ID   CCNB3_CHICK             Reviewed;         403 AA.
AC   P39963;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=G2/mitotic-specific cyclin-B3;
GN   Name=CCNB3; Synonyms=CYCB3;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8313904; DOI=10.1002/j.1460-2075.1994.tb06297.x;
RA   Gallant P., Nigg E.A.;
RT   "Identification of a novel vertebrate cyclin: cyclin B3 shares properties
RT   with both A- and B-type cyclins.";
RL   EMBO J. 13:595-605(1994).
CC   -!- FUNCTION: Cyclins are positive regulatory subunits of the cyclin-
CC       dependent kinases (CDKs), and thereby play an essential role in the
CC       control of the cell cycle, notably via their destruction during cell
CC       division. Could be involved at the G2/M (mitosis or meiosis)
CC       transition. G2/M cyclins accumulate steadily during G2 and are abruptly
CC       destroyed at mitosis.
CC   -!- SUBUNIT: Interacts with the CDK1 and CDK2 protein kinases.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- DOMAIN: The N-terminal destruction box (D-box) probably acts as a
CC       recognition signal for degradation via the ubiquitin-proteasome
CC       pathway. {ECO:0000250}.
CC   -!- PTM: Ubiquitinated, leading to its degradation. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cyclin family. Cyclin AB subfamily.
CC       {ECO:0000305}.
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DR   EMBL; X75757; CAA53385.1; -; mRNA.
DR   PIR; S41708; S41708.
DR   RefSeq; NP_990570.2; NM_205239.2.
DR   AlphaFoldDB; P39963; -.
DR   SMR; P39963; -.
DR   STRING; 9031.ENSGALP00000041819; -.
DR   GeneID; 396167; -.
DR   KEGG; gga:396167; -.
DR   CTD; 85417; -.
DR   VEuPathDB; HostDB:geneid_396167; -.
DR   eggNOG; KOG0653; Eukaryota.
DR   InParanoid; P39963; -.
DR   OrthoDB; 993640at2759; -.
DR   PhylomeDB; P39963; -.
DR   PRO; PR:P39963; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR   GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IBA:GO_Central.
DR   GO; GO:0019901; F:protein kinase binding; IEA:InterPro.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0044772; P:mitotic cell cycle phase transition; IBA:GO_Central.
DR   GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; IEA:InterPro.
DR   CDD; cd00043; CYCLIN; 2.
DR   InterPro; IPR039361; Cyclin.
DR   InterPro; IPR013763; Cyclin-like.
DR   InterPro; IPR036915; Cyclin-like_sf.
DR   InterPro; IPR015452; Cyclin_B3.
DR   InterPro; IPR004367; Cyclin_C-dom.
DR   InterPro; IPR006671; Cyclin_N.
DR   PANTHER; PTHR10177; PTHR10177; 1.
DR   PANTHER; PTHR10177:SF214; PTHR10177:SF214; 1.
DR   Pfam; PF02984; Cyclin_C; 1.
DR   Pfam; PF00134; Cyclin_N; 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; Nucleus; Reference proteome;
KW   Ubl conjugation.
FT   CHAIN           1..403
FT                   /note="G2/mitotic-specific cyclin-B3"
FT                   /id="PRO_0000080375"
FT   REGION          1..86
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          102..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           51..59
FT                   /note="D-box"
FT   COMPBIAS        1..21
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   403 AA;  45952 MW;  7BDC46808F3F7C1B CRC64;
     MPVARSSKAQ SSKQPRASKA PSVTENVPPE KEEGCQAKRS PSSPQGGPKK RSAFGDITNA
     HKNQVVTGKK EGVKAPTRKA TRAPPAPIVA KNNEINLKKS LRKTPPADVP VEPEKDSVPE
     EPVQQVPVVE DIDKEQLGDP YANAEYAKEI FDYMREREEK FLLPDYMEKQ SDISRDMRAI
     LVDWMVEVQE NFELNHETLY LAVKLVDHYL VEVVSMRDKL QLIGSTAVLI ASKFEERCPP
     CVDDFLYICD DAYKREELIA METSILRTLN FDINIPIPYR FLRRFAKCAR ASMETLTLAR
     FVCEMTLQEY DYARERPSKL AASSLLLALT MKNLGGWTPT LEYYSGYCAQ DLHPLVKRLN
     FLLTYQPCDK LKAVRTKYSH RVFFEVAKTT PMDMMKLEEK LKS