ID   DDB1_DROME              Reviewed;        1140 AA.
AC   Q9XYZ5;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 149.
DE   RecName: Full=DNA damage-binding protein 1;
DE            Short=D-DDB1;
DE   AltName: Full=Damage-specific DNA-binding protein 1;
DE   AltName: Full=Protein piccolo;
GN   Name=pic; Synonyms=DDB1; ORFNames=CG7769;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RX   PubMed=10731138; DOI=10.1126/science.287.5461.2222;
RA   Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., Stapleton M.,
RA   Harvey D.A.;
RT   "A Drosophila complementary DNA resource.";
RL   Science 287:2222-2224(2000).
RN   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=16428319; DOI=10.1093/jb/mvj006;
RA   Shimanouchi K., Takata K., Yamaguchi M., Murakami S., Ishikawa G.,
RA   Takeuchi R., Kanai Y., Ruike T., Nakamura R., Abe Y., Sakaguchi K.;
RT   "Drosophila damaged DNA binding protein 1 contributes to genome stability
RT   in somatic cells.";
RL   J. Biochem. 139:51-58(2006).
RN   [5]
RP   FUNCTION, AND INTERACTION WITH FBW5 AND GIG.
RX   PubMed=18381890; DOI=10.1101/gad.1624008;
RA   Hu J., Zacharek S., He Y.J., Lee H., Shumway S., Duronio R.J., Xiong Y.;
RT   "WD40 protein FBW5 promotes ubiquitination of tumor suppressor TSC2 by
RT   DDB1-CUL4-ROC1 ligase.";
RL   Genes Dev. 22:866-871(2008).
RN   [6]
RP   INTERACTION WITH OHGT.
RX   PubMed=27702999; DOI=10.1074/jbc.m116.757823;
RA   Wakabayashi S., Sawamura N., Voelzmann A., Broemer M., Asahi T., Hoch M.;
RT   "Ohgata, the single Drosophila ortholog of Human Cereblon, regulates
RT   insulin signaling-dependent organismic growth.";
RL   J. Biol. Chem. 291:25120-25132(2016).
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 preferentially binds to cyclobutane
CC       pyrimidine dimers (CPD), 6-4 photoproducts (6-4 PP), apurinic sites and
CC       short mismatches (By similarity). Also functions as a component of
CC       numerous distinct DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase
CC       complexes which mediate the ubiquitination and subsequent proteasomal
CC       degradation of target proteins (By similarity). The functional
CC       specificity of the DCX E3 ubiquitin-protein ligase complex is
CC       determined by the variable substrate recognition component recruited by
CC       DDB1 (By similarity). Required for degradation of gig
CC       (PubMed:18381890). Required for genomic stability in the face of
CC       endogenous DNA lesions and for the response to MMS-induced DNA damage
CC       (PubMed:16428319). Required for normal wing development
CC       (PubMed:16428319). {ECO:0000250|UniProtKB:Q16531,
CC       ECO:0000250|UniProtKB:Q3U1J4, ECO:0000269|PubMed:16428319,
CC       ECO:0000269|PubMed:18381890}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000250|UniProtKB:Q16531}.
CC   -!- SUBUNIT: Component of the UV-DDB complex which includes DDB1 and DDB2;
CC       the heterodimer dimerizes to give rise to a heterotetramer when bound
CC       to damaged DNA (By similarity). The UV-DDB complex interacts with
CC       monoubiquitinated histone H2A and binds to XPC via the DDB2 subunit (By
CC       similarity). Component of numerous DCX (DDB1-CUL4-X-box) E3 ubiquitin-
CC       protein ligase complexes which consist of a core of DDB1, CUL4A or
CC       CUL4B and RBX1 (By similarity). DDB1 may recruit specific substrate
CC       targeting subunits to the DCX complex (By similarity). These substrate
CC       targeting subunits are generally known as DCAF (DDB1- and CUL4-
CC       associated factor) or CDW (CUL4-DDB1-associated WD40-repeat) proteins
CC       (By similarity). Interacts with Fbw5 and gig (PubMed:18381890). May
CC       interact with ohgt (PubMed:27702999). {ECO:0000250|UniProtKB:Q16531,
CC       ECO:0000269|PubMed:18381890, ECO:0000269|PubMed:27702999}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Reduced tissue growth in the wing imaginal disk.
CC       {ECO:0000269|PubMed:16428319}.
CC   -!- SIMILARITY: Belongs to the DDB1 family. {ECO:0000305}.
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DR   EMBL; AE014297; AAF54901.1; -; Genomic_DNA.
DR   EMBL; AF132145; AAD33592.1; -; mRNA.
DR   RefSeq; NP_650257.1; NM_142000.3.
DR   AlphaFoldDB; Q9XYZ5; -.
DR   SMR; Q9XYZ5; -.
DR   BioGRID; 66698; 21.
DR   IntAct; Q9XYZ5; 2.
DR   STRING; 7227.FBpp0082177; -.
DR   PaxDb; Q9XYZ5; -.
DR   PRIDE; Q9XYZ5; -.
DR   EnsemblMetazoa; FBtr0082709; FBpp0082177; FBgn0260962.
DR   GeneID; 41611; -.
DR   KEGG; dme:Dmel_CG7769; -.
