P50525 (APN1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	342 AA.
Sequence status	Complete.
Protein existence	Uncertain

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.
Cofactor	Binds 3 zinc ions By similarity.
Subcellular location	Nucleus By similarity.
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 process	DNA damage DNA repair
Cellular component	Nucleus
Ligand	Metal-binding Zinc
Molecular function	Lyase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	DNA repair Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Inferred from direct assay. Source: GeneDB_Spombe mitochondrion Inferred from sequence or structural similarity. Source: GeneDB_Spombe nucleus Inferred from direct assay. Source: GeneDB_Spombe
Molecular function	DNA binding Inferred from electronic annotation. Source: InterPro DNA-(apurinic or apyrimidinic site) lyase activity Inferred from electronic annotation. Source: EC deoxyribonuclease IV (phage-T4-induced) activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 342	342	DNA-(apurinic or apyrimidinic site) lyase 1		PRO_0000190897
Sites
	Metal binding	61	1	Zinc 1 By similarity
	Metal binding	136	1	Zinc 1 By similarity
	Metal binding	136	1	Zinc 2 By similarity
	Metal binding	170	1	Zinc 2 By similarity
	Metal binding	173	1	Zinc 3 By similarity
	Metal binding	207	1	Zinc 2 By similarity
	Metal binding	220	1	Zinc 3 By similarity
	Metal binding	222	1	Zinc 3 By similarity
	Metal binding	252	1	Zinc 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	P50525 [UniParc]. Last modified June 7, 2004. Version 3. Checksum: C6711EC23691C51D	FASTA	342	38,657
	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

References

	« Hide 'large scale' referencesShow '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: 14704348] [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. , 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: 11859360] [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: 9524207] [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: 21193357] [Abstract] Cited for: LACK OF FUNCTION.
+	Additional computationally mapped references.

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.
PIR	T52563.
RefSeq	NP_588189.2. NM_001023179.1.
3D structure databases
ProteinModelPortal	P50525.
ModBase	Search...
Protein-protein interaction databases
STRING	P50525.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2538794.
GenomeReviews	Gene locus apn1 in contig CU329672_GR.
KEGG	spo:SPCC622.17.
Organism-specific databases
GeneDB_Spombe	SPCC622.17.
Phylogenomic databases
eggNOG	fuNOG05174.
GeneTree	EFGT00050000006647.
HOGENOM	HBG565018.
OMA	GLYNFHP.
OrthoDB	EOG4KSSTN.
Gene expression databases
ArrayExpress	P50525.
Family and domain databases
InterPro	IPR018246. AP_endonuc_F2_Zn_BS. IPR001719. Endodeoxyribonuclease_IV. IPR013022. Xyl_isomerase-like_TIM-brl. IPR012307. Xyl_isomerase_TIM-brl. [Graphical view]
Gene3D	G3DSA:3.20.20.150. Xyl_isomerase-like_TIM-brl. 1 hit.
KO	K10771.
PANTHER	PTHR21445. AP_endnuclease2. 1 hit.
Pfam	PF01261. AP_endonuc_2. 1 hit. [Graphical view]
SMART	SM00518. AP2Ec. 1 hit. [Graphical view]
SUPFAM	SSF51658. Xyl_isomerase-like_TIM-brl. 1 hit.
TIGRFAMs	TIGR00587. Nfo. 1 hit.
PROSITE	PS00729. 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]
ProtoNet	Search...

Entry information

Entry name

APN1_SCHPO

Accession

Primary (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:	December 14, 2011
This is version 91 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program