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GBG1_DROME
ID   GBG1_DROME              Reviewed;          70 AA.
AC   P38040; A4UZ90; Q540Y8; Q9V4Z3;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 162.
DE   RecName: Full=Guanine nucleotide-binding protein subunit gamma-1;
DE   Flags: Precursor;
GN   Name=Ggamma1; Synonyms=G1; ORFNames=CG8261;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=1372898; DOI=10.1016/s0021-9258(18)42665-8;
RA   Ray K., Ganguly R.;
RT   "The Drosophila G protein gamma subunit gene (D-G gamma 1) produces three
RT   developmentally regulated transcripts and is predominantly expressed in the
RT   central nervous system.";
RL   J. Biol. Chem. 267:6086-6092(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Embryo;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC   -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC       as a modulator or transducer in various transmembrane signaling
CC       systems. The beta and gamma chains are required for the GTPase
CC       activity, for replacement of GDP by GTP, and for G protein-effector
CC       interaction. {ECO:0000269|PubMed:1372898}.
CC   -!- SUBUNIT: G proteins are composed of 3 units, alpha, beta and gamma.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in the central nervous
CC       system. {ECO:0000269|PubMed:1372898}.
CC   -!- SIMILARITY: Belongs to the G protein gamma family. {ECO:0000305}.
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DR   EMBL; M85042; AAA28570.1; -; mRNA.
DR   EMBL; AE013599; AAF59030.1; -; Genomic_DNA.
DR   EMBL; AE013599; AAM71087.1; -; Genomic_DNA.
DR   EMBL; AY118489; AAM49858.1; -; mRNA.
DR   PIR; A42155; A42155.
DR   RefSeq; NP_523662.1; NM_078938.3.
DR   RefSeq; NP_724718.1; NM_165631.2.
DR   RefSeq; NP_724719.1; NM_165632.2.
DR   AlphaFoldDB; P38040; -.
DR   SMR; P38040; -.
DR   BioGRID; 61721; 4.
DR   STRING; 7227.FBpp0087728; -.
DR   PaxDb; P38040; -.
DR   PRIDE; P38040; -.
DR   DNASU; 35881; -.
DR   EnsemblMetazoa; FBtr0088645; FBpp0087726; FBgn0004921.
DR   EnsemblMetazoa; FBtr0088646; FBpp0087727; FBgn0004921.
DR   EnsemblMetazoa; FBtr0088647; FBpp0087728; FBgn0004921.
DR   GeneID; 35881; -.
DR   KEGG; dme:Dmel_CG8261; -.
DR   CTD; 35881; -.
DR   FlyBase; FBgn0004921; Ggamma1.
DR   VEuPathDB; VectorBase:FBgn0004921; -.
DR   eggNOG; KOG4280; Eukaryota.
DR   GeneTree; ENSGT01050000244876; -.
DR   HOGENOM; CLU_168377_3_2_1; -.
DR   InParanoid; P38040; -.
DR   OMA; MDIMASN; -.
DR   OrthoDB; 1581168at2759; -.
DR   PhylomeDB; P38040; -.
DR   Reactome; R-DME-1296041; Activation of G protein gated Potassium channels.
DR   Reactome; R-DME-202040; G-protein activation.
DR   Reactome; R-DME-2485179; Activation of the phototransduction cascade.
DR   Reactome; R-DME-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR   Reactome; R-DME-392170; ADP signalling through P2Y purinoceptor 12.
DR   Reactome; R-DME-392451; G beta:gamma signalling through PI3Kgamma.
DR   Reactome; R-DME-392851; Prostacyclin signalling through prostacyclin receptor.
DR   Reactome; R-DME-400042; Adrenaline,noradrenaline inhibits insulin secretion.
DR   Reactome; R-DME-4086398; Ca2+ pathway.
DR   Reactome; R-DME-416476; G alpha (q) signalling events.
DR   Reactome; R-DME-416482; G alpha (12/13) signalling events.
