CG11_CANAL
ID CG11_CANAL Reviewed; 693 AA.
AC Q59YH3; A0A1D8PN87;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=G1/S-specific cyclin CCN1;
GN Name=CCN1; Synonyms=CLN1; OrderedLocusNames=CAALFM_C501680CA;
GN ORFNames=CaO19.10719, CaO19.3207;
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 IDENTIFICATION.
RX PubMed=7830719; DOI=10.1007/bf00297278;
RA Sherlock G., Bahman A.M., Mahal A., Shieh J.C., Ferreira M., Rosamond J.;
RT "Molecular cloning and analysis of CDC28 and cyclin homologues from the
RT human fungal pathogen Candida albicans.";
RL Mol. Gen. Genet. 245:716-723(1994).
RN [5]
RP FUNCTION.
RX PubMed=10330142; DOI=10.1128/mcb.19.6.4019;
RA Loeb J.D., Sepulveda-Becerra M., Hazan I., Liu H.;
RT "A G1 cyclin is necessary for maintenance of filamentous growth in Candida
RT albicans.";
RL Mol. Cell. Biol. 19:4019-4027(1999).
RN [6]
RP INDUCTION.
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 [7]
RP INTERACTION WITH CDC28, AND FUNCTION.
RX PubMed=17765684; DOI=10.1016/j.devcel.2007.06.011;
RA Sinha I., Wang Y.M., Philp R., Li C.R., Yap W.H., Wang Y.;
RT "Cyclin-dependent kinases control septin phosphorylation in Candida
RT albicans hyphal development.";
RL Dev. Cell 13:421-432(2007).
RN [8]
RP INDUCTION.
RX PubMed=17557192; DOI=10.1007/s11010-007-9516-4;
RA Singh A., Sharma S., Khuller G.K.;
RT "cAMP regulates vegetative growth and cell cycle in Candida albicans.";
RL Mol. Cell. Biochem. 304:331-341(2007).
RN [9]
RP INDUCTION.
RX PubMed=19528234; DOI=10.1128/mcb.01502-08;
RA Wang A., Raniga P.P., Lane S., Lu Y., Liu H.;
RT "Hyphal chain formation in Candida albicans: Cdc28-Hgc1 phosphorylation of
RT Efg1 represses cell separation genes.";
RL Mol. Cell. Biol. 29:4406-4416(2009).
RN [10]
RP FUNCTION OF THE CDC28-CCN1 COMPLEX.
RX PubMed=20639857; DOI=10.1038/emboj.2010.158;
RA Bishop A., Lane R., Beniston R., Chapa-y-Lazo B., Smythe C., Sudbery P.;
RT "Hyphal growth in Candida albicans requires the phosphorylation of Sec2 by
RT the Cdc28-Ccn1/Hgc1 kinase.";
RL EMBO J. 29:2930-2942(2010).
RN [11]
RP FUNCTION.
RX PubMed=23049891; DOI=10.1371/journal.pone.0045912;
RA Chauvel M., Nesseir A., Cabral V., Znaidi S., Goyard S.,
RA Bachellier-Bassi S., Firon A., Legrand M., Diogo D., Naulleau C.,
RA Rossignol T., d'Enfert C.;
RT "A versatile overexpression strategy in the pathogenic yeast Candida
RT albicans: identification of regulators of morphogenesis and fitness.";
RL PLoS ONE 7:E45912-E45912(2012).
CC -!- FUNCTION: G1/S-specific cyclin essential for the control of the cell
CC cycle at the G1/S (start) transition and for maintenance of filamentous
CC growth. Through binding to CDC28 controls the phosphorylation of CDC11
CC and SEC2 upon induction of filamentous growth.
CC {ECO:0000269|PubMed:10330142, ECO:0000269|PubMed:17765684,
CC ECO:0000269|PubMed:20639857, ECO:0000269|PubMed:23049891}.
CC -!- SUBUNIT: Interacts with CDC28. The CDC28-CCN1 complex associates with
CC septin CDC11 upon hyphal induction. {ECO:0000269|PubMed:17765684}.
