DDB1_CHICK
ID DDB1_CHICK Reviewed; 1140 AA.
AC Q805F9;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=DNA damage-binding protein 1;
DE AltName: Full=DDB p127 subunit;
DE AltName: Full=Damage-specific DNA-binding protein 1;
DE AltName: Full=UV-damaged DNA-binding factor;
GN Name=DDB1; ORFNames=RCJMB04_6h2;
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 [MRNA], AND SUBCELLULAR LOCATION.
RX PubMed=12773817; DOI=10.1266/ggs.78.169;
RA Fu D., Wakasugi M., Ishigaki Y., Nikaido O., Matsunaga T.;
RT "cDNA cloning of the chicken DDB1 gene encoding the p127 subunit of damaged
RT DNA-binding protein.";
RL Genes Genet. Syst. 78:169-177(2003).
RN [2]
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).
RN [3]
RP INTERACTION WITH CRBN.
RX PubMed=25043012; DOI=10.1038/nature13527;
RA Fischer E.S., Bohm K., Lydeard J.R., Yang H., Stadler M.B., Cavadini S.,
RA Nagel J., Serluca F., Acker V., Lingaraju G.M., Tichkule R.B.,
RA Schebesta M., Forrester W.C., Schirle M., Hassiepen U., Ottl J., Hild M.,
RA Beckwith R.E., Harper J.W., Jenkins J.L., Thoma N.H.;
RT "Structure of the DDB1-CRBN E3 ubiquitin ligase in complex with
RT thalidomide.";
RL Nature 512:49-53(2014).
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 (By similarity). Core component of the UV-DDB
CC complex (UV-damaged DNA-binding protein complex), a complex that
CC recognizes UV-induced DNA damage and recruit proteins of the nucleotide
CC excision repair pathway (the NER pathway) to initiate DNA repair (By
CC similarity). The UV-DDB complex may recognize UV-induced DNA damage and
CC recruit proteins of the nucleotide excision repair pathway (the NER
CC pathway) to initiate DNA repair (By similarity). Also functions as a
CC component of numerous distinct DCX (DDB1-CUL4-X-box) E3 ubiquitin-
CC protein ligase complexes which mediate the ubiquitination and
CC subsequent proteasomal degradation of target proteins (Probable). The
CC functional specificity of the DCX E3 ubiquitin-protein ligase complex
CC is determined by the variable substrate recognition component recruited
CC by DDB1 (By similarity). May play a role in the regulation of the
CC circadian clock (By similarity). {ECO:0000250|UniProtKB:Q16531,
CC ECO:0000305|PubMed:25043012}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000305|PubMed:25043012}.
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
CC (PubMed:25043012). DDB1 may recruit specific substrate targeting
CC subunits to the DCX complex. These substrate targeting subunits are
CC generally known as DCAF (DDB1- and CUL4-associated factor) or CDW
CC (CUL4-DDB1-associated WD40-repeat) proteins (By similarity).
CC {ECO:0000250|UniProtKB:Q16531, ECO:0000269|PubMed:25043012}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12773817}. Nucleus
CC {ECO:0000269|PubMed:12773817}.
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; AB074298; BAC56999.1; -; mRNA.
DR EMBL; AJ719779; CAG31438.1; -; mRNA.
DR RefSeq; NP_989547.1; NM_204216.3.
DR AlphaFoldDB; Q805F9; -.
DR SMR; Q805F9; -.
DR STRING; 9031.ENSGALP00000008338; -.
DR PaxDb; Q805F9; -.
DR GeneID; 374050; -.
DR KEGG; gga:374050; -.
DR CTD; 1642; -.
DR VEuPathDB; HostDB:geneid_374050; -.
DR eggNOG; KOG1897; Eukaryota.
DR InParanoid; Q805F9; -.
DR OrthoDB; 146622at2759; -.
DR PhylomeDB; Q805F9; -.
DR Reactome; R-GGA-353303; Nucleotide Excision Repair.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q805F9; -.
DR Proteomes; UP000000539; Unplaced.
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:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0035861; C:site of double-strand break; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
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; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR10644:SF3; PTHR10644:SF3; 1.
DR Pfam; PF03178; CPSF_A; 1.
DR Pfam; PF10433; MMS1_N; 1.
DR SUPFAM; SSF50998; SSF50998; 1.
PE 1: Evidence at protein 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_0000281039"
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; 126955 MW; 70F3AB4C64E27B95 CRC64;
MSYNYVVTAQ KPTAVNGCVT GHFTSAEDLN LLIAKNTRLE IYVVTAEGLR PVKEVGMYGK
TAVMELFRPK GESKDLLFIL TAKYNACILE YKQNGDNIDI ITRAHGNVQD RIGRPSETGI
IGIIDPECRM IGLRLYDGLF KVIPLDRENK ELKAFNIRLE ELQVIDVKFL YGCQAPTICF
VYQDPQGRHV KTYEVSLREK EFNKGPWKQE NVEAEASMVI AVPEPFGGAI IIGQESITYH
NGDKYLAIAP PIIKQSTIVC HNRVDPNGSR YLLGDMEGRL FMLLLEKEEQ MDGTVTLKDL
RVELLGETSI AECLTYLDNG VVFVGSRLGD SQLVKLNVDS NEQGSYVVAM ETFTNLGPIV
DMCVVDLERQ GQGQLVTCSG AFKEGSLRII RNGIGIHEHA SIDLPGIKGL WPLRSDSHRE
MDNMLVLSFV GQTRVLMLNG EEVEETELTG FVDDQQTFFC GNVAHQQLIQ ITSASVRLVS
QEPKALVSEW KEPNGKNISV ASCNSNQVVV AVGRALYYLE IRPQELRQIN CTEMEHEVAC
LDITPLGDTN GMSPLCAIGL WTDISARILK LPSFELLHKE MLGGEIIPRS ILMTTFESSH
YLLCALGDGA LFYFGLSLET GLLSDRKKVT LGTQPTVLRT FRSLSTTNVF ACSDRPTVIY
SSNHKLVFSN VNLKEVNYMC PLNSDGYPDS LALANNSTLT IGTIDEIQKL HIRTVPLYES
PRKICYQEVS QCFGVLSSRI EVQDASGGTT ALRPSASTQA LSSSVSTSKL FSSSTAPHET
SFGEEVEVHN LLIIDQHTFE VLHAHQFLQN EYALSLVSCK LGKDPNTYFI VGTAMVYPEE
AEPKQGRIVV FHYSDGKLQS LAEKEVKGAV YSMVEFNGKL LASINSTVRL YEWTAEKELR
TECNHYNNIM ALYLKTKGDF ILVGDLMRSV LLLAYKPMEG NFEEIARDFN PNWMSAVEIL
DDDNFLGAEN AFNLFVCQKD SAATTDEERQ HLQEVGLSHL GEFVNVFCHG SLVMQNLGET
STPTQGSVLF GTVNGMIGLV TSLSESWYNL LLDMQNRLNK VIKSVGKIEH SFWRSFHTER
KTEPATGFID GDLIESFLDI SRPKMQEVVA NLQIDDGSGM KREATVDDLI KIVEELTRIH
