GNAQ_RAT
ID GNAQ_RAT Reviewed; 359 AA.
AC P82471;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Guanine nucleotide-binding protein G(q) subunit alpha;
DE AltName: Full=Guanine nucleotide-binding protein alpha-q;
GN Name=Gnaq;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Strotmann R.;
RT "Rat G alpha q subunit.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 80-235.
RC TISSUE=Brain cortex;
RX PubMed=1333286; DOI=10.1016/0006-3223(92)90070-g;
RA Lesch K.-P., Manji H.K.;
RT "Signal-transducing G proteins and antidepressant drugs: evidence for
RT modulation of alpha subunit gene expression in rat brain.";
RL Biol. Psychiatry 32:549-579(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 244-337.
RC STRAIN=Sprague-Dawley; TISSUE=Kidney cortex;
RA Thomas C.P.;
RT "GTP-binding protein expression in glomerular mesangial cells.";
RL Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases.
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; AF234260; AAF59930.1; -; mRNA.
DR EMBL; L37294; AAB02848.1; -; mRNA.
DR RefSeq; NP_112298.1; NM_031036.1.
DR AlphaFoldDB; P82471; -.
DR SMR; P82471; -.
DR BioGRID; 249565; 4.
DR CORUM; P82471; -.
DR IntAct; P82471; 1.
DR MINT; P82471; -.
DR STRING; 10116.ENSRNOP00000019174; -.
DR iPTMnet; P82471; -.
DR PhosphoSitePlus; P82471; -.
DR SwissPalm; P82471; -.
DR World-2DPAGE; 0004:P82471; -.
DR jPOST; P82471; -.
DR PaxDb; P82471; -.
DR PRIDE; P82471; -.
DR GeneID; 81666; -.
DR KEGG; rno:81666; -.
DR UCSC; RGD:620770; rat.
DR CTD; 2776; -.
DR RGD; 620770; Gnaq.
DR eggNOG; KOG0085; Eukaryota.
DR InParanoid; P82471; -.
DR OrthoDB; 754573at2759; -.
DR PhylomeDB; P82471; -.
DR Reactome; R-RNO-112043; PLC beta mediated events.
DR Reactome; R-RNO-202040; G-protein activation.
DR Reactome; R-RNO-399997; Acetylcholine regulates insulin secretion.
DR Reactome; R-RNO-416476; G alpha (q) signalling events.
DR Reactome; R-RNO-418592; ADP signalling through P2Y purinoceptor 1.
DR Reactome; R-RNO-428930; Thromboxane signalling through TP receptor.
DR Reactome; R-RNO-434316; Fatty Acids bound to GPR40 (FFAR1) regulate insulin secretion.
DR Reactome; R-RNO-456926; Thrombin signalling through proteinase activated receptors (PARs).
DR PRO; PR:P82471; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005901; C:caveola; IDA:RGD.
DR GO; GO:0044297; C:cell body; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0030425; C:dendrite; ISO:RGD.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IDA:MGI.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0045202; C:synapse; IDA:RGD.
DR GO; GO:0047391; F:alkylglycerophosphoethanolamine phosphodiesterase activity; IDA:MGI.
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; ISO:RGD.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0001508; P:action potential; ISO:RGD.
DR GO; GO:0007202; P:activation of phospholipase C activity; IMP:RGD.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; ISO:RGD.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:1904888; P:cranial skeletal system development; ISO:RGD.
DR GO; GO:0048066; P:developmental pigmentation; ISO:RGD.
DR GO; GO:0042733; P:embryonic digit morphogenesis; ISO:RGD.
DR GO; GO:0086100; P:endothelin receptor signaling pathway; ISO:RGD.
DR GO; GO:0021884; P:forebrain neuron development; ISO:RGD.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:RGD.
DR GO; GO:0007215; P:glutamate receptor signaling pathway; ISO:RGD.
DR GO; GO:0007507; P:heart development; ISO:RGD.
DR GO; GO:0042711; P:maternal behavior; ISO:RGD.
DR GO; GO:0010259; P:multicellular organism aging; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
DR GO; GO:0043267; P:negative regulation of potassium ion transport; IMP:RGD.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; ISO:RGD.
DR GO; GO:0016322; P:neuron remodeling; ISO:RGD.
DR GO; GO:0060158; P:phospholipase C-activating dopamine receptor signaling pathway; ISO:RGD.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IMP:RGD.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IMP:RGD.
DR GO; GO:0009791; P:post-embryonic development; ISO:RGD.
DR GO; GO:0050821; P:protein stabilization; ISO:RGD.
DR GO; GO:0008217; P:regulation of blood pressure; ISO:RGD.
DR GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; ISO:RGD.
DR GO; GO:0045634; P:regulation of melanocyte differentiation; ISO:RGD.
DR GO; GO:0010543; P:regulation of platelet activation; ISS:UniProtKB.
DR GO; GO:0001501; P:skeletal system development; ISO:RGD.
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_0000203762"
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"
FT CONFLICT 91
FT /note="V -> I (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 359 AA; 42144 MW; 33569BEE7BFF42BF CRC64;
MTLESIMACC LSEEAKEARR INDEIERQLR RDKRDARREL KLLLLGTGES GKSTFIKQMR
IIHGSGYSDE DKRGFTKLVY QNIFTAMQAM VRAMDTLKIP YKYEHNKAHA QLVREVDVEK
VSAFENPYVD AIKSLWNDPG IQECYDRRRE YQLSDSTKYY LNDLDRVADP SYLPTQQDVL
RVRVPTTGII EYPFDLQSVI FRMVDVGGQR SERRKWIHCF ENVTSIMFLV ALSEYDQVLV
ESDNENRMEE SKALFRTIIT YPWFQNSSVI LFLNKKDLLE EKIMYSHLVD YFPEYDGPQR
DAQAAREFIL KMFVDLNPDS DKIIYSHFTC ATDTENIRFV FAAVKDTILQ LNLKEYNLV
