GNAS_ANOGA
ID GNAS_ANOGA Reviewed; 383 AA.
AC Q7PD79; A0EJE9;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Guanine nucleotide-binding protein G(s) subunit alpha;
DE AltName: Full=Adenylate cyclase-stimulating G alpha protein;
GN Name=G-s-alpha-60A {ECO:0000250|UniProtKB:P20354}; ORFNames=AGAP012095;
OS Anopheles gambiae (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7165;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=G3;
RX PubMed=17029251; DOI=10.1002/cne.21083;
RA Ruetzler M., Lu T., Zwiebel L.J.;
RT "Galpha encoding gene family of the malaria vector mosquito Anopheles
RT gambiae: expression analysis and immunolocalization of AGalphaq and
RT AGalphao in female antennae.";
RL J. Comp. Neurol. 499:533-545(2006).
RN [2] {ECO:0000305, ECO:0000312|EMBL:EAA00295.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PEST {ECO:0000312|EMBL:EAA00295.1};
RX PubMed=12364791; DOI=10.1126/science.1076181;
RA Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z.,
RA Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J.,
RA Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA Collins F.H., Hoffman S.L.;
RT "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL Science 298:129-149(2002).
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. Participates in olfactory
CC signal transduction. {ECO:0000269|PubMed:17029251}.
CC -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma. The
CC alpha chain contains the guanine nucleotide binding site.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the G-alpha family. G(s) subfamily.
CC {ECO:0000305}.
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DR EMBL; DQ182017; ABA56309.1; -; mRNA.
DR EMBL; AAAB01008986; EAA00295.1; -; Genomic_DNA.
DR RefSeq; XP_320433.1; XM_320433.1.
DR AlphaFoldDB; Q7PD79; -.
DR SMR; Q7PD79; -.
DR STRING; 7165.AGAP012095-PA; -.
DR PaxDb; Q7PD79; -.
DR GeneID; 1280580; -.
DR KEGG; aga:AgaP_AGAP012095; -.
DR CTD; 1280580; -.
DR VEuPathDB; VectorBase:AGAP029122; -.
DR eggNOG; KOG0099; Eukaryota.
DR HOGENOM; CLU_014184_3_0_1; -.
DR InParanoid; Q7PD79; -.
DR OMA; GPDFNYP; -.
DR PhylomeDB; Q7PD79; -.
DR Proteomes; UP000007062; Chromosome 3L.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007191; P:adenylate cyclase-activating dopamine receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007606; P:sensory perception of chemical stimulus; IBA:GO_Central.
DR GO; GO:0007608; P:sensory perception of smell; IEA:UniProtKB-KW.
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 Olfaction; Palmitate; Reference proteome; Sensory transduction; Transducer.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..383
FT /note="Guanine nucleotide-binding protein G(s) subunit
FT alpha"
FT /id="PRO_0000233312"
FT DOMAIN 43..383
FT /note="G-alpha"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 46..59
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 185..193
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 208..217
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 277..284
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 353..358
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT COMPBIAS 17..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 51..58
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P04695"
FT BINDING 58
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 187..193
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 193
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 212..216
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P04695"
FT BINDING 281..284
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P04695"
FT BINDING 355
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|UniProtKB:P04695"
SQ SEQUENCE 383 AA; 44701 MW; 56B4EB68F20DE0FB CRC64;
MGCFGSAGSK QSDSNSSEDT KSQKRRSDAI TRQLQKDKQV YRATHRLLLL GAGESGKSTI
VKQMRILHVN GFSDSERKQK IEDIKKNIRD AILTITGAMS TLTPPIQLEK PENQARVDYI
QDYASGPDFN YPPEFYEHTE ELWKDRGVQQ TYERSNEYQL IDCAKYFLDR VSEIKQPNYT
PTEQDILRCR VLTSGIFETR FQVDKVNFHM FDVGGQRDER RKWIQCFNDV TAIIFVTACS
SYNMVLREDP TQNRLRESLD LFKSIWNNRW LRTISVILFL NKQDLLAEKI KAGKSKLSDY
FGEFNRYQTP ADAVCEMGED PEVIRAKYFI RDEFLRISTA SGDGKHYCYP HFTCAVDTEN
IKRVFNDCRD IIQRMHLRQY ELL
