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Protein

Guanine nucleotide-binding protein G(q) subunit alpha

Gene

Gnaq

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi53 – 531MagnesiumBy similarity
Metal bindingi186 – 1861MagnesiumBy similarity
Binding sitei331 – 3311GTP; via amide nitrogenBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi46 – 538GTPBy similarity
Nucleotide bindingi180 – 1867GTPBy similarity
Nucleotide bindingi205 – 2095GTPBy similarity
Nucleotide bindingi274 – 2774GTPBy similarity

GO - Molecular functioni

  1. G-protein beta/gamma-subunit complex binding Source: GO_Central
  2. GTPase activator activity Source: MGI
  3. GTPase activity Source: GO_Central
  4. GTP binding Source: UniProtKB-KW
  5. metal ion binding Source: UniProtKB-KW
  6. signal transducer activity Source: GO_Central
  7. type 2A serotonin receptor binding Source: GO_Central

GO - Biological processi

  1. action potential Source: MGI
  2. adenylate cyclase-activating G-protein coupled receptor signaling pathway Source: MGI
  3. developmental pigmentation Source: MGI
  4. embryonic digit morphogenesis Source: MGI
  5. forebrain neuron development Source: MGI
  6. glutamate receptor signaling pathway Source: MGI
  7. G-protein coupled receptor signaling pathway Source: MGI
  8. heart development Source: MGI
  9. maternal behavior Source: MGI
  10. negative regulation of protein kinase activity Source: MGI
  11. neuron remodeling Source: MGI
  12. phospholipase C-activating dopamine receptor signaling pathway Source: MGI
  13. positive regulation of GTPase activity Source: MGI
  14. post-embryonic development Source: MGI
  15. protein stabilization Source: MGI
  16. regulation of catenin import into nucleus Source: MGI
  17. regulation of melanocyte differentiation Source: MGI
  18. skeletal system development Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Transducer

Keywords - Ligandi

GTP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_207651. G alpha (q) signalling events.
REACT_220322. Thrombin signalling through proteinase activated receptors (PARs).
REACT_233922. Thromboxane signalling through TP receptor.
REACT_247495. Acetylcholine regulates insulin secretion.
REACT_250548. Platelet sensitization by LDL.
REACT_258788. Fatty Acids bound to GPR40 (FFAR1) regulate insulin secretion.
REACT_259068. ADP signalling through P2Y purinoceptor 1.

Names & Taxonomyi

Protein namesi
Recommended name:
Guanine nucleotide-binding protein G(q) subunit alpha
Alternative name(s):
Guanine nucleotide-binding protein alpha-q
Gene namesi
Name:Gnaq
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 19

Organism-specific databases

MGIiMGI:95776. Gnaq.

Subcellular locationi

Nucleus 1 Publication. Membrane 1 Publication. Nucleus membrane 1 Publication
Note: Colocalizes with the adrenergic receptors, ADREN1A and ADREN1B, at the nuclear membrane of cardiac myocytes.

GO - Cellular componenti

  1. extracellular vesicular exosome Source: MGI
  2. heterotrimeric G-protein complex Source: GO_Central
  3. lysosomal membrane Source: MGI
  4. membrane Source: MGI
  5. nuclear membrane Source: UniProtKB-SubCell
  6. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi9 – 91C → S: Abolishes palmitoylation. 1 Publication
Mutagenesisi10 – 101C → S: Abolishes palmitoylation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 359359Guanine nucleotide-binding protein G(q) subunit alphaPRO_0000203761Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi9 – 91S-palmitoyl cysteine1 Publication
Lipidationi10 – 101S-palmitoyl cysteine1 Publication

Keywords - PTMi

Lipoprotein, Palmitate

Proteomic databases

MaxQBiP21279.
PaxDbiP21279.
PRIDEiP21279.

PTM databases

PhosphoSiteiP21279.

