GNAS2_BOVIN
ID GNAS2_BOVIN Reviewed; 394 AA.
AC P04896; Q0II85; Q3SZE7;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Guanine nucleotide-binding protein G(s) subunit alpha isoforms short;
DE AltName: Full=Adenylate cyclase-stimulating G alpha protein;
GN Name=GNAS; Synonyms=GNAS1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3080331; DOI=10.1016/0014-5793(86)80164-8;
RA Nukada T., Tanabe T., Takahashi H., Noda M., Hirose T., Inayama S.,
RA Numa S.;
RT "Primary structure of the alpha-subunit of bovine adenylate cyclase-
RT stimulating G-protein deduced from the cDNA sequence.";
RL FEBS Lett. 195:220-224(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3081893; DOI=10.1073/pnas.83.5.1251;
RA Robishaw J.D., Russell D.W., Harris B.A., Smigel M.D., Gilman A.G.;
RT "Deduced primary structure of the alpha subunit of the GTP-binding
RT stimulatory protein of adenylate cyclase.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:1251-1255(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus, and Kidney;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 69-90.
RX PubMed=3015900; DOI=10.1016/s0021-9258(18)67553-2;
RA Robishaw J.D., Smigel M.D., Gilman A.G.;
RT "Molecular basis for two forms of the G protein that stimulates adenylate
RT cyclase.";
RL J. Biol. Chem. 261:9587-9590(1986).
RN [5]
RP FUNCTION.
RX PubMed=2022671; DOI=10.1016/s0021-9258(18)93016-4;
RA Tang W.J., Krupinski J., Gilman A.G.;
RT "Expression and characterization of calmodulin-activated (type I)
RT adenylylcyclase.";
RL J. Biol. Chem. 266:8595-8603(1991).
RN [6]
RP CLEAVAGE OF INITIATOR METHIONINE, PALMITOYLATION AT GLY-2 AND CYS-3, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=12574119; DOI=10.1093/emboj/cdg095;
RA Kleuss C., Krause E.;
RT "Galpha(s) is palmitoylated at the N-terminal glycine.";
RL EMBO J. 22:826-832(2003).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF ISOFORM GNAS-2 IN COMPLEX WITH GTP
RP ANALOG; MAGNESIUM IONS AND CATALYTIC DOMAINS OF ADCY2 AND ADCY5,
RP MISCELLANEOUS, AND INTERACTION WITH ADCY2 AND ADCY5.
RX PubMed=9395396; DOI=10.1126/science.278.5345.1943;
RA Sunahara R.K., Tesmer J.J.G., Gilman A.G., Sprang S.R.;
RT "Crystal structure of the adenylyl cyclase activator Gsalpha.";
RL Science 278:1943-1947(1997).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF COMPLEX WITH GTP ANALOG; MAGNESIUM
RP IONS AND CATALYTIC DOMAINS OF ADCY2 AND ADCY5, MISCELLANEOUS, AND
RP INTERACTION WITH ADCY2 AND ADCY5.
RX PubMed=9417641; DOI=10.1126/science.278.5345.1907;
RA Tesmer J.J.G., Sunahara R.K., Gilman A.G., Sprang S.R.;
RT "Crystal structure of the catalytic domains of adenylyl cyclase in a
RT complex with Gsalpha.GTPgammaS.";
RL Science 278:1907-1916(1997).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF COMPLEX WITH GTP ANALOG; MAGNESIUM
RP IONS AND CATALYTIC DOMAINS OF ADCY2 AND ADCY5, MISCELLANEOUS, AND
RP INTERACTION WITH ADCY2 AND ADCY5.
RX PubMed=10427002; DOI=10.1126/science.285.5428.756;
RA Tesmer J.J.G., Sunahara R.K., Johnson R.A., Gosselin G., Gilman A.G.,
RA Sprang S.R.;
RT "Two-metal-ion catalysis in adenylyl cyclase.";
RL Science 285:756-760(1999).
RN [10] {ECO:0007744|PDB:1CS4, ECO:0007744|PDB:1CUL}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH GTP ANALOG;
RP MAGNESIUM IONS AND CATALYTIC DOMAINS OF ADCY2 AND ADCY5, MISCELLANEOUS,
RP INTERACTION WITH ADCY2 AND ADCY5, AND FUNCTION.
