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Database: UniProt
Entry: A0A3Q7RB25_VULVU
LinkDB: A0A3Q7RB25_VULVU
Original site: A0A3Q7RB25_VULVU 
ID   A0A3Q7RB25_VULVU        Unreviewed;      1140 AA.
AC   A0A3Q7RB25;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=DNA damage-binding protein 1 {ECO:0000256|ARBA:ARBA00014577, ECO:0000256|RuleBase:RU368023};
DE   AltName: Full=Damage-specific DNA-binding protein 1 {ECO:0000256|ARBA:ARBA00031668, ECO:0000256|RuleBase:RU368023};
GN   Name=DDB1 {ECO:0000313|RefSeq:XP_025843159.1};
OS   Vulpes vulpes (Red fox).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX   NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025843159.1};
RN   [1]
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (JAN-2019) to UniProtKB.
RN   [2] {ECO:0000313|RefSeq:XP_025843159.1}
RP   IDENTIFICATION.
RC   STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025843159.1};
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_025843159.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Component of complexes involved in DNA repair and protein
CC       ubiquitination. May play a role in the regulation of the circadian
CC       clock. {ECO:0000256|RuleBase:RU368023}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|RuleBase:RU368023}.
CC   -!- SUBUNIT: Component of the UV-DDB complex.
CC       {ECO:0000256|RuleBase:RU368023}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|RuleBase:RU368023}.
CC   -!- DOMAIN: The core of the protein consists of three WD40 beta-propeller
CC       domains. {ECO:0000256|RuleBase:RU368023}.
CC   -!- SIMILARITY: Belongs to the DDB1 family. {ECO:0000256|ARBA:ARBA00007453,
CC       ECO:0000256|RuleBase:RU368023}.
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DR   RefSeq; XP_025843159.1; XM_025987374.1.
DR   AlphaFoldDB; A0A3Q7RB25; -.
DR   STRING; 9627.ENSVVUP00000006429; -.
DR   Ensembl; ENSVVUT00000008581; ENSVVUP00000006429; ENSVVUG00000004987.
DR   KEGG; vvp:112911054; -.
DR   OMA; HQDFLMR; -.
DR   OrthoDB; 226997at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000286640; Unplaced.
DR   GO; GO:0031464; C:Cul4A-RING E3 ubiquitin ligase complex; IEA:Ensembl.
DR   GO; GO:0031465; C:Cul4B-RING E3 ubiquitin ligase complex; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR   GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0097602; F:cullin family protein binding; IEA:Ensembl.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:Ensembl.
DR   GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR   GO; GO:0160072; F:ubiquitin ligase complex scaffold activity; IEA:Ensembl.
DR   GO; GO:0071987; F:WD40-repeat domain binding; IEA:Ensembl.
DR   GO; GO:0006915; P:apoptotic process; IEA:Ensembl.
DR   GO; GO:0051702; P:biological process involved in interaction with symbiont; IEA:Ensembl.
DR   GO; GO:0035234; P:ectopic germ cell programmed cell death; IEA:Ensembl.
DR   GO; GO:0044725; P:epigenetic programming in the zygotic pronuclei; IEA:Ensembl.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR   GO; GO:0051093; P:negative regulation of developmental process; IEA:Ensembl.
DR   GO; GO:2000242; P:negative regulation of reproductive process; IEA:Ensembl.
DR   GO; GO:0046726; P:positive regulation by virus of viral protein levels in host cell; IEA:Ensembl.
DR   GO; GO:0045722; P:positive regulation of gluconeogenesis; IEA:Ensembl.
DR   GO; GO:0045732; P:positive regulation of protein catabolic process; IEA:Ensembl.
DR   GO; GO:0045070; P:positive regulation of viral genome replication; IEA:Ensembl.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniRule.
DR   GO; GO:0042752; P:regulation of circadian rhythm; IEA:Ensembl.
DR   GO; GO:1901990; P:regulation of mitotic cell cycle phase transition; IEA:Ensembl.
DR   GO; GO:0007056; P:spindle assembly involved in female meiosis; IEA:Ensembl.