Expressioni

Gene expression databases

BgeeiP21279.
ExpressionAtlasiP21279. baseline and differential.
GenevestigatoriP21279.

Interactioni

Subunit structurei

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).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
AipO089152EBI-771975,EBI-6935014

Protein-protein interaction databases

BioGridi199971. 2 interactions.
DIPiDIP-606N.
IntActiP21279. 5 interactions.
MINTiMINT-4096294.

Structurei

Secondary structure

1
359
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi39 – 457Combined sources
Beta strandi47 – 515Combined sources
Helixi52 – 6312Combined sources
Helixi69 – 735Combined sources
Helixi76 – 9621Combined sources
Helixi105 – 11410Combined sources
Helixi118 – 1203Combined sources
Helixi128 – 1369Combined sources
Helixi139 – 1468Combined sources
Helixi147 – 1504Combined sources
Helixi157 – 1615Combined sources
Helixi164 – 1685Combined sources
Helixi176 – 1794Combined sources
Beta strandi188 – 1969Combined sources
Beta strandi199 – 2068Combined sources
Helixi210 – 2134Combined sources
Helixi214 – 2196Combined sources
Beta strandi224 – 2318Combined sources
Helixi232 – 2365Combined sources
Beta strandi242 – 2443Combined sources
Helixi247 – 25913Combined sources
Helixi262 – 2643Combined sources
Beta strandi268 – 2747Combined sources
Helixi276 – 2827Combined sources
Turni283 – 2853Combined sources
Helixi288 – 2903Combined sources
Helixi302 – 31413Combined sources
Turni318 – 3214Combined sources
Beta strandi324 – 3285Combined sources
Helixi334 – 35017Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
4QJ3X-ray3.00A7-359[»]
4QJ4X-ray3.30A7-359[»]
4QJ5X-ray3.41A7-359[»]
ProteinModelPortaliP21279.
SMRiP21279. Positions 18-354.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP21279.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiNOG322962.
HOGENOMiHOG000038729.
HOVERGENiHBG063184.
InParanoidiP21279.
KOiK04634.
OMAiGDQSEEL.
OrthoDBiEOG7ZWD1W.
PhylomeDBiP21279.
TreeFamiTF300673.

Family and domain databases

Gene3Di1.10.400.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR000654. Gprotein_alpha_Q.
IPR001019. Gprotein_alpha_su.
IPR011025. GproteinA_insert.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR10218. PTHR10218. 1 hit.
PfamiPF00503. G-alpha. 1 hit.
[Graphical view]
PRINTSiPR00318. GPROTEINA.
PR00442. GPROTEINAQ.
SMARTiSM00275. G_alpha. 1 hit.
[Graphical view]
SUPFAMiSSF47895. SSF47895. 1 hit.
SSF52540. SSF52540. 2 hits.

Sequencei

Sequence statusi: Complete.

P21279-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTLESIMACC LSEEAKEARR INDEIERQLR RDKRDARREL KLLLLGTGES
60 70 80 90 100
GKSTFIKQMR IIHGSGYSDE DKRGFTKLVY QNIFTAMQAM IRAMDTLKIP
110 120 130 140 150
YKYEHNKAHA QLVREVDVEK VSAFENPYVD AIKSLWNDPG IQECYDRRRE
160 170 180 190 200
YQLSDSTKYY LNDLDRVADP SYLPTQQDVL RVRVPTTGII EYPFDLQSVI
210 220 230 240 250
FRMVDVGGQR SERRKWIHCF ENVTSIMFLV ALSEYDQVLV ESDNENRMEE
260 270 280 290 300
SKALFRTIIT YPWFQNSSVI LFLNKKDLLE EKIMYSHLVD YFPEYDGPQR
310 320 330 340 350
DAQAAREFIL KMFVDLNPDS DKIIYSHFTC ATDTENIRFV FAAVKDTILQ

