XPF_MOUSE
ID XPF_MOUSE Reviewed; 917 AA.
AC Q9QZD4; O54810; Q8R0I3;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 3.
DT 03-AUG-2022, entry version 157.
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.2, ECO:0000312|MGI:MGI:1354163};
GN Synonyms=Xpf {ECO:0000303|PubMed:10644440};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10644440; DOI=10.1006/geno.1999.6016;
RA Shannon M., Lamerdin J.E., Richardson L., McCutchen-Maloney S.L.,
RA Hwang M.H., Handel M.A., Stubbs L., Thelen M.P.;
RT "Characterization of the mouse xpf DNA repair gene and differential
RT expression during spermatogenesis.";
RL Genomics 62:427-435(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Lamerdin J.E., McCready P.M., Skowronski E., Adamson A.W.,
RA Burkhart-Schultz K., Gordon L., Kyle A., Ramirez M., Stilwagen S., Phan H.,
RA Velasco N., Garnes J., Danganan L., Poundstone P., Christensen M.,
RA Georgescu A., Avila J., Liu S., Attix C., Andreise T., Trankheim M.,
RA Amico-Keller G., Coefield J., Duarte S., Lucas S., Bruce R., Thomas P.,
RA Quan G., Kronmiller B., Arellano A., Montgomery M., Ow D., Nolan M.,
RA Trong S., Kobayashi A., Olsen A.O., Carrano A.V.;
RT "Sequence analysis of a mouse BAC containing the DNA repair gene Ercc-4
RT (XPF).";
RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-917.
RC TISSUE=Salivary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-522 AND SER-765, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 -!- PTM: Acetylation at Lys-912 by KAT5 promotes interaction with ERCC1 by
CC disrupting a salt bridge between Asp-908 and Lys-912, thereby exposing
CC a second binding site for ERCC1 (By similarity). Deacetylated by SIRT1
CC (By similarity). {ECO:0000250|UniProtKB:Q92889}.
CC -!- SIMILARITY: Belongs to the XPF family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH26792.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF189285; AAF03157.1; -; mRNA.
DR EMBL; AC004155; AAC03240.1; -; Genomic_DNA.
DR EMBL; BC026792; AAH26792.1; ALT_INIT; mRNA.
DR CCDS; CCDS37256.1; -.
DR RefSeq; NP_056584.2; NM_015769.2.
DR AlphaFoldDB; Q9QZD4; -.
DR SMR; Q9QZD4; -.
DR BioGRID; 206047; 5.
DR ComplexPortal; CPX-491; Ercc1-Xpf endonuclease complex.
DR STRING; 10090.ENSMUSP00000023206; -.
DR iPTMnet; Q9QZD4; -.
DR PhosphoSitePlus; Q9QZD4; -.
DR EPD; Q9QZD4; -.
DR jPOST; Q9QZD4; -.
DR MaxQB; Q9QZD4; -.
DR PaxDb; Q9QZD4; -.
DR PeptideAtlas; Q9QZD4; -.
DR PRIDE; Q9QZD4; -.
DR ProteomicsDB; 299782; -.
DR Antibodypedia; 24811; 545 antibodies from 32 providers.
DR Ensembl; ENSMUST00000023206; ENSMUSP00000023206; ENSMUSG00000022545.
DR GeneID; 50505; -.
DR KEGG; mmu:50505; -.
DR UCSC; uc007yfx.2; mouse.
DR CTD; 2072; -.
DR MGI; MGI:1354163; Ercc4.
DR VEuPathDB; HostDB:ENSMUSG00000022545; -.
DR eggNOG; KOG0442; Eukaryota.
DR GeneTree; ENSGT00390000004394; -.
DR HOGENOM; CLU_002265_1_0_1; -.
DR InParanoid; Q9QZD4; -.
DR OMA; FHKILQA; -.
DR OrthoDB; 324863at2759; -.
DR PhylomeDB; Q9QZD4; -.
DR TreeFam; TF101234; -.
DR Reactome; R-MMU-5696395; Formation of Incision Complex in GG-NER.
DR Reactome; R-MMU-5696400; Dual Incision in GG-NER.
DR Reactome; R-MMU-6782135; Dual incision in TC-NER.
DR Reactome; R-MMU-6783310; Fanconi Anemia Pathway.
DR BioGRID-ORCS; 50505; 12 hits in 111 CRISPR screens.
DR ChiTaRS; Ercc4; mouse.
DR PRO; PR:Q9QZD4; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q9QZD4; protein.
DR Bgee; ENSMUSG00000022545; Expressed in metanephric loop of Henle and 199 other tissues.
DR ExpressionAtlas; Q9QZD4; baseline and differential.
DR Genevisible; Q9QZD4; MM.
DR GO; GO:0000781; C:chromosome, telomeric region; ISO:MGI.
DR GO; GO:0070522; C:ERCC4-ERCC1 complex; ISS:UniProtKB.
DR GO; GO:0000109; C:nucleotide-excision repair complex; ISO:MGI.
DR GO; GO:0000110; C:nucleotide-excision repair factor 1 complex; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:1990599; F:3' overhang single-stranded DNA endodeoxyribonuclease activity; ISO:MGI.
