ID GNAS_LYMST Reviewed; 376 AA.
AC P30684;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 27-MAR-2024, entry version 107.
DE RecName: Full=Guanine nucleotide-binding protein G(s) subunit alpha;
DE AltName: Full=Adenylate cyclase-stimulating G alpha protein;
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(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; Z15096; CAA78808.1; -; mRNA.
DR PIR; S27015; S27015.
DR AlphaFoldDB; P30684; -.
DR SMR; P30684; -.
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; Lipoprotein; Magnesium; Metal-binding; Nucleotide-binding;
KW Palmitate; Transducer.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..376
FT /note="Guanine nucleotide-binding protein G(s) subunit
FT alpha"
FT /id="PRO_0000203728"
FT DOMAIN 36..376
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 178..186
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 201..210
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 270..277
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 346..351
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 180..186
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 186
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 205..209
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 274..277
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 348
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 376 AA; 44099 MW; A1596E119311CD7D CRC64;
MGCFRQTRDD EDDKLRKEAN KKIEKQLAKD KLLYRGTHRL LLLGAGESGK STIVKQMRIL
HVNGFSPEER KQKIEDIKRN VRDAILTITG AMSTLNPPVQ LEHPQNKAKV DYIQDKASQA
EFDYPPIFYE YTEILWKDKG VQAAFERSNE YQLIDCAQYF LDRVHIIRQA EYTPSEQDIL
RCRVLTSGIF ETKFSVDKVN FHMFDVGGQR DERRKWIQCF NDVTAIIFVT ACSGYNMVLR
EDATQNRLKE SLDLFKSIWN NRWLRTISVI LFLNKQDLLA EKVKAGKSKI EDYFPEYARY
QVPPDASSEP GEDTEVVRAK YFIRDEFLRI STASGDGRHY CYPHFTCAVD TENIRRVFDD
CRDIIQRMHL RQYELL
//