LNLKEYNLV
Length:359
Mass (Da):42,158
Last modified:July 7, 2009 - v4
Checksum:i3BCBA4EE7DADADBF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti28 – 292QL → HV in AAA63306. (PubMed:2123549)Curated
Sequence conflicti62 – 621Missing in AAH57583. (PubMed:15489334)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M55412 mRNA. Translation: AAA63306.1.
BC057583 mRNA. Translation: AAH57583.1.
CCDSiCCDS29684.1.
PIRiA38414. RGMSQ.
RefSeqiNP_032165.3. NM_008139.5.
UniGeneiMm.439701.
Mm.441601.

Genome annotation databases

EnsembliENSMUST00000025541; ENSMUSP00000025541; ENSMUSG00000024639.
GeneIDi14682.
KEGGimmu:14682.
UCSCiuc008gwt.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M55412 mRNA. Translation: AAA63306.1.
BC057583 mRNA. Translation: AAH57583.1.
CCDSiCCDS29684.1.
PIRiA38414. RGMSQ.
RefSeqiNP_032165.3. NM_008139.5.
UniGeneiMm.439701.
Mm.441601.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
4QJ3X-ray3.00A7-359[»]
4QJ4X-ray3.30A7-359[»]
4QJ5X-ray3.41A7-359[»]
ProteinModelPortaliP21279.
SMRiP21279. Positions 18-354.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199971. 2 interactions.
DIPiDIP-606N.
IntActiP21279. 5 interactions.
MINTiMINT-4096294.

PTM databases

PhosphoSiteiP21279.

Proteomic databases

MaxQBiP21279.
PaxDbiP21279.
PRIDEiP21279.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000025541; ENSMUSP00000025541; ENSMUSG00000024639.
GeneIDi14682.
KEGGimmu:14682.
UCSCiuc008gwt.1. mouse.

Organism-specific databases

CTDi2776.
MGIiMGI:95776. Gnaq.

Phylogenomic databases

eggNOGiNOG322962.
HOGENOMiHOG000038729.
HOVERGENiHBG063184.
InParanoidiP21279.
KOiK04634.
OMAiGDQSEEL.
OrthoDBiEOG7ZWD1W.
PhylomeDBiP21279.
TreeFamiTF300673.

Enzyme and pathway databases

ReactomeiREACT_207651. G alpha (q) signalling events.
REACT_220322. Thrombin signalling through proteinase activated receptors (PARs).
REACT_233922. Thromboxane signalling through TP receptor.
REACT_247495. Acetylcholine regulates insulin secretion.
REACT_250548. Platelet sensitization by LDL.
REACT_258788. Fatty Acids bound to GPR40 (FFAR1) regulate insulin secretion.
REACT_259068. ADP signalling through P2Y purinoceptor 1.

Miscellaneous databases

ChiTaRSiGnaq. mouse.
EvolutionaryTraceiP21279.
NextBioi286596.
PROiP21279.
SOURCEiSearch...

Gene expression databases

BgeeiP21279.
ExpressionAtlasiP21279. baseline and differential.
GenevestigatoriP21279.

Family and domain databases

Gene3Di1.10.400.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR000654. Gprotein_alpha_Q.
IPR001019. Gprotein_alpha_su.
IPR011025. GproteinA_insert.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR10218. PTHR10218. 1 hit.
PfamiPF00503. G-alpha. 1 hit.
[Graphical view]
PRINTSiPR00318. GPROTEINA.
PR00442. GPROTEINAQ.
SMARTiSM00275. G_alpha. 1 hit.
[Graphical view]
SUPFAMiSSF47895. SSF47895. 1 hit.
SSF52540. SSF52540. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: FUNCTION.

Entry informationi

Entry nameiGNAQ_MOUSE
AccessioniPrimary (citable) accession number: P21279
Secondary accession number(s): Q6PFF5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: July 7, 2009
Last modified: February 4, 2015
This is version 161 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.