CYCG_DROME
ID CYCG_DROME Reviewed; 566 AA.
AC Q95TJ9;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Cyclin G {ECO:0000303|PubMed:18667003};
GN Name=CycG {ECO:0000312|FlyBase:FBgn0039858};
GN ORFNames=CG11525 {ECO:0000312|FlyBase:FBgn0039858};
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 {ECO:0000312|EMBL:AAL13949.1};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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 [2] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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 [3] {ECO:0000312|EMBL:AAL13949.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL13949.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAL13949.1};
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).
RN [4] {ECO:0000305}
RP FUNCTION.
RX PubMed=18667003; DOI=10.1111/j.0018-0661.2008.02067.x;
RA Salvaing J., Mouchel-Vielh E., Bloyer S., Preiss A., Peronnet F.;
RT "Regulation of Abd-B expression by Cyclin G and Corto in the abdominal
RT epithelium of Drosophila.";
RL Hereditas 145:138-146(2008).
RN [5] {ECO:0000305}
RP FUNCTION, INTERACTION WITH CORTO, SUBCELLULAR LOCATION, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=18286205; DOI=10.1371/journal.pone.0001658;
RA Salvaing J., Nagel A.C., Mouchel-Vielh E., Bloyer S., Maier D., Preiss A.,
RA Peronnet F.;
RT "The enhancer of trithorax and polycomb corto interacts with cyclin G in
RT Drosophila.";
RL PLoS ONE 3:E1658-E1658(2008).
RN [6] {ECO:0000305}
RP FUNCTION, INTERACTION WITH CDK2 AND CDK4, AND DEVELOPMENTAL STAGE.
RX PubMed=21311225; DOI=10.4161/cc.10.5.14959;
RA Faradji F., Bloyer S., Dardalhon-Cumenal D., Randsholt N.B., Peronnet F.;
RT "Drosophila melanogaster Cyclin G coordinates cell growth and cell
RT proliferation.";
RL Cell Cycle 10:805-818(2011).
RN [7] {ECO:0000305}
RP FUNCTION.
RX PubMed=21998598; DOI=10.1371/journal.pgen.1002314;
RA Debat V., Bloyer S., Faradji F., Gidaszewski N., Navarro N.,
RA Orozco-Terwengel P., Ribeiro V., Schloetterer C., Deutsch J.S.,
RA Peronnet F.;
RT "Developmental stability: a major role for cyclin G in drosophila
RT melanogaster.";
RL PLoS Genet. 7:E1002314-E1002314(2011).
RN [8] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23121330; DOI=10.1111/j.1601-5223.2012.02273.x;
RA Nagel A.C., Szawinski J., Fischer P., Maier D., Wech I., Preiss A.;
RT "Dorso-ventral axis formation of the Drosophila oocyte requires Cyclin G.";
RL Hereditas 149:186-196(2012).
RN [9] {ECO:0000305}
RP FUNCTION, INTERACTION WITH BRCA2 AND RAD9, AND DISRUPTION PHENOTYPE.
RX PubMed=22976300; DOI=10.1242/jcs.113902;
RA Nagel A.C., Fischer P., Szawinski J., La Rosa M.K., Preiss A.;
RT "Cyclin G is involved in meiotic recombination repair in Drosophila
RT melanogaster.";
RL J. Cell Sci. 125:5555-5563(2012).
RN [10] {ECO:0000305}
RP FUNCTION, INTERACTION WITH ASX, AND SUBCELLULAR LOCATION.
RX PubMed=25995770; DOI=10.1186/s13072-015-0008-6;
RA Dupont C.A., Dardalhon-Cumenal D., Kyba M., Brock H.W., Randsholt N.B.,
RA Peronnet F.;
RT "Drosophila Cyclin G and epigenetic maintenance of gene expression during
RT development.";
RL Epigenetics Chromatin 8:18-18(2015).
RN [11] {ECO:0000305}
RP FUNCTION, INTERACTION WITH WDB, AND DISRUPTION PHENOTYPE.
RX PubMed=26274446; DOI=10.1371/journal.pgen.1005440;
RA Fischer P., La Rosa M.K., Schulz A., Preiss A., Nagel A.C.;
RT "Cyclin G functions as a positive regulator of growth and metabolism in
RT Drosophila.";
RL PLoS Genet. 11:E1005440-E1005440(2015).
