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Description:
DNA-(apurinic or apyrimidinic site) lyase 2 (EC 4.2.99.18) (APendonuclease 2) (Apurinic-apyrimidinic endonuclease 2).
Molecular weight: 60313
View which proteins in this organism that is involved with DNA Repair;
classified after biological processes (using data from the GOA project):
DNA repair( GO:0006281 )
Important dates:
07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
01-JUL-1997, sequence version 1.
07-FEB-2006, entry version 32.
Phylogenetic order:
Eukaryota Fungi Ascomycota Schizosaccharomycetes Schizosaccharomycetales Schizosaccharomycetaceae Schizosaccharomyces.
To calculate the pI (Isoelectric point - the pH where a protein has a neutral charge),
go to this page and enter the protein ID (e.g 3MG_ECOLI): http://us.expasy.org/tools/pi_tool.html
Links to references in other databases for protein APN2_SCHPO:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | AY483158 | AAR83752.1 | - |
| EMBL | Z95620 | CAB09119.1 | - |
| PIR | T40370 | T40370. | |
| HSSP | P27695 | 1E9N | |
| GeneDB_Spombe | SPBC3D6.10 | -.1 | |
| BioCyc | SPOM-XXX-01:SPOM-XXX-01-003581-MONOMER | -.1 | |
| GO | GO:0000302 | P:response to reactive oxygen species | IMP. |
| InterPro | IPR000097 | APendonclse1. | |
| InterPro | IPR005135 | Exo_endo_phos. | |
| InterPro | IPR004808 | ExoIII_xth. | |
| Pfam | PF03372 | Exo_endo_phos | 1. |
| TIGRFAMs | TIGR00633 | xth | 1. |
| PROSITE | PS00726 | AP_NUCLEASE_F1_1 | 1. |
| PROSITE | PS00727 | AP_NUCLEASE_F1_2 | 1. |
| PROSITE | PS00728 | AP_NUCLEASE_F1_3 | FALSE_NEG. |
Keywords:
Complete proteome; DNA damage; DNA repair; Lyase; Nuclear protein.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF
RP PHE-402; PHE-403; PRO-456; LEU-457 AND CYS-458.
RX PubMed=14704348; DOI=10.1093/nar/gkh151;
RA Ribar B., Izumi T., Mitra S.;
RT "The major role of human AP-endonuclease homolog Apn2 in repair of
RT abasic sites in Schizosaccharomyces pombe.";
RL Nucleic Acids Res. 32:115-126(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972;
RX MEDLINE=21848401; PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M.,
RA Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP FUNCTION.
RX PubMed=14599746; DOI=10.1016/j.dnarep.2003.08.005;
RA Fraser J.L.A., Neill E., Davey S.;
RT "Fission yeast Uve1 and Apn2 function in distinct oxidative damage
RT repair pathways in vivo.";
RL DNA Repair 2:1253-1267(2003).
Feature:
CHAIN 1 523 DNA-(apurinic or apyrimidinic site) lyase
2.
/FTId=PRO_0000200019.
MUTAGEN 402 402 F->A: No change in activity; when
associated with A-403.
MUTAGEN 403 403 F->A: No change in activity; when
associated with A-402.
MUTAGEN 456 456 P->A: No change in activity; when
associated with A-457 and A-458.
MUTAGEN 457 457 L->A: No change in activity; when
associated with A-456 and A-458.
MUTAGEN 458 458 C->A: No change in activity; when
associated with A-456 and A-457.
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.
-!- 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.
-!- SUBCELLULAR LOCATION: Nucleus (By similarity).
-!- SIMILARITY: Belongs to the DNA repair enzymes AP/exoA family.
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Sequence length: 523
MRILSWNVNG IQNPFNYFPW NKKNSYKEIF QELQADVICV QELKMQKDSF PQQYAVVEGF
DSYFTFPKIR KGYSGVGFYV KKDVAIPVKA EEGITGILPV RGQKYSYSEA PEHEKIGFFP
KDIDRKTANW IDSEGRCILL DFQMFILIGV YCPVNSGENR LEYRRAFYKA LRERIERLIK
EGNRKIILVG DVNILCNPID TADQKDIIRE SLIPSIMESR QWIRDLLLPS RLGLLLDIGR
IQHPTRKGMF TCWNTRLNTR PTNYGTRIDY TLATPDLLPW VQDADIMAEV MGSDHCPVYL
DLKEEYEGKK LSNFLSHSKE PPLLSTAHHS AYRPSKNIHS MFQHFNSMKK NKNNSPTQSE
NVSASASSGS SPTVSRANSV IDVDAYPPEK RRRKEQSKLL SFFAKQKEEK EETNKTEDVS
IEVLDNNNES DIGLTVKKKV ENGNAWKQIF SERAPPLCEG HKEPCKYLTV RKPGINYGRK
FWICARPVGE LIKNSNAVSE EDTQPFQCRF FIWDSDWRAN SKD