ERCC1_BOVIN
ID ERCC1_BOVIN Reviewed; 294 AA.
AC Q1LZ75;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=DNA excision repair protein ERCC-1;
GN Name=ERCC1;
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].
RC STRAIN=Hereford; TISSUE=Fetal cerebellum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Non-catalytic component of a structure-specific DNA repair
CC endonuclease responsible for the 5'-incision during DNA repair.
CC Responsible, in conjunction with SLX4, for the first step in the repair
CC of interstrand cross-links (ICL). Participates in the processing of
CC anaphase bridge-generating DNA structures, which consist in
CC incompletely processed DNA lesions arising during S or G2 phase, and
CC can result in cytokinesis failure. Also required for homology-directed
CC repair (HDR) of DNA double-strand breaks, in conjunction with SLX4 (By
CC similarity). {ECO:0000250|UniProtKB:P07992}.
CC -!- SUBUNIT: Heterodimer composed of ERCC1 and ERRC4/XPF (By similarity).
CC Interacts with USP4 (By similarity). {ECO:0000250|UniProtKB:P07992}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07992}.
CC -!- PTM: Ubiquitinated with both 'Lys-48' and 'Lys-63' linkages.
CC Deubiquitinated by USP45. {ECO:0000250|UniProtKB:P07992}.
CC -!- SIMILARITY: Belongs to the ERCC1/RAD10/SWI10 family. {ECO:0000305}.
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DR EMBL; BC116163; AAI16164.1; -; mRNA.
DR RefSeq; NP_001069853.1; NM_001076385.2.
DR RefSeq; XP_005219393.1; XM_005219336.3.
DR RefSeq; XP_005219394.1; XM_005219337.2.
DR RefSeq; XP_010813384.1; XM_010815082.2.
DR AlphaFoldDB; Q1LZ75; -.
DR BMRB; Q1LZ75; -.
DR SMR; Q1LZ75; -.
DR STRING; 9913.ENSBTAP00000023078; -.
DR PaxDb; Q1LZ75; -.
DR PRIDE; Q1LZ75; -.
DR Ensembl; ENSBTAT00000023078; ENSBTAP00000023078; ENSBTAG00000017355.
DR GeneID; 615637; -.
DR KEGG; bta:615637; -.
DR CTD; 2067; -.
DR VEuPathDB; HostDB:ENSBTAG00000017355; -.
DR VGNC; VGNC:28568; ERCC1.
DR eggNOG; KOG2841; Eukaryota.
DR GeneTree; ENSGT00390000011275; -.
DR HOGENOM; CLU_041616_3_1_1; -.
DR InParanoid; Q1LZ75; -.
DR OMA; LNPDYIC; -.
DR OrthoDB; 1336192at2759; -.
DR TreeFam; TF101231; -.
DR Reactome; R-BTA-5696395; Formation of Incision Complex in GG-NER.
DR Reactome; R-BTA-6783310; Fanconi Anemia Pathway.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000017355; Expressed in digestive system secreted substance and 106 other tissues.
DR GO; GO:0000781; C:chromosome, telomeric region; ISS:UniProtKB.
DR GO; GO:0070522; C:ERCC4-ERCC1 complex; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0000109; C:nucleotide-excision repair complex; ISS:UniProtKB.
DR GO; GO:0000110; C:nucleotide-excision repair factor 1 complex; IBA:GO_Central.
DR GO; GO:1990599; F:3' overhang single-stranded DNA endodeoxyribonuclease activity; IEA:Ensembl.
DR GO; GO:0003684; F:damaged DNA binding; ISS:UniProtKB.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IEA:Ensembl.
DR GO; GO:0008022; F:protein C-terminus binding; ISS:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0001094; F:TFIID-class transcription factor complex binding; IEA:Ensembl.
DR GO; GO:0008283; P:cell population proliferation; IEA:Ensembl.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IEA:Ensembl.
