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Description:
DNA-(apurinic or apyrimidinic site) lyase 1 (EC 4.2.99.18) (APendonuclease 1) (Apurinic-apyrimidinic endonuclease 1).
Molecular weight: 41308
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 ) base-excision repair( GO:0006284 )
Important dates:
01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
01-JUN-1994, sequence version 3.
07-MAR-2006, entry version 57.
Phylogenetic order:
Eukaryota Fungi Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces.
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 APN1_YEAST:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | M33667 | AAA34429.1 | - |
| EMBL | S93804 | AAB22003.1 | - |
| EMBL | Z28114 | CAA81954.1 | - |
| PIR | S29871 | S29871. | |
| HSSP | P12638 | 1QUM | |
| GermOnline | 139870 | -.1 | |
| Ensembl | YKL114C | Saccharomyces cerevisiae.1 | |
| GenomeReviews | Y13137_GR | YKL114C.1 | |
| SGD | S000001597 | APN1. | |
| LinkHub | P22936 | -.1 | |
| GO | GO:0005739 | C:mitochondrion | IDA. |
| GO | GO:0005634 | C:nucleus | IDA. |
| GO | GO:0003906 | F:DNA-(apurinic or apyrimidinic site) lyase a... | IDA. |
| GO | GO:0006284 | P:base-excision repair | IDA. |
| InterPro | IPR001719 | AP_endnuclease2. | |
| InterPro | IPR012307 | Xylisom_TIMbarrl. | |
| Pfam | PF01261 | AP_endonuc_2 | 1. |
| SMART | SM00518 | AP2Ec | 1. |
| TIGRFAMs | TIGR00587 | nfo | 1. |
| PROSITE | PS00729 | AP_NUCLEASE_F2_1 | 1. |
| PROSITE | PS00730 | AP_NUCLEASE_F2_2 | 1. |
| PROSITE | PS00731 | AP_NUCLEASE_F2_3 | 1. |
Keywords:
Complete proteome; Direct protein sequencing; DNA damage; DNA repair; Lyase; Metal-binding; Nuclear protein; Zinc.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX MEDLINE=90272680; PubMed=1693433;
RA Popoff S.C., Spira A.I., Johnson A.W., Demple B.;
RT "Yeast structural gene (APN1) for the major apurinic endonuclease:
RT homology to Escherichia coli endonuclease IV.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:4193-4197(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX MEDLINE=92221689; PubMed=1561835;
RA Jacquier A., Legrain P., Dujon B.;
RT "Sequence of a 10.7 kb segment of yeast chromosome XI identifies the
RT APN1 and the BAF1 loci and reveals one tRNA gene and several new open
RT reading frames including homologs to RAD2 and kinases.";
RL Yeast 8:121-132(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S288c / FY1679;
RX MEDLINE=94255012; PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M.,
RA Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C.,
RA Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G.,
RA Zimmermann J., Haasemann M., Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [4]
RP CHARACTERIZATION, AND PROTEIN SEQUENCE OF 1-25.
RX MEDLINE=89053965; PubMed=3056935;
RA Johnson A.W., Demple B.;
RT "Yeast DNA diesterase for 3'-fragments of deoxyribose: purification
RT and physical properties of a repair enzyme for oxidative DNA damage.";
RL J. Biol. Chem. 263:18009-18016(1988).
RN [5]
RP METAL-BINDING STUDIES.
RX MEDLINE=92078146; PubMed=1720775;
RA Levin J.D., Shapiro R., Demple B.;
RT "Metalloenzymes in DNA repair. Escherichia coli endonuclease IV and
RT Saccharomyces cerevisiae Apn1.";
RL J. Biol. Chem. 266:22893-22898(1991).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION.
RX MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA Dephoure N., O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
Feature:
INIT_MET 0 0
CHAIN 1 366 DNA-(apurinic or apyrimidinic site) lyase
1.
/FTId=PRO_0000190898.
METAL 82 82 Zinc 1 (By similarity).
METAL 122 122 Zinc 1 (By similarity).
METAL 157 157 Zinc 1 (By similarity).
METAL 157 157 Zinc 2 (By similarity).
METAL 191 191 Zinc 2 (By similarity).
METAL 194 194 Zinc 3 (By similarity).
METAL 228 228 Zinc 2 (By similarity).
METAL 241 241 Zinc 3 (By similarity).
METAL 243 243 Zinc 3 (By similarity).
METAL 273 273 Zinc 2 (By similarity).
CONFLICT 238 238 A -> S (in Ref. 1).
Comments:
-!- FUNCTION: DNA repair enzyme that cleaves apurinic/apyrimidinic
(AP) sites and removes 3'-blocking groups present at single strand
breaks of damaged DNA. APN1 accounts for > 97% of both apurinic/
apyrimidinic (AP) lyase and DNA 3'-repair diesterase activities.
-!- 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.
-!- SUBUNIT: Monomer.
-!- SUBCELLULAR LOCATION: Nucleus.
-!- MISCELLANEOUS: Present with 7250 molecules/cell.
-!- SIMILARITY: Belongs to the AP endonuclease 2 family.
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Sequence length: 366
PSTPSFVRSA VSKYKFGAHM SGAGGISNSV TNAFNTGCNS FAMFLKSPRK WVSPQYTQEE
IDKFKKNCAT YNYNPLTDVL PHGQYFINLA NPDREKAEKS YESFMDDLNR CEQLGIGLYN
LHPGSTLKGD HQLQLKQLAS YLNKAIKETK FVKIVLENMA GTGNLVGSSL VDLKEVIGMI
EDKSRIGVCI DTCHTFAAGY DISTTETFNN FWKEFNDVIG FKYLSAVHLN DSKAPLGANR
DLHERLGQGY LGIDVFRMIA HSEYLQGIPI VLETPYENDE GYGNEIKLME WLESKSESEL
LEDKEYKEKN DTLQKLGAKS RKEQLDKFEV KQKKRAGGTK RKKATAEPSD NDILSQMTKK
RKTKKE