ID   CCNA1_CARAU             Reviewed;         391 AA.
AC   Q92161;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Cyclin-A1;
DE            Short=Cyclin-A;
GN   Name=ccna1; Synonyms=ccna;
OS   Carassius auratus (Goldfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Cyprininae; Carassius.
OX   NCBI_TaxID=7957;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Ovary;
RX   PubMed=7649388; DOI=10.1006/dbio.1995.1241;
RA   Katsu Y., Yamashita M., Hirai T., Tokumoto T., Kajiura H., Nagahama Y.;
RT   "Molecular cloning and immunological analysis of goldfish cyclin A during
RT   oocyte maturation.";
RL   Dev. Biol. 170:616-625(1995).
CC   -!- FUNCTION: May be involved in the control of the cell cycle at the G1/S
CC       (start) and G2/M (mitosis) transitions. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with the CDK1 and the CDK2 protein kinases to form a
CC       serine/threonine kinase holoenzyme complex. The cyclin subunit imparts
CC       substrate specificity to the complex (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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; S79215; AAB35103.1; -; mRNA.
DR   AlphaFoldDB; Q92161; -.
DR   SMR; Q92161; -.
DR   Ensembl; ENSCART00000008208; ENSCARP00000007757; ENSCARG00000003581.
DR   Proteomes; UP000515129; Genome assembly.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   CDD; cd00043; CYCLIN; 1.
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   2: Evidence at transcript level;
KW   Cell cycle; Cell division; Cyclin; Mitosis; Nucleus; Reference proteome.
FT   CHAIN           1..391
FT                   /note="Cyclin-A1"
FT                   /id="PRO_0000080336"
SQ   SEQUENCE   391 AA;  43594 MW;  00402E02AFCB45F3 CRC64;
     MASRGFAPLS GRQENIMVLG RADGLHALKP GQRVVLGVLT ENDQHNRVFG QVSSKYVPAL
     RDASTLDVST SSATLGVHVV EPVIAQATKP TSFLLPSELL LVDDVVQDLG SGSCMDSSMQ
     SLPEEAAYED ILCVPEYAED IHRYLRECEV KYRPKPGYMR KQPDITNCMR VILVDWLVEV
     GEEYKLCSET LFLAVNYLDR FLSCMSVLRG KLQLVGTAAV LLAAKYEEVY PPEVDEFVYI
     TDDTYTKKQL LRMEQHLLRV LAFDMTAPTV HQFLMQYTLE GHICARTVNL ALYLSELSLL
     EVDPFVQYLP SKTAAAAYCL ANYTLNGVLW PENLYAFTGY SLAVIIPCLM ELHKLHLGAA
     GRPQQAIQEK YKGSKYCGVS LLEPVESLPL P