DDB1_SOLLC
ID DDB1_SOLLC Reviewed; 1090 AA.
AC Q6QNU4;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=DNA damage-binding protein 1;
DE AltName: Full=High pigmentation protein 1;
DE AltName: Full=UV-damaged DNA-binding protein 1;
GN Name=DDB1; Synonyms=hp1;
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, VARIANT HP1 TYR-311, AND MUTAGENESIS
RP OF GLU-798.
RX PubMed=15178762; DOI=10.1073/pnas.0400935101;
RA Liu Y., Roof S., Ye Z., Barry C., van Tuinen A., Vrebalov J., Bowler C.,
RA Giovannoni J.;
RT "Manipulation of light signal transduction as a means of modifying fruit
RT nutritional quality in tomato.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9897-9902(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], VARIANT HP1 TYR-311, AND MUTANT HP1W.
RX PubMed=14968305; DOI=10.1007/s00122-004-1584-1;
RA Lieberman M., Segev O., Gilboa N., Lalazar A., Levin I.;
RT "The tomato homolog of the gene encoding UV-damaged DNA binding protein 1
RT (DDB1) underlined as the gene that causes the high pigment-1 mutant
RT phenotype.";
RL Theor. Appl. Genet. 108:1574-1581(2004).
CC -!- FUNCTION: Component of light signal transduction machinery. Involved in
CC fruit pigmentation and fruit nutritional quality. Acts as a negative
CC regulator of fruit pigmentation. Probably acts by participating in the
CC CDD complex, a complex probably required to regulate the activity of
CC ubiquitin conjugating enzymes. Repression of photomorphogenesis is
CC probably mediated by ubiquitination and subsequent degradation of
CC photomorphogenesis-promoting factors such as HY5.
CC {ECO:0000269|PubMed:15178762}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Probable component of the CDD complex, which probably also
CC contains DET1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- MISCELLANEOUS: The hp1 variant was originally discovered as a
CC spontaneous mutant at the Campbell Soup company farms (Riverton, N.J.).
CC -!- SIMILARITY: Belongs to the DDB1 family. {ECO:0000305}.
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DR EMBL; AY531660; AAS21683.1; -; mRNA.
DR EMBL; AY452480; AAR20885.1; -; mRNA.
DR RefSeq; NP_001234275.1; NM_001247346.1.
DR AlphaFoldDB; Q6QNU4; -.
DR SMR; Q6QNU4; -.
DR STRING; 4081.Solyc02g021650.2.1; -.
DR PaxDb; Q6QNU4; -.
DR PRIDE; Q6QNU4; -.
DR GeneID; 778355; -.
DR KEGG; sly:778355; -.
DR eggNOG; KOG1897; Eukaryota.
DR InParanoid; Q6QNU4; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000004994; Unplaced.
DR ExpressionAtlas; Q6QNU4; baseline and differential.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003684; F:damaged DNA binding; IEA:EnsemblPlants.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0009585; P:red, far-red light phototransduction; 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; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR Pfam; PF03178; CPSF_A; 1.
DR Pfam; PF10433; MMS1_N; 1.
DR SUPFAM; SSF50998; SSF50998; 1.
PE 1: Evidence at protein level;
KW Nucleus; Phytochrome signaling pathway; Reference proteome.
FT CHAIN 1..1090
FT /note="DNA damage-binding protein 1"
FT /id="PRO_0000079842"
FT VARIANT 311
FT /note="N -> Y (in hp1; induces exaggerated light
FT responsiveness)"
FT /evidence="ECO:0000269|PubMed:14968305,
FT ECO:0000269|PubMed:15178762"
FT MUTAGEN 798
FT /note="E->K: In hp1w; induces exaggerated light
FT responsiveness."
FT /evidence="ECO:0000269|PubMed:15178762"
SQ SEQUENCE 1090 AA; 121733 MW; CF44BC8C1B1F1DF9 CRC64;
MSVWNYVVTA HKPTNVTHSC VGNFTGPQEL NLIIAKCTRI EIHLLTPQGL QPMLDVPIYG
RIATLELFRP HGETQDLLFI ATERYKFCVL QWDTEASEVI TRAMGDVSDR IGRPTDNGQI
GIIDPDCRLI GLHLYDGLFK VIPFDNKGQL KEAFNIRLEE LQVLDIKFLY GCPKPTIVVL
YQDNKDARHV KTYEVSLKDK DFIEGPWAQN NLDNGASLLI PVPPPLCGVL IIGEETIVYC
SASAFKAIPI RPSITRAYGR VDADGSRYLL GDHNGLLHLL VITHEKEKVT GLKIELLGET
SIASTISYLD NAFVFIGSSY GDSQLVKLNL QPDTKGSYVE VLERYVNLGP IVDFCVVDLE
RQGQGQVVTC SGAYKDGSLR IVRNGIGINE QASVELQGIK GMWSLRSATD DPYDTFLVVS
FISETRVLAM NLEDELEETE IEGFNSQVQT LFCHDAVYNQ LVQVTSNSVR LVSSTSRDLK
NEWFAPVGYS VNVATANATQ VLLATGGGHL VYLEIGDGVL NEVKYAKLDY DISCLDINPI
GENPNYSNIA AVGMWTDISV RIYSLPDLNL ITKEQLGGEI IPRSVLMCSF EGISYLLCAL
GDGHLLNFVL SMSTGELTDR KKVSLGTQPI TLRTFSSKDT THVFAASDRP TVIYSSNKKL
LYSNVNLKEV SHMCPFNVAA FPDSLAIAKE GELTIGTIDE IQKLHIRSIP LGEHARRISH
QEQTRTFALC SVKYTQSNAD DPEMHFVRLL DDQTFEFIST YPLDQFEYGC SILSCSFSDD
SNVYYCIGTA YVMPEENEPT KGRILVFIVE DGKLQLIAEK ETKGAVYSLN AFNGKLLAAI
NQKIQLYKWA SREDGGSREL QTECGHHGHI LALYVQTRGD FIVVGDLMKS ISLLIFKHEE
GAIEERARDY NANWMSAVEI LDDDIYLGAE NNFNLFTVRK NSEGATDEER SRLEVVGEYH
LGEFVNRFRH GSLVMRLPDS DVGQIPTVIF GTVNGVIGVI ASLPHDQYLF LEKLQTNLRK
VIKGVGGLSH EQWRSFYNEK KTVDAKNFLD GDLIESFLDL SRNRMEEISK AMSVPVEELM
KRVEELTRLH