ID   GNAS_GEOCY              Reviewed;         381 AA.
AC   Q9XZV5;
DT   30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Guanine nucleotide-binding protein G(s) subunit alpha;
DE   AltName: Full=Adenylate cyclase-stimulating G alpha protein;
OS   Geodia cydonium (Sponge).
OC   Eukaryota; Metazoa; Porifera; Demospongiae; Heteroscleromorpha;
OC   Tetractinellida; Astrophorina; Geodiidae; Geodia.
OX   NCBI_TaxID=6047;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9459489; DOI=10.1016/s0167-4889(97)00121-3;
RA   Seack J., Kruse M., Mueller W.E.G.;
RT   "Evolutionary analysis of G-proteins in early metazoans: cloning of
RT   alpha- and beta-subunits from the sponge Geodia cydonium.";
RL   Biochim. Biophys. Acta 1401:93-103(1998).
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; Y14249; CAB43528.1; -; mRNA.
DR   AlphaFoldDB; Q9XZV5; -.
DR   SMR; Q9XZV5; -.
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; Lipoprotein; Magnesium; Metal-binding; Nucleotide-binding;
KW   Palmitate; Transducer.
FT   CHAIN           1..381
FT                   /note="Guanine nucleotide-binding protein G(s) subunit
FT                   alpha"
FT                   /id="PRO_0000203726"
FT   DOMAIN          36..381
FT                   /note="G-alpha"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          39..52
FT                   /note="G1 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          181..189
FT                   /note="G2 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          204..213
FT                   /note="G3 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          273..280
FT                   /note="G4 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          351..356
FT                   /note="G5 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   BINDING         44..51
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         51
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         183..189
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         189
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         208..212
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         277..280
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         353
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"
SQ   SEQUENCE   381 AA;  44749 MW;  960162A80212638D CRC64;
     MSCFGGGVED DRTKEQKRQN KLIDQQLKKD KKAYRALHRL LLLGAGESGK STVVKQMKIL
     HKDGFSDEER KEKLVDIKSN IRDIVVTVTK AMSELDPPVS LGSPENEEHL QYLWSDEVTR
     KDYDYPEKFF EAVSKVWNDS GVQTCSARSN EYQLIDSAAY FMASEKQAQL KEPNYIPNDQ
     DILRCRVLTS GIFETRFVVD KVHFYMFGVG GQRIERRKWI QCFNDVTAII FVVACSSFNM
     VIREDLYTNR LRESLDLFEQ IWNNRWLRTV SIILFLNKQD ILKEKIDAGK RVENYFLEFN
     SYRPPDNLDL SKEPPGSSST FLKARYFFRD MFLRITNKSH DGRHFCYPHF TTAVDTENIR
     RVFDSCRDII QRMHLQKYEL L