DR GO; GO:0003684; F:damaged DNA binding; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; ISO:MGI.
DR GO; GO:0004520; F:endodeoxyribonuclease activity; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IDA:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
DR GO; GO:0003697; F:single-stranded DNA binding; ISO:MGI.
DR GO; GO:0000014; F:single-stranded DNA endodeoxyribonuclease activity; IBA:GO_Central.
DR GO; GO:0001094; F:TFIID-class transcription factor complex binding; IDA:MGI.
DR GO; GO:0034644; P:cellular response to UV; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IMP:MGI.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; ISO:MGI.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; ISO:MGI.
DR GO; GO:1905768; P:negative regulation of double-stranded telomeric DNA binding; ISO:MGI.
DR GO; GO:1905765; P:negative regulation of protection from non-homologous end joining at telomere; ISO:MGI.
DR GO; GO:0032205; P:negative regulation of telomere maintenance; ISO:MGI.
DR GO; GO:1904357; P:negative regulation of telomere maintenance via telomere lengthening; ISO:MGI.
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:0033683; P:nucleotide-excision repair, DNA incision; ISO:MGI.
DR GO; GO:0006295; P:nucleotide-excision repair, DNA incision, 3'-to lesion; ISO:MGI.
DR GO; GO:0006296; P:nucleotide-excision repair, DNA incision, 5'-to lesion; ISO:MGI.
DR GO; GO:0010506; P:regulation of autophagy; IMP:MGI.
DR GO; GO:0000712; P:resolution of meiotic recombination intermediates; IBA:GO_Central.
DR GO; GO:0009411; P:response to UV; ISO:MGI.
DR GO; GO:0000723; P:telomere maintenance; ISO:MGI.
DR GO; GO:0061819; P:telomeric DNA-containing double minutes formation; ISO:MGI.
DR GO; GO:0009650; P:UV protection; IMP:MGI.
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 1: Evidence at protein level;
KW Acetylation; Chromosome; DNA damage; DNA repair; DNA-binding; Endonuclease;
KW Hydrolase; Magnesium; Nuclease; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..917
FT /note="DNA repair endonuclease XPF"
FT /id="PRO_0000198854"
FT DOMAIN 684..764
FT /note="ERCC4"
FT REGION 1..457
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 454..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 643..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 659..814
FT /note="Nuclease"
FT /evidence="ECO:0000250|UniProtKB:Q92889"
FT REGION 838..906
FT /note="HhH2, dimerization with ERCC1"
FT /evidence="ECO:0000250|UniProtKB:Q92889"
FT MOTIF 487..492
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 454..489
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 522
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 765
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 912
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q92889"
FT CONFLICT 30
FT /note="D -> N (in Ref. 1; AAF03157)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 917 AA; 103690 MW; 2206DC264BC4E233 CRC64;
MEPGLSGERR SMAPLLEYER QQVLELLDSD GLVVCARGLG TDRLLYHFLR LHCHPACLVL
VLNTQPAEEE YFINQLKIEG VEHLPRRVTN EIASNSRYEV YTQGGIIFAT SRILVVDFLT
GRIPSDLITG ILVYRAHRII ESCQEAFILR LFRQKNKRGF IKAFTDNAVA FDTGFCHVER
VMRNLFVRKL YLWPRFHVAV NSFLEQHKPE VVEIHVSMTP AMLAIQTAIL DILNACLKEL
KCHNPSLEVE DLSLENALGK PFDKTIRHYL DPLWHQLGAK TKSLVQDLKI LRTLLQYLSQ
YDCVTFLNLL ESLRATEKVF GQNSGWLFLD ASTSMFVNAR ARVYRVPDVK LNKKAKTSEK
TSSPEVQETK KELVLESNPK WEALTDVLKE IEAENKESEA LGGPGRVLIC ASDDRTCCQL
RDYLSAGAET FLLRLYRKTF EKDGKAEEVW VNVRKGDGPK RTTKSDKRPK AAPNKERASA
KRGAPLKRKK QELTLTQVLG SAEEPPEDKA LEEDLCRQTS SSPEGCGVEI KRESFDLNVS
SDAAYGILKE PLTIIHPLLG CSDPYALTRV LHEVEPRYVV LYDAELTFVR QLEIYRASRP
GKPLRVYFLI YGGSTEEQRY LTALRKEKEA FEKLIREKAS MVVPEEREGR DETNLDLARG
SAALDAPTDT RKAGGQEQNG TQSSIVVDMR EFRSELPSLI HRRGIDIEPV TLEVGDYILT
PELCVERKSV SDLIGSLHSG RLYSQCLAMS RYYRRPVLLI EFDPSKPFSL APRGAFFQEM
SSSDVSSKLT LLTLHFPRLR LLWCPSPHAT AELFEELKQN KPQPDAATAM AITADSETLP
ESDRYNPGPQ DFVLKMPGVN AKNCRSLMNQ VKNIAELATL SLERLTTILG HSGNAKQLHD
FLHTAYADLV SKGRVRK