CC -!- FUNCTION: Cyclin with roles in multiple processes including
CC transcription, meiotic recombination repair, cell cycle regulation, and
CC promotion of normal growth and metabolism (PubMed:18667003,
CC PubMed:18286205, PubMed:21311225, PubMed:22976300, PubMed:25995770,
CC PubMed:26274446). Binds to the promoter region of the homeobox gene
CC Abd-B and is involved in maintaining Abd-B expression in the pupal
CC epithelium (PubMed:18667003, PubMed:18286205). Involved in the
CC transcriptional repression of the homeotic genes Scr and Ubx
CC (PubMed:25995770). Plays a role in meiotic recombination repair of DNA
CC double-strand breaks which ensures efficient translation of grk and
CC promotes grk activity in the oocyte, leading to oocyte dorso-ventral
CC axis formation following secretion of grk from the oocyte and its
CC binding to Egfr in the directly overlying follicle cells
CC (PubMed:23121330, PubMed:22976300). Negatively regulates the binding of
CC serine/threonine-protein kinase Akt1 to the protein phosphatase 2A
CC subunit wdb, promoting normal growth and metabolism (PubMed:26274446).
CC Required for the formation of bilateral symmetry (PubMed:21998598).
CC Negatively regulates cell cycle progression by preventing G1 to S
CC transition and retarding S-phase progression (PubMed:21311225).
CC {ECO:0000269|PubMed:18286205, ECO:0000269|PubMed:18667003,
CC ECO:0000269|PubMed:21311225, ECO:0000269|PubMed:21998598,
CC ECO:0000269|PubMed:22976300, ECO:0000269|PubMed:23121330,
CC ECO:0000269|PubMed:25995770, ECO:0000269|PubMed:26274446}.
CC -!- SUBUNIT: Interacts with corto (PubMed:18286205). Interacts with the
CC cyclin-dependent kinases Cdk2 and Cdk4 (PubMed:21311225). Interacts
CC with Brca2 and Rad9 (PubMed:22976300). Interacts with polycomb protein
CC Asx (PubMed:25995770). Interacts with protein phosphatase 2A subunit
CC wdb (PubMed:26274446). {ECO:0000269|PubMed:18286205,
CC ECO:0000269|PubMed:21311225, ECO:0000269|PubMed:22976300,
CC ECO:0000269|PubMed:25995770, ECO:0000269|PubMed:26274446}.
CC -!- INTERACTION:
CC Q95TJ9; Q9VB23: wdb; NbExp=6; IntAct=EBI-458558, EBI-103072;
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:18286205,
CC ECO:0000269|PubMed:25995770}. Note=Localizes mainly on active
CC chromatin. {ECO:0000269|PubMed:25995770}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout all stages of the cell cycle
CC (at protein level) (PubMed:21311225). Expressed throughout development
CC with notably less expression in third instar larva than in embryo or
CC adult (PubMed:18286205). {ECO:0000269|PubMed:18286205,
CC ECO:0000269|PubMed:21311225}.
CC -!- DISRUPTION PHENOTYPE: Viable but females are sterile and produce eggs
CC with a ventralized phenotype where the dorsal respiratory appendages
CC are fused (PubMed:23121330, PubMed:22976300). Reduced levels of grk
CC protein in the oocyte cytoplasm and very low levels in follicle cells
CC and in the extracellular space separating the oocyte from the
CC follicular epithelium but no effect on grk transcription
CC (PubMed:23121330). Increased incidence of DNA double-strand breaks in
CC mutant germaria (PubMed:22976300). Reduced body size and weight and
CC reduced cell size and number with mutants showing signs of starvation
CC under normal feeding conditions and disturbed fat metabolism marked by
CC elevated levels of stored fat (PubMed:26274446). Reduced
CC phosphorylation levels of Akt1, Thor/4E-BP and S6k (PubMed:26274446).
CC Accumulation of insulin-like peptide Ilp5 in larval brains is reduced
CC to levels comparable to starved control animals (PubMed:26274446).
CC {ECO:0000269|PubMed:22976300, ECO:0000269|PubMed:23121330,
CC ECO:0000269|PubMed:26274446}.
CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin G subfamily.
CC {ECO:0000305}.
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DR EMBL; AE014297; AAF57168.2; -; Genomic_DNA.
DR EMBL; AE014297; AAF57169.2; -; Genomic_DNA.
DR EMBL; AE014297; AAF57170.2; -; Genomic_DNA.
DR EMBL; AE014297; AAF57171.2; -; Genomic_DNA.
DR EMBL; AE014297; AGB96525.1; -; Genomic_DNA.
DR EMBL; AY058720; AAL13949.1; -; mRNA.
DR RefSeq; NP_001263146.1; NM_001276217.2.
DR RefSeq; NP_524609.2; NM_079870.4.
DR RefSeq; NP_733434.1; NM_170555.3.
DR RefSeq; NP_733435.1; NM_170556.3.
DR RefSeq; NP_733436.1; NM_170557.3.
DR AlphaFoldDB; Q95TJ9; -.
DR IntAct; Q95TJ9; 75.
DR STRING; 7227.FBpp0305520; -.
