A4VDN2 · FEN1_TETTS

Function

function

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 structures 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.

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: 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.

Features

Showing features for binding site.

138450100150200250300350
TypeIDPosition(s)Description
Binding site34Mg2+ 1 (UniProtKB | ChEBI)
Binding site74DNA (UniProtKB | ChEBI)
Binding site90Mg2+ 1 (UniProtKB | ChEBI)
Binding site162DNA (UniProtKB | ChEBI)
Binding site162Mg2+ 1 (UniProtKB | ChEBI)
Binding site164Mg2+ 1 (UniProtKB | ChEBI)
Binding site183Mg2+ 2 (UniProtKB | ChEBI)
Binding site185Mg2+ 2 (UniProtKB | ChEBI)
Binding site232DNA (UniProtKB | ChEBI)
Binding site234DNA (UniProtKB | ChEBI)
Binding site234Mg2+ 2 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentmitochondrion
Cellular Componentnucleolus
Cellular Componentnucleoplasm
Molecular Function5'-3' exonuclease activity
Molecular Function5'-flap endonuclease activity
Molecular FunctionDNA binding
Molecular Functionmagnesium ion binding
Biological Processbase-excision repair
Biological ProcessDNA replication, removal of RNA primer

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Flap endonuclease 1
  • EC number
  • Short names
    FEN-1
  • Alternative names
    • Flap structure-specific endonuclease 1

Gene names

    • Name
      FEN1
    • ORF names
      TTHERM_00437617

Organism names

  • Taxonomic identifier
  • Strain
    • SB210
  • Taxonomic lineage
    Eukaryota > Sar > Alveolata > Ciliophora > Intramacronucleata > Oligohymenophorea > Hymenostomatida > Tetrahymenina > Tetrahymenidae > Tetrahymena

Accessions

  • Primary accession
    A4VDN2

Proteomes

Subcellular Location

Nucleus, nucleolus
Nucleus, nucleoplasm
Mitochondrion
Note: Resides mostly in the nucleoli and relocalizes to the nucleoplasm upon DNA damage.

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004035431-384Flap endonuclease 1

Post-translational modification

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

Keywords

Interaction

Subunit

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.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, compositional bias.

Type
IDPosition(s)Description
Region1-108N-domain
Region126-254I-domain
Region340-384Disordered
Region346-354Interaction with PCNA
Compositional bias350-375Polar residues

Sequence similarities

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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    384
  • Mass (Da)
    43,111
  • Last updated
    2007-05-29 v1
  • Checksum
    33E81B5CB5835B79
MGIHKLMDLLKEKAPGCIKTSDLKFYAGRMIACDASMAMYQFLATTSSASDFQIQNLTDKDGNKTGHLVGLLNRTVMLIENGLKPVWVFDGKPPQFKSGELARRQKAKDEAAEKQKTAIETGDMQEALKQEQRNLHITKEMKADAIKLLQLVGVPVILAPCEAEAQCAALAKAKKVFATVTEDMDALTFATPFLLRNLNSKKEPITEINYEKMLQELKLSHNEFVDLCILCGCDYLGRIEGVGPVNAFKLITEHKSLEKVLEHMEEVNKQSTKKQKYTVPSSYDYVSARDLFINPEVTDPETIQLEWKKPDVEELKKFLVEEKGFSEQRVTSQMEKVLNAKEHKGSQTRLNDFFKVQPKDTSSTSKASKKPTNTKSANKKGGKK

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias350-375Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
GG662663
EMBL· GenBank· DDBJ
EDK31639.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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