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Protein

Flap endonuclease 1

Gene

crn-1

Organism
Caenorhabditis elegans
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 (By similarity). Can associate and cooperate with cps-6 to promote stepwise DNA fragmentation, utilizing the endonuclease activity of cps-6 and both of its own 5'-3' exonuclease activity and gap-dependent endonuclease activity. May play a critical role in switching the state of cells from DNA replication/repair to DNA degradation during apoptosis.UniRule annotation1 Publication

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
  • exonuclease activity Source: UniProtKB-KW
  • flap endonuclease activity Source: WormBase
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • apoptotic DNA fragmentation Source: WormBase
  • DNA repair Source: WormBase
  • DNA replication Source: WormBase

Keywordsi

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

Enzyme and pathway databases

ReactomeiR-CEL-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):
Cell death-related nuclease 1
Flap structure-specific endonuclease 1UniRule annotation
Gene namesi
Name:crn-1UniRule annotation
ORF Names:Y47G6A.8
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome I

Organism-specific databases

WormBaseiY47G6A.8 ; CE22109 ; WBGene00000794 ; crn-1

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_00004035131 – 382Flap endonuclease 1Add BLAST382

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9N3T2
PaxDbiQ9N3T2
PeptideAtlasiQ9N3T2
PRIDEiQ9N3T2

Expressioni

Gene expression databases

BgeeiWBGene00000794

Interactioni

Subunit structurei

Interacts with PCNA. Three molecules of crn-1 bind to one PCNA trimer with each molecule binding to one PCNA monomer. PCNA stimulates the nuclease activity without altering cleavage specificity (By similarity). Interacts with cps-6.UniRule annotation1 Publication

Protein-protein interaction databases

BioGridi37393, 3 interactors
DIPiDIP-26974N
IntActiQ9N3T2, 2 interactors
MINTiQ9N3T2
STRINGi6239.Y47G6A.8

Structurei

3D structure databases

ProteinModelPortaliQ9N3T2
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
GeneTreeiENSGT00640000091478
HOGENOMiHOG000193853
InParanoidiQ9N3T2
KOiK04799
OMAiGSQDYDS
OrthoDBiEOG091G0C0E
PhylomeDBiQ9N3T2

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
PS00842 XPG_2, 1 hit

Sequencei

Sequence statusi: Complete.

Q9N3T2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGIKGLSQVI ADNAPSAIKV NEMKAFFGRT VAIDASMCLY QFLIAVRQDG
60 70 80 90 100
SQLQSEDGET TSHLMGMLNR TVRMFENGVK PVYVFDGKPP DMKGGELEKR
110 120 130 140 150
SERRAEAEKA LTEAKEKGDV KEAEKFERRL VKVTKQQNDE AKRLLGLMGI
160 170 180 190 200
PVVEAPCEAE AQCAHLVKAG KVFGTVTEDM DALTFGSTVL LRHFLAPVAK
210 220 230 240 250
KIPIKEFNLS LALEEMKLSV EEFIDLCILL GCDYCGTIRG VGPKKAVELI
260 270 280 290 300
RQHKNIETIL ENIDQNKYPP PEDWPYKRAR ELFLNPEVTK PEEVELTWKE
310 320 330 340 350
ADVEGVIQFL CGEKNFNEER IRNALAKLKT SRKSGTQGRI DSFFGNSTKV
360 370 380
TCVTAATKRK AEEAEKAKKG AKKGGPPKKR AK
Length:382
Mass (Da):42,549
Last modified:October 1, 2000 - v1
Checksum:iFDFE0BA0707321EB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY303575 mRNA Translation: AAP57297.1
FO081580 Genomic DNA Translation: CCD72553.1
RefSeqiNP_491168.1, NM_058767.6
UniGeneiCel.6649

Genome annotation databases

EnsemblMetazoaiY47G6A.8.1; Y47G6A.8.1; WBGene00000794
Y47G6A.8.2; Y47G6A.8.2; WBGene00000794
GeneIDi171917
KEGGicel:CELE_Y47G6A.8
UCSCiY47G6A.8 c. elegans

Similar proteinsi

Entry informationi

Entry nameiFEN1_CAEEL
AccessioniPrimary (citable) accession number: Q9N3T2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 11, 2011
Last sequence update: October 1, 2000
Last modified: May 23, 2018
This is version 125 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

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