ID   GNAQ_MIZYE              Reviewed;         353 AA.
AC   O15975;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Guanine nucleotide-binding protein G(q) subunit alpha;
DE   AltName: Full=Guanine nucleotide-binding protein alpha-q;
GN   Name=SCGQA;
OS   Mizuhopecten yessoensis (Japanese scallop) (Patinopecten yessoensis).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC   Autobranchia; Pteriomorphia; Pectinida; Pectinoidea; Pectinidae;
OC   Mizuhopecten.
OX   NCBI_TaxID=6573;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Eye;
RX   PubMed=9287291; DOI=10.1074/jbc.272.37.22979;
RA   Kojima D., Terakita A., Ishikawa T., Tsukahara Y., Maeda A., Shichida Y.;
RT   "A novel Go-mediated phototransduction cascade in scallop visual cells.";
RL   J. Biol. Chem. 272:22979-22982(1997).
CC   -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC       as modulators or transducers in various transmembrane signaling
CC       systems.
CC   -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma. The
CC       alpha chain contains the guanine nucleotide binding site.
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; AB006456; BAA22219.1; -; mRNA.
DR   AlphaFoldDB; O15975; -.
DR   SMR; O15975; -.
DR   OrthoDB; 754573at2759; -.
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:0007186; P:G protein-coupled receptor signaling pathway; IEA:InterPro.
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   GTP-binding; Lipoprotein; Magnesium; Metal-binding; Nucleotide-binding;
KW   Palmitate; Transducer.
FT   CHAIN           1..353
FT                   /note="Guanine nucleotide-binding protein G(q) subunit
FT                   alpha"
FT                   /id="PRO_0000203768"
FT   DOMAIN          32..353
FT                   /note="G-alpha"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          35..48
FT                   /note="G1 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          172..180
FT                   /note="G2 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          195..204
FT                   /note="G3 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          264..271
FT                   /note="G4 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          323..328
FT                   /note="G5 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   BINDING         40..47
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         47
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         174..180
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         180
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         199..203
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         268..271
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         325
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   LIPID           3
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000255"
FT   LIPID           4
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   353 AA;  41237 MW;  5FDECC3C1C738B17 CRC64;
     MACCLSEEAK EQKRINCEIE KELRKAKRDA RRELKLLLLG TGESGKSTFI KQMRIIHGTG
     YSEEDKRGFI KIVYQNIFMA MHSMIRAMDT IKISFEVADN EENAIMIRQV DYETVTTLDS
     QSVEAILSLW ADAGIQECYD RRREYQLTDS AKYYLDAVDR IAEPNYLPTL QDILRVRVPT
     TGIIEYPFDL DSIIFRMVDV GGQRSERRKW IHCFENVTSI MFLVALSEYD QVLVESDNEN
     RMEESKALFR TIITYPWFQN SSVILFLNKK DLLEEKIMHS HLVDYFPEFD GQKKDAQGAR
     EFILRMFVDL NPDPDKIIYS HFTCATDTEN IRFVFAAVKD TILQLNLKEY NLV