DR   Reactome; R-DME-418217; G beta:gamma signalling through PLC beta.
DR   Reactome; R-DME-418555; G alpha (s) signalling events.
DR   Reactome; R-DME-418594; G alpha (i) signalling events.
DR   Reactome; R-DME-418597; G alpha (z) signalling events.
DR   Reactome; R-DME-428930; Thromboxane signalling through TP receptor.
DR   Reactome; R-DME-500657; Presynaptic function of Kainate receptors.
DR   Reactome; R-DME-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR   Reactome; R-DME-8964315; G beta:gamma signalling through BTK.
DR   Reactome; R-DME-8964616; G beta:gamma signalling through CDC42.
DR   Reactome; R-DME-9009391; Extra-nuclear estrogen signaling.
DR   Reactome; R-DME-997272; Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
DR   BioGRID-ORCS; 35881; 0 hits in 3 CRISPR screens.
DR   ChiTaRS; Ggamma1; fly.
DR   GenomeRNAi; 35881; -.
DR   PRO; PR:P38040; -.
DR   Proteomes; UP000000803; Chromosome 2R.
DR   Bgee; FBgn0004921; Expressed in wing disc and 31 other tissues.
DR   Genevisible; P38040; DM.
DR   GO; GO:0005834; C:heterotrimeric G-protein complex; IDA:FlyBase.
DR   GO; GO:0031681; F:G-protein beta-subunit binding; IBA:GO_Central.
DR   GO; GO:0045176; P:apical protein localization; TAS:FlyBase.
DR   GO; GO:0055059; P:asymmetric neuroblast division; IMP:FlyBase.
DR   GO; GO:0061343; P:cell adhesion involved in heart morphogenesis; IMP:FlyBase.
DR   GO; GO:0060027; P:convergent extension involved in gastrulation; IMP:FlyBase.
DR   GO; GO:0007391; P:dorsal closure; IMP:FlyBase.
DR   GO; GO:0035050; P:embryonic heart tube development; IMP:FlyBase.
DR   GO; GO:0003380; P:establishment or maintenance of cytoskeleton polarity involved in gastrulation; IMP:FlyBase.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:FlyBase.
DR   GO; GO:0003015; P:heart process; IMP:FlyBase.
DR   GO; GO:0048383; P:mesectoderm development; IMP:FlyBase.
DR   GO; GO:0007637; P:proboscis extension reflex; IMP:FlyBase.
DR   GO; GO:0010470; P:regulation of gastrulation; IMP:FlyBase.
DR   GO; GO:0043519; P:regulation of myosin II filament organization; IMP:FlyBase.
DR   CDD; cd00068; GGL; 1.
DR   Gene3D; 4.10.260.10; -; 1.
DR   InterPro; IPR015898; G-protein_gamma-like_dom.
DR   InterPro; IPR036284; GGL_sf.
DR   InterPro; IPR001770; Gprotein-gamma.
DR   PANTHER; PTHR13809; PTHR13809; 1.
DR   Pfam; PF00631; G-gamma; 1.
DR   SMART; SM00224; GGL; 1.
DR   SUPFAM; SSF48670; SSF48670; 1.
DR   PROSITE; PS50058; G_PROTEIN_GAMMA; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Lipoprotein; Membrane; Methylation; Prenylation;
KW   Reference proteome; Transducer.
FT   CHAIN           1..67
FT                   /note="Guanine nucleotide-binding protein subunit gamma-1"
FT                   /id="PRO_0000012677"
FT   PROPEP          68..70
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000012678"
FT   MOD_RES         67
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250"
FT   LIPID           67
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   70 AA;  8130 MW;  1CD46E3BBF8FE4F3 CRC64;
     MDVMSSSLQQ QRVVVEQLRR EAAIDRQTIS ESCAKMMKYI TEHEQEDYLL TGFTSQKVNP
     FREKSSCTVL
 
 
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