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Protein

Flap endonuclease 1-A

Gene

fen1-a

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score: -Experimental evidence at protein 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 annotation2 Publications

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 annotationBy similarity1
Binding sitei70DNA substrateUniRule annotationBy similarity1
Metal bindingi86Magnesium 1UniRule annotation1
Metal bindingi158Magnesium 1UniRule annotation1
Binding sitei158DNA substrateUniRule annotationBy similarity1
Metal bindingi160Magnesium 1UniRule annotation1
Metal bindingi179Magnesium 2UniRule annotation1
Metal bindingi181Magnesium 2UniRule annotation1
Binding sitei231DNA substrateUniRule annotationBy similarity1
Metal bindingi233Magnesium 2UniRule annotation1
Binding sitei233DNA substrateUniRule annotationBy similarity1

GO - Molecular functioni

  • 5'-flap endonuclease activity Source: UniProtKB
  • DNA binding Source: InterPro
  • exonuclease activity Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • base-excision repair Source: UniProtKB
  • DNA replication Source: UniProtKB

Keywordsi

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

Names & Taxonomyi

Protein namesi
Recommended name:
Flap endonuclease 1-AUniRule annotation (EC:3.1.-.-UniRule annotation)
Short name:
FEN-1-AUniRule annotation
Alternative name(s):
Flap structure-specific endonuclease 1-AUniRule annotation
Short name:
xFEN-1a
Gene namesi
Name:fen1-a
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-955523 fen1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Mitochondrion, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002444911 – 382Flap endonuclease 1-AAdd BLAST382

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP70040

Expressioni

Developmental stagei

First expressed at a low level in stage II oocytes. Expression increases dramatically from oocyte stages III to V (at protein level). Also expressed in embryos.1 Publication

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

BioGridi98905, 1 interactor
IntActiP70040, 2 interactors

Structurei

3D structure databases

ProteinModelPortaliP70040
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

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

Sequence similaritiesi

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

Phylogenomic databases

HOVERGENiHBG000844
KOiK04799

Family and domain databases

CDDicd09867 PIN_FEN1, 1 hit
HAMAPiMF_00614 Fen, 1 hit
InterProiView protein in InterPro
IPR036279 5-3_exonuclease_C_sf
IPR023426 Flap_endonuc
IPR008918 HhH2
IPR029060 PIN-like_dom_sf
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

Sequencei

Sequence statusi: Complete.

P70040-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGIHGLAKLI ADVAPAAIKE HDIKSYFGRK VAVDASMCIY QFLIAVRQDG
60 70 80 90 100
NTLQNEEGET TSHLMGMFYR TIRMVEHGIK PVYVFDGKPP QMKSGELAKR
110 120 130 140 150
SERRAEAEKL LEAAEEAGEV ENIEKFTKRL VKVTKQHNEE CKKLLTLMGI
160 170 180 190 200
PYVDAPCEAE ATCAALVKAG KVYAAATEDM DALTFGTPVL LRHLTASEAK
210 220 230 240 250
KLPIQEFHLN RVIQDIGITH EQFVDLCILL GSDYCETIRG IGPKRAIDLI
260 270 280 290 300
RQHKTIDEII DNIDLKKYPV PENWLHKEAK HLFLEPEVVD TDITELKWIE
310 320 330 340 350
PDEEGLVAFM CGEKQFSEDR IRNGAKKLAK NRQGSTQGRL DDFFKVTGSV
360 370 380
SSTKRKEAES KGSAKKKAKT GGTPAGKFKR GK
Length:382
Mass (Da):42,668
Last modified:February 1, 1997 - v1
Checksum:i9B1DB0EDAD158D57
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti33V → I in allele fen-1a'. 3 Publications1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF036327 mRNA Translation: AAB88707.1
U64563 mRNA Translation: AAB06176.1
AF065397 mRNA Translation: AAD02814.1
BC169761 mRNA Translation: AAI69761.1
BC169765 mRNA Translation: AAI69765.1
BC124977 mRNA Translation: AAI24978.1
RefSeqiNP_001080960.1, NM_001087491.1
UniGeneiXl.440

Genome annotation databases

GeneIDi394303
KEGGixla:394303

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiFEN1A_XENLA
AccessioniPrimary (citable) accession number: P70040
Secondary accession number(s): B7ZQC8, O57351, Q08AW7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: February 1, 1997
Last modified: March 28, 2018
This is version 89 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health