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UniProtKB/Swiss-Prot entry P38013


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name AHP1_YEAST
Primary accession number P38013
Secondary accession numbers None
Integrated into Swiss-Prot on October 1, 1994
Sequence was last modified on January 23, 2007 (Sequence version 4)
Annotations were last modified on    September 2, 2008 (Entry version 90)
Name and origin of the protein
Protein name Peroxiredoxin type-2
Synonyms EC 1.11.1.15
Peroxiredoxin type II
Peroxisomal alkyl hydroperoxide reductase
Thioredoxin peroxidase type II
Thioredoxin reductase type II
TPx type II
Cytoplasmic thiol peroxidase 3
cTPx 3
Thiol-specific antioxidant II
TSA II
AHPC1
Gene name
Name: AHP1
OrderedLocusNames: YLR109W
ORFNames: L2916, L9354.5
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 90840 / EAY235 / FY23;
DOI=10.1002/(SICI)1097-0061(19970315)13:3<241::AID-YEA61>3.0.CO;2-#; PubMed=9090053 [NCBI, ExPASy, EBI, Israel, Japan]
Verhasselt P., Volckaert G.;
"Sequence analysis of a 37.6 kbp cosmid clone from the right arm of Saccharomyces cerevisiae chromosome XII, carrying YAP3, HOG1, SNR6, tRNA-Arg3 and 23 new open reading frames, among which several homologies to proteins involved in cell division control and to mammalian growth factors and other animal proteins are found.";
Yeast 13:241-250(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204511 / S288c / AB972;
PubMed=9169871 [NCBI, ExPASy, EBI, Israel, Japan]
Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
Nature 387:87-90(1997).
[3]
PROTEIN SEQUENCE OF 2-8; 16-48; 80-102 AND 114-176, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, AND MASS SPECTROMETRY.
Bienvenut W.V., Peters C.;
Submitted (MAY-2005) to UniProtKB.
[4]
PROTEIN SEQUENCE OF 8-15; 33-41; 80-102 AND 125-176, AND CONJUGATION TO URM1.
DOI=10.1128/EC.2.5.930-936.2003; PubMed=14555475 [NCBI, ExPASy, EBI, Israel, Japan]
Goehring A.S., Rivers D.M., Sprague G.F. Jr.;
"Attachment of the ubiquitin-related protein Urm1p to the antioxidant protein Ahp1p.";
Eukaryot. Cell 2:930-936(2003).
[5]
PROTEIN SEQUENCE OF 16-41; 49-68; 82-96; 114-123 AND 142-150, POST-TRANSLATIONAL MODIFICATION, DISULFIDE BONDS, AND BIOPHYSICOCHEMICAL PROPERTIES.
DOI=10.1021/bi9817818; PubMed=9888818 [NCBI, ExPASy, EBI, Israel, Japan]
Jeong J.S., Kwon S.J., Kang S.W., Rhee S.G., Kim K.;
"Purification and characterization of a second type thioredoxin peroxidase (type II TPx) from Saccharomyces cerevisiae.";
Biochemistry 38:776-783(1999).
[6]
PROTEIN SEQUENCE OF 82-99.
STRAIN=ATCC 204508 / S288c;
PubMed=7895733 [NCBI, ExPASy, EBI, Israel, Japan]
Garrels J.I., Futcher B., Kobayashi R., Latter G.I., Schwender B., Volpe T., Warner J.R., McLaughlin C.S.;
"Protein identifications for a Saccharomyces cerevisiae protein database.";
Electrophoresis 15:1466-1486(1994).
[7]
CHARACTERIZATION.
DOI=10.1074/jbc.274.8.4537; PubMed=9988687 [NCBI, ExPASy, EBI, Israel, Japan]
Lee J., Spector D., Godon C., Labarre J., Toledano M.B.;
"A new antioxidant with alkyl hydroperoxide defense properties in yeast.";
J. Biol. Chem. 274:4537-4544(1999).
[8]
CHARACTERIZATION.
PubMed=10635552 [NCBI, ExPASy, EBI, Israel, Japan]
Farcasanu I.C., Hirata D., Tsuchiya E., Mizuta K., Miyakawa T.;
"Involvement of thioredoxin peroxidase type II (Ahp1p) of Saccharomyces cerevisiae in Mn2+ homeostasis.";
Biosci. Biotechnol. Biochem. 63:1871-1881(1999).
[9]
CHARACTERIZATION, INDUCTION, AND SUBCELLULAR LOCATION.
DOI=10.1074/jbc.275.8.5723; PubMed=10681558 [NCBI, ExPASy, EBI, Israel, Japan]
Park S.G., Cha M.-K., Jeong W., Kim I.-H.;
"Distinct physiological functions of thiol peroxidase isoenzymes in Saccharomyces cerevisiae.";
J. Biol. Chem. 275:5723-5732(2000).
[10]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION AT SER-2, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M400219-MCP200; PubMed=15665377 [NCBI, ExPASy, EBI, Israel, Japan]
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.;
"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway.";
Mol. Cell. Proteomics 4:310-327(2005).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0607084104; PubMed=17287358 [NCBI, ExPASy, EBI, Israel, Japan]
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59 AND SER-171, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan]
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[13]
3D-STRUCTURE MODELING, AND STRUCTURE BY NMR.
DOI=10.1021/bi035551r; PubMed=14640681 [NCBI, ExPASy, EBI, Israel, Japan]
Trivelli X., Krimm I., Ebel C., Verdoucq L., Prouzet-Mauleon V., Chartier Y., Tsan P., Lauquin G., Meyer Y., Lancelin J.-M.;
"Characterization of the yeast peroxiredoxin Ahp1 in its reduced active and overoxidized inactive forms using NMR.";
Biochemistry 42:14139-14149(2003).
[14]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
Comments
