ID   CCNA1_XENLA             Reviewed;         418 AA.
AC   P18606;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=Cyclin-A1;
GN   Name=ccna1;
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].
RC   TISSUE=Ovary;
RX   PubMed=2143983; DOI=10.1002/j.1460-2075.1990.tb07476.x;
RA   Minshull J., Golsteyn R., Hill C.S., Hunt T.;
RT   "The A- and B-type cyclin associated cdc2 kinases in Xenopus turn on and
RT   off at different times in the cell cycle.";
RL   EMBO J. 9:2865-2875(1990).
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   -!- DEVELOPMENTAL STAGE: Present in eggs and early embryos but cannot be
CC       detected in late embryos.
CC   -!- SIMILARITY: Belongs to the cyclin family. Cyclin AB subfamily.
CC       {ECO:0000305}.
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DR   EMBL; X53745; CAA37775.1; -; mRNA.
DR   PIR; S11678; S11678.
DR   AlphaFoldDB; P18606; -.
DR   SMR; P18606; -.
DR   ELM; P18606; -.
DR   Proteomes; UP000186698; 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; 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   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..418
FT                   /note="Cyclin-A1"
FT                   /id="PRO_0000080335"
SQ   SEQUENCE   418 AA;  46773 MW;  FEA0B7A1F8011E6A CRC64;
     MRRSMASNGH ILTASSVVGA SSAFQNPCLA KVEVQPNLPQ RTVLGVIGDN EQRRRSVSRG
     GVPAKSLPGI ENVLAFPGKI LSANPAPVAP KPSFTVYVDE PTETYSVEID CPSLGDEDSN
     IVKQNIHLLL DISEASPMVV DTSPQTSPED DSVTDPDAVA VSEYIHEIHQ YLREAELKHR
     PKAYYMRKQP DITSAMRTIL VDWLVEVGEE YKLHTETLYL AMNYLDRFLS CMSVLRGKLQ
     LVGTAAILLA SKYEEIYPPD VDEFVYITDD TYSKKQLLRM EHVLLKVLAF DLTVPTVNQF
     LLQYLQRHAV SVKMEHLAMY MAELTLLEVE PFLKYVPSLT AAAAYCLANY ALNKVFWPDT
     LEAFTGYALS DIAPCLSDLH QFCLGAPYQA QQAIREKYKT TKYMQVSLLE MPSILPLN