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Q9QZD4 (XPF_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA repair endonuclease XPF

EC=3.1.-.-
Alternative name(s):
DNA excision repair protein ERCC-4
Gene names
Name:Ercc4
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length917 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalytic component of a structure-specific DNA repair endonuclease responsible for the 5-prime incision during DNA repair. Involved in homologous recombination that assists in removing interstrand cross-link By similarity.

Cofactor

Magnesium By similarity.

Subunit structure

Heterodimer composed of ERCC1 and XPF/ERCC4. Interacts with SLX4/BTBD12; this interaction is direct and links the ERCC1-XPF/ERCC1 complex to SLX4, which may coordinate the action of the structure-specific endonuclease during DNA repair By similarity.

Subcellular location

Nucleus By similarity.

Sequence similarities

Belongs to the XPF family.

Contains 1 ERCC4 domain.

Sequence caution

The sequence AAH26792.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
   Cellular componentNucleus
   DomainRepeat
   LigandDNA-binding
Magnesium
   Molecular functionEndonuclease
Hydrolase
Nuclease
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA catabolic process, endonucleolytic

Inferred from Biological aspect of Ancestor. Source: GOC

DNA repair

Inferred from mutant phenotype PubMed 14729965. Source: MGI

UV protection

Inferred from mutant phenotype PubMed 14729965. Source: MGI

double-strand break repair via homologous recombination

Inferred from Biological aspect of Ancestor. Source: RefGenome

meiotic mismatch repair

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of telomere maintenance

Inferred from electronic annotation. Source: Ensembl

nucleotide-excision repair

Inferred from sequence orthology Ref.1. Source: MGI

nucleotide-excision repair, DNA incision, 3'-to lesion

Inferred from electronic annotation. Source: Ensembl

nucleotide-excision repair, DNA incision, 5'-to lesion

Inferred from Biological aspect of Ancestor. Source: RefGenome

resolution of meiotic recombination intermediates

Inferred from Biological aspect of Ancestor. Source: RefGenome

telomere maintenance via telomere shortening

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentnuclear chromosome, telomeric region

Inferred from electronic annotation. Source: Ensembl

nucleotide-excision repair complex

Inferred from sequence orthology Ref.1. Source: MGI

nucleotide-excision repair factor 1 complex

Inferred from Biological aspect of Ancestor. Source: RefGenome

transcription factor TFIID complex

Inferred from direct assay PubMed 22323595. Source: MGI

   Molecular_functionTFIID-class transcription factor binding

Inferred from direct assay PubMed 22323595. Source: MGI

damaged DNA binding

Inferred from electronic annotation. Source: Ensembl

single-stranded DNA binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

single-stranded DNA endodeoxyribonuclease activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 917917DNA repair endonuclease XPF
PRO_0000198854

Regions

Domain684 – 76481ERCC4
Region1 – 457457Helicase-like By similarity
Region233 – 25422Leucine-zipper 1
Region270 – 29829Leucine-zipper 2
Region659 – 814156Nuclease By similarity
Region838 – 90669HhH2, dimerization with ERCC1 By similarity
Motif487 – 4926Nuclear localization signal Potential

Amino acid modifications

Modified residue2891N6-acetyllysine By similarity

Experimental info

Sequence conflict301D → N in AAF03157. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9QZD4 [UniParc].

Last modified May 5, 2009. Version 3.
Checksum: 2206DC264BC4E233

FASTA917103,690
        10         20         30         40         50         60 
MEPGLSGERR SMAPLLEYER QQVLELLDSD GLVVCARGLG TDRLLYHFLR LHCHPACLVL 

        70         80         90        100        110        120 
VLNTQPAEEE YFINQLKIEG VEHLPRRVTN EIASNSRYEV YTQGGIIFAT SRILVVDFLT 

       130        140        150        160        170        180 
GRIPSDLITG ILVYRAHRII ESCQEAFILR LFRQKNKRGF IKAFTDNAVA FDTGFCHVER 

       190        200        210        220        230        240 
VMRNLFVRKL YLWPRFHVAV NSFLEQHKPE VVEIHVSMTP AMLAIQTAIL DILNACLKEL 

       250        260        270        280        290        300 
KCHNPSLEVE DLSLENALGK PFDKTIRHYL DPLWHQLGAK TKSLVQDLKI LRTLLQYLSQ 

       310        320        330        340        350        360 
YDCVTFLNLL ESLRATEKVF GQNSGWLFLD ASTSMFVNAR ARVYRVPDVK LNKKAKTSEK 

       370        380        390        400        410        420 
TSSPEVQETK KELVLESNPK WEALTDVLKE IEAENKESEA LGGPGRVLIC ASDDRTCCQL 

