CG24_CANAL
ID CG24_CANAL Reviewed; 486 AA.
AC Q5A0A9; A0A1D8PRH5; Q3MNW4;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=G2/mitotic-specific cyclin-4;
GN Name=CLB4; Synonyms=CYB2; OrderedLocusNames=CAALFM_C703940CA;
GN ORFNames=CaO19.7186;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP INDUCTION, AND FUNCTION.
RX PubMed=15888543; DOI=10.1091/mbc.e04-12-1081;
RA Bensen E.S., Clemente-Blanco A., Finley K.R., Correa-Bordes J., Berman J.;
RT "The mitotic cyclins Clb2p and Clb4p affect morphogenesis in Candida
RT albicans.";
RL Mol. Biol. Cell 16:3387-3400(2005).
RN [5]
RP INTERACTION WITH IQG1.
RX PubMed=18923418; DOI=10.1038/emboj.2008.219;
RA Li C.R., Wang Y.M., Wang Y.;
RT "The IQGAP Iqg1 is a regulatory target of CDK for cytokinesis in Candida
RT albicans.";
RL EMBO J. 27:2998-3010(2008).
RN [6]
RP INDUCTION.
RX PubMed=20064588; DOI=10.1016/j.bbagen.2010.01.001;
RA Wu X.Z., Chang W.Q., Cheng A.X., Sun L.M., Lou H.X.;
RT "Plagiochin E, an antifungal active macrocyclic bis(bibenzyl), induced
RT apoptosis in Candida albicans through a metacaspase-dependent apoptotic
RT pathway.";
RL Biochim. Biophys. Acta 1800:439-447(2010).
CC -!- FUNCTION: 2/mitotic-specific cyclin essential for the control of the
CC cell cycle at the G2/M (mitosis) transition. G2/M cyclins accumulate
CC steadily during G2 and are abruptly destroyed at mitosis. Degradation
CC is necessary for the cell to exit from mitosis. Plays a role in
CC morphogenesis by negatively regulating polarized growth. Through
CC binding to CDC28 regulates cytokinesis, partly by phosphorylation of
CC the actomyosin ring component IQG1. {ECO:0000269|PubMed:15888543}.
CC -!- SUBUNIT: Interacts with IQG1. {ECO:0000269|PubMed:18923418}.
CC -!- INDUCTION: Expressed from S phase through G2 and M phases and is
CC degraded at the end of mitosis. Expression is down-regulated by the
CC anti-fungal agent plagiochin E (PLE). {ECO:0000269|PubMed:15888543,
CC ECO:0000269|PubMed:20064588}.
CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin AB subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP017629; AOW30733.1; -; Genomic_DNA.
DR RefSeq; XP_715235.1; XM_710142.1.
DR AlphaFoldDB; Q5A0A9; -.
DR SMR; Q5A0A9; -.
DR BioGRID; 1226196; 2.
DR IntAct; Q5A0A9; 1.
DR MINT; Q5A0A9; -.
DR STRING; 237561.Q5A0A9; -.
DR PRIDE; Q5A0A9; -.
DR GeneID; 3643102; -.
DR KEGG; cal:CAALFM_C703940CA; -.
DR CGD; CAL0000175354; CLB4.
DR VEuPathDB; FungiDB:C7_03940C_A; -.
DR eggNOG; KOG0653; Eukaryota.
DR HOGENOM; CLU_020695_12_0_1; -.
DR InParanoid; Q5A0A9; -.
DR OMA; NTHIPMQ; -.
DR OrthoDB; 993640at2759; -.
DR Proteomes; UP000000559; Chromosome 7.
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; IMP:CGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0030447; P:filamentous growth; IMP:CGD.
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; IMP:CGD.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IMP:CGD.
DR CDD; cd00043; CYCLIN; 2.
DR InterPro; IPR039361; Cyclin.
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 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 1: Evidence at protein level;
KW Cell cycle; Cell division; Coiled coil; Cyclin; Mitosis;
KW Reference proteome.
FT CHAIN 1..486
FT /note="G2/mitotic-specific cyclin-4"
FT /id="PRO_0000424605"
FT DOMAIN 234..359
FT /note="Cyclin N-terminal"
FT REGION 1..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 105..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 122..184
FT /evidence="ECO:0000255"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..123
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 486 AA; 57249 MW; 1743090E4312FFA7 CRC64;
MRSYKSSITD ENELTKQRLR AKSIANLSSN HTTAGQPSTS SQHREALTDL TSQENKNHPR
VKLTQTNTNH HRNSSSSSNK IQIYQQIEQK KTDIHQFKKP RLEKVLLNDD DDETDDEFDD
EEDKENRYHD LELNEDDSKH QLISEAFETI DDRGISEGEN DTAQEARERL EEETQSHTQD
MRSIYGVHVP MQPMWNNAII NELKYVIQKY SRNTLDENDE DTYDTTMVAE YSPEIFNYLH
ELENKFTPDP NYMDFQDDLK WEMRAVLIDW VVQVHARFNL FSETLYLTVN YIDRFLSKRR
VSLSRFQLVG AVALFIAAKY EEINCPTVQE IAYMADNAYS IDEFLKAERF MIDVLEFDLG
WPGPMSFLRR ISKADDYDYE TRTLAKYFLE ITIMDSKFVA SPPSWLAAGA HYISRILLGR
GEWTELHVFY SGYTEKQLQP LADVLLENCR HAEINHKAIF EKYKERRYRK SSLFVQEYFR
HIMSQS
