GNAS1_MOUSE
ID GNAS1_MOUSE Reviewed; 1133 AA.
AC Q6R0H7; A2A607; A2A608; Q6R0H4; Q6R0H5; Q6R2J5; Q9JJX0; Q9Z1N8;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Guanine nucleotide-binding protein G(s) subunit alpha isoforms XLas;
DE AltName: Full=Adenylate cyclase-stimulating G alpha protein;
DE AltName: Full=Extra large alphas protein;
DE Short=XLalphas;
GN Name=Gnas {ECO:0000312|MGI:MGI:95777};
GN Synonyms=Gnas1 {ECO:0000312|MGI:MGI:95777};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAS00601.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS XLAS-1; XLAS-2 AND XLAS-3), AND
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 935-1018 (ISOFORM XLAS-1).
RC STRAIN=129/Sv {ECO:0000312|EMBL:AAR99381.1},
RC BALB/cJ {ECO:0000312|EMBL:AAR99382.1},
RC C57BL/6J {ECO:0000312|EMBL:AAR99383.1}, and
RC FVB/N {ECO:0000312|EMBL:AAS00601.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAS00601.1};
RX PubMed=15148396; DOI=10.1073/pnas.0308758101;
RA Abramowitz J., Grenet D., Birnbaumer M., Torres H.N., Birnbaumer L.;
RT "XL alpha-s, the extra-long form of the alpha subunit of the Gs G protein,
RT is significantly longer than suspected, and so is its companion Alex.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:8366-8371(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3] {ECO:0000305, ECO:0000312|EMBL:CAB83219.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-785.
RX PubMed=10749992; DOI=10.1093/hmg/9.5.835;
RA Hayward B.E., Bonthron D.T.;
RT "An imprinted antisense transcript at the human GNAS1 locus.";
RL Hum. Mol. Genet. 9:835-841(2000).
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAD14686.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 357-1133 (ISOFORM XLAS-4).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAD14686.1};
RX PubMed=10931851; DOI=10.1074/jbc.m006594200;
RA Klemke M., Pasolli H.A., Kehlenbach R.H., Offermanns S., Schultz G.,
RA Huttner W.B.;
RT "Characterization of the extra-large G protein alpha-subunit XLalphas. II.
RT Signal transduction properties.";
RL J. Biol. Chem. 275:33633-33640(2000).
RN [5] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12145344; DOI=10.1210/me.2002-0054;
RA Bastepe M., Gunes Y., Perez-Villamil B., Hunzelman J., Weinstein L.S.,
RA Jueppner H.;
RT "Receptor-mediated adenylyl cyclase activation through XLalpha(s), the
RT extra-large variant of the stimulatory G protein alpha-subunit.";
RL Mol. Endocrinol. 16:1912-1919(2002).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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. GNAS functions downstream of several GPCRs, including
CC beta-adrenergic receptors. XLas isoforms interact with the same set of
CC receptors as Gnas isoforms. {ECO:0000269|PubMed:12145344}.
CC -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma. The
CC alpha chain contains the guanine nucleotide binding site. Interacts
CC through its N-terminal region with ALEX which is produced from the same
CC locus in a different open reading frame. This interaction may inhibit
CC its adenylyl cyclase-stimulating activity (By similarity). Interacts
CC with MAGED2. {ECO:0000250|UniProtKB:Q5JWF2,
CC ECO:0000250|UniProtKB:Q63803}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q63803};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q63803}. Apical cell
CC membrane {ECO:0000250|UniProtKB:Q5JWF2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=9;
CC Name=XLas-1; Synonyms=XXL {ECO:0000269|PubMed:15148396};
CC IsoId=Q6R0H7-1; Sequence=Displayed;
CC Name=XLas-2; Synonyms=XXLb1 {ECO:0000269|PubMed:15148396};
CC IsoId=Q6R0H7-2; Sequence=VSP_052176, VSP_052180;
CC Name=XLas-3; Synonyms=XXLb2 {ECO:0000269|PubMed:15148396};
CC IsoId=Q6R0H7-3; Sequence=VSP_052177, VSP_052179;
CC Name=XLas-4;
CC IsoId=Q6R0H7-4; Sequence=VSP_052178;
CC Name=Gnas-1 {ECO:0000305};
CC IsoId=P63094-1; Sequence=External;
CC Name=Gnas-2 {ECO:0000305};
CC IsoId=P63094-2; Sequence=External;
CC Name=Gnas-3 {ECO:0000305}; Synonyms=NTas {ECO:0000305};
CC IsoId=P63094-3; Sequence=External;
CC Name=Nesp55-1 {ECO:0000305};
CC IsoId=Q9Z0F1-1; Sequence=External;
CC Name=Nesp55-2 {ECO:0000305};
CC IsoId=Q9Z0F1-2; Sequence=External;
CC -!- DISRUPTION PHENOTYPE: Mice cells lacking XLas isoforms which are then
CC transfected with these isoforms and a range of receptors demonstrate
CC that the XLas isoforms are capable of functionally coupling to the same
CC receptors as the Gnas isoforms including Adrb2, Crfr1, Pthr1 and Tshr.