       430        440        450        460        470        480 
RDYLSAGAET FLLRLYRKTF EKDGKAEEVW VNVRKGDGPK RTTKSDKRPK AAPNKERASA 

       490        500        510        520        530        540 
KRGAPLKRKK QELTLTQVLG SAEEPPEDKA LEEDLCRQTS SSPEGCGVEI KRESFDLNVS 

       550        560        570        580        590        600 
SDAAYGILKE PLTIIHPLLG CSDPYALTRV LHEVEPRYVV LYDAELTFVR QLEIYRASRP 

       610        620        630        640        650        660 
GKPLRVYFLI YGGSTEEQRY LTALRKEKEA FEKLIREKAS MVVPEEREGR DETNLDLARG 

       670        680        690        700        710        720 
SAALDAPTDT RKAGGQEQNG TQSSIVVDMR EFRSELPSLI HRRGIDIEPV TLEVGDYILT 

       730        740        750        760        770        780 
PELCVERKSV SDLIGSLHSG RLYSQCLAMS RYYRRPVLLI EFDPSKPFSL APRGAFFQEM 

       790        800        810        820        830        840 
SSSDVSSKLT LLTLHFPRLR LLWCPSPHAT AELFEELKQN KPQPDAATAM AITADSETLP 

       850        860        870        880        890        900 
ESDRYNPGPQ DFVLKMPGVN AKNCRSLMNQ VKNIAELATL SLERLTTILG HSGNAKQLHD 

       910 
FLHTAYADLV SKGRVRK 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of the mouse xpf DNA repair gene and differential expression during spermatogenesis."
Shannon M., Lamerdin J.E., Richardson L., McCutchen-Maloney S.L., Hwang M.H., Handel M.A., Stubbs L., Thelen M.P.
Genomics 62:427-435(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Sequence analysis of a mouse BAC containing the DNA repair gene Ercc-4 (XPF)."
Lamerdin J.E., McCready P.M., Skowronski E., Adamson A.W., Burkhart-Schultz K., Gordon L., Kyle A., Ramirez M., Stilwagen S., Phan H., Velasco N., Garnes J., Danganan L., Poundstone P., Christensen M., Georgescu A., Avila J., Liu S. expand/collapse author list , Attix C., Andreise T., Trankheim M., Amico-Keller G., Coefield J., Duarte S., Lucas S., Bruce R., Thomas P., Quan G., Kronmiller B., Arellano A., Montgomery M., Ow D., Nolan M., Trong S., Kobayashi A., Olsen A.O., Carrano A.V.
Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-917.
Tissue: Salivary gland.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF189285 mRNA. Translation: AAF03157.1.
AC004155 Genomic DNA. Translation: AAC03240.1.
BC026792 mRNA. Translation: AAH26792.1. Different initiation.
RefSeqNP_056584.2. NM_015769.2.
UniGeneMm.287837.

3D structure databases

ProteinModelPortalQ9QZD4.
SMRQ9QZD4. Positions 677-917.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ9QZD4.

Proteomic databases

PaxDbQ9QZD4.
PRIDEQ9QZD4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000023206; ENSMUSP00000023206; ENSMUSG00000022545.
GeneID50505.
KEGGmmu:50505.
UCSCuc007yfx.2. mouse.

Organism-specific databases

CTD2072.
MGIMGI:1354163. Ercc4.

Phylogenomic databases

eggNOGCOG1948.
GeneTreeENSGT00390000004394.
HOGENOMHOG000202204.
HOVERGENHBG051500.
InParanoidQ9QZD4.
KOK10848.
OMARIIWSSS.
OrthoDBEOG7VTDM8.
PhylomeDBQ9QZD4.
TreeFamTF101234.

Gene expression databases

ArrayExpressQ9QZD4.
BgeeQ9QZD4.
GenevestigatorQ9QZD4.

Family and domain databases

Gene3D3.40.50.10130. 1 hit.
InterProIPR020819. DNA_repair_nuc_XPF/helicase.
IPR006166. ERCC4_domain.
IPR006167. Rad1.
IPR011335. Restrct_endonuc-II-like.
IPR010994. RuvA_2-like.
[Graphical view]
PfamPF02732. ERCC4. 1 hit.
[Graphical view]
SMARTSM00891. ERCC4. 1 hit.
[Graphical view]
SUPFAMSSF47781. SSF47781. 1 hit.
SSF52980. SSF52980. 1 hit.
TIGRFAMsTIGR00596. rad1. 1 hit.
ProtoNetSearch...

Other

NextBio307508.
PROQ9QZD4.
SOURCESearch...

Entry information

Entry nameXPF_MOUSE
AccessionPrimary (citable) accession number: Q9QZD4
Secondary accession number(s): O54810, Q8R0I3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: May 5, 2009
Last modified: April 16, 2014
This is version 102 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot