ID   E9QM61_MOUSE            Unreviewed;      1170 AA.
AC   E9QM61;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 96.
DE   SubName: Full=Excision repair cross-complementing rodent repair deficiency, complementation group 5 {ECO:0000313|Ensembl:ENSMUSP00000027214.4};
GN   Name=Ercc5 {ECO:0000313|Ensembl:ENSMUSP00000027214.4,
GN   ECO:0000313|MGI:MGI:103582};
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 {ECO:0000313|Ensembl:ENSMUSP00000027214.4, ECO:0000313|Proteomes:UP000000589};
RN   [1] {ECO:0007829|PubMed:17242355}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [2] {ECO:0000313|Ensembl:ENSMUSP00000027214.4, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000027214.4,
RC   ECO:0000313|Proteomes:UP000000589};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3] {ECO:0007829|PubMed:21183079}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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).
RN   [4] {ECO:0000313|Ensembl:ENSMUSP00000027214.4}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000027214.4};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. XPG subfamily.
CC       {ECO:0000256|ARBA:ARBA00005283}.
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DR   RefSeq; NP_035859.2; NM_011729.2.
DR   AlphaFoldDB; E9QM61; -.
DR   SMR; E9QM61; -.
DR   jPOST; E9QM61; -.
DR   MaxQB; E9QM61; -.
DR   ProteomicsDB; 315946; -.
DR   DNASU; 22592; -.
DR   Ensembl; ENSMUST00000027214.4; ENSMUSP00000027214.4; ENSMUSG00000026048.17.
DR   GeneID; 22592; -.
DR   KEGG; mmu:22592; -.
DR   UCSC; uc007awi.2; mouse.
DR   AGR; MGI:103582; -.
DR   CTD; 2073; -.
DR   MGI; MGI:103582; Ercc5.
DR   VEuPathDB; HostDB:ENSMUSG00000026048; -.
DR   GeneTree; ENSGT00510000048601; -.
DR   HOGENOM; CLU_003018_2_0_1; -.
DR   OMA; PNSMDFS; -.
DR   OrthoDB; 26655at2759; -.
DR   PhylomeDB; E9QM61; -.
DR   TreeFam; TF101235; -.
DR   BioGRID-ORCS; 22592; 4 hits in 116 CRISPR screens.
DR   ChiTaRS; Ercc5; mouse.
DR   Proteomes; UP000000589; Chromosome 1.
DR   Bgee; ENSMUSG00000026048; Expressed in rostral migratory stream and 256 other cell types or tissues.
DR   GO; GO:0005662; C:DNA replication factor A complex; IEA:Ensembl.
DR   GO; GO:0000109; C:nucleotide-excision repair complex; IEA:Ensembl.
DR   GO; GO:0000405; F:bubble DNA binding; IEA:Ensembl.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:Ensembl.
DR   GO; GO:0004520; F:DNA endonuclease activity; IEA:Ensembl.
DR   GO; GO:0003690; F:double-stranded DNA binding; IEA:Ensembl.
DR   GO; GO:0008047; F:enzyme activator activity; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR   GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR   GO; GO:0000993; F:RNA polymerase II complex binding; IEA:Ensembl.
DR   GO; GO:0003697; F:single-stranded DNA binding; IEA:Ensembl.
DR   GO; GO:0006285; P:base-excision repair, AP site formation; IEA:Ensembl.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:Ensembl.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR   GO; GO:0010225; P:response to UV-C; IEA:Ensembl.
DR   GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; IEA:Ensembl.
DR   CDD; cd09904; H3TH_XPG; 1.
DR   CDD; cd09868; PIN_XPG_RAD2; 2.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   Gene3D; 3.40.50.1010; 5'-nuclease; 2.
DR   InterPro; IPR036279; 5-3_exonuclease_C_sf.
DR   InterPro; IPR008918; HhH2.
DR   InterPro; IPR029060; PIN-like_dom_sf.
DR   InterPro; IPR006086; XPG-I_dom.
DR   InterPro; IPR006084; XPG/Rad2.
DR   InterPro; IPR001044; XPG/Rad2_eukaryotes.
DR   InterPro; IPR019974; XPG_CS.
DR   InterPro; IPR006085; XPG_DNA_repair_N.
DR   NCBIfam; TIGR00600; rad2; 1.
DR   PANTHER; PTHR16171:SF7; DNA EXCISION REPAIR PROTEIN ERCC-5; 1.
