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UniProtKB/Swiss-Prot entry P30048


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

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Entry information
Entry name PRDX3_HUMAN
Primary accession number P30048
Secondary accession numbers P35690 Q0D2H1 Q13776 Q5T5V2 Q96HK4
Integrated into Swiss-Prot on April 1, 1993
Sequence was last modified on November 1, 1997 (Sequence version 3)
Annotations were last modified on    November 25, 2008 (Entry version 108)
Name and origin of the protein
Protein name Thioredoxin-dependent peroxide reductase, mitochondrial [Precursor]
Synonyms EC 1.11.1.15
Peroxiredoxin-3
PRX III
Antioxidant protein 1
AOP-1
Protein MER5 homolog
HBC189
Gene name
Name: PRDX3
Synonyms: AOP1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Blood;
PubMed=7733872 [NCBI, ExPASy, EBI, Israel, Japan]
Tsuji K., Copeland N.G., Jenkins N.A., Obinata M.;
"Mammalian antioxidant protein complements alkylhydroperoxide reductase (ahpC) mutation in Escherichia coli.";
Biochem. J. 307:377-381(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201).";
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-55; THR-218 AND ILE-234.
NIEHS SNPs program;
Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature02462; PubMed=15164054 [NCBI, ExPASy, EBI, Israel, Japan]
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Bone marrow, Skeletal muscle, Testis, Urinary bladder, and Uterus;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 63-72.
TISSUE=Liver;
DOI=10.1002/elps.11501301201; PubMed=1286669 [NCBI, ExPASy, EBI, Israel, Japan]
Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F., Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R., Appel R.D., Hughes G.J.;
"Human liver protein map: a reference database established by microsequencing and gel comparison.";
Electrophoresis 13:992-1001(1992).
[8]
PROTEIN SEQUENCE OF 150-166 AND 171-207, AND MASS SPECTROMETRY.
TISSUE=Brain, and Cajal-Retzius cell;
Lubec G., Vishwanath V.;
Submitted (MAR-2007) to UniProtKB.
[9]
OVEROXIDATION AT CYS-108.
DOI=10.1042/BJ20020525; PubMed=12059788 [NCBI, ExPASy, EBI, Israel, Japan]
Wagner E., Luche S., Penna L., Chevallet M., van Dorsselaer A., Leize-Wagner E., Rabilloud T.;
"A method for detection of overoxidation of cysteines: peroxiredoxins are oxidized in vivo at the active-site cysteine during oxidative stress.";
Biochem. J. 366:777-785(2002).
[10]
FUNCTION, AND INTERACTION WITH MAP3K13.
DOI=10.1046/j.1432-1033.2003.03363.x; PubMed=12492477 [NCBI, ExPASy, EBI, Israel, Japan]
Masaki M., Ikeda A., Shiraki E., Oka S., Kawasaki T.;
"Mixed lineage kinase LZK and antioxidant protein-1 activate NF-kappaB synergistically.";
Eur. J. Biochem. 270:76-83(2003).
Comments
  • FUNCTION: Involved in redox regulation of the cell. Protects radical-sensitive enzymes from oxidative damage by a radical-generating system. Acts synergistically with MAP3K13 to regulate the activation of NF-kappa-B in the cytosol.
  • CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.
  • SUBUNIT: Homodimer; disulfide-linked, upon oxidation (By similarity). Binds MAP3K13.
  • SUBCELLULAR LOCATION: Mitochondrion.
  • MISCELLANEOUS: The active site is the redox-active Cys-108 oxidized to Cys-SOH. Cys-SOH rapidly reacts with Cys-229-SH of the other subunit to form an intermolecular disulfide with a concomitant homodimer formation. The enzyme may be subsequently regenerated by reduction of the disulfide by thioredoxin.
  • MISCELLANEOUS: Irreversibly inactivated by overoxidation of Cys-108 (to Cys-SO(3)H) upon oxidative stress.
  • SIMILARITY: Belongs to the ahpC/TSA family.
  • SIMILARITY: Contains 1 thioredoxin domain.
  • WEB RESOURCE: Name=NIEHS SNPs; URL="http://egp.gs.washington.edu/data/prdx3/";.
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
D49396; BAA08389.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR450344; CAG29340.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT020007; AAV38810.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ298752; ABB84468.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL355861; CAI15802.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC002685; AAH02685.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC007062; AAH07062.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC008435; AAH08435.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC009601; AAH09601.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC021691; AAH21691.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC022373; AAH22373.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC059169; AAH59169.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC111397; AAI11398.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_006784.1; -.
NP_054817.2; -.
UniGene Hs.523302
3D structure databases
HSSP P32119; 1QMV. [HSSP ENTRY / PDB]
SMR P30048; 63-223.
ModBase P30048.
Protein-protein interaction databases
IntAct P30048; -.