CC -!- INDUCTION: Expression peaks at G1/S. CCN1 is stabilized during germ
CC tube formation. {ECO:0000269|PubMed:15888543,
CC ECO:0000269|PubMed:17557192, ECO:0000269|PubMed:19528234}.
CC -!- SIMILARITY: Belongs to the cyclin family. {ECO:0000305}.
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DR EMBL; CP017627; AOW29599.1; -; Genomic_DNA.
DR RefSeq; XP_714623.2; XM_709530.2.
DR AlphaFoldDB; Q59YH3; -.
DR SMR; Q59YH3; -.
DR BioGRID; 1226721; 2.
DR STRING; 237561.Q59YH3; -.
DR PRIDE; Q59YH3; -.
DR GeneID; 3643735; -.
DR KEGG; cal:CAALFM_C501680CA; -.
DR CGD; CAL0000199358; CCN1.
DR VEuPathDB; FungiDB:C5_01680C_A; -.
DR eggNOG; KOG0653; Eukaryota.
DR HOGENOM; CLU_029626_0_0_1; -.
DR InParanoid; Q59YH3; -.
DR OrthoDB; 993640at2759; -.
DR PRO; PR:Q59YH3; -.
DR Proteomes; UP000000559; Chromosome 5.
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: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:2000045; P:regulation of G1/S transition of mitotic cell cycle; IEA:InterPro.
DR CDD; cd00043; CYCLIN; 1.
DR InterPro; IPR028857; CCNF_metazoan.
DR InterPro; IPR039361; Cyclin.
DR InterPro; IPR013763; Cyclin-like.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR004367; Cyclin_C-dom.
DR InterPro; IPR014399; Cyclin_CLN.
DR InterPro; IPR006671; Cyclin_N.
DR PANTHER; PTHR10177; PTHR10177; 1.
DR PANTHER; PTHR10177:SF252; PTHR10177:SF252; 1.
DR Pfam; PF02984; Cyclin_C; 1.
DR Pfam; PF00134; Cyclin_N; 1.
DR PIRSF; PIRSF001770; Cyclin_CLN; 1.
DR SMART; SM00385; CYCLIN; 1.
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; Cyclin; Mitosis; Reference proteome.
FT CHAIN 1..693
FT /note="G1/S-specific cyclin CCN1"
FT /id="PRO_0000413034"
FT REGION 273..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 465..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 595..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 662..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 474..560
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 693 AA; 78370 MW; 8539900A01AE63DA CRC64;
MTSLQQQRVK YGPPHHIKRR PYHPILESLE FQTNQHLIQE YSLDIVNTLS QLESLTLVNP
AMIDLQPEIQ WFMRPFLLDF LIELHSSFKL QPTTLFLCLN IIDRYCAKRI VFKRHYQLVG
CTALWIASKY EDKKSRVPTL KELTIMCRNA YDEEMFVQME MHILSTLDWS IGHPTLEDCL
QLAIDSNNLS NNTTNDIENK SVRPNRKSSI SSAVTAVARF LCELSLYDKY FLSVPPSLIA
ITANLLSCSM LQIPHASITL KNLIEQEIIN PQQKKQKKAL SSNSSRTTTA SYTHQNQSDV
RHSSFDEDID LDSGDEEDDD EDYIDEFYET NNYDDTNATT FDESISKSTT VNDENQPPQI
HTPFLSGLDE DSILSIKKIC LMLIIQLSKV TEVLSKKYEN LGVIQVINNF HSNYKFIIQS
IYENQELLLN TINDSTNNNE IDYKLIQSSE ILLQFPKFDE YLTEDEDENV STDDEANSQP
QGYDGSGSDG NNQLFTPKSP NAFSSNSSLT LNNHPQSMVP VTPPSATSQY SLFSNKNNRT
HESTSGLNST CNTPTHISIS SFAPPQPPPG SILKPKLTSI NSTNSLKIKK LTSNSNSSNI
NIHHGHHNTK QEKRYSHISI GSNSSSKYDG FSPIKSISTN GSLITNNGSL ITNNGSFTNI
VNNTNSSSPL MNQQQQQQVT QSSLYQHHHQ YHQ