DR   GO; GO:0070914; P:UV-damage excision repair; IEA:Ensembl.
DR   GO; GO:0019076; P:viral release from host cell; IEA:Ensembl.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:Ensembl.
DR   Gene3D; 1.10.150.910; -; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 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   PANTHER; PTHR10644:SF3; DNA DAMAGE-BINDING PROTEIN 1; 1.
DR   PANTHER; PTHR10644; DNA REPAIR/RNA PROCESSING CPSF FAMILY; 1.
DR   Pfam; PF03178; CPSF_A; 1.
DR   Pfam; PF10433; MMS1_N; 1.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|RuleBase:RU368023};
KW   DNA repair {ECO:0000256|RuleBase:RU368023};
KW   Nucleus {ECO:0000256|RuleBase:RU368023};
KW   Reference proteome {ECO:0000313|Proteomes:UP000286640}.
FT   DOMAIN          75..543
FT                   /note="Cleavage/polyadenylation specificity factor A
FT                   subunit N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF10433"
FT   DOMAIN          790..1099
FT                   /note="Cleavage/polyadenylation specificity factor A
FT                   subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03178"
SQ   SEQUENCE   1140 AA;  126940 MW;  D511585C2FDFA6B4 CRC64;
     MSYNYVVTAQ KPTAVNGCVT GHFTSAEDLN LLIAKNTRLE IYVVTAEGLR PVKEVGMYGK
     IAVMELFRPK GESKDLLFIL TAKYNACILE YKQSGESIDI ITRAHGNVQD RIGRPSETGI
     IGIIDPECRM IGLRLYDGLF KVIPLDRDNK ELKAFNIRLE ELHVIDVKFL YGCQAPTICF
     VYQDPQGRHV KTYEVSLREK EFNKGPWKQE NVEAEASMVI AVPEPFGGAI IIGQESITYH
     NGDKYLAIAP PIIKQSTIVC HNRVDPNGSR YLLGDMEGRL FMLLLEKEEQ MDGTVTLKDL
     RVELLGETSI AECLTYLDNG VVFVGSRLGD SQLVKLNVDS NEQGSYVVAM ETFTNLGPIV
     DMCVVDLERQ GQGQLVTCSG AFKEGSLRII RNGIGIHEHA SIDLPGIKGL WPLRSDPNRE
     TDDTLVLSFV GQTRVLMLNG EEVEETELMG FVDDQQTFFC GNVAHQQLIQ ITSASVRLVS
     QEPKALVSEW KEPQGKNISV ASCNSSQVVV AVGRALYYLQ IHPQELRQIS HTEMEHEVAC
     LDITPLGDSN GLSPLCAIGL WTDISARILK LPSFELLHKE MLGGEIIPRS ILMTTFESSH
     YLLCALGDGA LFYFGLNVET GLLSDRKKVT LGTQPTVLRT FRSLSTTNVF ACSDRPTVIY
     SSNHKLVFSN VNLKEVNYMC PLNSDGYPDS LALANNSTLT IGTIDEIQKL HIRTVPLYES
     PRKICYQEVS QCFGVLSSRI EVQDTSGGTT ALRPSASTQA LSSSVSSSKL FSSSTAPHET
     SFGEEVEVHN LLIIDQHTFE VLHAHQFLQN EYALSLVSCK LGKDPNTYFI VGTAMVYPEE
     AEPKQGRIVV FQYSDGKLQT VAEKEVKGAV YSMVEFNGKL LASINSTVRL YEWTTEKELR
     TECNHYNNIM ALYLKTKGDF ILVGDLMRSV LLLAYKPMEG NFEEIARDFN PNWMSAVEIL
     DDDNFLGAEN AFNLFVCQKD SAATTDEERQ HLQEVGLFHL GEFVNVFCHG SLVMQNLGET
     STPTQGSVLF GTVNGMIGLV TSLSESWYNL LLDMQNRLNK VIKSVGKIEH SFWRSFHTER
     KTEPATGFID GDLIESFLDI SRPKMQEVVA NLQYDDGSGM KREATADDLI KVVEELTRIH
//
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