RX PubMed=11087399; DOI=10.1021/bi0015562;
RA Tesmer J.J., Dessauer C.W., Sunahara R.K., Murray L.D., Johnson R.A.,
RA Gilman A.G., Sprang S.R.;
RT "Molecular basis for P-site inhibition of adenylyl cyclase.";
RL Biochemistry 39:14464-14471(2000).
RN [11] {ECO:0007744|PDB:1TL7, ECO:0007744|PDB:1U0H}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH GTP ANALOG;
RP MAGNESIUM IONS AND CATALYTIC DOMAINS OF ADCY2 AND ADCY5, MISCELLANEOUS,
RP INTERACTION WITH ADCY2 AND ADCY5, AND FUNCTION.
RX PubMed=15591060; DOI=10.1074/jbc.m409076200;
RA Mou T.C., Gille A., Fancy D.A., Seifert R., Sprang S.R.;
RT "Structural basis for the inhibition of mammalian membrane adenylyl cyclase
RT by 2 '(3')-O-(N-Methylanthraniloyl)-guanosine 5 '-triphosphate.";
RL J. Biol. Chem. 280:7253-7261(2005).
RN [12] {ECO:0007744|PDB:2GVD, ECO:0007744|PDB:2GVZ}
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN COMPLEX WITH GTP ANALOG;
RP MANGANESE IONS AND CATALYTIC DOMAINS OF ADCY2 AND ADCY5, MISCELLANEOUS,
RP INTERACTION WITH ADCY2 AND ADCY5, AND FUNCTION.
RX PubMed=16766715; DOI=10.1124/mol.106.026427;
RA Mou T.C., Gille A., Suryanarayana S., Richter M., Seifert R., Sprang S.R.;
RT "Broad specificity of mammalian adenylyl cyclase for interaction with
RT 2',3'-substituted purine- and pyrimidine nucleotide inhibitors.";
RL Mol. Pharmacol. 70:878-886(2006).
RN [13] {ECO:0007744|PDB:3C14, ECO:0007744|PDB:3C15, ECO:0007744|PDB:3C16, ECO:0007744|PDB:3MAA}
RP X-RAY CRYSTALLOGRAPHY (2.68 ANGSTROMS) IN COMPLEX WITH GTP ANALOG;
RP MAGNESIUM IONS AND CATALYTIC DOMAINS OF ADCY2 AND ADCY5, MISCELLANEOUS,
RP INTERACTION WITH ADCY2 AND ADCY5, AND FUNCTION.
RX PubMed=19243146; DOI=10.1021/bi802122k;
RA Mou T.C., Masada N., Cooper D.M., Sprang S.R.;
RT "Structural basis for inhibition of mammalian adenylyl cyclase by
RT calcium.";
RL Biochemistry 48:3387-3397(2009).
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) function as
CC transducers in numerous signaling pathways controlled by G protein-
CC coupled receptors (GPCRs). Signaling involves the activation of
CC adenylyl cyclases, resulting in increased levels of the signaling
CC molecule cAMP (PubMed:2022671, PubMed:9395396, PubMed:11087399,
CC PubMed:15591060, PubMed:16766715, PubMed:19243146). GNAS functions
CC downstream of several GPCRs, including beta-adrenergic receptors.
CC Stimulates the Ras signaling pathway via RAPGEF2 (By similarity).
CC {ECO:0000250|UniProtKB:P63092, ECO:0000269|PubMed:11087399,
CC ECO:0000269|PubMed:2022671, ECO:0000269|PubMed:9395396,
CC ECO:0000305|PubMed:15591060, ECO:0000305|PubMed:16766715,
CC ECO:0000305|PubMed:19243146}.
CC -!- SUBUNIT: Heterotrimeric G proteins are composed of 3 units; alpha, beta
CC and gamma. The alpha chain contains the guanine nucleotide binding site
CC (PubMed:9395396, PubMed:9417641, PubMed:10427002, PubMed:11087399,
CC PubMed:15591060, PubMed:16766715, PubMed:19243146). Interacts with
CC CRY1; the interaction may block GPCR-mediated regulation of cAMP
CC concentrations. Interacts with ADCY6 and stimulates its adenylyl
CC cyclase activity (By similarity). Interacts with ADCY2 and ADCY5
CC (PubMed:9395396, PubMed:9417641, PubMed:10427002, PubMed:11087399,
CC PubMed:15591060, PubMed:16766715, PubMed:19243146). Stimulates the
CC ADCY5 adenylyl cyclase activity (By similarity). Interaction with SASH1
CC (By similarity). Interacts with GASL2L2 (By similarity).
