CDT2_SCHPO
ID CDT2_SCHPO Reviewed; 490 AA.
AC Q10990;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Cell division cycle protein cdt2;
GN Name=cdt2; ORFNames=SPAC17H9.19c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Hofmann J.F.X., Beach D.;
RT "cdt2 is a novel target of the Cdc10 transcription factor: coupling START
RT with cytokinesis.";
RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12871901; DOI=10.1093/genetics/164.3.881;
RA Yoshida S.-H., Al-Amodi H., Nakamura T., McInerny C.J., Shimoda C.;
RT "The Schizosaccharomyces pombe cdt2(+) gene, a target of G1-S phase-
RT specific transcription factor complex DSC1, is required for mitotic and
RT premeiotic DNA replication.";
RL Genetics 164:881-893(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [4]
RP FUNCTION.
RX PubMed=16252005; DOI=10.1038/sj.emboj.7600854;
RA Liu C., Poitelea M., Watson A., Yoshida S.H., Shimoda C., Holmberg C.,
RA Nielsen O., Carr A.M.;
RT "Transactivation of Schizosaccharomyces pombe cdt2+ stimulates a Pcu4-Ddb1-
RT CSN ubiquitin ligase.";
RL EMBO J. 24:3940-3951(2005).
RN [5]
RP FUNCTION.
RX PubMed=17039252; DOI=10.1038/sj.embor.7400827;
RA Ralph E., Boye E., Kearsey S.E.;
RT "DNA damage induces Cdt1 proteolysis in fission yeast through a pathway
RT dependent on Cdt2 and Ddb1.";
RL EMBO Rep. 7:1134-1139(2006).
CC -!- FUNCTION: Substrate-specific adapter of a DCX (DDB1-CUL4-X-box) E3
CC ubiquitin-protein ligase complex required for DNA replication during
CC mitosis and meiosis. The DCX(DTL) complex, also named CRL4(CDT2)
CC complex, mediates the polyubiquitination and subsequent degradation of
CC cdt1 and spd1. Involved in the regulation of mitotic and pre-meiotic S-
CC phase progression. {ECO:0000269|PubMed:12871901,
CC ECO:0000269|PubMed:16252005, ECO:0000269|PubMed:17039252}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Component of the DCX(DTL) E3 ubiquitin ligase complex, at
CC least composed of cul4, ddb1, cdt2 and pip1.
CC -!- INTERACTION:
CC Q10990; O94308: csn1; NbExp=2; IntAct=EBI-3505190, EBI-3647868;
CC Q10990; O13807: ddb1; NbExp=4; IntAct=EBI-3505190, EBI-3647902;
CC Q10990; O94603: jhd1; NbExp=2; IntAct=EBI-3505190, EBI-3505187;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12871901}.
CC -!- SIMILARITY: Belongs to the WD repeat cdt2 family. {ECO:0000305}.
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DR EMBL; L75944; AAA85478.1; -; mRNA.
DR EMBL; CU329670; CAB11228.1; -; Genomic_DNA.
DR PIR; T37884; T37884.
DR RefSeq; NP_593588.1; NM_001019020.2.
DR AlphaFoldDB; Q10990; -.
DR SMR; Q10990; -.
DR BioGRID; 278838; 256.
DR IntAct; Q10990; 10.
DR STRING; 4896.SPAC17H9.19c.1; -.
DR iPTMnet; Q10990; -.
DR PaxDb; Q10990; -.
DR PRIDE; Q10990; -.
DR EnsemblFungi; SPAC17H9.19c.1; SPAC17H9.19c.1:pep; SPAC17H9.19c.
DR GeneID; 2542374; -.
DR KEGG; spo:SPAC17H9.19c; -.
DR PomBase; SPAC17H9.19c; cdt2.
DR VEuPathDB; FungiDB:SPAC17H9.19c; -.
DR eggNOG; KOG0321; Eukaryota.
DR HOGENOM; CLU_555698_0_0_1; -.
DR InParanoid; Q10990; -.
DR OMA; DSRVHTY; -.
DR PhylomeDB; Q10990; -.
DR Reactome; R-SPO-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR Reactome; R-SPO-8951664; Neddylation.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q10990; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:PomBase.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IPI:PomBase.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:2000779; P:regulation of double-strand break repair; IMP:PomBase.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:PomBase.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF00400; WD40; 3.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 3.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Meiosis; Mitosis; Nucleus; Reference proteome;
KW Repeat; Ubl conjugation pathway; WD repeat.
FT CHAIN 1..490
FT /note="Cell division cycle protein cdt2"
FT /id="PRO_0000050905"
FT REPEAT 178..208
FT /note="WD 1"
FT REPEAT 226..257
FT /note="WD 2"
FT REPEAT 285..317
FT /note="WD 3"
FT REPEAT 339..369
FT /note="WD 4"
FT REPEAT 387..419
FT /note="WD 5"
FT REPEAT 435..464
FT /note="WD 6"
FT REGION 18..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 490 AA; 54294 MW; 4BB352E3AC3110E6 CRC64;
MNMDIGKALS DVGGLRDITS RANNSLPPTP DSSPAAPSKK HKLYDFLESR GKIETPRKRI
VFEKKPLLHK PVHIQKKPAQ LCKELLIRQL GGSRSHPFST KTSRHVGGRL NLETYYSRPS
ECLMMLNQLP FCLGFANNES LLAVCTETGA LELFDSRFYD RQNEENQPSA RRIHGWLAHN
NAIFSVNFSK DDSLLATSSG DQTSKVFDLS TQQCITRLGR RGVDGYHSHS VKQVNFCNDS
PYNLVSCSRD GSIIFWDMRT HGITIDGEHF QKPVLRIRKA HENSGRDCSI TSATWLPQST
SQVISSCSAN SALKLWDLRT VHTVRPLPAA TTPELTTSKR DFGVTNVCTS PDGERIYAAS
RDSIIYEYSS RHLNSGFCKT YKDPRLRISS FYVKLACSPD GATLACGGGV QDKTSGVVVF
DTTRNCSSSA MLTGGHTKDV TAVDWSSEGQ LASISDDGSV RVWNSSLHGS AANLREKNFS
EIFYWGFSEK
