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CG21_CANAL
ID   CG21_CANAL              Reviewed;         492 AA.
AC   Q5ALY0; A0A1D8PGE1;
DT   13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=G2/mitotic-specific cyclin CLB2;
GN   Name=CLB2; Synonyms=CYB1; OrderedLocusNames=CAALFM_C201410CA;
GN   ORFNames=CaO19.1446, CaO19.9021;
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 CDC28 AND IQG1, AND FUNCTION.
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).
RN   [7]
RP   FUNCTION.
RX   PubMed=20639412; DOI=10.1128/ec.00038-10;
RA   Ofir A., Kornitzer D.;
RT   "Candida albicans cyclin Clb4 carries S-phase cyclin activity.";
RL   Eukaryot. Cell 9:1311-1319(2010).
RN   [8]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=20123707; DOI=10.1128/iai.00001-10;
RA   McKenzie C.G., Koser U., Lewis L.E., Bain J.M., Mora-Montes H.M.,
RA   Barker R.N., Gow N.A., Erwig L.P.;
RT   "Contribution of Candida albicans cell wall components to recognition by
RT   and escape from murine macrophages.";
RL   Infect. Immun. 78:1650-1658(2010).
RN   [9]
RP   INDUCTION.
RX   PubMed=22090345; DOI=10.1091/mbc.e11-08-0729;
RA   Senn H., Shapiro R.S., Cowen L.E.;
RT   "Cdc28 provides a molecular link between Hsp90, morphogenesis, and cell
RT   cycle progression in Candida albicans.";
RL   Mol. Biol. Cell 23:268-283(2012).
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. Also involved in the
CC       phosphorylation of CDC6 and CDC54. {ECO:0000269|PubMed:15888543,
CC       ECO:0000269|PubMed:18923418, ECO:0000269|PubMed:20639412}.
CC   -!- INDUCTION: Expressed from S phase through G2 and M phases and are
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, ECO:0000269|PubMed:22090345}.
CC   -!- DISRUPTION PHENOTYPE: Impairs macrophage killing during infection.
CC       {ECO:0000269|PubMed:20123707}.
CC   -!- SIMILARITY: Belongs to the cyclin family. Cyclin AB subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CP017624; AOW27187.1; -; Genomic_DNA.
DR   RefSeq; XP_722496.1; XM_717403.1.
DR   AlphaFoldDB; Q5ALY0; -.
DR   SMR; Q5ALY0; -.
DR   BioGRID; 1218934; 5.
DR   IntAct; Q5ALY0; 1.
DR   MINT; Q5ALY0; -.
DR   STRING; 237561.Q5ALY0; -.
DR   PRIDE; Q5ALY0; -.
DR   GeneID; 3635840; -.
DR   KEGG; cal:CAALFM_C201410CA; -.
DR   CGD; CAL0000189817; CLB2.
DR   VEuPathDB; FungiDB:C2_01410C_A; -.
DR   eggNOG; KOG0653; Eukaryota.
DR   HOGENOM; CLU_020695_11_0_1; -.
DR   InParanoid; Q5ALY0; -.
DR   OMA; DYKFIGM; -.
DR   OrthoDB; 993640at2759; -.
DR   PRO; PR:Q5ALY0; -.
DR   Proteomes; UP000000559; Chromosome 2.
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; IDA:CGD.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0030447; P:filamentous growth; IMP:CGD.
DR   GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IBA:GO_Central.
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; IDA: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; Cyclin; Mitosis; Reference proteome.
FT   CHAIN           1..492
FT                   /note="G2/mitotic-specific cyclin CLB2"
FT                   /id="PRO_0000424365"
FT   DOMAIN          208..334
FT                   /note="Cyclin N-terminal"
FT   REGION          1..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..83
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        98..138
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        146..162
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   492 AA;  56799 MW;  8DA096012E50538B CRC64;
     MPQVTKTNNE NEFRLTRSKV QHQESISTIK NTTISNSQHK QQTQQQISSP PQVSVTSSEG
     VSHVNTRQYL GDVSNQYITN AKPTNKRKPL GGDNAPLQKQ QHRPSRPIPI ASDNNNNGST
     SSSSNSSNNN NNDANRLASL AVPSRLPQKR QATESSTNLV EKLRVPQPEV GERSQSYHKK
     SRLIDYEWQD LDEEDSDDQL MVSEYVNEIF SYYYELETRM LPDPQYLFKQ TLLKPRMRSI
     LVDWLVEMHL KFKLLPESLF LAVNVMDRFM SVEVVQIDKL QLLATAALFT AAKYEEVFSP
     SVKNYAYFTD GSYTPEEVVQ AEKYMLTILN FDLNYPNPMN FLRRISKADD YDVQSRTLGK
     YLLEITIVDY KFIGMRPSLC CASAMYLARL ILGKLPVWNG NLIHYSGGYR ISDMRECIEL
     MFQYLIAPIE HDEFFKKYAM RKFMRASTLC RNWAKKFQAS GRDLFDERLS THRLTLEDDD
     EEEEIVVAEA EE
 
 
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