CC {ECO:0000250|UniProtKB:P63092, ECO:0000269|PubMed:10427002,
CC ECO:0000269|PubMed:11087399, ECO:0000269|PubMed:15591060,
CC ECO:0000269|PubMed:16766715, ECO:0000269|PubMed:19243146,
CC ECO:0000269|PubMed:9395396, ECO:0000269|PubMed:9417641}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P63094};
CC Lipid-anchor {ECO:0000250|UniProtKB:P63094}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=Gnas-1; Synonyms=Alpha-S2;
CC IsoId=P04896-1; Sequence=Displayed;
CC Name=Gnas-2; Synonyms=Alpha-S1;
CC IsoId=P04896-2; Sequence=VSP_001832;
CC Name=Nesp55;
CC IsoId=O18979-1; Sequence=External;
CC -!- MISCELLANEOUS: The GNAS locus is imprinted in a complex manner, giving
CC rise to distinct paternally, maternally and biallelically expressed
CC proteins.
CC -!- MISCELLANEOUS: Crystal structures were determined for GNAS in complex
CC with an adenylyl cyclase catalytic domain that was reconstructed from
CC ADCY2 and ADCY5 N- and C-terminal domains.
CC {ECO:0000269|PubMed:10427002, ECO:0000269|PubMed:11087399,
CC ECO:0000269|PubMed:15591060, ECO:0000269|PubMed:16766715,
CC ECO:0000269|PubMed:19243146, ECO:0000269|PubMed:9395396,
CC ECO:0000269|PubMed:9417641}.
CC -!- SIMILARITY: Belongs to the G-alpha family. G(s) subfamily.
CC {ECO:0000305}.
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DR EMBL; X03404; CAA27137.1; -; mRNA.
DR EMBL; M13006; AAA30560.1; -; mRNA.
DR EMBL; BC102905; AAI02906.1; -; mRNA.
DR EMBL; BC122757; AAI22758.1; -; mRNA.
DR EMBL; M14014; AAA30557.1; -; mRNA.
DR PIR; A23818; RGBOGA.
DR PIR; I45904; I45904.
DR RefSeq; NP_001258700.1; NM_001271771.1.
DR RefSeq; NP_851364.1; NM_181021.3. [P04896-1]
DR PDB; 1AZS; X-ray; 2.30 A; C=1-394.
DR PDB; 1AZT; X-ray; 2.30 A; A/B=1-394.
DR PDB; 1CJK; X-ray; 3.00 A; C=1-394.
DR PDB; 1CJT; X-ray; 2.80 A; C=1-394.
DR PDB; 1CJU; X-ray; 2.80 A; C=1-394.
DR PDB; 1CJV; X-ray; 3.00 A; C=1-394.
DR PDB; 1CS4; X-ray; 2.50 A; C=1-394.
DR PDB; 1CUL; X-ray; 2.40 A; C=1-394.
DR PDB; 1TL7; X-ray; 2.80 A; C=1-394.
DR PDB; 1U0H; X-ray; 2.90 A; C=1-394.
DR PDB; 2GVD; X-ray; 2.90 A; C=1-394.
DR PDB; 2GVZ; X-ray; 3.27 A; C=1-394.
DR PDB; 3C14; X-ray; 2.68 A; C=1-394.
DR PDB; 3C15; X-ray; 2.78 A; C=1-394.
DR PDB; 3C16; X-ray; 2.87 A; C=1-394.
DR PDB; 3G82; X-ray; 3.11 A; C=1-394.
DR PDB; 3MAA; X-ray; 3.00 A; C=1-394.
DR PDB; 3SN6; X-ray; 3.20 A; A=1-394.
DR PDB; 6NBF; EM; 3.00 A; A=1-67, A=208-394.
DR PDB; 6NBH; EM; 3.50 A; A=1-67, A=208-394.
DR PDB; 6NBI; EM; 4.00 A; A=1-67, A=208-394.
