CCNB3_CAEEL
ID CCNB3_CAEEL Reviewed; 385 AA.
AC Q10654; Q95ZP8; Q9U378;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=G2/mitotic-specific cyclin-B3;
GN Name=cyb-3; Synonyms=cyb-2; ORFNames=T06E6.2;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RC STRAIN=Bristol N2;
RX PubMed=7545687; DOI=10.1242/jcs.108.6.2415;
RA Kreutzer M.A., Richards J.P., de Silva-Udawatta M.N., Temenak J.J.,
RA Knoblich J.A., Lehner C.F., Bennett K.L.;
RT "Caenorhabditis elegans cyclin A- and B-type genes: a cyclin A multigene
RT family, an ancestral cyclin B3 and differential germline expression.";
RL J. Cell Sci. 108:2415-2424(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20599902; DOI=10.1016/j.ydbio.2010.06.016;
RA Fortin S.M., Marshall S.L., Jaeger E.C., Greene P.E., Brady L.K.,
RA Isaac R.E., Schrandt J.C., Brooks D.R., Lyczak R.;
RT "The PAM-1 aminopeptidase regulates centrosome positioning to ensure
RT anterior-posterior axis specification in one-cell C. elegans embryos.";
RL Dev. Biol. 344:992-1000(2010).
CC -!- FUNCTION: Could be involved at the G2/M (mitosis) transition
CC (Probable). Interacts with the CDK1 and CDK2 protein kinases
CC (Probable). G2/M cyclins accumulate steadily during G2 and are abruptly
CC destroyed at mitosis (Probable). Plays a role during oocyte meiosis II
CC (PubMed:20599902). {ECO:0000269|PubMed:20599902, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=Q10654-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q10654-2; Sequence=VSP_041644;
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes a longer meiosis
CC II in 1-cell embryos without affecting meiotic exit timing. In a pam-1
CC (or282) mutant background, restores normal timing for meiotic exit.
CC {ECO:0000269|PubMed:20599902}.
CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin AB subfamily.
CC {ECO:0000305}.
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DR EMBL; U21282; AAA84395.1; -; mRNA.
DR EMBL; Z81117; CAB03311.2; -; Genomic_DNA.
DR EMBL; Z81117; CAC42336.2; -; Genomic_DNA.
DR PIR; T24596; T24596.
DR RefSeq; NP_001024112.2; NM_001028941.3. [Q10654-2]
DR RefSeq; NP_506825.4; NM_074424.6. [Q10654-1]
DR AlphaFoldDB; Q10654; -.
DR SMR; Q10654; -.
DR BioGRID; 45035; 3.
DR DIP; DIP-25112N; -.
DR IntAct; Q10654; 1.
DR STRING; 6239.T06E6.2a.2; -.
DR EPD; Q10654; -.
DR PaxDb; Q10654; -.
DR PeptideAtlas; Q10654; -.
DR EnsemblMetazoa; T06E6.2a.1; T06E6.2a.1; WBGene00000868. [Q10654-1]
DR EnsemblMetazoa; T06E6.2a.2; T06E6.2a.2; WBGene00000868. [Q10654-1]
DR EnsemblMetazoa; T06E6.2b.1; T06E6.2b.1; WBGene00000868. [Q10654-2]
DR GeneID; 180040; -.
DR KEGG; cel:CELE_T06E6.2; -.
DR UCSC; T06E6.2a.1; c. elegans. [Q10654-1]
DR CTD; 180040; -.
DR WormBase; T06E6.2a; CE45171; WBGene00000868; cyb-3. [Q10654-1]
DR WormBase; T06E6.2b; CE45189; WBGene00000868; cyb-3. [Q10654-2]
DR eggNOG; KOG0653; Eukaryota.
DR GeneTree; ENSGT00940000160459; -.
DR InParanoid; Q10654; -.
DR OMA; VEPLMWE; -.
DR OrthoDB; 993640at2759; -.
DR PhylomeDB; Q10654; -.
DR PRO; PR:Q10654; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00000868; Expressed in embryo and 4 other tissues.
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; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IDA:WormBase.
DR GO; GO:0019901; F:protein kinase binding; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007098; P:centrosome cycle; IMP:WormBase.
DR GO; GO:0051383; P:kinetochore organization; IMP:WormBase.
DR GO; GO:0051321; P:meiotic cell cycle; IMP:UniProtKB.
DR GO; GO:0045144; P:meiotic sister chromatid segregation; IMP:WormBase.
DR GO; GO:0000278; P:mitotic cell cycle; IMP:WormBase.
DR GO; GO:0044772; P:mitotic cell cycle phase transition; IBA:GO_Central.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IMP:WormBase.
DR GO; GO:0045138; P:nematode male tail tip morphogenesis; IMP:UniProtKB.
DR GO; GO:0001556; P:oocyte maturation; IGI:WormBase.
DR GO; GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; IMP:WormBase.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:WormBase.
DR GO; GO:0035046; P:pronuclear migration; IMP:WormBase.
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 GO; GO:0051445; P:regulation of meiotic cell cycle; IMP:UniProtKB.
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.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell cycle; Cell division; Cyclin; Meiosis; Mitosis;
KW Nucleus; Reference proteome.
FT CHAIN 1..385
FT /note="G2/mitotic-specific cyclin-B3"
FT /id="PRO_0000080381"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 63..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..84
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 16
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_041644"
SQ SEQUENCE 385 AA; 44757 MW; 74CEDA847A76E695 CRC64;
MMLRSQAKNV DLTSQADSRH QQKRKQAEQL DALKNPSEPA AKKQHSKGLT ELRAHISGFK
IDSAKRDPLG KSRTSRRDVE NLPPQKSRYV DPCPHYDYDL EEAGNPDSIS DYAQGIFDYY
RHREVHFRVR KYLHKHPEVD VKTRAILIDW MVEIQETFEL NHETLYNAVK LTDMYLCKTK
NVDKNTIQKL ACVAIFIAAK YDERSPPLVD DLIYLSGDRF SRDELLAMER ELFATVGYDL
GSPLSYRYLR RFGRVCRVDM KTLTMGRFIL ETSLMVYEYA MVSQSRLAAA AFVLAMRMLD
KNNEYEWNPV LEKYSGFTGE EVMPLVEHMN HILHFSKDKW AQLTSVRQKY SHEVFFHVAS
IPMLPDTLKV VDSHTYAPVP MLSYP