CC {ECO:0000269|PubMed:12145344}.
CC -!- MISCELLANEOUS: This protein is produced by a bicistronic gene which
CC also produces the ALEX protein from an overlapping reading frame.
CC {ECO:0000250|UniProtKB:Q63803}.
CC -!- MISCELLANEOUS: The GNAS locus is imprinted in a complex manner, giving
CC rise to distinct paternally, maternally and biallelically expressed
CC proteins. The XLas isoforms are paternally derived, the Gnas isoforms
CC are biallelically derived and the Nesp55 isoforms are maternally
CC derived.
CC -!- SIMILARITY: Belongs to the G-alpha family. G(s) subfamily.
CC {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD14686.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAB83219.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY518305; AAR99380.1; -; Genomic_DNA.
DR EMBL; AY518306; AAR99381.1; -; Genomic_DNA.
DR EMBL; AY518307; AAR99382.1; -; Genomic_DNA.
DR EMBL; AY518308; AAR99383.1; -; Genomic_DNA.
DR EMBL; AY519501; AAS00601.1; -; mRNA.
DR EMBL; AY519503; AAS00603.1; -; mRNA.
DR EMBL; AY519504; AAS00604.1; -; mRNA.
DR EMBL; AL593857; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJ251761; CAB83219.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF116268; AAD14686.1; ALT_INIT; mRNA.
DR CCDS; CCDS17151.1; -. [Q6R0H7-1]
DR CCDS; CCDS38354.1; -. [Q6R0H7-4]
DR CCDS; CCDS38355.1; -. [Q6R0H7-2]
DR CCDS; CCDS89590.1; -. [Q6R0H7-3]
DR RefSeq; NP_001070975.1; NM_001077507.2. [Q6R0H7-4]
DR RefSeq; NP_001297014.1; NM_001310085.1. [Q6R0H7-3]
DR RefSeq; NP_034439.2; NM_010309.4. [Q6R0H7-1]
DR RefSeq; NP_963911.1; NM_201617.2. [Q6R0H7-2]
DR AlphaFoldDB; Q6R0H7; -.
DR SMR; Q6R0H7; -.
DR BioGRID; 199972; 37.
DR IntAct; Q6R0H7; 2.
DR STRING; 10090.ENSMUSP00000079341; -.
DR iPTMnet; Q6R0H7; -.
DR SwissPalm; Q6R0H7; -.
DR EPD; Q6R0H7; -.
DR jPOST; Q6R0H7; -.
DR MaxQB; Q6R0H7; -.
DR PaxDb; Q6R0H7; -.
DR PeptideAtlas; Q6R0H7; -.
DR PRIDE; Q6R0H7; -.
DR ProteomicsDB; 271024; -. [Q6R0H7-1]
DR ProteomicsDB; 271025; -. [Q6R0H7-2]
DR ProteomicsDB; 271026; -. [Q6R0H7-3]
DR ProteomicsDB; 271027; -. [Q6R0H7-4]
DR ABCD; Q6R0H7; 1 sequenced antibody.
DR Antibodypedia; 4152; 809 antibodies from 44 providers.