DR PDB; 6R3Q; EM; 3.40 A; B=1-394.
DR PDB; 6R4O; EM; 4.20 A; B=1-394.
DR PDB; 6R4P; EM; 3.10 A; B=1-394.
DR PDB; 7D68; EM; 3.00 A; A=1-67, A=208-394.
DR PDB; 7DTY; EM; 2.98 A; A=1-394.
DR PDB; 7FIM; EM; 3.40 A; A=1-394.
DR PDB; 7FIN; EM; 3.10 A; A=1-394.
DR PDB; 7FIY; EM; 3.40 A; A=1-394.
DR PDB; 7JJO; EM; 2.60 A; A=1-394.
DR PDB; 7PDE; EM; 4.50 A; B=1-394.
DR PDB; 7PDF; EM; 3.80 A; B=1-394.
DR PDB; 7S0G; EM; 3.86 A; A=384-394.
DR PDBsum; 1AZS; -.
DR PDBsum; 1AZT; -.
DR PDBsum; 1CJK; -.
DR PDBsum; 1CJT; -.
DR PDBsum; 1CJU; -.
DR PDBsum; 1CJV; -.
DR PDBsum; 1CS4; -.
DR PDBsum; 1CUL; -.
DR PDBsum; 1TL7; -.
DR PDBsum; 1U0H; -.
DR PDBsum; 2GVD; -.
DR PDBsum; 2GVZ; -.
DR PDBsum; 3C14; -.
DR PDBsum; 3C15; -.
DR PDBsum; 3C16; -.
DR PDBsum; 3G82; -.
DR PDBsum; 3MAA; -.
DR PDBsum; 3SN6; -.
DR PDBsum; 6NBF; -.
DR PDBsum; 6NBH; -.
DR PDBsum; 6NBI; -.
DR PDBsum; 6R3Q; -.
DR PDBsum; 6R4O; -.
DR PDBsum; 6R4P; -.
DR PDBsum; 7D68; -.
DR PDBsum; 7DTY; -.
DR PDBsum; 7FIM; -.
DR PDBsum; 7FIN; -.
DR PDBsum; 7FIY; -.
DR PDBsum; 7JJO; -.
DR PDBsum; 7PDE; -.
DR PDBsum; 7PDF; -.
DR PDBsum; 7S0G; -.
DR AlphaFoldDB; P04896; -.
DR SMR; P04896; -.
DR CORUM; P04896; -.
DR DIP; DIP-588N; -.
DR IntAct; P04896; 4.
DR SwissPalm; P04896; -.
DR PaxDb; P04896; -.
DR PRIDE; P04896; -.
DR ABCD; P04896; 3 sequenced antibodies.
DR Ensembl; ENSBTAT00000070189; ENSBTAP00000072381; ENSBTAG00000052413. [P04896-1]
DR GeneID; 281793; -.
DR KEGG; bta:281793; -.
DR CTD; 2778; -.
DR VEuPathDB; HostDB:ENSBTAG00000052413; -.
DR eggNOG; KOG0099; Eukaryota.
DR GeneTree; ENSGT00940000156300; -.
DR HOGENOM; CLU_014184_3_0_1; -.
DR InParanoid; P04896; -.
DR OMA; QENRATC; -.
DR OrthoDB; 1550241at2759; -.
DR BRENDA; 3.6.5.1; 908.
DR EvolutionaryTrace; P04896; -.
DR Proteomes; UP000009136; Chromosome 13.
DR Bgee; ENSBTAG00000052413; Expressed in neurohypophysis and 104 other tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
DR GO; GO:0031224; C:intrinsic component of membrane; IEA:Ensembl.
DR GO; GO:0032588; C:trans-Golgi network membrane; IEA:Ensembl.
DR GO; GO:0010856; F:adenylate cyclase activator activity; ISS:UniProtKB.
DR GO; GO:0031698; F:beta-2 adrenergic receptor binding; IBA:GO_Central.
DR GO; GO:0051430; F:corticotropin-releasing hormone receptor 1 binding; IBA:GO_Central.
DR GO; GO:0031748; F:D1 dopamine receptor binding; IBA:GO_Central.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IBA:GO_Central.
DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0005159; F:insulin-like growth factor receptor binding; IBA:GO_Central.
