ERCC8_BOVIN
ID ERCC8_BOVIN Reviewed; 397 AA.
AC Q5BIM8;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=DNA excision repair protein ERCC-8;
GN Name=ERCC8;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
CC -!- FUNCTION: Substrate-recognition component of the CSA complex, a DCX
CC (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex, involved in
CC transcription-coupled nucleotide excision repair (By similarity). The
CC CSA complex (DCX(ERCC8) complex) promotes the ubiquitination and
CC subsequent proteasomal degradation of ERCC6 in a UV-dependent manner;
CC ERCC6 degradation is essential for the recovery of RNA synthesis after
CC transcription-coupled repair (By similarity). It is required for the
CC recruitment of XAB2, HMGN1 and TCEA1/TFIIS to a transcription-coupled
CC repair complex which removes RNA polymerase II-blocking lesions from
CC the transcribed strand of active genes (By similarity). Plays a role in
CC DNA single-strand and double-strand breaks (DSSBs) repair; involved in
CC repair of DSSBs by non-homologous end joining (NHEJ) (By similarity).
CC {ECO:0000250|UniProtKB:Q13216}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Part of the CSA complex (DCX(ERCC8) complex), a DCX E3
CC ubiquitin-protein ligase complex containing ERCC8, RBX1, DDB1 and
CC CUL4A; the CSA complex interacts with RNA polymerase II; upon UV
CC irradiation it interacts with the COP9 signalosome and preferentially
CC with the hyperphosphorylated form of RNA polymerase II. Interacts with
CC ERCC6 and KIAA1530/UVSSA. Interacts with a subunit of RNA polymerase II
CC TFIIH. Interacts with DDB1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q13216}. Nucleus
CC matrix {ECO:0000250|UniProtKB:Q13216}. Note=UV-induced translocation to
CC the nuclear matrix is dependent on ERCC6.
CC {ECO:0000250|UniProtKB:Q13216}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BT021196; AAX31378.1; -; mRNA.
DR RefSeq; NP_001103651.1; NM_001110181.1.
DR AlphaFoldDB; Q5BIM8; -.
DR SMR; Q5BIM8; -.
DR STRING; 9913.ENSBTAP00000028792; -.
DR PaxDb; Q5BIM8; -.
DR Ensembl; ENSBTAT00000028792; ENSBTAP00000028792; ENSBTAG00000021606.
DR GeneID; 518857; -.
DR KEGG; bta:518857; -.
DR CTD; 1161; -.
DR VEuPathDB; HostDB:ENSBTAG00000021606; -.
DR VGNC; VGNC:28574; ERCC8.
DR eggNOG; KOG4283; Eukaryota.
DR GeneTree; ENSGT00390000009065; -.
DR HOGENOM; CLU_032951_2_2_1; -.
DR InParanoid; Q5BIM8; -.
DR OMA; MTAVKAF; -.
DR OrthoDB; 800636at2759; -.
DR TreeFam; TF101237; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000009136; Chromosome 20.
DR Bgee; ENSBTAG00000021606; Expressed in oocyte and 106 other tissues.
DR ExpressionAtlas; Q5BIM8; baseline.
DR GO; GO:0031464; C:Cul4A-RING E3 ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0016363; C:nuclear matrix; ISS:UniProtKB.
DR GO; GO:0000109; C:nucleotide-excision repair complex; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; ISS:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:Ensembl.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0097680; P:double-strand break repair via classical nonhomologous end joining; ISS:UniProtKB.
DR GO; GO:0045739; P:positive regulation of DNA repair; ISS:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0051865; P:protein autoubiquitination; ISS:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; ISS:UniProtKB.
DR GO; GO:0090262; P:regulation of transcription-coupled nucleotide-excision repair; ISS:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; ISS:UniProtKB.
DR GO; GO:0009411; P:response to UV; ISS:UniProtKB.
DR GO; GO:0010165; P:response to X-ray; IEA:Ensembl.
DR GO; GO:0000012; P:single strand break repair; ISS:UniProtKB.
DR GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR042238; Rad28/ERCC8/Ckn1/ATCSA-1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR46202; PTHR46202; 1.
DR Pfam; PF00400; WD40; 4.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 2: Evidence at transcript level;
KW DNA damage; DNA repair; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Ubl conjugation pathway; WD repeat.
FT CHAIN 1..397
FT /note="DNA excision repair protein ERCC-8"
FT /id="PRO_0000050969"
FT REPEAT 41..81
FT /note="WD 1"
FT REPEAT 97..137
FT /note="WD 2"
FT REPEAT 184..224
FT /note="WD 3"
FT REPEAT 243..282
FT /note="WD 4"
FT REPEAT 332..371
FT /note="WD 5"
FT REGION 370..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 391
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13216"
FT MOD_RES 392
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13216"
FT MOD_RES 393
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13216"
SQ SEQUENCE 397 AA; 44113 MW; 2D787B4C80CDA03F CRC64;
MLGFLSARQA GLEDPLRLRR AESTRRVLGL ELNKDRDVER IHCSGVNTLD IEPVEGRYML
SGGSDGVIVL YDLENSSRQP YYTCKAVCSV GRSHPDVHKY SVETVQWYPH DTGMFTSSSF
DKTLKVWDTN TLQIADVFNF EETVYSHHMS PVATKHCLVA VGTRGPKVQL CDLKSGSCSH
ILQGHRQEIL AVSWSPRYEY ILATASADSR AKLWDVRRAS GCLITLDQHN GKKSQAAESA
NTAHNGKVNG LCFTSDGLHL LTVGTDNRMR LWNSSNGENT LVNYGKVYND SRKGLKFTVS
SGCSSEFVFV PYGSTIAVYT IYSGEQITML KGHYKSVDCC VFQSNFQELY SGSRDCNILA
WVPSLCESVP DDDDETSTRS QLNPAFEDAW SSSDEEG