Protein family/group databases
PeroxiBase 4492; Hs2CysPrx03.
PTM databases
PhosphoSite P30048; -.
2D gel databases
SWISS-2DPAGE P30048; -.
OGP P30048; -.
Siena-2DPAGE P30048; -.
Organism-specific databases
H-InvDB HIX0009251; -.
HIX0035477; -.
HIX0060125; -.
HGNC HGNC:9354; PRDX3.
GenAtlas PRDX3.
HPA CAB008656; -.
MIM 604769; gene. [NCBI / EBI]
PharmGKB PA33724; -.
GeneCards P30048.
Gene expression databases
ArrayExpress P30048; -.
CleanEx HS_PRDX3; -.
GermOnline ENSG00000165672; Homo sapiens.
Ontologies
GO
GO:0005769; Cellular component: early endosome (inferred from direct assay from UniProtKB).
GO:0005739; Cellular component: mitochondrion (inferred from direct assay from UniProtKB).
GO:0008785; Molecular function: alkyl hydroperoxide reductase activity (non-traceable author statement from UniProtKB).
GO:0043027; Molecular function: caspase inhibitor activity (inferred from mutant phenotype from UniProtKB).
GO:0051920; Molecular function: peroxiredoxin activity (inferred from electronic annotation from EC).
GO:0008022; Molecular function: protein C-terminus binding (inferred from physical interaction from UniProtKB).
GO:0019901; Molecular function: protein kinase binding (inferred from physical interaction from UniProtKB).
GO:0045454; Biological process: cell redox homeostasis (inferred from electronic annotation from InterPro).
GO:0034614; Biological process: cellular response to reactive oxygen species (inferred from mutant phenotype from UniProtKB).
GO:0042744; Biological process: hydrogen peroxide catabolic process (inferred from mutant phenotype from UniProtKB).
GO:0007005; Biological process: mitochondrion organization (inferred from mutant phenotype from UniProtKB).
GO:0030099; Biological process: myeloid cell differentiation (inferred from sequence or structural similarity from UniProtKB).
GO:0043066; Biological process: negative regulation of apoptosis (inferred from mutant phenotype from UniProtKB).
GO:0033673; Biological process: negative regulation of kinase activity (inferred from direct assay from UniProtKB).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0008284; Biological process: positive regulation of cell proliferation (inferred from direct assay from UniProtKB).
GO:0051092; Biological process: positive regulation of NF-kappaB transcription factor activity (inferred from direct assay from UniProtKB).
GO:0051881; Biological process: regulation of mitochondrial membrane potential (inferred from mutant phenotype from UniProtKB).
GO:0032496; Biological process: response to lipopolysaccharide (inferred from sequence or structural similarity from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR000866; AhpC-TSA.
IPR012335; Thioredoxin_fold.
Graphical view of domain structure.
Gene3D G3DSA:3.40.30.10; Thioredoxin_fold; 1.
Pfam PF00578; AhpC-TSA; 1.
Pfam graphical view of domain structure.
PROSITE PS51352; THIOREDOXIN_2; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P30048.
ProtoNet P30048.
Proteomic databases
PeptideAtlas P30048; -.
Genome annotation databases
Ensembl ENSG00000165672; Homo sapiens. [Contig view]
GeneID 10935; -.
KEGG hsa:10935; -.
NMPDR fig|9606.3.peg.4727; -.
Phylogenomic databases
HOGENOM P30048; -.
HOVERGEN P30048; -.
Other
NextBio 41537; -.
SOURCE PRDX3; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Antioxidant; Direct protein sequencing; Mitochondrion; Oxidoreductase; Peroxidase; Redox-active center; Transit peptide.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
TRANSIT   1    62  62     Mitochondrion. 
CHAIN   63   256  194     Thioredoxin-dependent peroxide reductase, mitochondrial. PRO_0000023782
DOMAIN   63   221  159     Thioredoxin. 
ACT_SITE   108   108        Cysteine sulfenic acid (-SOH) intermediate (By similarity). 
DISULFID   108   108        Interchain (with C-229); in linked form (By similarity). 
DISULFID   229   229        Interchain (with C-108); in linked form (By similarity). 
VARIANT   55    55  1     S -> R. VAR_025052 
VARIANT   218   218  1     A -> T. VAR_025053 
VARIANT   234   234  1     T -> I. VAR_025054 
CONFLICT   31    31        R -> W (in Ref. 6; AAH08435). 
Sequence information
Length: 256 AA [This is the length of the unprocessed precursor] Molecular weight: 27693 Da [This is the MW of the unprocessed precursor] CRC64: 8BEB7F5E55BFE9BE [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAAAVGRLLR ASVARHVSAI PWGISATAAL RPAACGRTSL TNLLCSGSSQ AKLFSTSSSC 

        70         80         90        100        110        120 
HAPAVTQHAP YFKGTAVVNG EFKDLSLDDF KGKYLVLFFY PLDFTFVCPT EIVAFSDKAN 

       130        140        150        160        170        180 
EFHDVNCEVV AVSVDSHFSH LAWINTPRKN GGLGHMNIAL LSDLTKQISR DYGVLLEGSG 

       190        200        210        220        230        240 
LALRGLFIID PNGVIKHLSV NDLPVGRSVE ETLRLVKAFQ YVETHGEVCP ANWTPDSPTI 

       250 
KPSPAASKEY FQKVNQ 

P30048 in FASTA format

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