P87175 (APN2_SCHPO) Reviewed, UniProtKB/Swiss-Prot

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 (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces › Schizosaccharomyces pombe

Protein attributes

Sequence length	523 AA.
Sequence status	Complete.
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
Cofactor	Magnesium. Can also utilize manganese. Probably binds two magnesium or manganese ions per subunit By similarity.
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
Ligand	Magnesium Metal-binding
Molecular function	Lyase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	base-excision repair Inferred by curator. Source: PomBase cellular response to reactive oxygen species Inferred from mutant phenotype Ref.3. Source: PomBase
Cellular_component	nucleus Inferred from direct assay PubMed 16857169. Source: PomBase
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 PubMed 16857169. Source: PomBase endonuclease activity Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphodiesterase I activity Inferred from sequence orthology. Source: PomBase
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
Sites
	Active site	151	1	By similarity
	Active site	191	1	Proton donor/acceptor By similarity
	Metal binding	42	1	Magnesium 1 By similarity
	Metal binding	191	1	Magnesium 2 By similarity
	Metal binding	193	1	Magnesium 2 By similarity
	Metal binding	294	1	Magnesium 1 By similarity
	Site	193	1	Transition state stabilizer By similarity
	Site	269	1	Important for catalytic activity By similarity
	Site	295	1	Interaction with DNA substrate By similarity
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 [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 972 / ATCC 24843.
[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] [Europe PMC] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY483158 mRNA. Translation: AAR83752.1. CU329671 Genomic DNA. Translation: CAB09119.1.
PIR	T40370.
RefSeq	NP_595522.1. NM_001021431.2.
3D structure databases
ProteinModelPortal	P87175.
ModBase	Search...
Protein-protein interaction databases
STRING	4896.SPBC3D6.10-1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPBC3D6.10.1; SPBC3D6.10.1:pep; SPBC3D6.10.
GeneID	2540679.
KEGG	spo:SPBC3D6.10.
Organism-specific databases
PomBase	SPBC3D6.10.
Phylogenomic databases
eggNOG	COG0708.
KO	K10772.
OMA	FIDSYRC.
OrthoDB	EOG4GQTDH.
Family and domain databases
InterPro	IPR020847. AP_endonuclease_F1_BS. IPR020848. AP_endonuclease_F1_CS. IPR005135. Endo/exonuclease/phosphatase. IPR004808. ExoDNase_III. [Graphical view]
PANTHER	PTHR22748. PTHR22748. 1 hit.
Pfam	PF03372. Exo_endo_phos. 1 hit. [Graphical view]
SUPFAM	SSF56219. Exo_endo_phos. 1 hit.
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...
Other
NextBio	20801803.

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:	May 1, 2013
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program