CCNA_DROME
ID CCNA_DROME Reviewed; 491 AA.
AC P14785; Q8IGR7; Q9VTP6; Q9VTP7;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 04-MAY-2001, sequence version 3.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=G2/mitotic-specific cyclin-A;
GN Name=CycA; ORFNames=CG5940;
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 [GENOMIC DNA / MRNA] (ISOFORM A).
RC STRAIN=Canton-S;
RX PubMed=1332913; DOI=10.1016/0378-1119(92)90141-b;
RA Takahisa M., Togashi S., Ueda R., Mikuni M., Tsurumura S., Kondo K.,
RA Miyake T.;
RT "Structure of the Drosophila melanogaster gene encoding cyclin A.";
RL Gene 121:343-346(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM A).
RX PubMed=2564316; DOI=10.1016/0092-8674(89)90629-6;
RA Lehner C.F., O'Farrell P.H.;
RT "Expression and function of Drosophila cyclin A during embryonic cell cycle
RT progression.";
RL Cell 56:957-968(1989).
RN [3]
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 [4]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND B).
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).
RN [6]
RP NUCLEOTIDE SEQUENCE OF 235-247 AND 288-300.
RX PubMed=2564167; DOI=10.1038/338337a0;
RA Whitfield W.G.F., Gonzalez C., Sanchez-Herrero E., Glover D.M.;
RT "Transcripts of one of two Drosophila cyclin genes become localized in pole
RT cells during embryogenesis.";
RL Nature 338:337-340(1989).
RN [7]
RP IDENTIFICATION IN A COMPLEX WITH Z600 AND CDK1, AND MUTAGENESIS OF MET-235;
RP LEU-239 AND TRP-242.
RX PubMed=17431409; DOI=10.1038/sj.embor.7400948;
RA Gawlinski P., Nikolay R., Goursot C., Lawo S., Chaurasia B., Herz H.M.,
RA Kussler-Schneider Y., Ruppert T., Mayer M., Grosshans J.;
RT "The Drosophila mitotic inhibitor Fruehstart specifically binds to the
RT hydrophobic patch of cyclins.";
RL EMBO Rep. 8:490-496(2007).
CC -!- FUNCTION: Essential for the control of the cell cycle at the G2/M
CC (mitosis) transition. Interacts with the Cdk1 and Cdk2 protein kinases
CC to form MPF. G2/M cyclins accumulate steadily during G2 and are
CC abruptly destroyed at mitosis.
CC -!- SUBUNIT: Component of the Frs-CycA-Cdk1 complex composed of CycA, Cdk1
CC and Z600. Interacts (via C-terminus) with Z600.
CC {ECO:0000269|PubMed:17431409}.
CC -!- INTERACTION:
CC P14785; P22469: Z600; NbExp=4; IntAct=EBI-240333, EBI-7376821;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A; Synonyms=Long;
CC IsoId=P14785-1; Sequence=Displayed;
CC Name=B; Synonyms=Short;
CC IsoId=P14785-2; Sequence=VSP_001249;
CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin AB subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D10857; BAA01628.1; -; Genomic_DNA.
DR EMBL; D10858; BAA01629.1; -; mRNA.
DR EMBL; M24841; AAA28435.1; -; Genomic_RNA.
DR EMBL; AE014296; AAF49999.2; -; Genomic_DNA.
DR EMBL; AE014296; AAF50000.3; -; Genomic_DNA.
DR EMBL; AY058712; AAL13941.1; -; mRNA.
DR EMBL; BT001635; AAN71390.1; -; mRNA.
DR PIR; JC1390; JC1390.
DR RefSeq; NP_524030.2; NM_079306.4. [P14785-1]
DR AlphaFoldDB; P14785; -.
DR SMR; P14785; -.
DR BioGRID; 64701; 67.
DR DIP; DIP-22019N; -.
DR IntAct; P14785; 26.
DR MINT; P14785; -.
DR STRING; 7227.FBpp0075807; -.
DR PaxDb; P14785; -.
DR PRIDE; P14785; -.
DR DNASU; 39340; -.
DR EnsemblMetazoa; FBtr0076075; FBpp0075807; FBgn0000404. [P14785-1]
DR GeneID; 39340; -.
DR KEGG; dme:Dmel_CG5940; -.
DR CTD; 39340; -.
DR FlyBase; FBgn0000404; CycA.
DR VEuPathDB; VectorBase:FBgn0000404; -.
DR eggNOG; KOG0654; Eukaryota.
DR GeneTree; ENSGT00940000165715; -.
DR InParanoid; P14785; -.
DR PhylomeDB; P14785; -.
DR Reactome; R-DME-1538133; G0 and Early G1.
DR Reactome; R-DME-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-DME-176408; Regulation of APC/C activators between G1/S and early anaphase.
DR Reactome; R-DME-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR Reactome; R-DME-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR Reactome; R-DME-2559586; DNA Damage/Telomere Stress Induced Senescence.
DR Reactome; R-DME-5689880; Ub-specific processing proteases.
DR Reactome; R-DME-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-DME-6804116; TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest.
DR Reactome; R-DME-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-DME-68911; G2 Phase.
DR Reactome; R-DME-68949; Orc1 removal from chromatin.
