ID   CCNA_SPISO              Reviewed;         422 AA.
AC   P04962;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   25-MAY-2022, entry version 104.
DE   RecName: Full=G2/mitotic-specific cyclin-A;
OS   Spisula solidissima (Atlantic surf-clam).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC   Autobranchia; Heteroconchia; Euheterodonta; Imparidentia; Neoheterodontei;
OC   Venerida; Mactroidea; Mactridae; Spisula.
OX   NCBI_TaxID=6584;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2946420; DOI=10.1016/0092-8674(86)90801-9;
RA   Swenson K.I., Farrell K.M., Ruderman J.V.;
RT   "The clam embryo protein cyclin A induces entry into M phase and the
RT   resumption of meiosis in Xenopus oocytes.";
RL   Cell 47:861-870(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2148535; DOI=10.1101/gad.4.12a.2157;
RA   Standart N.M., Dale M., Stewart E., Hunt T.;
RT   "Maternal mRNA from clam oocytes can be specifically unmasked in vitro by
RT   antisense RNA complementary to the 3'-untranslated region.";
RL   Genes Dev. 4:2157-2168(1990).
CC   -!- FUNCTION: Essential for the control of the cell cycle at the G2/M
CC       (mitosis) transition. Interacts with the CDC2 and CDK2 protein kinases
CC       to form MPF. G2/M cyclins accumulate steadily during G2 and are
CC       abruptly destroyed at mitosis.
CC   -!- SIMILARITY: Belongs to the cyclin family. Cyclin AB subfamily.
CC       {ECO:0000305}.
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DR   EMBL; M14535; AAA98921.1; -; mRNA.
DR   EMBL; X55127; CAA38921.1; -; mRNA.
DR   PIR; A26328; A26328.
DR   AlphaFoldDB; P04962; -.
DR   SMR; P04962; -.
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   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; Mitosis.
FT   CHAIN           1..422
FT                   /note="G2/mitotic-specific cyclin-A"
FT                   /id="PRO_0000080347"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   422 AA;  47778 MW;  C6C0003303A1267F CRC64;
     MSQPFALHHD GENQMQRRGK MNTRSNGLSG QKRAALGVIT NQVNQQVRIQ PSRAAKPKSS
     EFNIQDENAF TKKNAKTFGQ QPSQFSVFVD PTPAAPVQKA PTSHVTDIPA ALTTLQRVPL
     TEVPGSPDII SLEDSMESPM ILDLPEEEKP LDREAVILTV PEYEEDIYNY LRQAEMKNRA
     KPGYMKRQTD ITTSMRCILV DWLVEVSEED KLHRETLFLG VNYIDRFLSK ISVLRGKLQL
     VGAASMFLAA KYEEIYPPDV KEFAYITDDT YTSQQVLRME HLILKVLTFD VAVPTTNWFC
     EDFLKSCDAD DKLKSLTMFL TELTLIDMDA YLKYLPSITA AAALCLARYS LGIEPWPQNL
     VKKTGYEIGH FVDCLKDLHK TSLGAESHQQ QAVQEKYKQD KYHQVSDFSK NPVPHNLALL
     AL