GNAQ_XENLA
ID GNAQ_XENLA Reviewed; 359 AA.
AC P38410;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Guanine nucleotide-binding protein G(q) subunit alpha;
DE AltName: Full=Guanine nucleotide-binding protein alpha-q;
GN Name=gnaq;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Ladner K.J., Smith L.D.;
RT "Isolation of the Xenopus cDNA for G alpha q.";
RL Submitted (NOV-1992) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Oocyte;
RX PubMed=8026589; DOI=10.1016/0014-5793(94)00570-2;
RA Shapira H., Way J., Lipinsky D., Oron Y., Battey J.F.;
RT "Neuromedin B receptor, expressed in Xenopus laevis oocytes, selectively
RT couples to G alpha q and not G alpha 11.";
RL FEBS Lett. 348:89-92(1994).
RN [3]
RP ERRATUM OF PUBMED:8026589.
RA Shapira H., Way J., Lipinsky D., Oron Y., Battey J.F.;
RL FEBS Lett. 349:318-318(1994).
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC as modulators or transducers in various transmembrane signaling
CC systems. {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.
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}.
CC -!- PTM: Palmitoylated. Palmitoylation occurs in the Golgi and participates
CC in the localization of GNAQ to the plasma membrane.
CC {ECO:0000250|UniProtKB:P21279}.
CC -!- SIMILARITY: Belongs to the G-alpha family. G(q) subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L05540; AAA49730.1; -; mRNA.
DR EMBL; U10502; AAA52189.1; -; mRNA.
DR PIR; S45699; S45699.
DR RefSeq; NP_001081163.1; NM_001087694.1.
DR RefSeq; NP_001084029.1; NM_001090560.1.
DR AlphaFoldDB; P38410; -.
DR SMR; P38410; -.
DR PRIDE; P38410; -.
DR DNASU; 394425; -.
DR GeneID; 394425; -.
DR GeneID; 399261; -.
DR KEGG; xla:394425; -.
DR KEGG; xla:399261; -.
DR CTD; 394425; -.
DR CTD; 399261; -.
DR Xenbase; XB-GENE-973438; gnaq.L.
DR Xenbase; XB-GENE-6254188; gnaq.S.
DR OrthoDB; 754573at2759; -.
DR Proteomes; UP000186698; Chromosome 1L.
DR Proteomes; UP000186698; Chromosome 1S.
DR Bgee; 394425; Expressed in brain and 19 other tissues.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
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:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IEA:InterPro.
DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0007603; P:phototransduction, visible light; ISS:AgBase.
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_0000203763"
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 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 16
FT /note="E -> K (in Ref. 2; AAA52189)"
FT /evidence="ECO:0000305"
FT CONFLICT 85
FT /note="S -> T (in Ref. 2; AAA52189)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="L -> V (in Ref. 2; AAA52189)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="H -> Q (in Ref. 2; AAA52189)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 359 AA; 42216 MW; AB0AAED5B43372D8 CRC64;
MTLESIMACC LSEEAEEARR INDEIERQLR RDKRDARREL KLLLLGTGES GKSTFIKQMR
IIHGSGYSDE DKRGFTKLVY QNIFSAMQAM IRAMETLKIP YKYEHNKGHA LLVREVDVEK
VASFENPYVD AIKYLWNDPG IQECYDRRRE YQLSDSTKYY LNDLDRIATH GYLPTQQDVL
RVRVPTTGII EYPFDLQSVI FRMVDVGGQR SERRKWIHCF ENVTSIMFLV ALSEYDQVLV
ESDNENRMEE SKALFRTIIT YPWFQNSSVI LFLNKKDLLE EKIMYSHLVD YFPEYDGPQR
DAQAAREFIL KMFVDLNPDS DKIIYSHFTC ATDTENIRFV FAAVKDTILQ LNLKEYNLV
