ID   DDB1_XENLA              Reviewed;        1140 AA.
AC   Q6P6Z0;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=DNA damage-binding protein 1;
DE   AltName: Full=Damage-specific DNA-binding protein 1;
GN   Name=ddb1;
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=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Protein, which is both involved in DNA repair and protein
CC       ubiquitination, as part of the UV-DDB complex and DCX (DDB1-CUL4-X-box)
CC       complexes, respectively. Core component of the UV-DDB complex (UV-
CC       damaged DNA-binding protein complex), a complex that recognizes UV-
CC       induced DNA damage and recruit proteins of the nucleotide excision
CC       repair pathway (the NER pathway) to initiate DNA repair. The UV-DDB
CC       complex may recognize UV-induced DNA damage and recruit proteins of the
CC       nucleotide excision repair pathway (the NER pathway) to initiate DNA
CC       repair (By similarity). Also functions as a component of numerous
CC       distinct DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes
CC       which mediate the ubiquitination and subsequent proteasomal degradation
CC       of target proteins (By similarity). The functional specificity of the
CC       DCX E3 ubiquitin-protein ligase complex is determined by the variable
CC       substrate recognition component recruited by DDB1. May play a role in
CC       the regulation of the circadian clock (By similarity).
CC       {ECO:0000250|UniProtKB:Q16531, ECO:0000250|UniProtKB:Q805F9}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000250|UniProtKB:Q805F9}.
CC   -!- SUBUNIT: Component of the UV-DDB complex which includes ddb1 and ddb2
CC       (By similarity). Component of numerous DCX (DDB1-CUL4-X-box) E3
CC       ubiquitin-protein ligase complexes which consist of a core of ddb1,
CC       cul4a or cul4b and rbx1, and a substrate receptor, such as CRBN (By
CC       similarity). DDB1 may recruit specific substrate targeting subunits to
CC       the DCX complex. These substrate targeting subunits are generally known
CC       as DCAF (DDB1- and CUL4-associated factor) or CDW (CUL4-DDB1-associated
CC       WD40-repeat) proteins (By similarity). {ECO:0000250|UniProtKB:Q16531,
CC       ECO:0000250|UniProtKB:Q805F9}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q805F9}. Nucleus
CC       {ECO:0000250|UniProtKB:Q805F9}.
CC   -!- DOMAIN: The core of the protein consists of three WD40 beta-propeller
CC       domains. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DDB1 family. {ECO:0000305}.
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DR   EMBL; BC061946; AAH61946.1; -; mRNA.
DR   RefSeq; NP_001083624.1; NM_001090155.1.
DR   AlphaFoldDB; Q6P6Z0; -.
DR   SMR; Q6P6Z0; -.
DR   BioGRID; 100352; 4.
DR   PRIDE; Q6P6Z0; -.
DR   DNASU; 399026; -.
DR   GeneID; 399026; -.
DR   KEGG; xla:399026; -.
DR   CTD; 399026; -.
DR   Xenbase; XB-GENE-967911; ddb1.S.
DR   OMA; CTEMEHE; -.
DR   OrthoDB; 146622at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000186698; Chromosome 4S.
DR   Bgee; 399026; Expressed in muscle tissue and 19 other tissues.
DR   GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; ISS:UniProtKB.
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; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR   GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR   GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
DR   GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.130.10.10; -; 3.
DR   InterPro; IPR004871; Cleavage/polyA-sp_fac_asu_C.
DR   InterPro; IPR018846; Cleavage/polyA-sp_fac_asu_N.
DR   InterPro; IPR031297; DDB1.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   PANTHER; PTHR10644:SF3; PTHR10644:SF3; 1.
DR   Pfam; PF03178; CPSF_A; 1.
DR   Pfam; PF10433; MMS1_N; 1.
DR   SUPFAM; SSF50978; SSF50978; 1.
PE   2: Evidence at transcript level;
KW   Biological rhythms; Cytoplasm; DNA damage; DNA repair; DNA-binding;
KW   Nucleus; Reference proteome; Repeat; Ubl conjugation pathway.
FT   CHAIN           1..1140
FT                   /note="DNA damage-binding protein 1"
FT                   /id="PRO_0000351085"
FT   REGION          13..356
FT                   /note="WD repeat beta-propeller A"
FT                   /evidence="ECO:0000250"
FT   REGION          391..708
FT                   /note="WD repeat beta-propeller B; Interaction with CUL4A"
FT                   /evidence="ECO:0000250"
FT   REGION          709..1043
FT                   /note="WD repeat beta-propeller C"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1140 AA;  126833 MW;  78D5C14BE7E55AE3 CRC64;
     MSYNYVVTAQ KPTAVNACVT GHFTSEDDLN LLIAKNTRLE IYVVTPEGLR PVKEVGMYGK
     IAVMELFRPK GESKDLLFIL TAKYNACILE YKQSGDSIDI ITRAHGNVQD RIGRPSETGI
     IGIIDPDCRM IGLRLYDGLF KVIPLERDNK ELKAFNIRLE ELHVIDVKFL YSCQAPTICF
     VYQDPQGRHV KTYEVSLREK EFSKGPWKQE NVEAEASMVI AVPEPFGGAI IIGQESITYH
     NGDKYLAIAP PIIKQSTIVC HNRVDVNGSR YLLGDMEGRL FMLLLEKEEQ MDGSVTLKDL
     RVELLGETSI AECLTYLDNG VVFVGSRLGD SQLVKLTTES NEQGSYVVVM ETFTNLGPIV
     DMCVVDLERQ GQGQLVTCSG AFKEGSLRII RNGIGIHEHA SIDLPGIKGL WPLRVAADRD
     TDDTLVLSFV GQTRVLTLTG EEVEETDLAG FVDDQQTFFC GNVAHQQLIQ ITSASVRLVS
     QNPQNLVSEW KEPQGRKVSV CSCNSRQVLL AVGRVLYYLE IHPGELRQTS CTEMEHEVAC
     LDVTPLGGND TLSSLCAIGL WTDISARILS LPGFQLLHKE MLGGEIIPRS ILMTSFESSH
     YLLCALGDGA LFYFSLNTDT GLLSDRKKVT LGTQPTVLRT FRSLSTTNVF ACSDRPTVIY
     SSNHKLVFSN VNLKEVNYMC PLNSEGYPDS LALANNSTLT IGTIDEIQKL HIRTVPLFES
     PRKICYQEVS QCFGVLSSRI EVQDASGGSS PLRPSASTQA LSSSVSCSKL FSGSTSPHET
     SFGEEVEVHN LLIIDQHTFE VLHTHQFLQN EYTLSLVSCK LGKDPTTYFV VGTAMVYPDE
     AEPKQGRIVV FQYNDGKLQT VAEKEVKGAV YSMVEFNGKL LASINSTVRL YEWTAEKELR
     TECNHYNNIM ALYLKTKGDF ILVGDLMRSV LLLAYKPMEG NFEEIARDFN PNWMSAVEIL
     DDDNFLGAEN AFNLFVCQKD SAATTDEERQ HLQEVGLFHL GEFVNVFCHG SLVMQNLGET
     SPPTQGSVLF GTVNGMIGLV TSLSESWYNL LLDVQNRLNK VIKSVGKIEH SFWRSFHTER
     KTEPATGFID GDLIESFLDI SRPKMQEVIA NLQIDDGSGM KRETTVDDLI KVVEELTRIH