DR DNASU; 14683; -.
DR Ensembl; ENSMUST00000080493; ENSMUSP00000079341; ENSMUSG00000027523. [Q6R0H7-1]
DR Ensembl; ENSMUST00000087876; ENSMUSP00000085184; ENSMUSG00000027523. [Q6R0H7-4]
DR Ensembl; ENSMUST00000087877; ENSMUSP00000085185; ENSMUSG00000027523. [Q6R0H7-2]
DR Ensembl; ENSMUST00000154658; ENSMUSP00000158758; ENSMUSG00000027523. [Q6R0H7-3]
DR Ensembl; ENSMUST00000185956; ENSMUSP00000140174; ENSMUSG00000027523. [Q6R0H7-1]
DR GeneID; 14683; -.
DR UCSC; uc008oet.1; mouse. [Q6R0H7-2]
DR UCSC; uc033hrq.1; mouse. [Q6R0H7-4]
DR CTD; 2778; -.
DR MGI; MGI:95777; Gnas.
DR VEuPathDB; HostDB:ENSMUSG00000027523; -.
DR eggNOG; KOG0099; Eukaryota.
DR GeneTree; ENSGT00940000156300; -.
DR HOGENOM; CLU_010619_0_0_1; -.
DR InParanoid; Q6R0H7; -.
DR OrthoDB; 754573at2759; -.
DR PhylomeDB; Q6R0H7; -.
DR TreeFam; TF300673; -.
DR Reactome; R-MMU-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
DR Reactome; R-MMU-392851; Prostacyclin signalling through prostacyclin receptor.
DR Reactome; R-MMU-418555; G alpha (s) signalling events.
DR Reactome; R-MMU-420092; Glucagon-type ligand receptors.
DR Reactome; R-MMU-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
DR Reactome; R-MMU-9634597; GPER1 signaling.
DR BioGRID-ORCS; 14683; 12 hits in 74 CRISPR screens.
DR ChiTaRS; Gnas; mouse.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q6R0H7; protein.
DR Bgee; ENSMUSG00000027523; Expressed in superior cervical ganglion and 269 other tissues.
DR ExpressionAtlas; Q6R0H7; baseline and differential.
DR Genevisible; Q6R0H7; MM.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030142; C:COPI-coated Golgi to ER transport vesicle; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030425; C:dendrite; IDA:MGI.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; ISO:MGI.
DR GO; GO:0031224; C:intrinsic component of membrane; ISO:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0055037; C:recycling endosome; ISO:MGI.
DR GO; GO:0001726; C:ruffle; ISO:MGI.
DR GO; GO:0042383; C:sarcolemma; ISO:MGI.
DR GO; GO:0032588; C:trans-Golgi network membrane; ISO:MGI.
DR GO; GO:0010856; F:adenylate cyclase activator activity; ISS:UniProtKB.
DR GO; GO:0047391; F:alkylglycerophosphoethanolamine phosphodiesterase activity; ISO:MGI.
DR GO; GO:0043014; F:alpha-tubulin binding; ISO:MGI.
DR GO; GO:0031698; F:beta-2 adrenergic receptor binding; ISO:MGI.
DR GO; GO:0051430; F:corticotropin-releasing hormone receptor 1 binding; ISO:MGI.
DR GO; GO:0031748; F:D1 dopamine receptor binding; ISO:MGI.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IBA:GO_Central.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; ISO:MGI.
DR GO; GO:0031681; F:G-protein beta-subunit binding; ISO:MGI.
DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; ISO:MGI.
DR GO; GO:0003924; F:GTPase activity; ISO:MGI.
DR GO; GO:0005159; F:insulin-like growth factor receptor binding; ISO:MGI.
DR GO; GO:0035255; F:ionotropic glutamate receptor binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031852; F:mu-type opioid receptor binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; ISO:MGI.
DR GO; GO:0007191; P:adenylate cyclase-activating dopamine receptor signaling pathway; IGI:MGI.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IDA:MGI.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0060348; P:bone development; ISO:MGI.
DR GO; GO:0055074; P:calcium ion homeostasis; ISO:MGI.
