GNAQ_LOLFO
ID GNAQ_LOLFO Reviewed; 354 AA.
AC P38412;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Guanine nucleotide-binding protein G(q) subunit alpha;
DE AltName: Full=Guanine nucleotide-binding protein alpha-q;
OS Loligo forbesii (Veined squid).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC Coleoidea; Decapodiformes; Teuthida; Myopsina; Loliginidae; Loligo.
OX NCBI_TaxID=6618;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Eye;
RX PubMed=8503868; DOI=10.1042/bj2920333;
RA Ryba N.J.P., Findlay J.B.C., Reid J.D.;
RT "The molecular cloning of the squid (Loligo forbesi) visual Gq-alpha
RT subunit and its expression in Saccharomyces cerevisiae.";
RL Biochem. J. 292:333-341(1993).
RN [2]
RP PROTEIN SEQUENCE OF 130-151 AND 258-278, AND CHARACTERIZATION.
RX PubMed=1930153; DOI=10.1042/bj2790323;
RA Pottinger J.D.D., Ryba N.J.P., Keen J.N., Findlay J.B.C.;
RT "The identification and purification of the heterotrimeric GTP-binding
RT protein from squid (Loligo forbesi) photoreceptors.";
RL Biochem. J. 279:323-326(1991).
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC as modulators or transducers in various transmembrane signaling
CC systems.
CC -!- FUNCTION: The G(q) alpha subunit is involved in the light-dependent
CC activation of phospholipase C.
CC -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma. The
CC alpha chain contains the guanine nucleotide binding site.
CC -!- TISSUE SPECIFICITY: A high concentration was found in the retinal
CC light-sensitive outer segment.
CC -!- SIMILARITY: Belongs to the G-alpha family. G(q) subfamily.
CC {ECO:0000305}.
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DR EMBL; L10289; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; S33309; S33309.
DR AlphaFoldDB; P38412; -.
DR SMR; P38412; -.
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 1: Evidence at protein level;
KW Direct protein sequencing; GTP-binding; Lipoprotein; Magnesium;
KW Metal-binding; Nucleotide-binding; Palmitate; Transducer.
FT CHAIN 1..354
FT /note="Guanine nucleotide-binding protein G(q) subunit
FT alpha"
FT /id="PRO_0000203767"
FT DOMAIN 32..354
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 265..272
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 324..329
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 269..272
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 326
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 354 AA; 41563 MW; 3CFB93922982255B CRC64;
MACCLSEEAK EQKRINQEIE KQLRRDKRDA RRELKLLLLG TGESGKSTFI KQMRIIHGSG
YSEEDRKGFE KIVYQNIFSA IQTLIAAMET LSLEYKDPSN NEHAEFLNSI DADSADIFED
GHVTAIKGCW TDPGMQECYD RRREYQLTDS AKYYLDDVER IHEPGYIPTL QDILRVRVPT
TGIIEYPFDL YSIIFRMVDV GGQRSERRKW IHCFENVTSI MFLVALSEYD QVLVESDNEE
NRMEESKALF RTIITYPWFQ NSSVILFLNK KDLLEEKIMT SHLADYFPDY DGPKCDYEAA
REFMMDSYMD LNEDKEKMLY YHYTCATDTE NIRFVFAAVK DTILQLNLKE YNLV
