ID   DTLB_XENLA              Reviewed;         711 AA.
AC   Q6GPU3;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Denticleless protein homolog B;
GN   Name=dtl-b; Synonyms=cdt2-b;
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 [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION.
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: Substrate-specific adapter of a DCX (DDB1-CUL4-X-box) E3
CC       ubiquitin-protein ligase complex required for cell cycle control, DNA
CC       damage response and translesion DNA synthesis. The DCX(DTL) complex,
CC       also named CRL4(CDT2) complex, mediates the polyubiquitination and
CC       subsequent degradation of CDT1, CDKN1A/p21(CIP1), KMT5A and SDE2. CDT1
CC       degradation in response to DNA damage is necessary to ensure proper
CC       cell cycle regulation of DNA replication. CDKN1A/p21(CIP1) degradation
CC       during S phase or following UV irradiation is essential to control
CC       replication licensing. KMT5A degradation is also important for a proper
CC       regulation of mechanisms such as TGF-beta signaling, cell cycle
CC       progression, DNA repair and cell migration. Most substrates require
CC       their interaction with PCNA for their polyubiquitination: substrates
CC       interact with PCNA via their PIP-box, and those containing the 'K+4'
CC       motif in the PIP box, recruit the DCX(DTL) complex, leading to their
CC       degradation. In undamaged proliferating cells, the DCX(DTL) complex
CC       also promotes the 'Lys-164' monoubiquitination of PCNA, thereby being
CC       involved in PCNA-dependent translesion DNA synthesis. May play a role
CC       in the regulation of the circadian clock (By similarity).
CC       {ECO:0000250|UniProtKB:Q9NZJ0, ECO:0000269|PubMed:19595719}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Component of the DCX(DTL) E3 ubiquitin ligase complex, at
CC       least composed of cul4 (cul4a or cul4b), ddb1, dtl/cdt2 and rbx1.
CC       {ECO:0000250|UniProtKB:Q6P1W0}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NZJ0}.
CC       Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC       {ECO:0000250}. Chromosome {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the WD repeat cdt2 family. {ECO:0000305}.
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DR   EMBL; BC073015; AAH73015.1; -; mRNA.
DR   RefSeq; NP_001085609.1; NM_001092140.1.
DR   AlphaFoldDB; Q6GPU3; -.
DR   SMR; Q6GPU3; -.
DR   BioGRID; 102198; 4.
DR   MaxQB; Q6GPU3; -.
DR   DNASU; 444035; -.
DR   GeneID; 444035; -.
DR   KEGG; xla:444035; -.
DR   CTD; 444035; -.
DR   Xenbase; XB-GENE-985629; dtl.L.
DR   OrthoDB; 1288134at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000186698; Chromosome 5L.
DR   Bgee; 444035; Expressed in blastula and 16 other tissues.
DR   GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0031464; C:Cul4A-RING E3 ubiquitin ligase complex; ISS:UniProtKB.
DR   GO; GO:0031465; C:Cul4B-RING E3 ubiquitin ligase complex; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; ISS:UniProtKB.
DR   GO; GO:0006513; P:protein monoubiquitination; ISS:UniProtKB.
DR   GO; GO:0000209; P:protein polyubiquitination; ISS:UniProtKB.
DR   GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
DR   GO; GO:0009411; P:response to UV; ISS:UniProtKB.
DR   GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR   GO; GO:0019985; P:translesion synthesis; ISS:UniProtKB.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
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; 5.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 6.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 2.
DR   PROSITE; PS50082; WD_REPEATS_2; 5.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   2: Evidence at transcript level;
KW   Biological rhythms; Chromosome; Cytoplasm; Cytoskeleton; DNA damage;
KW   DNA replication; Nucleus; Reference proteome; Repeat;
KW   Ubl conjugation pathway; WD repeat.
FT   CHAIN           1..711
FT                   /note="Denticleless protein homolog B"
FT                   /id="PRO_0000396626"
FT   REPEAT          47..89
FT                   /note="WD 1"
FT   REPEAT          96..135
FT                   /note="WD 2"
FT   REPEAT          138..178
FT                   /note="WD 3"
FT   REPEAT          215..254
FT                   /note="WD 4"
FT   REPEAT          270..309
FT                   /note="WD 5"
FT   REPEAT          314..355
FT                   /note="WD 6"
FT   REPEAT          359..398
FT                   /note="WD 7"
FT   REGION          473..524
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          601..698
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           168..171
FT                   /note="DDB1-binding motif"
FT                   /evidence="ECO:0000250"
FT   MOTIF           197..204
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   MOTIF           244..247
FT                   /note="DDB1-binding motif"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        473..520
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        602..628
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        642..698
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   711 AA;  78124 MW;  D68C75007C521F33 CRC64;
     MLFRSVVNKP RFGCGHNGAP FTSPLQSLLQ CYQCVKQDEH ISYGDLGRAV PPFGCAFSTV
     PGMSHVLAVA NEEGIVRLYD TECGDMQRLV VKEFMAHTNA VFDIAWVPGE HKLVTASGDQ
     TAKLWDVKAG ELIGECKGHQ CSLKSVAFSK FERAVFSTGG RDGNIMVWDT RCNKKDGFYR
     QVNQITGAHN AIDKQTPSKV KKRKPSIRGL APSVDSQQSV TVVIFQDEYT VISAGAVDGV
     VKIWDLRKNY STYRQDPVPV KLFPYPGNST RKLGYSSLVL DPTGTNLFAS CTDDNVYMFN
     ATGLKTDPVS VFRGHQNSTF YIKASVSPDG QFLLSGSSDH SAYIWQVSDP LAAPINLIGH
     CQEVTSVAWC QSDFTKIATC SDDNTVRIWR LNRSSEDSSE SNKTDYVGWA CKKKFEPSSM
     AAILCTPGKP SMIPSSSLMS SPTPATCAPS NTGDLPLPSS TPLSALLPTS KLQTPKRINN
     GGLGASPKQM SSSKISIKDW VTRTPKSSKG TDSKTPSPRK AFTPVEQYPI VSNARVQLPY
     EKRAKRRLET SSEDVEHVCL DNCCVMELEP RLKKSKLDLC SLNERDCRDD KCLRLSDLSK
     EFDQELSPSP STSLHMNATD NPPTLSPLSE MKSDFVDKEN SSPEKNWLSA LGHKFKSDNS
     SPQFKSSSSP SSRNSTSKKH QPRNAPNSPV SVPTTPGSMR KICTYFFKKS E