DR   PANTHER; PTHR16171; DNA REPAIR PROTEIN COMPLEMENTING XP-G CELLS-RELATED; 1.
DR   Pfam; PF00867; XPG_I; 1.
DR   Pfam; PF00752; XPG_N; 1.
DR   PRINTS; PR00853; XPGRADSUPER.
DR   PRINTS; PR00066; XRODRMPGMNTG.
DR   SMART; SM00279; HhH2; 1.
DR   SMART; SM00484; XPGI; 1.
DR   SMART; SM00485; XPGN; 1.
DR   SUPFAM; SSF47807; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   SUPFAM; SSF88723; PIN domain-like; 1.
DR   PROSITE; PS00841; XPG_1; 1.
DR   PROSITE; PS00842; XPG_2; 1.
DR   Genevisible; E9QM61; MM.
PE   1: Evidence at protein level;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Proteomics identification {ECO:0007829|EPD:E9QM61,
KW   ECO:0007829|MaxQB:E9QM61};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589}.
FT   DOMAIN          1..98
FT                   /note="XPG N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00485"
FT   DOMAIN          776..845
FT                   /note="XPG-I"
FT                   /evidence="ECO:0000259|SMART:SM00484"
FT   REGION          304..479
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          520..587
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          600..701
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1034..1146
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        305..324
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        358..372
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        393..408
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        418..432
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        449..479
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        560..578
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        652..673
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        674..697
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1034..1063
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1079..1109
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1170 AA;  130812 MW;  AEB8F387BE7690FF CRC64;
     MGVQGLWKLL ECSGHRVSPE ALEGKVLAVD ISIWLNQALK GVRDSHGNVI ENAHLLTLFH
     RLCKLLFFRI RPIFVFDGDA PLLKKQTLAK RRQRKDSASI DSRKTTEKLL KTFLKRQALK
     TAFRSSRHEA PPSLTQVQRQ DDIYVLPPLP EEEKHSSEEE DEKQWQARMD QKQALQEEFF
     HNPQAIDIES EDFSSLPPEV KHEILTDMKE FTKRRRTLFE AMPEESNDFS QYQLKGLLKK
     NYLNQHIENV QKEMNQQHSG QIQRQYQDEG GFLKEVESRR VVSEDTSHYI LIKGIQGKKV
     MDVDSESLPS SSNVHSVSSN LKSSPHEKVK PEREPEAAPP SPRTLLAIQA AMLGSSSEDE
     PESREGRQSK ERNSGATADA GSISPRTCAA IQKALDDDND EKVSGSSDDL AEKMLLGSGL
     EQEEHADETA ERGGGVPFDT APLTPSVTEV KECVTSGSSA NGQTDSAHSF TTASHRCDTP
     KETVSLARAV KEASQISSEC EVEGRPAALS PAFIGTPSSH VSGVLSEREP TLAPPTTRTH
     SDQGIDIHPE DPELQNGLYP LETKCNSSRL SSDDETEGGQ NPAPKACSTV HVPAEAMSNL
     ENALPSNAEE RGDFQETIQL REVPEAAARE LISAPKPMGP MEMESEESES DGSFIEVQSV
     VSNSELQTES SEASTHLSEK DAEEPRETLE EGTSRDTECL LQDSSDIEAM EGHREADIDA
     EDMPNEWQDI NLEELDALES NLLAEQNSLK AQKQQQDRIA ASVTGQMFLE SQELLRLFGV
     PYIQAPMEAE AQCAMLDLTD QTSGTITDDS DIWLFGARHV YKNFFNKNKF VEYYQYVDFY
     SQLGLDRNKL INLAYLLGSD YTEGIPTVGC VTAMEILNEF PGRGLDPLLK FSEWWHEAQN
     NKKVAENPYD TKVKKKLRKL QLTPGFPNPA VADAYLRPVV DDSRGSFLWG KPDVDKIREF
     CQRYFGWNRM KTDESLYPVL KHLNAHQTQL RIDSFFRLAQ QEKQDAKLIK SHRLNRAVTC
     ILRKEREEKA PELTKVTEAL DDAKGKTQKR ELPYKKETSV PKRRRPSGNG GFLGDPYCSE
     SPQESSCEDG EGSSVMSARQ RSAAESSKIS CSDVPDLVRD PPHGRQGCVS TSSSSEDDED
     KAKTVLVTAR PVFGKKKLKL KSMKRRKKKT
//