DR GO; GO:0051216; P:cartilage development; IMP:MGI.
DR GO; GO:0071870; P:cellular response to catecholamine stimulus; ISO:MGI.
DR GO; GO:0071380; P:cellular response to prostaglandin E stimulus; ISO:MGI.
DR GO; GO:0050890; P:cognition; ISO:MGI.
DR GO; GO:0048589; P:developmental growth; ISO:MGI.
DR GO; GO:0006306; P:DNA methylation; IMP:MGI.
DR GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IMP:MGI.
DR GO; GO:0035116; P:embryonic hindlimb morphogenesis; IMP:MGI.
DR GO; GO:0001958; P:endochondral ossification; IMP:MGI.
DR GO; GO:0006112; P:energy reserve metabolic process; IMP:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0071514; P:genomic imprinting; IMP:MGI.
DR GO; GO:0060789; P:hair follicle placode formation; ISO:MGI.
DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR GO; GO:0045776; P:negative regulation of blood pressure; ISO:MGI.
DR GO; GO:0035814; P:negative regulation of renal sodium excretion; ISO:MGI.
DR GO; GO:0070527; P:platelet aggregation; ISO:MGI.
DR GO; GO:0043950; P:positive regulation of cAMP-mediated signaling; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISO:MGI.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IMP:MGI.
DR GO; GO:0045672; P:positive regulation of osteoclast differentiation; IMP:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0010765; P:positive regulation of sodium ion transport; ISO:MGI.
DR GO; GO:0040032; P:post-embryonic body morphogenesis; IMP:MGI.
DR GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR GO; GO:2000828; P:regulation of parathyroid hormone secretion; IMP:MGI.
DR GO; GO:0009966; P:regulation of signal transduction; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0071107; P:response to parathyroid hormone; ISO:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IMP:MGI.
DR GO; GO:0007606; P:sensory perception of chemical stimulus; IBA:GO_Central.
DR GO; GO:0001501; P:skeletal system development; IMP:MGI.
DR GO; GO:0043588; P:skin development; IMP:MGI.
DR GO; GO:0001894; P:tissue homeostasis; IMP:MGI.
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 ADP-ribosylation; Alternative splicing; Cell membrane; Coiled coil;
KW GTP-binding; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transducer.
FT CHAIN 1..1133
FT /note="Guanine nucleotide-binding protein G(s) subunit
FT alpha isoforms XLas"
FT /id="PRO_0000253985"
FT DOMAIN 778..1133
FT /note="G-alpha"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 1..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 322..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 611..648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 724..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 781..794
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 807..828
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 935..943
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 958..967
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 1027..1034
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 1103..1108
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT COILED 737..761
FT /evidence="ECO:0000255"
FT COMPBIAS 347..361
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..439
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..643
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 786..794
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P04896"
FT BINDING 793
