GNAQ_CANLF
ID GNAQ_CANLF Reviewed; 359 AA.
AC Q28294;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Guanine nucleotide-binding protein G(q) subunit alpha;
DE AltName: Full=Guanine nucleotide-binding protein alpha-q;
GN Name=GNAQ;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8836152; DOI=10.1042/bj3181023;
RA Johnson G.J., Leis L.A., Dunlop P.C.;
RT "Specificity of G alpha q and G alpha 11 gene expression in platelets and
RT erythrocytes. Expressions of cellular differentiation and species
RT differences.";
RL Biochem. J. 318:1023-1031(1996).
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC as modulators or transducers in various transmembrane signaling
CC systems. Required for platelet activation. Regulates B-cell selection
CC and survival and is required to prevent B-cell-dependent autoimmunity.
CC Regulates chemotaxis of BM-derived neutrophils and dendritic cells (in
CC vitro) (By similarity). Transduces FFAR4 signaling in response to long-
CC chain fatty acids (LCFAs) (By similarity). Together with GNA11,
CC required for heart development (By similarity).
CC {ECO:0000250|UniProtKB:P21279, ECO:0000250|UniProtKB:P50148}.
CC -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma. The
CC alpha chain contains the guanine nucleotide binding site. Binds
CC SLC9A3R1. Forms a complex with PECAM1 and BDKRB2. Interacts with PECAM1
CC (By similarity). Interacts with GAS2L2 (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P50148}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P50148};
CC Lipid-anchor {ECO:0000250|UniProtKB:P50148}. Golgi apparatus
CC {ECO:0000250|UniProtKB:P50148}. Nucleus {ECO:0000250|UniProtKB:P21279}.
CC Nucleus membrane {ECO:0000250|UniProtKB:P21279}. Note=Colocalizes with
CC the adrenergic receptors, ADREN1A and ADREN1B, at the nuclear membrane
CC of cardiac myocytes. {ECO:0000250|UniProtKB:P21279}.
CC -!- PTM: Palmitoylated by ZDHHC3 and ZDHHC7. Palmitoylation occurs in the
CC Golgi and participates in the localization of GNAQ to the plasma
CC membrane. {ECO:0000250|UniProtKB:P21279}.
CC -!- PTM: Histaminylated at Gln-209 residues by TGM2.
CC {ECO:0000250|UniProtKB:P21279}.
CC -!- SIMILARITY: Belongs to the G-alpha family. G(q) subfamily.
CC {ECO:0000305}.
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DR EMBL; L76257; AAB05548.1; -; mRNA.
DR RefSeq; NP_001003249.1; NM_001003249.1.
DR AlphaFoldDB; Q28294; -.
DR SMR; Q28294; -.
DR STRING; 9612.ENSCAFP00000028446; -.
DR PaxDb; Q28294; -.
DR Ensembl; ENSCAFT00030003901; ENSCAFP00030003462; ENSCAFG00030002067.
DR Ensembl; ENSCAFT00040005026; ENSCAFP00040004320; ENSCAFG00040002598.
DR GeneID; 403928; -.
DR KEGG; cfa:403928; -.
DR CTD; 2776; -.
DR eggNOG; KOG0085; Eukaryota.
DR InParanoid; Q28294; -.
DR OrthoDB; 754573at2759; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; ISS:AgBase.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001750; C:photoreceptor outer segment; ISS:AgBase.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IBA:GO_Central.
DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0001508; P:action potential; IBA:GO_Central.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0009649; P:entrainment of circadian clock; ISS:AgBase.
DR GO; GO:0007213; P:G protein-coupled acetylcholine receptor signaling pathway; ISS:AgBase.
DR GO; GO:0007215; P:glutamate receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007603; P:phototransduction, visible light; ISS:AgBase.
DR GO; GO:0010543; P:regulation of platelet activation; ISS:UniProtKB.
DR CDD; cd00066; G-alpha; 1.
DR Gene3D; 1.10.400.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR000654; Gprotein_alpha_Q.
DR InterPro; IPR001019; Gprotein_alpha_su.
DR InterPro; IPR011025; GproteinA_insert.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10218; PTHR10218; 1.
DR Pfam; PF00503; G-alpha; 1.
DR PRINTS; PR00318; GPROTEINA.
DR PRINTS; PR00442; GPROTEINAQ.
DR SMART; SM00275; G_alpha; 1.
DR SUPFAM; SSF47895; SSF47895; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51882; G_ALPHA; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Golgi apparatus; GTP-binding; Lipoprotein; Magnesium;
KW Membrane; Metal-binding; Nucleotide-binding; Nucleus; Palmitate;
KW Reference proteome; Transducer.
FT CHAIN 1..359
FT /note="Guanine nucleotide-binding protein G(q) subunit
FT alpha"
FT /id="PRO_0000203759"
FT DOMAIN 38..359
FT /note="G-alpha"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 41..54
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 178..186
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 201..210
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 270..277
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 329..334
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT BINDING 46..53
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P29992"
FT BINDING 53
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P27600"
FT BINDING 180..183
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P27600"
FT BINDING 186
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P27600"
FT BINDING 274..277
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P27600"
FT BINDING 331
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P27600"
FT MOD_RES 209
FT /note="5-glutamyl histamine"
FT /evidence="ECO:0000250|UniProtKB:P21279"
FT LIPID 9
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P21279"
FT LIPID 10
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P21279"
SQ SEQUENCE 359 AA; 42142 MW; 6F69C4F617DFA7C7 CRC64;
MTLESIMACC LSEEAKEARR INDEIERQLR RDKRDARREL KLLLLGTGES GKSTFIKQMR
IIHGSGYSDE DKRGFTKLVY QNIFTAMQAM IRAMDTLKIP YKYEHNKAHA QLVREVDVEK
VSAFENPYVD AIKSLWNDPG IQECYDRRRE YQLSDSTKYY LNDLDRVADP AYLPTQQDVL
RVRVPTTGII EYPFDLQSVI FRMVDVGGQR SERRKWIHCF ENVTSIMFLV ALSEYDQVLV
ESDNENRMEE SKALFRTIIT YPWFQNSSVI LFLNKKDLLE EKIMYSHLVD YFPEYDGPQR
DAQAAREFIL KMFVDLNPDS DKIIYSHFTC ATDTENIRFV FAAVKDTILQ LNLKEYNLV
