DTL_CHICK
ID DTL_CHICK Reviewed; 720 AA.
AC Q5ZJW8;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Denticleless protein homolog;
GN Name=DTL; Synonyms=CDT2; ORFNames=RCJMB04_15a2;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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 (By similarity).
CC May play a role in the regulation of the circadian clock (By
CC similarity). {ECO:0000250|UniProtKB:Q9NZJ0}.
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:Q9NZJ0}.
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; AJ720316; CAG31975.1; -; mRNA.
DR RefSeq; NP_001026219.1; NM_001031048.1.
DR AlphaFoldDB; Q5ZJW8; -.
DR SMR; Q5ZJW8; -.
DR STRING; 9031.ENSGALP00000015973; -.
DR PaxDb; Q5ZJW8; -.
DR PRIDE; Q5ZJW8; -.
DR Ensembl; ENSGALT00000015990; ENSGALP00000015973; ENSGALG00000009837.
DR GeneID; 421373; -.
DR KEGG; gga:421373; -.
DR CTD; 51514; -.
DR VEuPathDB; HostDB:geneid_421373; -.
DR eggNOG; KOG0321; Eukaryota.
DR GeneTree; ENSGT00530000064210; -.
DR HOGENOM; CLU_023407_0_0_1; -.
DR InParanoid; Q5ZJW8; -.
DR OMA; VSMRKIC; -.
DR OrthoDB; 1288134at2759; -.
DR PhylomeDB; Q5ZJW8; -.
DR TreeFam; TF324483; -.
DR Reactome; R-GGA-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR Reactome; R-GGA-8951664; Neddylation.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q5ZJW8; -.
DR Proteomes; UP000000539; Chromosome 3.
DR Bgee; ENSGALG00000009837; Expressed in testis and 5 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:0030674; F:protein-macromolecule adaptor activity; IBA:GO_Central.
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:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
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; 4.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
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..720
FT /note="Denticleless protein homolog"
FT /id="PRO_0000274869"
FT REPEAT 43..85
FT /note="WD 1"
FT REPEAT 92..131
FT /note="WD 2"
FT REPEAT 134..174
FT /note="WD 3"
FT REPEAT 211..250
FT /note="WD 4"
FT REPEAT 266..305
FT /note="WD 5"
FT REPEAT 310..351
FT /note="WD 6"
FT REPEAT 355..395
FT /note="WD 7"
FT REGION 411..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 607..698
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 164..167
FT /note="DDB1-binding motif"
FT /evidence="ECO:0000250"
FT MOTIF 193..200
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 240..243
FT /note="DDB1-binding motif"
FT /evidence="ECO:0000250"
FT COMPBIAS 419..434
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..639
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 675..698
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 720 AA; 78633 MW; 1B9101FCA671EB4E CRC64;
MLCRALLLRA AGHRQSSSLP LQHLLDGYRC SREDDHLSYG EIGMPVPPFG CSFSAAPNFE
HVLAVANEEG FVRLYDTEAQ NTTKLISKEW QAHSNAVFDL AWVPGEHRIV TASGDQTAKV
WDVRAGELLG ICKGHQCSLK SVAFSRFEKA VFCTGGRDGN IMVWDTRCNK KDGFYRQVNQ
ISGAHNVVDR QTPSKLRKKR QNLRGLAPLV DFQQSVTVVL LQDEHTLISA GAVDGVIKVW
DLRKNYAAYR QDPVPSKSFF YPGTSTRKLG YSSLVLDSTG ANLFANCTDD SIYMFNMTSL
KTFPVAVFSG HQNSTFYIKS SISPDDQFLV SGSSDCNAYI WKVSEPSLPP RILVGHSQEV
TSIAWCPSDF TKIATCSDDN TVRIWRLQHY PEEEKSVSNK AKLVGWVTQK KPEEQRGAGR
SASPQSTPAK AFSVGSPCAS SPRPAACAPS YSGDLPLSTN TPTVSLKTQM ATACTPAKLS
GASPRTSPKL VPSSKMSIKH WIARTPCSSP EVGKKTPSPR KALAEVTQSL LETSSTPKAQ
HSQAEKRAKR RLDCSKEDEA GQKCLQDCSC VTELDHVAKK SKLNLCHLAA GQRACDEGSL
SLADLDNEHE DSTHSPKELS FPGSLVNPSG TQTPPPVLQS PCERDSDVVD KENSSPERKN
WLSALGEKLR TGKAGSPPSS YTSSAKRQEA AVVTTSPKTA VNTSVSMRKI CTYFHRKPQN
