CDT1_XENLA
ID CDT1_XENLA Reviewed; 617 AA.
AC Q9I9A7; Q6GQH3;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 2.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=DNA replication factor Cdt1;
DE Short=XCDT1;
GN Name=cdt1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10766247; DOI=10.1038/35007104;
RA Maiorano D., Moreau J., Mechali M.;
RT "XCDT1 is required for the assembly of pre-replicative complexes in Xenopus
RT laevis.";
RL Nature 404:622-625(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP UBIQUITINATION, DOMAIN PIP-BOX K+4 MOTIF, MUTAGENESIS OF THR-7; ASP-8 AND
RP LYS-14, AND INTERACTION WITH PCNA.
RX PubMed=19595719; DOI=10.1016/j.molcel.2009.05.012;
RA Havens C.G., Walter J.C.;
RT "Docking of a specialized PIP Box onto chromatin-bound PCNA creates a
RT degron for the ubiquitin ligase CRL4Cdt2.";
RL Mol. Cell 35:93-104(2009).
CC -!- FUNCTION: DNA replication licensing factor, required for pre-
CC replication complex assembly. Cooperates with cdc6 to promote the
CC loading of the mini-chromosome maintenance complex onto chromatin to
CC form the pre-replication complex necessary to initiate DNA replication.
CC {ECO:0000269|PubMed:10766247}.
CC -!- SUBUNIT: Interacts with pcna. {ECO:0000269|PubMed:19595719}.
CC -!- INTERACTION:
CC Q9I9A7; O93352: gmnn.S; NbExp=4; IntAct=EBI-3511006, EBI-7120476;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10766247}.
CC -!- DOMAIN: The PIP-box K+4 motif mediates both the interaction with pcna
CC and the recruitment of the DCX(DTL) complex: while the PIP-box
CC interacts with pcna, the presence of the K+4 submotif, recruits the
CC DCX(DTL) complex, leading to its ubiquitination (PubMed:19595719).
CC {ECO:0000269|PubMed:19595719}.
CC -!- PTM: Ubiquitinated by the DCX(DTL) complex, also named CRL4(CDT2)
CC complex, in response to DNA damage, leading to its degradation.
CC Ubiquitination by the DCX(DTL) complex is necessary to ensure proper
CC cell cycle regulation and is pcna-dependent: interacts with pcna via
CC its PIP-box, while the presence of the containing the 'K+4' motif in
CC the PIP box, recruit the DCX(DTL) complex, leading to its degradation.
CC The interaction with GMNN protects it against ubiquitination.
CC {ECO:0000269|PubMed:19595719}.
CC -!- SIMILARITY: Belongs to the Cdt1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB87836.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ250122; CAB87836.1; ALT_INIT; mRNA.
DR EMBL; BC072771; AAH72771.1; -; mRNA.
DR RefSeq; NP_001081738.1; NM_001088269.1.
DR AlphaFoldDB; Q9I9A7; -.
DR SMR; Q9I9A7; -.
DR BioGRID; 99359; 5.
DR DIP; DIP-43926N; -.
DR IntAct; Q9I9A7; 3.
DR MINT; Q9I9A7; -.
DR PRIDE; Q9I9A7; -.
DR DNASU; 398024; -.
DR GeneID; 398024; -.
DR KEGG; xla:398024; -.
DR CTD; 398024; -.
DR Xenbase; XB-GENE-1014892; cdt1.L.
DR OrthoDB; 648388at2759; -.
DR Proteomes; UP000186698; Chromosome 4L.
DR Bgee; 398024; Expressed in blastula and 19 other tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0031490; F:chromatin DNA binding; IMP:UniProtKB.
DR GO; GO:0071163; P:DNA replication preinitiation complex assembly; IEA:InterPro.
DR GO; GO:0030174; P:regulation of DNA-templated DNA replication initiation; IEA:InterPro.
DR CDD; cd08767; Cdt1_c; 1.
DR CDD; cd08674; Cdt1_m; 1.
DR Gene3D; 1.10.10.1420; -; 1.
DR InterPro; IPR045173; Cdt1.
DR InterPro; IPR032054; Cdt1_C.
DR InterPro; IPR038090; Cdt1_C_WH_dom_sf.
DR InterPro; IPR014939; CDT1_Gemini-bd-like.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR28637; PTHR28637; 2.
DR Pfam; PF08839; CDT1; 1.
DR Pfam; PF16679; CDT1_C; 1.
DR SMART; SM01075; CDT1; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
PE 1: Evidence at protein level;
KW Cell cycle; DNA replication; Nucleus; Proto-oncogene; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..617
FT /note="DNA replication factor Cdt1"
FT /id="PRO_0000396627"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 51..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1..25
FT /note="PIP-box K+4 motif"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 7
FT /note="T->A: Abolishes degradation by the proteasome due to
FT the disrupted interaction with pcna."
FT /evidence="ECO:0000269|PubMed:19595719"
FT MUTAGEN 8
FT /note="D->A: Abolishes degradation by the proteasome due to
FT the disrupted interaction with pcna."
FT /evidence="ECO:0000269|PubMed:19595719"
FT MUTAGEN 14
FT /note="K->A: Abolishes degradation by the proteasome
FT without affecting the interaction with pcna."
FT /evidence="ECO:0000269|PubMed:19595719"
FT CONFLICT 11
FT /note="S -> A (in Ref. 2; AAH72771)"
FT /evidence="ECO:0000305"
FT CONFLICT 206
FT /note="R -> H (in Ref. 2; AAH72771)"
FT /evidence="ECO:0000305"
FT CONFLICT 471
FT /note="T -> N (in Ref. 2; AAH72771)"
FT /evidence="ECO:0000305"
FT CONFLICT 585
FT /note="P -> L (in Ref. 2; AAH72771)"
FT /evidence="ECO:0000305"
FT CONFLICT 596
FT /note="Q -> K (in Ref. 2; AAH72771)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 617 AA; 69536 MW; F42840DDDFE30E5E CRC64;
MSQMRVTDFF SQSKRGTAAQ NSKGRKVEAV LETRRAVTRS RAASVKAEEF LKAPCTPERA
SPTVSQCIGP SSKKRTRQDS DSEPLRTQQR QGKSARKKLK LPEGEHGGSV QQQLFSPCNK
VALEHVTPSS LGKKIKDMVN VSLSPKFNEL ARNPTTPETK SPAKENLLEL KSRLQRIQEL
AQKVNLPAAS SEGKVTITDL KARLKRAQEL DTKIRAKAEK TETQAIDLTE QPAQESEKAP
AYQRFHNLAQ DAAPGLTLPY KYKVLAEMFR SMDTIVGMLF NRSETITFSK VKQGVQDMMR
KQFEQRNVGQ IKTVYPNAYK YRQEKNIPTF KDGVKKTDYQ LTIEPLVAEG DMLSGRPHLS
ASRLLERKQL FHRSLTSIVK QHHRVFLTSL NPPMLVPDDK LTRWHPRFNV DEVLDVTPAE
LPLPPQVERL TTAQEVLSKA RGLITPKMEK ALANLALKTA ENAGETKNVS TEETKSTATT
STSTALKGVS QSLLERIRAK EAQKLQAIMT RRPQQEERLL MMSRLPELAR ILRNVFVAEK
KPALTLEVTC SRVIASCRSS MSPGEMEKHL ALLSEILPDW LSIHPVRKDT YYKLNQSMDL
NLILERLAKK TKEEESL
