XPF_CRIGR
ID XPF_CRIGR Reviewed; 913 AA.
AC Q9QYM7;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 3.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=DNA repair endonuclease XPF;
DE EC=3.1.-.- {ECO:0000250|UniProtKB:Q92889};
DE AltName: Full=DNA excision repair protein ERCC-4;
GN Name=ERCC4 {ECO:0000303|Ref.1};
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Hayashi T.;
RT "CHO ERCC4 cDNA.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalytic component of a structure-specific DNA repair
CC endonuclease responsible for the 5-prime incision during DNA repair,
CC and which is essential for nucleotide excision repair (NER) and
CC interstrand cross-link (ICL) repair. {ECO:0000250|UniProtKB:Q92889}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q92889};
CC -!- SUBUNIT: Heterodimer composed of ERCC1 and ERCC4/XPF. Interacts with
CC SLX4/BTBD12; this interaction is direct and links the ERCC1-ERCC4/XPF
CC complex to SLX4, which may coordinate the action of the structure-
CC specific endonuclease during DNA repair.
CC {ECO:0000250|UniProtKB:Q92889}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92889}.
CC Chromosome {ECO:0000250|UniProtKB:Q92889}. Note=Localizes to sites of
CC DNA damage. {ECO:0000250|UniProtKB:Q92889}.
CC -!- SIMILARITY: Belongs to the XPF family. {ECO:0000305}.
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DR EMBL; AB017635; BAA89229.1; -; mRNA.
DR RefSeq; NP_001230961.1; NM_001244032.1.
DR AlphaFoldDB; Q9QYM7; -.
DR SMR; Q9QYM7; -.
DR CORUM; Q9QYM7; -.
DR STRING; 10029.NP_001230961.1; -.
DR Ensembl; ENSCGRT00001004392; ENSCGRP00001003112; ENSCGRG00001003669.
DR GeneID; 100689044; -.
DR KEGG; cge:100689044; -.
DR CTD; 2072; -.
DR eggNOG; KOG0442; Eukaryota.
DR GeneTree; ENSGT00390000004394; -.
DR OrthoDB; 324863at2759; -.
DR GO; GO:0000781; C:chromosome, telomeric region; ISS:UniProtKB.
DR GO; GO:0070522; C:ERCC4-ERCC1 complex; ISS:UniProtKB.
DR GO; GO:0000110; C:nucleotide-excision repair factor 1 complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IEA:Ensembl.
DR GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
DR GO; GO:0047485; F:protein N-terminus 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:0034644; P:cellular response to UV; ISS:UniProtKB.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IEA:Ensembl.
DR GO; GO:1905768; P:negative regulation of double-stranded telomeric DNA binding; 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:1904357; P:negative regulation of telomere maintenance via telomere lengthening; IEA:Ensembl.
DR GO; GO:0006289; P:nucleotide-excision repair; ISS:UniProtKB.
DR GO; GO:1901255; P:nucleotide-excision repair involved in interstrand cross-link repair; ISS:UniProtKB.
DR GO; GO:0006295; P:nucleotide-excision repair, DNA incision, 3'-to lesion; ISS:UniProtKB.
DR GO; GO:0006296; P:nucleotide-excision repair, DNA incision, 5'-to lesion; ISS:UniProtKB.
DR GO; GO:0010506; P:regulation of autophagy; IEA:Ensembl.
DR GO; GO:0009411; P:response to UV; ISS:UniProtKB.
DR GO; GO:0061819; P:telomeric DNA-containing double minutes formation; IEA:Ensembl.
DR GO; GO:0009650; P:UV protection; IEA:Ensembl.
DR InterPro; IPR006166; ERCC4_domain.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR InterPro; IPR010994; RuvA_2-like.
DR InterPro; IPR006167; XPF.
DR Pfam; PF02732; ERCC4; 1.
DR SMART; SM00891; ERCC4; 1.
DR SUPFAM; SSF47781; SSF47781; 1.
DR SUPFAM; SSF52980; SSF52980; 1.
DR TIGRFAMs; TIGR00596; rad1; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Chromosome; DNA damage; DNA repair; DNA-binding; Endonuclease;
KW Hydrolase; Magnesium; Nuclease; Nucleus; Phosphoprotein; Repeat.
FT CHAIN 1..913
FT /note="DNA repair endonuclease XPF"
FT /id="PRO_0000198852"
FT DOMAIN 680..760
FT /note="ERCC4"
FT REGION 1..454
FT /note="Helicase-like"
FT /evidence="ECO:0000250|UniProtKB:Q92889"
FT REGION 233..254
FT /note="Leucine-zipper 1"
FT /evidence="ECO:0000250|UniProtKB:Q92889"
FT REGION 270..298
FT /note="Leucine-zipper 2"
FT /evidence="ECO:0000250|UniProtKB:Q92889"
FT REGION 453..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 638..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 655..810
FT /note="Nuclease"
FT /evidence="ECO:0000250|UniProtKB:Q92889"
FT REGION 834..902
FT /note="HhH2, dimerization with ERCC1"
FT /evidence="ECO:0000250|UniProtKB:Q92889"
FT MOTIF 483..488
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 453..476
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 289
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q92889"
FT MOD_RES 518
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QZD4"
SQ SEQUENCE 913 AA; 103187 MW; D1C0DFF990A0F0C3 CRC64;
MDRGISAVRK AMAPLLEYER QLVLELLDSD GLVVCARGLG ADRLLYHFLR LHCHPACLVL
VLNTQPAEEE YFINQLKIEG VEHLPRRVTN EITSNSRYEV YTQGGIIFAT SRILVVDFLT
DRIPSDLITG ILVYRAHRII ESCQEAFILR LFRQKNKRGF IKAFTDNAVA FDTGFCHVER
VMRNLFVRKL YLWPRFHVAV NSFLEQHKPE VVEIHVSMTP AMLSIQTAIL DILNACLKEL
KCHNPSLEVE DLSLENALGK PFDKTIRHYL DPLWHQLGAK TKSLVQDLKI LRTLLQYLSQ
YDCVTFLNLL ESLRATEKVF GQNSGWLFLD ASTSMFVNAR ARVYRVPDVK LNKKAKMSES
AEGQETKKEL VLESNPKWEA LSEVLKEIEA ENKESEALGG PGQVLICASD DRTCCQLRDY
LTAGAEAFLL RLYRKTFEKD SKAEEVWVNL RKGDGPKRTM KSDKRPKDTK NKERASTKKG
APKRKKRELT LTQVMGTAEE PPEEGAAEED QQRQATSSPE GCGGEIQHEA FDLNLSSDSA
YGILKEPLTI IHPLVGCSDP YALTRVLHEV EPRYVVLYDA ELTFVRQLEI YRASRPGKPL
RVYFLIYGGS TEEQRYLTAL RKEKEAFEKL IREKASMVVP EEREGRDETN LDLARGTVST
DAPADTRKAG GQEHNGTQPS IVVDMREFRS ELPSLIHRRG IDIEPVTLEV GDYILTPELC
VERKSVSDLI GSLNSGRLYS QCLAMSRYYR RPVLLIEFDA GKPFSLAPRG SFFQEMSSSD
VSSKLTLLTL HFPRLRLLWC PSPHATAELF EELKQNKPQP DAATAMAITA DSETLPESDK
YNPGPQDFVL KMPGINAKNC HSLMNHVKNI AELASLSQER LTSILGHAGN AKQLYDFLHT
AYADVVSGGR VRK
