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   27-MAR-2024, entry version 166.
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; 10090-ENSMUSP00000023206; -.
DR   PeptideAtlas; Q9QZD4; -.
DR   ProteomicsDB; 299782; -.
DR   Pumba; Q9QZD4; -.
DR   Antibodypedia; 24811; 603 antibodies from 32 providers.
DR   Ensembl; ENSMUST00000023206.14; ENSMUSP00000023206.8; ENSMUSG00000022545.14.
DR   GeneID; 50505; -.
DR   KEGG; mmu:50505; -.
DR   UCSC; uc007yfx.2; mouse.
DR   AGR; MGI:1354163; -.
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; THILDIM; -.
DR   OrthoDB; 277005at2759; -.
DR   PhylomeDB; Q9QZD4; -.
DR   TreeFam; TF101234; -.
DR   Reactome; R-MMU-5685938; HDR through Single Strand Annealing (SSA).
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 116 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 202 other cell types or tissues.
DR   ExpressionAtlas; Q9QZD4; baseline and differential.
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; IEA:Ensembl.
DR   GO; GO:0003684; F:damaged DNA binding; ISO:MGI.
DR   GO; GO:0004520; F:DNA endonuclease 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: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: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: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   CDD; cd20078; XPF_nuclease_XPF_euk; 1.
DR   Gene3D; 3.40.50.10130; -; 1.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   InterPro; IPR006166; ERCC4_domain.
DR   InterPro; IPR011335; Restrct_endonuc-II-like.
DR   InterPro; IPR010994; RuvA_2-like.
DR   InterPro; IPR006167; XPF.
DR   InterPro; IPR047520; XPF_nuclease.
DR   NCBIfam; TIGR00596; rad1; 1.
DR   PANTHER; PTHR10150; DNA REPAIR ENDONUCLEASE XPF; 1.
DR   PANTHER; PTHR10150:SF0; DNA REPAIR ENDONUCLEASE XPF; 1.
DR   Pfam; PF02732; ERCC4; 1.
DR   SMART; SM00891; ERCC4; 1.
DR   SUPFAM; SSF52980; Restriction endonuclease-like; 1.
DR   SUPFAM; SSF47781; RuvA domain 2-like; 1.
DR   Genevisible; Q9QZD4; MM.
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
//