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 27-MAR-2024, entry version 132.
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.P30669; -.
DR GeneID; 8349413; -.
DR KEGG; smm:Smp_059340.1; -.
DR CTD; 8349413; -.
DR eggNOG; KOG0099; Eukaryota.
DR HOGENOM; CLU_014184_3_0_1; -.
DR InParanoid; P30669; -.
DR OMA; DHVAKCW; -.
DR OrthoDB; 2897309at2759; -.
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; GI Alpha 1, domain 2-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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:SF212; G PROTEIN ALPHA S SUBUNIT; 1.
DR PANTHER; PTHR10218; GTP-BINDING PROTEIN ALPHA SUBUNIT; 1.
DR Pfam; PF00503; G-alpha; 1.
DR PRINTS; PR00318; GPROTEINA.
DR PRINTS; PR00443; GPROTEINAS.
DR SMART; SM00275; G_alpha; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF47895; Transducin (alpha subunit), insertion domain; 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
//
