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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)DescriptionActionsGraphical viewLength
Metal bindingi53MagnesiumBy similarity1
Metal bindingi186MagnesiumBy similarity1
Binding sitei331GTP; via amide nitrogenBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi46 – 53GTPBy similarity8
Nucleotide bindingi180 – 186GTPBy similarity7
Nucleotide bindingi205 – 209GTPBy similarity5
Nucleotide bindingi274 – 277GTPBy similarity4

GO - Molecular functioni

GO - Biological processi

  • action potential Source: MGI
  • adenylate cyclase-activating G-protein coupled receptor signaling pathway Source: MGI
  • developmental pigmentation Source: MGI
  • embryonic digit morphogenesis Source: MGI
  • forebrain neuron development Source: MGI
  • glutamate receptor signaling pathway Source: MGI
  • G-protein coupled receptor signaling pathway Source: MGI
  • heart development Source: MGI
  • maternal behavior Source: MGI
  • negative regulation of protein kinase activity Source: MGI
  • neuron remodeling Source: MGI
  • phospholipase C-activating dopamine receptor signaling pathway Source: MGI
  • post-embryonic development Source: MGI
  • protein heterotrimerization Source: MGI
  • protein stabilization Source: MGI
  • regulation of catenin import into nucleus Source: MGI
  • regulation of insulin secretion Source: Reactome
  • regulation of melanocyte differentiation Source: MGI
  • 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

ReactomeiR-MMU-399997. Acetylcholine regulates insulin secretion.
R-MMU-416476. G alpha (q) signalling events.
R-MMU-418592. ADP signalling through P2Y purinoceptor 1.
R-MMU-428930. Thromboxane signalling through TP receptor.
R-MMU-432142. Platelet sensitization by LDL.
R-MMU-434316. Fatty Acids bound to GPR40 (FFAR1) regulate insulin secretion.
R-MMU-456926. Thrombin signalling through proteinase activated receptors (PARs).

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
Proteomesi
  • UP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:95776. Gnaq.

Subcellular locationi

GO - Cellular componenti

  • cell body Source: MGI
  • dendrite Source: MGI
  • extracellular exosome Source: MGI
  • heterotrimeric G-protein complex Source: MGI
  • lysosomal membrane Source: MGI
  • membrane Source: MGI
  • nuclear membrane Source: UniProtKB-SubCell
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi9C → S: Abolishes palmitoylation. 1 Publication1
Mutagenesisi10C → S: Abolishes palmitoylation. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002037611 – 359Guanine nucleotide-binding protein G(q) subunit alphaAdd BLAST359

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi9S-palmitoyl cysteine1 Publication1
Lipidationi10S-palmitoyl cysteine1 Publication1

Keywords - PTMi

Lipoprotein, Palmitate

Proteomic databases

EPDiP21279.
PaxDbiP21279.
PeptideAtlasiP21279.
PRIDEiP21279.

PTM databases

iPTMnetiP21279.
PhosphoSitePlusiP21279.
SwissPalmiP21279.

Expressioni

Gene expression databases

BgeeiENSMUSG00000024639.
ExpressionAtlasiP21279. baseline and differential.
GenevisibleiP21279. MM.

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

GO - Molecular functioni

Protein-protein interaction databases

BioGridi199971. 2 interactors.
DIPiDIP-606N.
IntActiP21279. 5 interactors.
MINTiMINT-4096294.
STRINGi10090.ENSMUSP00000025541.

Structurei

Secondary structure

1359
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi39 – 45Combined sources7
Beta strandi47 – 51Combined sources5
Helixi52 – 63Combined sources12
Helixi69 – 73Combined sources5
Helixi76 – 96Combined sources21
Helixi105 – 114Combined sources10
Helixi118 – 120Combined sources3
Helixi128 – 136Combined sources9
Helixi139 – 146Combined sources8
Helixi147 – 150Combined sources4
Helixi157 – 161Combined sources5
Helixi164 – 168Combined sources5
Helixi176 – 181Combined sources6
Beta strandi188 – 195Combined sources8
Beta strandi197 – 206Combined sources10
Helixi210 – 213Combined sources4
Helixi214 – 219Combined sources6
Beta strandi224 – 231Combined sources8
Helixi232 – 236Combined sources5
Beta strandi240 – 244Combined sources5
Helixi247 – 260Combined sources14
Helixi262 – 264Combined sources3
Beta strandi267 – 274Combined sources8
Helixi276 – 282Combined sources7
Turni283 – 285Combined sources3
Helixi288 – 290Combined sources3
Helixi302 – 314Combined sources13
Turni318 – 321Combined sources4
Beta strandi324 – 328Combined sources5
Helixi334 – 346Combined sources13
Turni347 – 349Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5DO9X-ray2.60A/C/E37-350[»]
ProteinModelPortaliP21279.
SMRiP21279.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP21279.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG0085. Eukaryota.
ENOG410XNVQ. LUCA.
GeneTreeiENSGT00760000118851.
HOGENOMiHOG000038729.
HOVERGENiHBG063184.
InParanoidiP21279.
KOiK04634.
OMAiFIKELWE.
OrthoDBiEOG091G0VUT.
PhylomeDBiP21279.
TreeFamiTF300673.

Family and domain databases

CDDicd00066. G-alpha. 1 hit.
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)DescriptionActionsGraphical viewLength
Sequence conflicti28 – 29QL → HV in AAA63306 (PubMed:2123549).Curated2
Sequence conflicti62Missing in AAH57583 (PubMed:15489334).Curated1

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
PDB 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[»]
5DO9X-ray2.60A/C/E37-350[»]
ProteinModelPortaliP21279.
SMRiP21279.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199971. 2 interactors.
DIPiDIP-606N.
IntActiP21279. 5 interactors.
MINTiMINT-4096294.
STRINGi10090.ENSMUSP00000025541.

PTM databases

iPTMnetiP21279.
PhosphoSitePlusiP21279.
SwissPalmiP21279.

Proteomic databases

EPDiP21279.
PaxDbiP21279.
PeptideAtlasiP21279.
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

eggNOGiKOG0085. Eukaryota.
ENOG410XNVQ. LUCA.
GeneTreeiENSGT00760000118851.
HOGENOMiHOG000038729.
HOVERGENiHBG063184.
InParanoidiP21279.
KOiK04634.
OMAiFIKELWE.
OrthoDBiEOG091G0VUT.
PhylomeDBiP21279.
TreeFamiTF300673.

Enzyme and pathway databases

ReactomeiR-MMU-399997. Acetylcholine regulates insulin secretion.
R-MMU-416476. G alpha (q) signalling events.
R-MMU-418592. ADP signalling through P2Y purinoceptor 1.
R-MMU-428930. Thromboxane signalling through TP receptor.
R-MMU-432142. Platelet sensitization by LDL.
R-MMU-434316. Fatty Acids bound to GPR40 (FFAR1) regulate insulin secretion.
R-MMU-456926. Thrombin signalling through proteinase activated receptors (PARs).

Miscellaneous databases

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

Gene expression databases

BgeeiENSMUSG00000024639.
ExpressionAtlasiP21279. baseline and differential.
GenevisibleiP21279. MM.

Family and domain databases

CDDicd00066. G-alpha. 1 hit.
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...

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: November 30, 2016
This is version 181 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

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 one 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.