DR Reactome; R-DME-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-DME-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR Reactome; R-DME-69563; p53-Dependent G1 DNA Damage Response.
DR Reactome; R-DME-69656; Cyclin A:Cdk2-associated events at S phase entry.
DR Reactome; R-DME-8951664; Neddylation.
DR Reactome; R-DME-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR BioGRID-ORCS; 39340; 1 hit in 3 CRISPR screens.
DR ChiTaRS; CycA; fly.
DR GenomeRNAi; 39340; -.
DR PRO; PR:P14785; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0000404; Expressed in egg cell and 63 other tissues.
DR ExpressionAtlas; P14785; baseline and differential.
DR Genevisible; P14785; DM.
DR GO; GO:0097124; C:cyclin A2-CDK2 complex; IBA:GO_Central.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0045169; C:fusome; IDA:CACAO.
DR GO; GO:0001673; C:male germ cell nucleus; IDA:CACAO.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0045170; C:spectrosome; IDA:FlyBase.
DR GO; GO:0045202; C:synapse; IDA:FlyBase.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IDA:FlyBase.
DR GO; GO:0055059; P:asymmetric neuroblast division; IMP:FlyBase.
DR GO; GO:0000278; P:mitotic cell cycle; IMP:FlyBase.
DR GO; GO:0044772; P:mitotic cell cycle phase transition; IBA:GO_Central.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IMP:FlyBase.
DR GO; GO:2000738; P:positive regulation of stem cell differentiation; IMP:FlyBase.
DR GO; GO:0035561; P:regulation of chromatin binding; IGI:FlyBase.
DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0007096; P:regulation of exit from mitosis; IMP:FlyBase.
DR GO; GO:0009794; P:regulation of mitotic cell cycle, embryonic; IMP:FlyBase.
DR GO; GO:0007088; P:regulation of mitotic nuclear division; IEP:UniProtKB.
DR GO; GO:0035186; P:syncytial blastoderm mitotic cell cycle; IGI:FlyBase.
DR CDD; cd00043; CYCLIN; 2.
DR InterPro; IPR039361; Cyclin.
DR InterPro; IPR013763; Cyclin-like.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR004367; Cyclin_C-dom.
DR InterPro; IPR006671; Cyclin_N.
DR PANTHER; PTHR10177; PTHR10177; 1.
DR Pfam; PF02984; Cyclin_C; 1.
DR Pfam; PF00134; Cyclin_N; 1.
DR SMART; SM00385; CYCLIN; 2.
DR SMART; SM01332; Cyclin_C; 1.
DR SUPFAM; SSF47954; SSF47954; 2.
DR PROSITE; PS00292; CYCLINS; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Cyclin; Mitosis;
KW Reference proteome.
FT CHAIN 1..491
FT /note="G2/mitotic-specific cyclin-A"
FT /id="PRO_0000080345"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..146
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_001249"
FT MUTAGEN 235
FT /note="M->A: Abolishes binding to Z600; when associated
FT with A-239 and A-242."
FT /evidence="ECO:0000269|PubMed:17431409"
FT MUTAGEN 239
FT /note="L->A: Abolishes binding to Z600; when associated
FT with A-235 and A-242."
FT /evidence="ECO:0000269|PubMed:17431409"
FT MUTAGEN 242
FT /note="W->A: Abolishes binding to Z600; when associated
FT with A-235 and A-239."
FT /evidence="ECO:0000269|PubMed:17431409"
FT CONFLICT 147
FT /note="M -> I (in Ref. 1; BAA01629)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="V -> A (in Ref. 1; BAA01628/BAA01629)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="V -> M (in Ref. 1; BAA01629)"
FT /evidence="ECO:0000305"
FT CONFLICT 220
FT /note="P -> A (in Ref. 5; AAN71390)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="L -> R (in Ref. 2; AAA28435)"
FT /evidence="ECO:0000305"
FT CONFLICT 474
FT /note="H -> Q (in Ref. 1; BAA01629)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 491 AA; 56152 MW; 6B700EB48A18ED99 CRC64;
MASFQIHQDM SNKENPGIKI PAGVKNTKQP LAVIGGKAEK NALAPRANFA VLNGNNNVPR
PAGKVQVFRD VRNLNVDENV EYGAKKSNVV PVVEQFKTFS VYEDNNDTQV APSGKSLASL
VDKENHDVKF GAGQKELVDY DLDSTPMSVT DVQSPMSVDR SILGVIQSSD ISVGTETGVS
PTGRVKELPP RNDRQRFLEV VQYQMDILEY FRESEKKHRP KPLYMRRQKD ISHNMRSILI
DWLVEVSEEY KLDTETLYLS VFYLDRFLSQ MAVVRSKLQL VGTAAMYIAA KYEEIYPPEV
GEFVFLTDDS YTKAQVLRME QVILKILSFD LCTPTAYVFI NTYAVLCDMP EKLKYMTLYI
SELSLMEGET YLQYLPSLMS SASVALARHI LGMEMWTPRL EEITTYKLED LKTVVLHLCH
THKTAKELNT QAMREKYNRD TYKKVAMMES VEMSKDDFDQ LCEAYNCKQK EDEHQQPDIN
TKSNVNLFYK F
