Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Flap endonuclease 1

Gene

Fen1

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. It enters the flap from the 5'-end and then tracks to cleave the flap base, leaving a nick for ligation. Also involved in the long patch base excision repair (LP-BER) pathway, by cleaving within the apurinic/apyrimidinic (AP) site-terminated flap. Acts as a genome stabilization factor that prevents flaps from equilibrating into structurs that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA, and exhibits RNase H activity. Also involved in replication and repair of rDNA and in repairing mitochondrial DNA.UniRule annotation

Cofactori

Mg2+UniRule annotationNote: Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding.UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi34Magnesium 1UniRule annotation1
Binding sitei47DNA substrateUniRule annotation1
Binding sitei70DNA substrateUniRule annotation1
Metal bindingi86Magnesium 1UniRule annotation1
Metal bindingi158Magnesium 1UniRule annotation1
Binding sitei158DNA substrateUniRule annotation1
Metal bindingi160Magnesium 1UniRule annotation1
Metal bindingi179Magnesium 2UniRule annotation1
Metal bindingi181Magnesium 2UniRule annotation1
Binding sitei231DNA substrateUniRule annotation1
Metal bindingi233Magnesium 2UniRule annotation1
Binding sitei233DNA substrateUniRule annotation1

GO - Molecular functioni

  • DNA binding Source: InterPro
  • endonuclease activity Source: FlyBase
  • exonuclease activity Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

Keywordsi

Molecular functionEndonuclease, Exonuclease, Hydrolase, Nuclease
Biological processDNA damage, DNA repair, DNA replication
LigandMagnesium, Metal-binding

Enzyme and pathway databases

ReactomeiR-DME-5651801. PCNA-Dependent Long Patch Base Excision Repair.
R-DME-5685939. HDR through MMEJ (alt-NHEJ).
R-DME-69166. Removal of the Flap Intermediate.

Names & Taxonomyi

Protein namesi
Recommended name:
Flap endonuclease 1UniRule annotation (EC:3.1.-.-UniRule annotation)
Short name:
FEN-1UniRule annotation
Alternative name(s):
Flap structure-specific endonuclease 1UniRule annotation
Gene namesi
Name:Fen1UniRule annotation
ORF Names:CG8648
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraHolometabolaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0025832. Fen1.

Subcellular locationi

  • Nucleusnucleolus UniRule annotation
  • Nucleusnucleoplasm UniRule annotation
  • Mitochondrion UniRule annotation

  • Note: Resides mostly in the nucleoli and relocalizes to the nucleoplasm upon DNA damage.UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Mitochondrion, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004035001 – 385Flap endonuclease 1Add BLAST385

Post-translational modificationi

Phosphorylated. Phosphorylation upon DNA damage induces relocalization to the nuclear plasma.UniRule annotation

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ7K7A9.
PRIDEiQ7K7A9.

Expressioni

Gene expression databases

BgeeiFBgn0025832.
GenevisibleiQ7K7A9. DM.

Interactioni

Subunit structurei

Interacts with PCNA. Three molecules of FEN1 bind to one PCNA trimer with each molecule binding to one PCNA monomer. PCNA stimulates the nuclease activity without altering cleavage specificity.UniRule annotation

Protein-protein interaction databases

BioGridi62595. 1 interactor.
IntActiQ7K7A9. 2 interactors.
STRINGi7227.FBpp0086223.

Structurei

3D structure databases

ProteinModelPortaliQ7K7A9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 104N-domainAdd BLAST104
Regioni122 – 253I-domainAdd BLAST132
Regioni336 – 344Interaction with PCNAUniRule annotation9

Sequence similaritiesi

Belongs to the XPG/RAD2 endonuclease family. FEN1 subfamily.UniRule annotation

Phylogenomic databases

eggNOGiKOG2519. Eukaryota.
COG0258. LUCA.
InParanoidiQ7K7A9.
KOiK04799.
OMAiGSQDYDS.
OrthoDBiEOG091G0C0E.
PhylomeDBiQ7K7A9.

Family and domain databases

CDDicd09867. PIN_FEN1. 1 hit.
Gene3Di3.40.50.1010. 1 hit.
HAMAPiMF_00614. Fen. 1 hit.
InterProiView protein in InterPro
IPR020045. 5-3_exonuclease_C.
IPR023426. Flap_endonuc.
IPR008918. HhH2.
IPR029060. PIN_domain-like.
IPR006086. XPG-I_dom.
IPR006084. XPG/Rad2.
IPR019974. XPG_CS.
IPR006085. XPG_DNA_repair_N.
PANTHERiPTHR11081. PTHR11081. 1 hit.
PfamiView protein in Pfam
PF00867. XPG_I. 1 hit.
PF00752. XPG_N. 1 hit.
PRINTSiPR00853. XPGRADSUPER.
SMARTiView protein in SMART
SM00279. HhH2. 1 hit.
SM00484. XPGI. 1 hit.
SM00485. XPGN. 1 hit.
SUPFAMiSSF47807. SSF47807. 1 hit.
SSF88723. SSF88723. 1 hit.
PROSITEiView protein in PROSITE
PS00841. XPG_1. 1 hit.
PS00842. XPG_2. 1 hit.

Sequencei

Sequence statusi: Complete.

Q7K7A9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGILGLSKLI ADLAPQAIRE SEMKHFFGRK VAIDASMCLY QFLIAVRSEG
60 70 80 90 100
AQLATVNGDP TSHLMGMFYR TIRLLDNGIK PVYVFDGKPP DLKSGELAKR
110 120 130 140 150
AERREEAEKA LKAATDAGDD AGIEKFNRRL VRVTKEHAKE AKELLTLMGV
160 170 180 190 200
PYVDAPCEAE AQCAALVKAG KVYATATEDM DALTFGSTKL LRYLTYSEAR
210 220 230 240 250
KMPVKEFSYD KLLEGLAINN REFIDLCILL GCDYCESIKG IGPKRAIELI
260 270 280 290 300
NTYRDIETIL DNLDSSKYTV PENWNYKVAR ELFIEPEVAD ADSIDLKWVE
310 320 330 340 350
PDEEGLVKFL CGDRQFNEER VRNGAKKLMK SKQAQTQVRL DSFFKTLPST
360 370 380
PNATNAAKRK AEEAKKSANN KKAKTSGGGR GRRPK
Length:385
Mass (Da):42,948
Last modified:October 3, 2006 - v1
Checksum:iD0A0831C2BDA9240
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE013599 Genomic DNA. Translation: AAF57944.1.
AL031863 Genomic DNA. Translation: CAA21320.1.
BT100031 mRNA. Translation: ACX54939.1.
PIRiT13692.
RefSeqiNP_523765.1. NM_079041.2.
UniGeneiDm.23253.

Genome annotation databases

EnsemblMetazoaiFBtr0087075; FBpp0086223; FBgn0025832.
GeneIDi36887.
KEGGidme:Dmel_CG8648.
UCSCiCG8648-RA. d. melanogaster.

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Entry informationi

Entry nameiFEN1_DROME
AccessioniPrimary (citable) accession number: Q7K7A9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 11, 2011
Last sequence update: October 3, 2006
Last modified: July 5, 2017
This is version 98 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families