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P50525 (APN1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 107. 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-(apurinic or apyrimidinic site) lyase 1

EC=4.2.99.18
Alternative name(s):
Apurinic-apyrimidinic endonuclease 1
Short name=AP endonuclease 1
Gene names
Name:apn1
ORF Names:SPCC622.17
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length342 AA.
Sequence statusComplete.
Protein existenceUncertain

General annotation (Comments)

Function

DNA repair enzyme that cleaves apurinic/apyrimidinic (AP) sites and removes 3'-blocking groups present at single strand breaks of damaged DNA. Provides back-up AP endonuclease (APE) activity to apn2 together with uve1. Ref.1 Ref.5

Catalytic activity

The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate. HAMAP-Rule MF_00152

Cofactor

Binds 3 zinc ions By similarity. HAMAP-Rule MF_00152

Subcellular location

Nucleus By similarity HAMAP-Rule MF_00152.

Sequence similarities

Belongs to the AP endonuclease 2 family.

Caution

Could be the product of a pseudogene. This is a truncated version of AP endonuclease 1. In strain 972 and its derivative FY527, this gene has a stop codon in position 5, which disrupts the gene coding for this protein. Ref.5 shows that the truncated protein is not functional. A full sequence for apn1 can be found in strains SPK19802 (S.pombe var. kambucha), NCYC 132, NCYC 683, NCYC 936 and NCYC 2722 (Ref.5).

Sequence caution

The sequence AAC28163.1 differs from that shown. Reason: Frameshift at position 298.

The sequence AAC28163.1 differs from that shown. Reason: Intron retention.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
   Cellular componentNucleus
   LigandMetal-binding
Zinc
   Molecular functionLyase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA repair

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: InterPro

DNA-(apurinic or apyrimidinic site) lyase activity

Inferred from electronic annotation. Source: UniProtKB-EC

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 342342DNA-(apurinic or apyrimidinic site) lyase 1 HAMAP-Rule MF_00152
PRO_0000190897

Sites

Metal binding611Zinc 1 By similarity
Metal binding1361Zinc 1 By similarity
Metal binding1361Zinc 2 By similarity
Metal binding1701Zinc 2 By similarity
Metal binding1731Zinc 3 By similarity
Metal binding2071Zinc 2 By similarity
Metal binding2201Zinc 3 By similarity
Metal binding2221Zinc 3 By similarity
Metal binding2521Zinc 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
P50525 [UniParc].

Last modified June 7, 2004. Version 3.
Checksum: C6711EC23691C51D

FASTA34238,657
        10         20         30         40         50         60 
MCAINKAYLL TKFYISANSC AFFVKSQRKW TSPDLSEDVA QKFLETASEM KFDASKQVLV 

        70         80         90        100        110        120 
HGSYLINMAN ADEQKREQAF NCFVDDLKRC ERLGVGLYNF HPGSTASCTK EEGINNLAEC 

       130        140        150        160        170        180 
INRAHEETKS VIIVTENMAG QGNCLGGTFD DFAALKSKIK NLDRWRVCLD TCHTFAAGYD 

       190        200        210        220        230        240 
IRTEESYKKV IDEFDEKVGA KYVSGWHLND SKAPLGSNRD LHENIGLGFL GLEPFRLIMN 

       250        260        270        280        290        300 
DSRWDGIPLV LETPAKSPEQ WKKEVELLRF MVGKSSDDVE LMKESARLSN LGAASRKEHL 

       310        320        330        340 
NKFEKKEAKK DRKKKSKDGD QTTLLLRKKQ KLGNAEVKSL DE 

« Hide

References

« Hide 'large scale' references
[1]"The major role of human AP-endonuclease homolog Apn2 in repair of abasic sites in Schizosaccharomyces pombe."
Ribar B., Izumi T., Mitra S.
Nucleic Acids Res. 32:115-126(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
[2]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[3]Seeger K., Harris D., Lyne M., Rajandream M.A., Barrell B.G.
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[4]"Schizosaccharomyces pombe apn1 encodes a homologue of the Escherichia coli endonuclease IV family of DNA repair proteins."
Ramotar D., Vadnais J., Masson J.Y., Tremblay S.
Biochim. Biophys. Acta 1396:15-20(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-319.
[5]"Schizosaccharomyces pombe encodes a mutated AP endonuclease 1."
Laerdahl J.K., Korvald H., Nilsen L., Dahl-Michelsen K., Rognes T., Bjoras M., Alseth I.
DNA Repair 10:296-305(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: LACK OF FUNCTION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY483157 mRNA. Translation: AAR83751.1.
CU329672 Genomic DNA. No translation available.
U33625 mRNA. Translation: AAC28163.1. Sequence problems.
PIRT52563.

3D structure databases

ProteinModelPortalP50525.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid275375. 9 interactions.
MINTMINT-4690690.
STRING4896.SPCC622.17-1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG0648.
HOGENOMHOG000224893.
OMADEINWIN.
OrthoDBEOG71VT48.
PhylomeDBP50525.

Family and domain databases

Gene3D3.20.20.150. 1 hit.
HAMAPMF_00152. Nfo.
InterProIPR001719. AP_endonuc_2.
IPR018246. AP_endonuc_F2_Zn_BS.
IPR013022. Xyl_isomerase-like_TIM-brl.
[Graphical view]
PANTHERPTHR21445. PTHR21445. 1 hit.
PfamPF01261. AP_endonuc_2. 1 hit.
[Graphical view]
SMARTSM00518. AP2Ec. 1 hit.
[Graphical view]
SUPFAMSSF51658. SSF51658. 1 hit.
TIGRFAMsTIGR00587. nfo. 1 hit.
PROSITEPS00729. AP_NUCLEASE_F2_1. 1 hit.
PS00730. AP_NUCLEASE_F2_2. 1 hit.
PS00731. AP_NUCLEASE_F2_3. 1 hit.
PS51432. AP_NUCLEASE_F2_4. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20799976.
PROP50525.

Entry information

Entry nameAPN1_SCHPO
AccessionPrimary (citable) accession number: P50525
Secondary accession number(s): Q9USI8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: June 7, 2004
Last modified: May 14, 2014
This is version 107 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names