, 2009. Version 4.
Checksum: 3BCBA4EE7DADADBF

FASTA35942,158
        10         20         30         40         50         60 
MTLESIMACC LSEEAKEARR INDEIERQLR RDKRDARREL KLLLLGTGES GKSTFIKQMR 

        70         80         90        100        110        120 
IIHGSGYSDE DKRGFTKLVY QNIFTAMQAM IRAMDTLKIP YKYEHNKAHA QLVREVDVEK 

       130        140        150        160        170        180 
VSAFENPYVD AIKSLWNDPG IQECYDRRRE YQLSDSTKYY LNDLDRVADP SYLPTQQDVL 

       190        200        210        220        230        240 
RVRVPTTGII EYPFDLQSVI FRMVDVGGQR SERRKWIHCF ENVTSIMFLV ALSEYDQVLV 

       250        260        270        280        290        300 
ESDNENRMEE SKALFRTIIT YPWFQNSSVI LFLNKKDLLE EKIMYSHLVD YFPEYDGPQR 

       310        320        330        340        350 
DAQAAREFIL KMFVDLNPDS DKIIYSHFTC ATDTENIRFV FAAVKDTILQ LNLKEYNLV 

« Hide

References

« Hide 'large scale' references
[1]"G protein diversity: a distinct class of alpha subunits is present in vertebrates and invertebrates."
Strathmann M., Simon M.I.
Proc. Natl. Acad. Sci. U.S.A. 87:9113-9117(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6.
Tissue: Brain.
[3]Lubec G., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 20-27; 61-73; 78-92; 121-133; 159-181; 184-210; 283-300; 312-338 AND 346-354, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain.
[4]"Palmitoylation is required for signaling functions and membrane attachment of Gq alpha and Gs alpha."
Wedegaertner P.B., Chu D.H., Wilson P.T., Levis M.J., Bourne H.R.
J. Biol. Chem. 268:25001-25008(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PALMITOYLATION AT CYS-9 AND CYS-10, MUTAGENESIS OF CYS-9 AND CYS-10.
Tissue: Brain.
[5]"Identification of an alternative G{alpha}q-dependent chemokine receptor signal transduction pathway in dendritic cells and granulocytes."
Shi G., Partida-Sanchez S., Misra R.S., Tighe M., Borchers M.T., Lee J.J., Simon M.I., Lund F.E.
J. Exp. Med. 204:2705-2718(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"Nuclear alpha1-adrenergic receptors signal activated ERK localization to caveolae in adult cardiac myocytes."
Wright C.D., Chen Q., Baye N.L., Huang Y., Healy C.L., Kasinathan S., O'Connell T.D.
Circ. Res. 103:992-1000(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[7]"G alpha q-containing G proteins regulate B cell selection and survival and are required to prevent B cell-dependent autoimmunity."
Misra R.S., Shi G., Moreno-Garcia M.E., Thankappan A., Tighe M., Mousseau B., Kusser K., Becker-Herman S., Hudkins K.L., Dunn R., Kehry M.R., Migone T.S., Marshak-Rothstein A., Simon M., Randall T.D., Alpers C.E., Liggitt D., Rawlings D.J., Lund F.E.
J. Exp. Med. 207:1775-1789(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M55412 mRNA. Translation: AAA63306.1.
BC057583 mRNA. Translation: AAH57583.1.
CCDSCCDS29684.1.
PIRRGMSQ. A38414.
RefSeqNP_032165.3. NM_008139.5.
UniGeneMm.439701.
Mm.441601.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2BCJX-ray3.06Q37-359[»]
2RGNX-ray3.50A/D37-359[»]
3AH8X-ray2.90A37-359[»]
3OHMX-ray2.70A35-359[»]
4EKCX-ray7.40A/C18-359[»]
4EKDX-ray2.71A18-359[»]
4GNKX-ray4.00A/C7-359[»]
ProteinModelPortalP21279.
SMRP21279. Positions 18-354.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199971. 2 interactions.
DIPDIP-606N.
IntActP21279. 5 interactions.
MINTMINT-4096294.

PTM databases

PhosphoSiteP21279.

Proteomic databases

MaxQBP21279.
PaxDbP21279.
PRIDEP21279.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000025541; ENSMUSP00000025541; ENSMUSG00000024639.
GeneID14682.
KEGGmmu:14682.
UCSCuc008gwt.1. mouse.

Organism-specific databases

CTD2776.
MGIMGI:95776. Gnaq.

Phylogenomic databases

eggNOGNOG322962.
HOGENOMHOG000038729.
HOVERGENHBG063184.
InParanoidP21279.
KOK04634.
OMALKISYGV.
OrthoDBEOG7ZWD1W.
PhylomeDBP21279.
TreeFamTF300673.

Enzyme and pathway databases

ReactomeREACT_188937. Metabolism.

Gene expression databases

ArrayExpressP21279.
BgeeP21279.
GenevestigatorP21279.

Family and domain databases

Gene3D1.10.400.10. 1 hit.
3.40.50.300. 2 hits.
InterProIPR000654. Gprotein_alpha_Q.
IPR001019. Gprotein_alpha_su.
IPR011025. GproteinA_insert.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERPTHR10218. PTHR10218. 1 hit.
PfamPF00503. G-alpha. 1 hit.
[Graphical view]
PRINTSPR00318. GPROTEINA.
PR00442. GPROTEINAQ.
SMARTSM00275. G_alpha. 1 hit.
[Graphical view]
SUPFAMSSF47895. SSF47895. 1 hit.
SSF52540. SSF52540. 2 hits.
ProtoNetSearch...

Other

EvolutionaryTraceP21279.
NextBio286596.
PROP21279.
SOURCESearch...

Entry information

Entry nameGNAQ_MOUSE
AccessionPrimary (citable) accession number: P21279
Secondary accession number(s): Q6PFF5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: July 7, 2009
Last modified: July 9, 2014
This is version 155 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot