ID   CCNB3_CANLF             Reviewed;        1330 AA.
AC   Q659K0;
DT   09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=G2/mitotic-specific cyclin-B3;
GN   Name=CCNB3;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Cocker spaniel; TISSUE=Kidney;
RA   Lozano J.-C., Guyon R., Schatt P., Andre C., Picard A.;
RT   "Molecular phylogeny of cyclin B3.";
RL   Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
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. Its tissue specificity suggest that it may be required during
CC       early meiotic prophase I (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with CDK2 kinase. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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 (Probable). Ubiquitination leads to its degradation
CC       during anaphase entry, after degradation of CCNB1 (By similarity).
CC       {ECO:0000250, ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the cyclin family. Cyclin AB subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AJ833648; CAH55770.1; -; mRNA.
DR   RefSeq; NP_001005763.1; NM_001005763.1.
DR   AlphaFoldDB; Q659K0; -.
DR   SMR; Q659K0; -.
DR   STRING; 9612.ENSCAFP00000023556; -.
DR   PaxDb; Q659K0; -.
DR   PRIDE; Q659K0; -.
DR   GeneID; 449494; -.
DR   KEGG; cfa:449494; -.
DR   CTD; 85417; -.
DR   eggNOG; KOG0653; Eukaryota.
DR   InParanoid; Q659K0; -.
DR   OrthoDB; 993640at2759; -.
DR   Proteomes; UP000002254; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0019901; F:protein kinase binding; IEA:InterPro.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IEA:InterPro.
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   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; Meiosis; Nucleus; Reference proteome;
KW   Ubl conjugation.
FT   CHAIN           1..1330
FT                   /note="G2/mitotic-specific cyclin-B3"
FT                   /id="PRO_0000080372"
FT   REGION          1..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1002..1059
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           54..62
FT                   /note="D-box"
FT   COMPBIAS        19..33
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1002..1051
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1330 AA;  152093 MW;  1BFD81DB5F911E79 CRC64;
     MPLPLPSRSS KPETKKSRSS KIVPSGNNGQ SEKRGENYQE KISSSSPRRL CKKRSAFEDL
     TNASQSQPAQ LKKEANKEFV KDVPKKIKGN TPALGLAKSN EVNMVSYKLE SSPGVVSTTL
     VPNITEKPLI LERSTTSGTI TTEEASFFRK PLILKEESTT EDTGLIKRSL FLKKFTNKGE
     ISLMEKPTSV QEEADSNDEF VVKLITFGKK HKTEEVAITK GTLSLKKMCT YQEDLALQDI
     TVEENSFFME PTNFRKKPKT DDVTPTKKML SLKKKKYITL GKVSRMKKPL VLQKTNSEDE
     SPLIKEPLAF KKKPTKKETT FTLRPLSLKK YTTQGKMAHL KKPLESQNTS GEKALIKEPL
     SFKKKPITKE ESLFQEFSAS QEKHTTDREV VLLKKPQVLQ EEKDSKDKFL MEPMFLRKKC
     TTKETNPTKK PLPIKKKCTI QGKMYYLKKP LVLQKTTPGE ESFVKEPLSF KKNTTELSML
     QEKYTTQEEV SVLKKALTLQ KTLTEEESHL KEPLAFKKKH TTEEATPTKK LSSLKRKRFT
     AQGKRSCLMK PLVLQTSSGE KTHIKEPLSF KKRSAIEESF FKESPVLQEK HTMQGEVALL
     EKPGALQENV SSEDEFLMEP ISFRKTHTTN EVVSTKEPLS LKKKKCTTQI TMSICQELLD
     LQNIISKDKA SFFMEPVSLR EKSLAEEVIL TKTPLSLKKK EITQGKIFLL KKPLVSEKTT
     SEEESLFKKL LPFNKKSTTE GEFLFQDPSV LQEKHTTPQE VSLSTKPLTL PEKTTTEEEP
     YIKEPLTLEE RPTTKEEFLS QEPFSLHAKP TNEDESLFWK ALGLQKTQTK EDSLKKLLTL
     QEKNTTDEES LLNKPSILKE ELSTKVATSI EKELSLKKKP TAQGEVFLLK KQLALQENIT
     NEESLIKQPL AFLKPSIEEA ILRESLALQE KPRSEEETLF KEPLSFQEKP TLNEAFHFKE
     IISLNEKHST GKELSLKEPL ALQENPTQKE DTSLEDSLIL QVETSSRVPS TPPESRAGMS
     SVGKLSTTSK SSVCESSSNK PSSSWGESSQ KEMTPLEDID RNHGDPFFNS IYAKDIFSYM
     KEREEKFILK EYMNKQTDIS SCMRAILVDW LVEVQMTFEM SHETLYLAVK LVDHYLMEVI
     CKRDKLQLLG STAFLIAAKF EEPCPPCVDD FLYICDDIYQ RHEMLSMEIS ILQTLKFDIN
     IPIAYHFLRR YARCLHASMK TLTLSRFICE MTLQEYDYVQ ERASKLAAGS FLLALYMMKL
     RYWVPALEYY SGYKTSDLHP LVKQLNILLT LRPSNKLKTV YSKYSHQVFF EATKIPPLDM
     LKLEEILNYC