ID   GNAS_SCHMA              Reviewed;         379 AA.
AC   P30669;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Guanine nucleotide-binding protein G(s) subunit alpha;
DE   AltName: Full=Adenylate cyclase-stimulating G alpha protein;
OS   Schistosoma mansoni (Blood fluke).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX   NCBI_TaxID=6183;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1378444; DOI=10.1016/s0021-9258(19)49741-x;
RA   Iltzsch M.H., Bieber D., Vijayasarathy S., Webster P., Zurita M., Ding J.,
RA   Mansour T.E.;
RT   "Cloning and characterization of a cDNA coding for the alpha-subunit of a
RT   stimulatory G protein from Schistosoma mansoni.";
RL   J. Biol. Chem. 267:14504-14508(1992).
CC   -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC       as modulators or transducers in various transmembrane signaling
CC       systems. The G(s) protein is involved in hormonal regulation of
CC       adenylate cyclase: it activates the cyclase in response to beta-
CC       adrenergic stimuli.
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(s) subfamily.
CC       {ECO:0000305}.
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DR   EMBL; M81085; AAA29886.1; -; mRNA.
DR   PIR; A42964; A42964.
DR   RefSeq; XP_018644269.1; XM_018792763.1.
DR   AlphaFoldDB; P30669; -.
DR   SMR; P30669; -.
DR   STRING; 6183.Smp_059340.1; -.
DR   GeneID; 8349413; -.
DR   KEGG; smm:Smp_059340.1; -.
DR   CTD; 8349413; -.
DR   eggNOG; KOG0099; Eukaryota.
DR   HOGENOM; CLU_014184_3_0_1; -.
DR   OMA; QENRATC; -.
DR   OrthoDB; 754573at2759; -.
DR   PhylomeDB; P30669; -.
DR   Proteomes; UP000008854; Unassembled WGS sequence.
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; IPR000367; Gprotein_alpha_S.
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; PR00443; GPROTEINAS.
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; Magnesium; Metal-binding; Nucleotide-binding;
KW   Reference proteome; Transducer.
FT   CHAIN           1..379
FT                   /note="Guanine nucleotide-binding protein G(s) subunit
FT                   alpha"
FT                   /id="PRO_0000203729"
FT   DOMAIN          38..379
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          180..188
FT                   /note="G2 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          203..212
FT                   /note="G3 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          272..279
FT                   /note="G4 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          349..354
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"
FT   BINDING         53
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         182..188
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         188
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         207..211
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         276..279
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         351
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   379 AA;  44045 MW;  ECC50E5E89C6E8EF CRC64;
     MVIGCCTLNN ISEDAKTRSD ANKQIEKLIE KEKKNFKSTH RLLLLGAGES GKSTIVKQMR
     ILHIDGFSER EKKEKIDAIR KNLRDAICSI AGAMGSLKPP VKLELSENRK LRDYILETAS
     KPDFDYPPEF FTYCAKLWKD GGIQETFERS NEYQLIDCAK YFLDKALEVG APNYIPSEQD
     ILRCRVLTSG IFETKFSVDK VNFHMFDVGG QREERRKWIQ CFNDVTAIIF VAACSSYNMV
     LREDPSQNRV KESLELLASI WNNRWLRNIS VILFLNKQDL LTEKVLAGKS KIEVYFPHYA
     TYQAPADTLA EYRHENSEVV RARFFFRDEF LKVTSNNNGG RHYCYPHLTC AVDTENIRRV
     FNDCRDIIQR MHLRQYELL