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P04896"
FT BINDING 936..943
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P04896"
FT BINDING 943
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P04896"
FT BINDING 962..966
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P63096"
FT BINDING 1031..1034
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P63096"
FT BINDING 1105
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P04896"
FT MOD_RES 940
FT /note="ADP-ribosylarginine; by cholera toxin"
FT /evidence="ECO:0000250"
FT MOD_RES 1091
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JWF2"
FT VAR_SEQ 787..876
FT /note="AGESGKSTIVKQMRILHVNGFNGEGGEEDPQAARSNSDGEKATKVQDIKNNL
FT KEAIETIVAAMSNLVPPVELANPENQFRVDYILSVMNV -> RKVVPSDTEGRYRPEAS
FT ASASDRRLDRRGREVSPELLGWALRGSPGSIVRDRGGLGPSGCAPPPRLARLLRLRQLV
FT VGVCWCPFSVFACA (in isoform XLas-2)"
FT /evidence="ECO:0000303|PubMed:15148396"
FT /id="VSP_052176"
FT VAR_SEQ 787..827
FT /note="AGESGKSTIVKQMRILHVNGFNGEGGEEDPQAARSNSDGEK -> RKVVPSD
FT TEGRYRPEASASASDRRLDRRGREVLESLAKAPL (in isoform XLas-3)"
FT /evidence="ECO:0000303|PubMed:15148396"
FT /id="VSP_052177"
FT VAR_SEQ 810..825
FT /note="EGGEEDPQAARSNSDG -> DS (in isoform XLas-4)"
FT /evidence="ECO:0000303|PubMed:10931851"
FT /id="VSP_052178"
FT VAR_SEQ 828..1133
FT /note="Missing (in isoform XLas-3)"
FT /evidence="ECO:0000303|PubMed:15148396"
FT /id="VSP_052179"
FT VAR_SEQ 877..1133
FT /note="Missing (in isoform XLas-2)"
FT /evidence="ECO:0000303|PubMed:15148396"
FT /id="VSP_052180"
FT CONFLICT 371
FT /note="A -> G (in Ref. 4; CAB83219)"
FT /evidence="ECO:0000305"
FT CONFLICT 381
FT /note="P -> S (in Ref. 4; CAB83219)"
FT /evidence="ECO:0000305"
FT CONFLICT 578..591
FT /note="SLSATPAARASLPA -> YSRYSQLLPPLGHPFLPR (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 595..596
FT /note="Missing (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 599
FT /note="A -> Q (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 613..617
FT /note="SAAPS -> LPPH (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 622..628
FT /note="RPPSPEI -> DPQPRD (in Ref. 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1133 AA; 121505 MW; C1497D45498172F7 CRC64;
MGMFNCLHGN NMSGQHDIPP EVGEQPEQEP LEAPGAAAPG AGAGPAEEMA TEPDSEPSNN
EPVPDETGSE ISGPPEDSKS DIQSPCQAFE EVRVGGDYSP PPEEAMPFET QQPSLGDFWP
TLEQPGPSGT PSGLQAFNPA ILEPGTPTGA SPGLGAYTPP PEEAMPFEFN EPAQGDHSQP
PLQVPDLAPG GPEALVPRAL PAEPGNIRFE NAGFREDYSP PPEESVPFQV GGEEFGGDSP
PPGLPRVIPQ IGIGGEFPTV AVPSALCLAP AENAPPLWVR GAIDRPFREA VRSPPNFACD
SPPMEITRPL LEIGRASIGV DDDTAVNMDS PPIASDGPPI EVSGAPDKSE CAERPPVERE
AAEMEGSPTT ATAVEGKVPS PERGDGSSTQ PEAMDAKPAP AAQAVSTGSD AGAPTDSAML
TDSQSDAGED GTAPGTPSDL QSDPEELEEA PAVRADPDGG AAPVAPATPA ESESEGSRDP
AAEPASEAVP ATTAESASGA APVTQVEPAA AAVSATLAEP AARAAPITPK EPTTRAVPSA
RAHPAAGAVP GAPAMSASAR AAAARAAYAG PLVWGARSLS ATPAARASLP ARAAAAARAA
SAARAVAAGR SASAAPSRAH LRPPSPEIQV ADPPTPRPPP RPTAWPDKYE RGRSCCRYEA
SSGICEIESS SDESEEGATG CFQWLLRRNR RPGLPRSHTV GSNPVRNFFT RAFGSCFGLS
ECTRSRSLSP GKAKDPMEER RKQMRKEAIE MREQKRADKK RSKLIDKQLE EEKMDYMCTH
RLLLLGAGES GKSTIVKQMR ILHVNGFNGE GGEEDPQAAR SNSDGEKATK VQDIKNNLKE
AIETIVAAMS NLVPPVELAN PENQFRVDYI LSVMNVPNFD FPPEFYEHAK ALWEDEGVRA
CYERSNEYQL IDCAQYFLDK IDVIKQADYV PSDQDLLRCR VLTSGIFETK FQVDKVNFHM
FDVGGQRDER RKWIQCFNDV TAIIFVVASS SYNMVIREDN QTNRLQEALN LFKSIWNNRW
LRTISVILFL NKQDLLAEKV LAGKSKIEDY FPEFARYTTP EDATPEPGED PRVTRAKYFI
RDEFLRISTA SGDGRHYCYP HFTCAVDTEN IRRVFNDCRD IIQRMHLRQY ELL
