ID   GNAS_HOMAM              Reviewed;         379 AA.
AC   O16118;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Guanine nucleotide-binding protein G(s) subunit alpha;
DE   AltName: Full=Adenylate cyclase-stimulating G alpha protein;
OS   Homarus americanus (American lobster).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC   Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Astacidea;
OC   Nephropoidea; Nephropidae; Homarus.
OX   NCBI_TaxID=6706;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Olfactory organ;
RX   PubMed=9349521; DOI=10.1046/j.1471-4159.1997.69051793.x;
RA   Xu F., Hollins B., Gress A.M., Landers T.M., McClintock T.S.;
RT   "Molecular cloning and characterization of a lobster G alphaS protein
RT   expressed in neurons of olfactory organ and brain.";
RL   J. Neurochem. 69:1793-1800(1997).
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; AF010292; AAB66332.1; -; mRNA.
DR   AlphaFoldDB; O16118; -.
DR   SMR; O16118; -.
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   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..379
FT                   /note="Guanine nucleotide-binding protein G(s) subunit
FT                   alpha"
FT                   /id="PRO_0000203727"
FT   DOMAIN          39..379
FT                   /note="G-alpha"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          42..55
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          349..354
FT                   /note="G5 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   COMPBIAS        11..28
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         47..54
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         54
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         351
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   LIPID           2
FT                   /note="N-palmitoyl glycine"
FT                   /evidence="ECO:0000250"
FT   LIPID           3
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   379 AA;  44425 MW;  9CB598EB5441A094 CRC64;
     MGCFGSAGAK GDAEENKKRK EANKNINKQI QKDKQVYRAT HRLLLLGAGE SGKSTIVKQM
     RILHVDGFSE EEKREKIHAI RCNIRDAILT ITGNMSTLTP PIALENPAHQ FRVDYIQDVA
     SQKDFDYPEE FYEHTEMLWK DKGVQACYER ANEYQLIDCA KYFLDRVHIV RQTDYTPTEQ
     DILRCRVLTL GIFETRFQVD KVNFHMFDVG GQRDERRKWI QCFNDVTAII FVTACSSYNM
     VLREDPSQNR LRESLDLFKS IWNNRWLRTI SVILFLNKQD LLAEKIRAGK SKLEDYFPDF
     ARYQTPLDAT VEPGEDPEVV RAKYFIRDEF LRISTASGDG KHYCYPHFTC AVDTENIRRV
     FNDCRDIIQR MHLRQYELL