ID   GNAQ_HOMAM              Reviewed;         353 AA.
AC   P91950;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Guanine nucleotide-binding protein G(q) subunit alpha;
DE   AltName: Full=Guanine nucleotide-binding protein alpha-q;
OS   Homarus americanus (American lobster).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC   Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Astacidea;
OC   Nephropoidea; Nephropidae; Homarus.
OX   NCBI_TaxID=6706;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Olfactory organ;
RX   PubMed=9166716; DOI=10.1046/j.1471-4159.1997.68062248.x;
RA   McClintock T.S., Xu F., Quintero J., Gress A.M., Landers T.M.;
RT   "Molecular cloning of a lobster G alpha(q) protein expressed in neurons of
RT   olfactory organ and brain.";
RL   J. Neurochem. 68:2248-2254(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}.
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DR   EMBL; U89139; AAB49314.1; -; mRNA.
DR   AlphaFoldDB; P91950; -.
DR   SMR; P91950; -.
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_0000203765"
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;  41521 MW;  218B92CA16540408 CRC64;
     MACCLSEEAK EQKRINQEIE RQLRKDKRDA RRELKLLLLG TGESGKSTFI KQMRIIHGAG
     YSDEDKRGFI KLVFQNIFMA MQSMIRAMDL LQISYGDSAN IEHADLVRSV DYESVTTFEE
     PYVTAMNSLW QDTGIQHCYD RRREYQLTDS AKYYLTDLDR IAAKDYVSTL QDILRVRAPT
     TGIIEYPFDL EEIRFRMVDV GGQRSERRKW IHCFENVTSI IFLVALSEYD QILFESDNEN
     RMEESKALFK TIITYPWFQH SSVILFLNKK DLLEEKIMYS HLVDYFPEYD GPRKDAIAAR
     EFILRMFVEL NPDPEKIIYS HFTCATDTEN IRFVFAAVKD TILQLNLKEY NLV