  • FUNCTION: Thiol-specific antioxidant protein with alkyl hydroperoxidase activity. Involved in osmotic stress resistance and detoxification of the cell. Preferentially eliminates organic peroxides rather than H(2)O(2). Involved in cellular Mn(2+) homeostasis.
  • CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.
  • BIOPHYSICOCHEMICAL PROPERTIES:
    Kinetic parameters:   KM=150 µM for H2O2;
    KM=45 µM for cumene hydroperoxide;
    KM=8 µM for tert-butyl hydroperoxide;
    KM=3 µM for TRX1;
    KM=2 µM for TRX2;
    Vmax=20 µmol/min/mg enzyme for H2O2;
    Vmax=17 µmol/min/mg enzyme for cumene hydroperoxide;
    Vmax=14 µmol/min/mg enzyme for tert-butyl hydroperoxide;
    Vmax=17 µmol/min/mg enzyme for TRX1;
    Vmax=16 µmol/min/mg enzyme for TRX2;
    pH dependence:   Optimum pH is 6.5;
  • SUBUNIT: Homodimer; disulfide-linked, upon oxidation.
  • INTERACTION:
    P22803:TRX2; NbExp=1; IntAct=EBI-2382, EBI-19598;
  • SUBCELLULAR LOCATION: Cytoplasm.
  • INDUCTION: By H(2)O(2).
  • PTM: The Cys-62-SH group is the primary site of oxidation by H(2)O(2), and the oxidized Cys-62 (probably Cys-SOH) rapidly reacts with Cys-120-SH of the other subunit to form an intermolecular disulfide. This disulfide is subsequently reduced by thioredoxin to restore the reduced active form of the enzyme.
  • PTM: Conjugated to URM1, an ubiquitin-like protein.
  • MISCELLANEOUS: Present with 16228 molecules/cell in log phase SD medium.
  • SIMILARITY: Belongs to the peroxiredoxin 2 family.
  • SIMILARITY: Contains 1 thioredoxin domain.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X89514; CAA61687.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z73281; CAA97676.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U53878; AAB67554.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S64946; S64946.
RefSeq NP_013210.1; -.
3D structure databases
HSSP P44758; 1NM3. [HSSP ENTRY / PDB]
ModBase P38013.
Protein-protein interaction databases
DIP DIP:6375N; -.
IntAct P38013; -.
2D gel databases
COMPLUYEAST-2DPAGE P38013; -.
Organism-specific databases
CYGD YLR109w; -.
SGD S000004099; AHP1.
Yeast-GFP YLR109W.
Gene expression databases
ArrayExpress P38013; -.
GermOnline YLR109W; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from direct assay from SGD).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0008379; Molecular function: thioredoxin peroxidase activity (inferred from direct assay from SGD).
GO:0030503; Biological process: regulation of cell redox homeostasis (inferred from direct assay from SGD).
GO:0010038; Biological process: response to metal ion (inferred from mutant phenotype from SGD).
GO:0006979; Biological process: response to oxidative stress (inferred from genetic interaction from SGD).
QuickGo view.
Family and domain databases
InterPro IPR013740; Redoxin.
IPR012335; Thioredoxin_fold.
Graphical view of domain structure.
Gene3D G3DSA:3.40.30.10; Thioredoxin_fold; 1.
Pfam PF08534; Redoxin; 1.
Pfam graphical view of domain structure.
PROSITE PS51352; THIOREDOXIN_2; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P38013.
Proteomic databases
PeptideAtlas P38013; -.
Genome annotation databases
Ensembl YLR109W; Saccharomyces cerevisiae. [Contig view]
GeneID 850799; -.
GenomeReviews Y13138_GR; YLR109W.
KEGG sce:YLR109W; -.
NMPDR fig|4932.3.peg.4202; -.
Phylogenomic databases
HOGENOM P38013; -.
Other
LinkHub P38013; -.
ProtoNet P38013.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Antioxidant; Complete proteome; Cytoplasm; Direct protein sequencing; Oxidoreductase; Peroxidase; Phosphoprotein; Redox-active center; Ubl conjugation.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   176  175     Peroxiredoxin type-2. PRO_0000056610
DOMAIN   9   176  168     Thioredoxin. 
ACT_SITE   62    62        Cysteine sulfenic acid (-SOH) intermediate (Potential). 
MOD_RES   2     2        N-acetylserine. 
MOD_RES   2     2        Phosphoserine. 
MOD_RES   22    22        Phosphoserine. 
MOD_RES   59    59        Phosphoserine. 
MOD_RES   171   171        Phosphoserine. 
DISULFID   62    62        Interchain (with C-120); in linked form. 
DISULFID   120   120        Interchain (with C-62); in linked form. 
CONFLICT   21    21        I -> T (in Ref. 5; AA sequence). 
CONFLICT   65    65        S -> V (in Ref. 5; AA sequence). 
CONFLICT   87    87        I -> E (in Ref. 5; AA sequence). 
Sequence information
Length: 176 AA [This is the length of the unprocessed precursor] Molecular weight: 19115 Da [This is the MW of the unprocessed precursor] CRC64: 11B730781306A015 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSDLVNKKFP AGDYKFQYIA ISQSDADSES CKMPQTVEWS KLISENKKVI ITGAPAAFSP 

        70         80         90        100        110        120 
TCTVSHIPGY INYLDELVKE KEVDQVIVVT VDNPFANQAW AKSLGVKDTT HIKFASDPGC 

       130        140        150        160        170 
AFTKSIGFEL AVGDGVYWSG RWAMVVENGI VTYAAKETNP GTDVTVSSVE SVLAHL 

P38013 in FASTA format

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