Guanine nucleotide-binding protein G(q) subunit alpha

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P21279 (GNAQ_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 143. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Guanine nucleotide-binding protein G(q) subunit alpha

Alternative name(s):
Guanine nucleotide-binding protein alpha-q

Gene names

Name:

Gnaq

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	359 AA.
Sequence status	Complete.
Protein existence	Evidence 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 component	Membrane Nucleus
Ligand	GTP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Transducer
PTM	Lipoprotein Palmitate
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	adenylate cyclase-activating G-protein coupled receptor signaling pathway Inferred from direct assay PubMed 10481072. Source: MGI behavior Inferred from mutant phenotype PubMed 15340067. 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 negative regulation of protein kinase activity Inferred from electronic annotation. Source: Compara 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: Compara regulation of action potential Inferred from mutant phenotype PubMed 10818132. Source: MGI regulation of catenin import into nucleus Inferred from electronic annotation. Source: Compara regulation of melanocyte differentiation Inferred from mutant phenotype PubMed 15322542. Source: MGI skeletal system development Inferred from mutant phenotype PubMed 9687499. Source: MGI
Cellular_component	heterotrimeric G-protein complex Inferred from Biological aspect of Ancestor. Source: RefGenome nuclear membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	G-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 signal transducer activity Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 359

359

Guanine nucleotide-binding protein G(q) subunit alpha

PRO_0000203761

Regions

Nucleotide binding

46 – 53

GTP By similarity

Nucleotide binding

180 – 186

GTP By similarity

Nucleotide binding

205 – 209

GTP By similarity

Nucleotide binding

274 – 277

GTP By similarity

Sites

Metal binding

Magnesium By similarity

Metal binding

186

Magnesium By similarity

Binding site

331

GTP; via amide nitrogen By similarity

Amino acid modifications

Lipidation

S-palmitoyl cysteine Ref.4

Lipidation

S-palmitoyl cysteine Ref.4

Experimental info

Mutagenesis

C → S: Abolishes palmitoylation. Ref.4

Mutagenesis

C → S: Abolishes palmitoylation. Ref.4

Sequence conflict

28 – 29

QL → HV in AAA63306. Ref.1

Sequence conflict

Missing in AAH57583. Ref.2

Secondary structure

359

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P21279 [UniParc].

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

359

42,158

        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' referencesShow '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, 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.

IPI

IPI00228618.

PIR

RGMSQ. A38414.

RefSeq

NP_032165.3. NM_008139.5.

UniGene

Mm.439701.
Mm.441601.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2BCJ	X-ray	3.06	Q	37-353	[»]
2RGN	X-ray	3.50	A/D	37-359	[»]
3AH8	X-ray	2.90	A	37-359	[»]
3OHM	X-ray	2.70	A	35-359	[»]
4EKC	X-ray	7.40	A/C	18-359	[»]
4EKD	X-ray	2.71	A	18-359	[»]
4GNK	X-ray	4.00	A/C	7-359	[»]

ProteinModelPortal

P21279.

SMR

P21279. Positions 37-354.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-606N.

IntAct

P21279. 2 interactions.

PTM databases

PhosphoSite

P21279.

Proteomic databases

PaxDb

P21279.

PRIDE

P21279.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000025541; ENSMUSP00000025541; ENSMUSG00000024639.

GeneID

14682.

KEGG

mmu:14682.

Organism-specific databases

CTD

2776.

MGI

MGI:95776. Gnaq.

Phylogenomic databases

eggNOG

NOG322962.

HOGENOM

HOG000038729.

HOVERGEN

HBG063184.

InParanoid

P21279.

K04634.

OMA

SPYVDAI.

OrthoDB

EOG4S4PGD.

Enzyme and pathway databases

Reactome

REACT_112621. Metabolism.

Gene expression databases

ArrayExpress

P21279.

Bgee

P21279.

Genevestigator

P21279.

GermOnline

ENSMUSG00000024639. Mus musculus.

Family and domain databases

Gene3D

1.10.400.10. 1 hit.

InterPro

IPR000654. Gprotein_alpha_Q.
IPR001019. Gprotein_alpha_su.
IPR011025. GproteinA_insert.
[Graphical view]

PANTHER

PTHR10218. PTHR10218. 1 hit.

Pfam

PF00503. G-alpha. 1 hit.
[Graphical view]

PRINTS

PR00318. GPROTEINA.
PR00442. GPROTEINAQ.

SMART

SM00275. G_alpha. 1 hit.
[Graphical view]

SUPFAM

SSF47895. Transducn_insert. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P21279.

NextBio

286596.

SOURCE

Search...

Entry information

Entry name

GNAQ_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 143 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents