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Database: UniProt
Entry: I3IYJ9_ORENI
LinkDB: I3IYJ9_ORENI
Original site: I3IYJ9_ORENI 
ID   I3IYJ9_ORENI            Unreviewed;       434 AA.
AC   I3IYJ9;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   RecName: Full=Cyclin-A2 {ECO:0000256|ARBA:ARBA00019673};
GN   Name=ccna2 {ECO:0000313|Ensembl:ENSONIP00000001689.1};
OS   Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX   NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000001689.1, ECO:0000313|Proteomes:UP000005207};
RN   [1] {ECO:0000313|Proteomes:UP000005207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Broad Institute Genome Assembly Team;
RG   Broad Institute Sequencing Platform;
RA   Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSONIP00000001689.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Essential for the control of the cell cycle at the G2/M
CC       (mitosis) transition. {ECO:0000256|ARBA:ARBA00003222}.
CC   -!- SUBUNIT: Interacts with the CDK1 protein kinase to form a
CC       serine/threonine kinase holoenzyme complex also known as maturation
CC       promoting factor (MPF). The cyclin subunit imparts substrate
CC       specificity to the complex. {ECO:0000256|ARBA:ARBA00025821}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the cyclin family.
CC       {ECO:0000256|RuleBase:RU000383}.
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DR   RefSeq; XP_003443464.1; XM_003443416.3.
DR   RefSeq; XP_005467294.1; XM_005467237.2.
DR   AlphaFoldDB; I3IYJ9; -.
DR   STRING; 8128.ENSONIP00000001689; -.
DR   Ensembl; ENSONIT00000001688.2; ENSONIP00000001689.1; ENSONIG00000001338.2.
DR   GeneID; 100711022; -.
DR   KEGG; onl:100711022; -.
DR   CTD; 890; -.
DR   eggNOG; KOG0654; Eukaryota.
DR   GeneTree; ENSGT00940000155372; -.
DR   HOGENOM; CLU_020695_3_2_1; -.
DR   InParanoid; I3IYJ9; -.
DR   OMA; HQPFSIH; -.
DR   OrthoDB; 5474295at2759; -.
DR   TreeFam; TF101002; -.
DR   Proteomes; UP000005207; Linkage group LG2.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IEA:InterPro.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0044772; P:mitotic cell cycle phase transition; IEA:InterPro.
DR   CDD; cd20561; CYCLIN_CCNA2_rpt1; 1.
DR   CDD; cd20564; CYCLIN_CCNA2_rpt2; 1.
DR   Gene3D; 1.10.472.10; Cyclin-like; 2.
DR   InterPro; IPR039361; Cyclin.
DR   InterPro; IPR032447; Cyclin-A_N.
DR   InterPro; IPR013763; Cyclin-like_dom.
DR   InterPro; IPR036915; Cyclin-like_sf.
DR   InterPro; IPR046965; Cyclin_A/B-like.
DR   InterPro; IPR004367; Cyclin_C-dom.
DR   InterPro; IPR006671; Cyclin_N.
DR   InterPro; IPR048258; Cyclins_cyclin-box.
DR   PANTHER; PTHR10177:SF444; CYCLIN-A2; 1.
DR   PANTHER; PTHR10177; CYCLINS; 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; Cyclin-like; 2.
DR   PROSITE; PS00292; CYCLINS; 1.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618};
KW   Cyclin {ECO:0000256|ARBA:ARBA00023127, ECO:0000256|RuleBase:RU000383};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005207}.
FT   DOMAIN          218..302
FT                   /note="Cyclin-like"
FT                   /evidence="ECO:0000259|SMART:SM00385"
FT   DOMAIN          311..428
FT                   /note="Cyclin C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01332"
FT   DOMAIN          315..397
FT                   /note="Cyclin-like"
FT                   /evidence="ECO:0000259|SMART:SM00385"
FT   REGION          1..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..24
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   434 AA;  48432 MW;  D496CADD582899C1 CRC64;
     MSGANRAQGS AASDYQNQEN VLQRLRGSLK ARPVASENQE NLPPKQAANR TVLGALQNNQ
     RNKSQVGGKQ DSTQSLSCKN EDFGKSCFDK PLAKQPAFQI HIDEPDGACI KKPQQAVESI
     KAKPTVEESP LAINAVARLR QPLATIEIPS AMDVSFDSPM DMSVVEGEEK PVNVNEAPEY
     AAEIHSYLRE MEVKTRPKAG YMKKQPDITN SMRAILVDWL VEVGEEYKLQ NETLYLAVNY
     IDRFLSSMSV LRGKLQLVGT AAMLLASKFE EIYPPEVAEF VYITDDTYTK KQVLRMEHLV
     LKVLSFDLAS PTINQFLTQY FLQHTVTKQV ESLAMYLGEL SLVDSDPFLK YLPSQTAAAA
     YILANTTVTG ASWPKSLNEM TGYSLEDLMP CIEDLHRTYL NAPQHAQQSV REKYKGSKYH
     EVSSINAPTK LQLN
//
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