Reviewed, UniProtKB/Swiss-Prot P87175 (APN2_SCHPO)

Names and origin

Protein names

Recommended name:
    DNA-(apurinic or apyrimidinic site) lyase 2
    EC=4.2.99.18
Alternative name(s):
    AP endonuclease 2
    Apurinic-apyrimidinic endonuclease 2

Gene names

Name:	apn2
ORF Names:	SPBC3D6.10

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	523 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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 the majority of the AP-endonuclease (APE) activity. Repairs phleomycin D1-induced DNA damage. Plays a role in oxidative damage repair. Ref.1 Ref.3
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. Ref.1
Subcellular location	Nucleus By similarity. UniProtKB P38207
Sequence similarities	Belongs to the DNA repair enzymes AP/exoA family.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Cellular component	Nucleus
Molecular function	Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	base-excision repair Inferred by curator. Source: GeneDB_SPombe cellular response to reactive oxygen species Ref.3 Inferred from mutant phenotype. Source: GeneDB_SPombe
Cellular component	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 double-stranded DNA specific 3'-5' exodeoxyribonuclease activity Inferred from mutant phenotype. Source: GeneDB_SPombe endonuclease activity 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 – 523	523	DNA-(apurinic or apyrimidinic site) lyase 2		PRO_0000200019
Experimental info
	Mutagenesis	402	1	F → A: No change in activity; when associated with A-403. Ref.1
	Mutagenesis	403	1	F → A: No change in activity; when associated with A-402. Ref.1
	Mutagenesis	456	1	P → A: No change in activity; when associated with A-457 and A-458. Ref.1
	Mutagenesis	457	1	L → A: No change in activity; when associated with A-456 and A-458. Ref.1
	Mutagenesis	458	1	C → A: No change in activity; when associated with A-456 and A-457. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P87175-1 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: B2A79AE61579FA1C	FASTA	523	60,313
	10 20 30 40 50 60 MRILSWNVNG IQNPFNYFPW NKKNSYKEIF QELQADVICV QELKMQKDSF PQQYAVVEGF 70 80 90 100 110 120 DSYFTFPKIR KGYSGVGFYV KKDVAIPVKA EEGITGILPV RGQKYSYSEA PEHEKIGFFP 130 140 150 160 170 180 KDIDRKTANW IDSEGRCILL DFQMFILIGV YCPVNSGENR LEYRRAFYKA LRERIERLIK 190 200 210 220 230 240 EGNRKIILVG DVNILCNPID TADQKDIIRE SLIPSIMESR QWIRDLLLPS RLGLLLDIGR 250 260 270 280 290 300 IQHPTRKGMF TCWNTRLNTR PTNYGTRIDY TLATPDLLPW VQDADIMAEV MGSDHCPVYL 310 320 330 340 350 360 DLKEEYEGKK LSNFLSHSKE PPLLSTAHHS AYRPSKNIHS MFQHFNSMKK NKNNSPTQSE 370 380 390 400 410 420 NVSASASSGS SPTVSRANSV IDVDAYPPEK RRRKEQSKLL SFFAKQKEEK EETNKTEDVS 430 440 450 460 470 480 IEVLDNNNES DIGLTVKKKV ENGNAWKQIF SERAPPLCEG HKEPCKYLTV RKPGINYGRK 490 500 510 520 FWICARPVGE LIKNSNAVSE EDTQPFQCRF FIWDSDWRAN SKD

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, CATALYTIC ACTIVITY, MUTAGENESIS OF PHE-402; PHE-403; PRO-456; LEU-457 AND CYS-458.
[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: ATCC 38366 / 972.
[3]	"Fission yeast Uve1 and Apn2 function in distinct oxidative damage repair pathways in vivo." Fraser J.L.A., Neill E., Davey S. DNA Repair 2:1253-1267(2003) [PubMed: 14599746] [Abstract] Cited for: FUNCTION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AY483158 mRNA. Translation: AAR83752.1. CU329671 Genomic DNA. Translation: CAB09119.1.
PIR	T40370.
RefSeq	NP_595522.1.
3D structure databases
HSSP	HSSP built from PDB template 1E9N based on UniProtKB P27695.
ModBase	Search...
Protein-protein interaction databases
STRING	P87175.
Genome annotation databases
GeneID	2540679.
GenomeReviews	Gene locus apn2 in contig CU329671_GR.
KEGG	spo:SPBC3D6.10.
NMPDR	fig|4896.1.peg.1388.
Organism-specific databases
GeneDB_Spombe	SPBC3D6.10.
Phylogenomic databases
OMA	RLDYVLG.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-003581-MON.
BRENDA	4.2.99.18. 653.
Gene expression databases
ArrayExpress	P87175.
Family and domain databases
InterPro	IPR000097. AP_endonuclease_F1. IPR005135. Endo/exonuclease/phosphatase. IPR004808. exoDNase_III. [Graphical view]
PANTHER	PTHR22748. ExoIII_xth. 1 hit.
Pfam	PF03372. Exo_endo_phos. 1 hit. [Graphical view]
TIGRFAMs	TIGR00633. xth. 1 hit.
PROSITE	PS00726. AP_NUCLEASE_F1_1. 1 hit. PS00727. AP_NUCLEASE_F1_2. 1 hit. PS00728. AP_NUCLEASE_F1_3. False negative. PS51435. AP_NUCLEASE_F1_4. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

APN2_SCHPO

Accession

Primary (citable) accession number: P87175

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2004
Last sequence update:	July 1, 1997
Last modified:	November 3, 2009
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)