DR iPTMnet; Q95TJ9; -.
DR PaxDb; Q95TJ9; -.
DR DNASU; 43724; -.
DR EnsemblMetazoa; FBtr0085799; FBpp0085160; FBgn0039858.
DR EnsemblMetazoa; FBtr0085800; FBpp0085161; FBgn0039858.
DR EnsemblMetazoa; FBtr0085802; FBpp0085163; FBgn0039858.
DR EnsemblMetazoa; FBtr0085803; FBpp0085164; FBgn0039858.
DR EnsemblMetazoa; FBtr0333328; FBpp0305520; FBgn0039858.
DR GeneID; 43724; -.
DR KEGG; dme:Dmel_CG11525; -.
DR UCSC; CG11525-RA; d. melanogaster.
DR CTD; 43724; -.
DR FlyBase; FBgn0039858; CycG.
DR VEuPathDB; VectorBase:FBgn0039858; -.
DR eggNOG; KOG0653; Eukaryota.
DR HOGENOM; CLU_471956_0_0_1; -.
DR InParanoid; Q95TJ9; -.
DR OMA; FFKFYQQ; -.
DR OrthoDB; 687843at2759; -.
DR PhylomeDB; Q95TJ9; -.
DR SignaLink; Q95TJ9; -.
DR BioGRID-ORCS; 43724; 0 hits in 3 CRISPR screens.
DR ChiTaRS; CycG; fly.
DR GenomeRNAi; 43724; -.
DR PRO; PR:Q95TJ9; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0039858; Expressed in cleaving embryo and 25 other tissues.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; ISS:FlyBase.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; IPI:FlyBase.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006302; P:double-strand break repair; IMP:FlyBase.
DR GO; GO:0060429; P:epithelium development; IGI:FlyBase.
DR GO; GO:0007143; P:female meiotic nuclear division; IMP:FlyBase.
DR GO; GO:0000711; P:meiotic DNA repair synthesis; IMP:FlyBase.
DR GO; GO:0044772; P:mitotic cell cycle phase transition; IBA:GO_Central.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IGI:FlyBase.
DR GO; GO:0045746; P:negative regulation of Notch signaling pathway; IGI:FlyBase.
DR GO; GO:0045927; P:positive regulation of growth; IMP:FlyBase.
DR GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; IMP:FlyBase.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IMP:FlyBase.
DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR CDD; cd00043; CYCLIN; 1.
DR InterPro; IPR028895; CCNG2.
DR InterPro; IPR039361; Cyclin.
DR InterPro; IPR013763; Cyclin-like.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR006671; Cyclin_N.
DR PANTHER; PTHR10177; PTHR10177; 1.
DR PANTHER; PTHR10177:SF473; PTHR10177:SF473; 1.
DR Pfam; PF00134; Cyclin_N; 1.
DR SMART; SM00385; CYCLIN; 1.
DR SUPFAM; SSF47954; SSF47954; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Chromosome; Cyclin; Developmental protein;
KW DNA damage; DNA repair; DNA-binding; Growth regulation; Meiosis;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..566
FT /note="Cyclin G"
FT /evidence="ECO:0000305"
FT /id="PRO_0000436049"
FT DOMAIN 285..368
FT /note="Cyclin N-terminal"
FT /evidence="ECO:0000255"
SQ SEQUENCE 566 AA; 62791 MW; E004BCC7F134E0F2 CRC64;
MSVPVRYSSA AAEYAAEVDC ELESTLQQQQ QLHLQQQYEQ YQHYQYQREQ DIAYYCQLQA
ARQQEQLMQQ RTSMSSSVMP GLALPQDHQD HPAALLNGPH NNNIGLAMDA HSINAILVDD
EQPSTSAQAA AAAAASAGGS AGAGSGSGLG GAIGGGKLAN GINRNAEMPT DWMRIADEGR
YGTPGAAGLE YQKYEQQQQL EDLAESEAGA VGGASNNNGE SSSSLKKLED QLHALTSDEL
YETLKEYDVL QDKFHTVLLL PKESRREVTA GGRDGSAYVL RCLKMWYELP SDVLFSAMSL
VDRFLDRMAV KPKHMACMSV ASFHLAIKQL DLKPIPAEDL VTISQCGCTA GDLERMAGVI
ANKLGVQMGH APITSVSYLR IYYALFRNLA KEIGGDFFKF YQQLIKLEEL ENRLEILMCD
VKTTVITPST LALVLICLHL DFHIKESYTR GSPELKHVFE YILFLQQYMR IPDRVFTCGF
SIVSGILSHY NGQNKAPYKQ RLVWKLSSRT LRVLRPINRF SSDLPTIEEG IPNALDDGLR
SRTESISSEE EEDWPTSPII PIFEQC
