ID   GNAO_LYMST              Reviewed;         354 AA.
AC   P30683;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Guanine nucleotide-binding protein G(o) subunit alpha;
OS   Lymnaea stagnalis (Great pond snail) (Helix stagnalis).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Heterobranchia; Euthyneura; Panpulmonata; Hygrophila; Lymnaeoidea;
OC   Lymnaeidae; Lymnaea.
OX   NCBI_TaxID=6523;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=CNS;
RX   PubMed=1468550; DOI=10.1016/0014-5793(92)81474-z;
RA   Knol J.C., Weidemann W., Planta R.J., Vreugdenhil E., van Heerikhuizen H.;
RT   "Molecular cloning of G protein alpha subunits from the central nervous
RT   system of the mollusc Lymnaea stagnalis.";
RL   FEBS Lett. 314:215-219(1992).
CC   -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC       as modulators or transducers in various transmembrane signaling
CC       systems. The G(o) protein function is not clear.
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(i/o/t/z) subfamily.
CC       {ECO:0000305}.
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DR   EMBL; Z15094; CAA78806.1; -; mRNA.
DR   PIR; S27014; S27014.
DR   AlphaFoldDB; P30683; -.
DR   SMR; P30683; -.
DR   GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt.
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:0007188; P:adenylate cyclase-modulating 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; IPR001408; Gprotein_alpha_I.
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; PR00441; GPROTEINAI.
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; Myristate;
KW   Nucleotide-binding; Palmitate; Transducer.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..354
FT                   /note="Guanine nucleotide-binding protein G(o) subunit
FT                   alpha"
FT                   /id="PRO_0000203712"
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          174..182
FT                   /note="G2 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          197..206
FT                   /note="G3 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          266..273
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         176..182
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         182
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         201..205
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         270..273
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           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000255"
FT   LIPID           3
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   354 AA;  40272 MW;  2A4CA2A20FEA42C0 CRC64;
     MGCTLSAEER AAMERSKAIE KNLKEDGMQA AKDIKLLLLG AGESGKSTIV KQMKIIHEGG
     FTSEDNKQYK PVVYSNTIQS LVAIIRAMGT LSIPFGDNER ESDAKMVLDV IARMEDTEPF
     SEELLAAMKR LWVDSGVQEC LGRANEYQLN DSAKYFLDDL DRLGAKDYMP TEQDILRTRV
     KTTGIVEVHF SFKNLNFKLF DVGGQRSERK KWIHCFEDVT AIIFCVAMSE YDQVLHEDET
     TNRMQESLKL FDSICNNKWF TETSIILFLN KKDLFEEKIK KSPLTICFPE YTGKQMYQEA
     SAYIQAQFEA KNKSSAKEIY CHQTCATDTN NIQFVFDAVT DVIIANNLRG CGLY