DR   UCSC; CG7769-RA; d. melanogaster.
DR   CTD; 41611; -.
DR   FlyBase; FBgn0260962; pic.
DR   VEuPathDB; VectorBase:FBgn0260962; -.
DR   eggNOG; KOG1897; Eukaryota.
DR   GeneTree; ENSGT00950000183151; -.
DR   HOGENOM; CLU_002893_0_1_1; -.
DR   InParanoid; Q9XYZ5; -.
DR   OMA; CTEMEHE; -.
DR   OrthoDB; 146622at2759; -.
DR   PhylomeDB; Q9XYZ5; -.
DR   Reactome; R-DME-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR   Reactome; R-DME-5696394; DNA Damage Recognition in GG-NER.
DR   Reactome; R-DME-5696395; Formation of Incision Complex in GG-NER.
DR   Reactome; R-DME-5696400; Dual Incision in GG-NER.
DR   Reactome; R-DME-6781823; Formation of TC-NER Pre-Incision Complex.
DR   Reactome; R-DME-6782135; Dual incision in TC-NER.
DR   Reactome; R-DME-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR   Reactome; R-DME-8951664; Neddylation.
DR   SignaLink; Q9XYZ5; -.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 41611; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 41611; -.
DR   PRO; PR:Q9XYZ5; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0260962; Expressed in eye disc (Drosophila) and 27 other tissues.
DR   Genevisible; Q9XYZ5; DM.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
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:0006974; P:cellular response to DNA damage stimulus; IMP:UniProtKB.
DR   GO; GO:0050832; P:defense response to fungus; IMP:FlyBase.
DR   GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR   GO; GO:0007307; P:eggshell chorion gene amplification; IDA:FlyBase.
DR   GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IMP:FlyBase.
DR   GO; GO:0045732; P:positive regulation of protein catabolic process; IMP:FlyBase.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR   GO; GO:0035220; P:wing disc development; IMP:UniProtKB.
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; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   Pfam; PF03178; CPSF_A; 1.
DR   Pfam; PF10433; MMS1_N; 1.
DR   SUPFAM; SSF50978; SSF50978; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; DNA damage; DNA repair; DNA-binding; Nucleus;
KW   Reference proteome; Ubl conjugation pathway.
FT   CHAIN           1..1140
FT                   /note="DNA damage-binding protein 1"
FT                   /id="PRO_0000351086"
SQ   SEQUENCE   1140 AA;  126045 MW;  F7397BE9903D9A14 CRC64;
     MSHHYVVTAQ KPTAVVACLT GNFTSPTDLN LIIARNNQVE IDLVTPEGLR PLKEININGT
     IAVMRHFRPP DSNKDLLFIL TRRYNVMILE ARMVNDVITV VTKANGNVSD SVGIPSEGGV
     IAAIDPKARV IGMCLYQGLF TIIPMDKDAS ELKATNLRMD ELNVYDVEFL HGCLNPTVIV
     IHKDSDGRHV KSHEINLRDK EFMKIAWKQD NVETEATMLI PVPSPIGGVI VIGRESIVYH
     DGSNYHAVAP LTFRQSTINC YARVSSNGLR YLLGNMDGQL YMLFLGTAET SKGVTVKDIK
     VEQLGEISIP ECITYLDNGF LYIGARHGDS QLVRLNSEAI DGSYVVPVEN FTNLAPILDI
     AVVDLDRQGQ GQIITCSGSF KDGSLRIIRI GIGIQEHACI DLPGIKGMWS LKVGVDESPY
     ENTLVLAFVG HTRILTLSGE EVEETEIPGF ASDLQTFLCS NVDYDQLIQV TSDSVRLVSS
     ATKALVAEWR PTGDRTIGVV SCNTTQILVA SACDIFYIVI EDGSLREQSR RTLAYEVACL
     DITPLDETQK KSDLVAVGLW TDISAVILSL PDLETIYTEK LSGEIIPRSI LMTTFEGIHY
     LLCALGDGSM YYFIMDQTTG QLTDKKKVTL GTQPTTLRTF RSLSTTNVFA CSDRPTVIYS
     SNHKLVFSNV NLKEVNHMCS LNAQAYPDSL ALANKNAVIL GTIDEIQKLH IRTVPLGEGP
     RRIAYQESSQ TFAVSTLRID VHGRGGAKPL RNSASTQAQN ITCSSNFLPK PGGGNSTAAN
     AEVGQEIDVH NLLVIDQNTF EVLHAHQFVA PETISSLMSA KLGDDPNTYY VVATSLVIPE
     EPEPKVGRII IFHYHENKLT QVAETKVDGT CYALVEFNGK VLAGIGSFVR LYEWTNEKEL
     RMECNIQNMI AALFLKAKGD FILVGDLMRS ITLLQHKQME GIFVEIARDC EPKWMRAVEI
     LDDDTFLGSE TNGNLFVCQK DSAATTDEER QLLPELARFH LGDTVNVFRH GSLVMQNVGE
     RTTPINGCVL YGTCNGAIGI VTQIPQDFYD FLHGLEERLK KIIKSVGKIE HTYYRNFQIN
     SKVEPSEGFI DGDLIESFLD LSRDKMRDAV QGLELTLNGE RKSADVEDVI KIVEDLTRMH