ID   CCNA2_CHICK             Reviewed;         395 AA.
AC   P43449;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Cyclin-A2 {ECO:0000305};
DE            Short=Cyclin-A {ECO:0000303|PubMed:8282760};
GN   Name=CCNA2 {ECO:0000250|UniProtKB:P20248}; Synonyms=CCNA, CYCA;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND SUBUNIT.
RX   PubMed=8282760; DOI=10.1242/jcs.106.2.535;
RA   Maridor G., Gallant P., Golsteyn R., Nigg E.A.;
RT   "Nuclear localization of vertebrate cyclin A correlates with its ability to
RT   form complexes with cdk catalytic subunits.";
RL   J. Cell Sci. 106:535-544(1993).
CC   -!- FUNCTION: Cyclin which controls both the G1/S and the G2/M transition
CC       phases of the cell cycle. Functions through the formation of specific
CC       serine/threonine kinase holoenzyme complexes with the cyclin-dependent
CC       protein kinases CDK1 and CDK2. The cyclin subunit confers the substrate
CC       specificity of these complexes and differentially interacts with and
CC       activates CDK1 and CDK2 throughout the cell cycle.
CC       {ECO:0000250|UniProtKB:P20248}.
CC   -!- SUBUNIT: Interacts with the CDK1 and CDK2 protein kinases to form
CC       serine/threonine kinase holoenzyme complexes.
CC       {ECO:0000269|PubMed:8282760}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8282760}. Cytoplasm
CC       {ECO:0000250|UniProtKB:P20248}.
CC   -!- SIMILARITY: Belongs to the cyclin family. Cyclin AB subfamily.
CC       {ECO:0000305}.
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DR   EMBL; X72892; CAA51410.1; -; mRNA.
DR   PIR; S38812; S38812.
DR   RefSeq; NP_990575.1; NM_205244.2.
DR   AlphaFoldDB; P43449; -.
DR   SMR; P43449; -.
DR   STRING; 9031.ENSGALP00000019361; -.
DR   GeneID; 396172; -.
DR   KEGG; gga:396172; -.
DR   CTD; 890; -.
DR   VEuPathDB; HostDB:geneid_396172; -.
DR   InParanoid; P43449; -.
DR   OrthoDB; 993640at2759; -.
DR   PhylomeDB; P43449; -.
DR   PRO; PR:P43449; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0097124; C:cyclin A2-CDK2 complex; IBA:GO_Central.
DR   GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IBA:GO_Central.
DR   GO; GO:0044843; P:cell cycle G1/S phase transition; ISS:UniProtKB.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0000086; P:G2/M transition of mitotic cell cycle; ISS:UniProtKB.
DR   GO; GO:0044772; P:mitotic cell cycle phase transition; IBA:GO_Central.
DR   GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR   CDD; cd00043; CYCLIN; 2.
DR   InterPro; IPR039361; Cyclin.
DR   InterPro; IPR032447; Cyclin-A_N.
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   Pfam; PF16500; Cyclin_N2; 1.
DR   PIRSF; PIRSF001771; Cyclin_A_B_D_E; 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   Cell cycle; Cell division; Cyclin; Cytoplasm; Mitosis; Nucleus;
KW   Reference proteome.
FT   CHAIN           1..395
FT                   /note="Cyclin-A2"
FT                   /id="PRO_0000080341"
FT   REGION          1..93
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        66..89
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   395 AA;  44080 MW;  42B45DEF0EEA1A45 CRC64;
     MLAEQENQEN VPPAAKAPPP AAGTRVALGL LRGGPARPGP AAQAARNGEG RGAAAGQQQQ
     PFSVYVDEPD EERRRPQRKK ERDEEAADAP GLRAALGTVG ERRPLAPLGN AMELSLDSPS
     IMDISITSEA EERPNVNNVP DYVSDIHTYL REMEVKCKPK IGYMKKQPDI TNNMRAILVD
     WLVEVGEEYK LQNETLHLAV NYIDRFLSSM SVLRGKLQLV GTAAMLLASK FEEIYPPEVA
     EFVYITDDTY NKKQVLRMEH LILKVLSFDL AAPTINQFLT QYFLHQQTNA KVESLSMYLG
     ELTLIDADPY LKYLPSVIAA AAFHLASYTI TGQTWPESLC KVTGYTLEHI KPCLMDLHRT
     YLKAAQHTQQ SIREKYKSTK YHAVSLIDAP ETLDL