ID   CCNA2_XENLA             Reviewed;         415 AA.
AC   P47827;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=Cyclin-A2 {ECO:0000305};
DE            Short=Cyclin-A {ECO:0000303|PubMed:7758942};
GN   Name=ccna2;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Ovary;
RX   PubMed=7758942; DOI=10.1101/gad.9.10.1164;
RA   Howe J., Howell M., Hunt T., Newport J.;
RT   "Identification of a developmental timer regulating the stability of
RT   embryonic cyclin A and a new somatic A-type cyclin at gastrulation.";
RL   Genes Dev. 9:1164-1176(1995).
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:0000250|UniProtKB:P20248}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P20248}. Cytoplasm
CC       {ECO:0000250|UniProtKB:P20248}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:7758942}.
CC   -!- DEVELOPMENTAL STAGE: Accumulates steadily during G2 and is abruptly
CC       destroyed at mitosis. {ECO:0000269|PubMed:7758942}.
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; X85746; CAA59748.1; -; mRNA.
DR   PIR; I51637; I51637.
DR   AlphaFoldDB; P47827; -.
DR   SMR; P47827; -.
DR   OMA; QDLHQTY; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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   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   2: Evidence at transcript level;
KW   Cell cycle; Cell division; Cyclin; Cytoplasm; Mitosis; Nucleus;
KW   Reference proteome.
FT   CHAIN           1..415
FT                   /note="Cyclin-A2"
FT                   /id="PRO_0000080342"
SQ   SEQUENCE   415 AA;  46670 MW;  B0D5300093A1764D CRC64;
     MSDHLLRDEH QENVQPRKLL VPVGGRTVLG VLQENHRGPK ALKVSKPALQ QTQVLSVNHL
     GVNDENYGKI PARKAASKQP AFTIHVDEPD CATNKRKAVH KKTVQDENLQ QLNSVLGSIG
     TRKPLHPIQI AMETSFGSPM DVSIVDEEQK VVGCNNVADY AKEIHTYLRE MEVKCKPKAG
     YMQKQPDITG NMRAILVDWL VEVGEEYKLQ NETLYLAVNY IDRFLSSMSV LRGKLQLVGT
     AAMLLASKFE EIYPPEVAEF VYITDDTYTK KQVLKMEHLV LKVLSFDLAA PTILQYLNQY
     FQIHPVSPKV ESLSMFLGEL SLVDADPFLR YLPSVVAAAA FVIANCTINE RTWSDPLVEY
     TSYTLETLKP CILDLYQTYL SAASHQQQAV REKYKAPKNH AVSLIIPPES MSTFL