DR GO; GO:0035255; F:ionotropic glutamate receptor binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031852; F:mu-type opioid receptor binding; IBA:GO_Central.
DR GO; GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0007191; P:adenylate cyclase-activating dopamine receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0060348; P:bone development; IEA:Ensembl.
DR GO; GO:0050890; P:cognition; IEA:Ensembl.
DR GO; GO:0048589; P:developmental growth; IEA:Ensembl.
DR GO; GO:0060789; P:hair follicle placode formation; IEA:Ensembl.
DR GO; GO:0070527; P:platelet aggregation; IEA:Ensembl.
DR GO; GO:0043950; P:positive regulation of cAMP-mediated signaling; ISS:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0007606; P:sensory perception of chemical stimulus; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; GTP-binding;
KW Isopeptide bond; Lipoprotein; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Palmitate; Phosphoprotein; Reference proteome;
KW Transducer; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12574119"
FT CHAIN 2..394
FT /note="Guanine nucleotide-binding protein G(s) subunit
FT alpha isoforms short"
FT /id="PRO_0000203717"
FT DOMAIN 39..394
FT /note="G-alpha"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 1..23
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 68..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..204
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 219..228
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 288..295
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 364..369
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT COMPBIAS 9..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 47..55
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000305|PubMed:10427002,
FT ECO:0000305|PubMed:11087399, ECO:0000305|PubMed:15591060,
FT ECO:0000305|PubMed:16766715, ECO:0000305|PubMed:19243146,
FT ECO:0000305|PubMed:9395396, ECO:0000305|PubMed:9417641"
FT BINDING 54
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:10427002,
FT ECO:0000269|PubMed:11087399, ECO:0000269|PubMed:15591060,
FT ECO:0000269|PubMed:19243146, ECO:0000269|PubMed:9395396,
FT ECO:0000269|PubMed:9417641, ECO:0000305|PubMed:16766715"
FT BINDING 197..204
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000305|PubMed:10427002,
FT ECO:0000305|PubMed:11087399, ECO:0000305|PubMed:15591060,
FT ECO:0000305|PubMed:16766715, ECO:0000305|PubMed:19243146,
FT ECO:0000305|PubMed:9395396, ECO:0000305|PubMed:9417641"
FT BINDING 204
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:10427002,
FT ECO:0000269|PubMed:11087399, ECO:0000269|PubMed:15591060,
FT ECO:0000269|PubMed:19243146, ECO:0000269|PubMed:9395396,
FT ECO:0000269|PubMed:9417641, ECO:0000305|PubMed:16766715"
FT BINDING 223..227
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000305|PubMed:10427002,
FT ECO:0000305|PubMed:11087399, ECO:0000305|PubMed:15591060,
FT ECO:0000305|PubMed:16766715, ECO:0000305|PubMed:19243146,
FT ECO:0000305|PubMed:9395396, ECO:0000305|PubMed:9417641"
FT BINDING 292..295
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000305|PubMed:10427002,
FT ECO:0000305|PubMed:11087399, ECO:0000305|PubMed:15591060,
FT ECO:0000305|PubMed:16766715, ECO:0000305|PubMed:19243146,
FT ECO:0000305|PubMed:9395396, ECO:0000305|PubMed:9417641"
FT BINDING 366
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000305|PubMed:10427002,