DR GO; GO:0036297; P:interstrand cross-link repair; IEA:Ensembl.
DR GO; GO:0045190; P:isotype switching; IEA:Ensembl.
DR GO; GO:0008584; P:male gonad development; IEA:Ensembl.
DR GO; GO:0000710; P:meiotic mismatch repair; IBA:GO_Central.
DR GO; GO:0006312; P:mitotic recombination; ISS:UniProtKB.
DR GO; GO:0010259; P:multicellular organism aging; IEA:Ensembl.
DR GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
DR GO; GO:1905765; P:negative regulation of protection from non-homologous end joining at telomere; IEA:Ensembl.
DR GO; GO:0032205; P:negative regulation of telomere maintenance; ISS:UniProtKB.
DR GO; GO:0006289; P:nucleotide-excision repair; ISS:UniProtKB.
DR GO; GO:0006296; P:nucleotide-excision repair, DNA incision, 5'-to lesion; IBA:GO_Central.
DR GO; GO:0048477; P:oogenesis; IEA:Ensembl.
DR GO; GO:1904431; P:positive regulation of t-circle formation; IEA:Ensembl.
DR GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; IEA:Ensembl.
DR GO; GO:0035166; P:post-embryonic hemopoiesis; IEA:Ensembl.
DR GO; GO:0000720; P:pyrimidine dimer repair by nucleotide-excision repair; IEA:Ensembl.
DR GO; GO:0090399; P:replicative senescence; IEA:Ensembl.
DR GO; GO:0006979; P:response to oxidative stress; ISS:UniProtKB.
DR GO; GO:0010165; P:response to X-ray; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR GO; GO:0006949; P:syncytium formation; IEA:Ensembl.
DR GO; GO:0090656; P:t-circle formation; IEA:Ensembl.
DR GO; GO:0061819; P:telomeric DNA-containing double minutes formation; IEA:Ensembl.
DR GO; GO:0009650; P:UV protection; IEA:Ensembl.
DR GO; GO:0070914; P:UV-damage excision repair; IBA:GO_Central.
DR InterPro; IPR004579; ERCC1/RAD10/SWI10.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR InterPro; IPR010994; RuvA_2-like.
DR PANTHER; PTHR12749; PTHR12749; 1.
DR Pfam; PF03834; Rad10; 1.
DR SUPFAM; SSF47781; SSF47781; 1.
DR SUPFAM; SSF52980; SSF52980; 1.
DR TIGRFAMs; TIGR00597; rad10; 1.
PE 2: Evidence at transcript level;
KW DNA damage; DNA repair; DNA-binding; Isopeptide bond; Nucleus;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..294
FT /note="DNA excision repair protein ERCC-1"
FT /id="PRO_0000290359"
FT DNA_BIND 130..152
FT /evidence="ECO:0000255"
FT REGION 1..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 220..294
FT /note="HhH2, dimerization with ERRC4/XPF"
FT /evidence="ECO:0000250|UniProtKB:P07992"
FT MOTIF 13..19
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT CROSSLNK 17
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P07992"
FT CROSSLNK 33
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P07992"
FT CROSSLNK 239
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P07992"
SQ SEQUENCE 294 AA; 32544 MW; 078113580EAC1015 CRC64;
MDEEGVHKPA GPPTRKKFLI PTDEDVVPPP GAKPLFRSTR SLPTVETSPP PGPQTYAEYA
LSGPPGGAEA TRPVGPEPLA EETPNQAPKP GAKSNSIIVS PRQRGNPVLR FVRNVPWEFG
DVLPDYVLGQ STCALFLSLR YHNLHPDYIH QRLQSLGKSY ALRVLLVQVD VKDPQQALKE
LAKMCILADC TLILAWSPEE AGRYLETYKA YEQKPADLLM EKLEQDFVSR VTECLTTVKS
VNKTDSQTLL TTFGSLEQLI AASREDLSLC PGLGPQKARR LFDVFHEPFL KVPH