FT ECO:0000305|PubMed:11087399, ECO:0000305|PubMed:15591060,
FT ECO:0000305|PubMed:16766715, ECO:0000305|PubMed:19243146,
FT ECO:0000305|PubMed:9395396, ECO:0000305|PubMed:9417641"
FT MOD_RES 352
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P63092"
FT LIPID 2
FT /note="N-palmitoyl glycine"
FT /evidence="ECO:0000269|PubMed:12574119"
FT LIPID 3
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:12574119"
FT CROSSLNK 300
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P63092"
FT VAR_SEQ 71..84
FT /note="Missing (in isoform Gnas-2)"
FT /evidence="ECO:0000305"
FT /id="VSP_001832"
FT CONFLICT 18
FT /note="A -> G (in Ref. 2; AAA30560)"
FT /evidence="ECO:0000305"
FT CONFLICT 85
FT /note="D -> S (in Ref. 2; AAA30560)"
FT /evidence="ECO:0000305"
FT CONFLICT 363
FT /note="F -> S (in Ref. 2; AAA30560)"
FT /evidence="ECO:0000305"
FT HELIX 36..39
FT /evidence="ECO:0007829|PDB:1AZT"
FT STRAND 40..48
FT /evidence="ECO:0007829|PDB:1AZS"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:6NBF"
FT HELIX 53..64
FT /evidence="ECO:0007829|PDB:1AZS"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:2GVZ"
FT HELIX 90..112
FT /evidence="ECO:0007829|PDB:1AZS"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:1AZS"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:1AZS"
FT HELIX 125..133
FT /evidence="ECO:0007829|PDB:1AZS"
FT TURN 134..136
FT /evidence="ECO:0007829|PDB:1AZS"
FT HELIX 144..155
FT /evidence="ECO:0007829|PDB:1AZS"
FT HELIX 157..163
FT /evidence="ECO:0007829|PDB:1AZS"
FT HELIX 164..168
FT /evidence="ECO:0007829|PDB:1AZS"
FT HELIX 175..179
FT /evidence="ECO:0007829|PDB:1AZS"
FT HELIX 182..185
FT /evidence="ECO:0007829|PDB:1AZS"
FT STRAND 186..189
FT /evidence="ECO:0007829|PDB:6R4P"
FT HELIX 194..199
FT /evidence="ECO:0007829|PDB:1AZS"
FT STRAND 206..214
FT /evidence="ECO:0007829|PDB:1AZS"
FT STRAND 217..224
FT /evidence="ECO:0007829|PDB:1AZS"
FT HELIX 228..237
FT /evidence="ECO:0007829|PDB:1AZS"
FT TURN 238..240
FT /evidence="ECO:0007829|PDB:1AZS"
FT STRAND 243..249
FT /evidence="ECO:0007829|PDB:1AZS"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:1AZS"
FT TURN 258..260
FT /evidence="ECO:0007829|PDB:1AZS"
FT STRAND 261..264
FT /evidence="ECO:0007829|PDB:2GVZ"
FT HELIX 265..277
FT /evidence="ECO:0007829|PDB:1AZS"
FT HELIX 280..282
FT /evidence="ECO:0007829|PDB:1AZT"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:1U0H"
FT STRAND 287..292
FT /evidence="ECO:0007829|PDB:1AZS"
FT HELIX 294..303
FT /evidence="ECO:0007829|PDB:1AZS"
FT HELIX 308..310
FT /evidence="ECO:0007829|PDB:1AZS"
FT HELIX 313..316
FT /evidence="ECO:0007829|PDB:1AZS"
FT STRAND 322..324
FT /evidence="ECO:0007829|PDB:6NBF"
FT HELIX 332..350
FT /evidence="ECO:0007829|PDB:1AZS"
FT TURN 354..356
FT /evidence="ECO:0007829|PDB:7JJO"
FT STRAND 359..363
FT /evidence="ECO:0007829|PDB:1AZS"
FT STRAND 365..367
FT /evidence="ECO:0007829|PDB:3SN6"
FT HELIX 369..392
FT /evidence="ECO:0007829|PDB:1AZS"
SQ SEQUENCE 394 AA; 45709 MW; 4D07A734AFF2A6BC CRC64;
MGCLGNSKTE DQRNEEKAQR EANKKIEKQL QKDKQVYRAT HRLLLLGAGE SGKSTIVKQM
RILHVNGFNG EGGEEDPQAA RSNSDGEKAT KVQDIKNNLK EAIETIVAAM SNLVPPVELA
NPENQFRVDY ILSVMNVPDF DFPPEFYEHA KALWEDEGVR ACYERSNEYQ LIDCAQYFLD
KIDVIKQDDY VPSDQDLLRC RVLTSGIFET KFQVDKVNFH MFDVGGQRDE RRKWIQCFND
VTAIIFVVAS SSYNMVIRED NQTNRLQEAL NLFKSIWNNR WLRTISVILF LNKQDLLAEK
VLAGKSKIED YFPEFARYTT PEDATPEPGE DPRVTRAKYF IRDEFLRIST ASGDGRHYCY
PHFTCAVDTE NIRRVFNDCR DIIQRMHLRQ YELL
