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UniProtKB/Swiss-Prot entry O35244


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

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Entry information
Entry name PRDX6_RAT
Primary accession number O35244
Secondary accession numbers None
Integrated into Swiss-Prot on July 15, 1999
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    December 16, 2008 (Entry version 71)
Name and origin of the protein
Protein name Peroxiredoxin-6
Synonyms EC 1.11.1.15
Antioxidant protein 2
1-Cys peroxiredoxin
1-Cys PRX
Acidic calcium-independent phospholipase A2
aiPLA2
EC 3.1.1.-
Non-selenium glutathione peroxidase
NSGPx
EC 1.11.1.7
Thiol-specific antioxidant protein
Gene name
Name: Prdx6
Synonyms: Aipla2, Aop2, Tsa
From
Rattus norvegicus (Rat) [TaxID: 10116] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Rattus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley;
TISSUE=Lung;
Kim T.-S., Feinstein S.I., Dodia C., Hennigan B.B., Fisher A.B.;
Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Wistar;
TISSUE=Olfactory epithelium;
Andreeva S.;
Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
[3]
PROTEIN SEQUENCE OF 2-41; 57-84; 98-118; 133-142; 156-162 AND 183-199, AND MASS SPECTROMETRY.
STRAIN=Sprague-Dawley;
TISSUE=Hippocampus, and Spinal cord;
Lubec G., Afjehi-Sadat L., Chen W.-Q.;
Submitted (APR-2007) to UniProtKB.
[4]
PROTEIN SEQUENCE OF 26-42 AND 146-163.
DOI=10.1074/jbc.272.4.2542; PubMed=8999971 [NCBI, ExPASy, EBI, Israel, Japan]
Kim T.-S., Sundaresh C.S., Feinstein S.I., Dodia C., Skach W.R., Jain M.K., Nagase T., Seki N., Ishikawa K., Nomura N., Fisher A.B.;
"Identification of a human cDNA clone for lysosomal type Ca2+-independent phospholipase A2 and properties of the expressed protein.";
J. Biol. Chem. 272:2542-2550(1997).
[5]
ERRATUM.
Kim T.-S., Sundaresh C.S., Feinstein S.I., Dodia C., Skach W.R., Jain M.K., Nagase T., Seki N., Ishikawa K., Nomura N., Fisher A.B.;
J. Biol. Chem. 272:10981-10981(1997).
Comments
  • FUNCTION: Involved in redox regulation of the cell. Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides. May play a role in the regulation of phospholipid turnover as well as in protection against oxidative injury.
  • CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.
  • CATALYTIC ACTIVITY: Donor + H2O2 = oxidized donor + 2 H2O.
  • SUBUNIT: Homotetramer. May interact with HTR2A. Interacts with STH (By similarity).
  • SUBCELLULAR LOCATION: Cytoplasm. Lysosome. Note=Also found in lung secretory organelles.
  • MISCELLANEOUS: The active site is the redox-active Cys-47 oxidized to Cys-SOH. Cys-SOH may rapidly react with a Cys-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 (By similarity).
  • MISCELLANEOUS: Irreversibly inactivated by overoxidation of Cys-47 (to Cys-SO(3)H) upon oxidative stress (By similarity).
  • SIMILARITY: Belongs to the ahpC/TSA family. Rehydrin subfamily.
  • 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
AF014009; AAB66341.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Y17295; CAA76732.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_446028.1; -.
UniGene Rn.42
3D structure databases
HSSP P30041; 1PRX. [HSSP ENTRY / PDB]
SMR O35244; 5-224.
ModBase O35244.
Protein family/group databases
PeroxiBase 4427; Rno1CysPrx.
Organism-specific databases
RGD 71005; Prdx6.
Gene expression databases
ArrayExpress O35244; -.
GermOnline ENSRNOG00000002896; Rattus norvegicus.
Ontologies
GO
GO:0005764; Cellular component: lysosome (inferred from electronic annotation from UniProtKB-KW).
GO:0051920; Molecular function: peroxiredoxin activity (inferred from electronic annotation from EC).
GO:0045454; Biological process: cell redox homeostasis (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
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).
Proteomics databases
PRIDE O35244; -.
Genome annotation databases
Ensembl ENSRNOG00000002896; Rattus norvegicus. [Contig view]
GeneID 94167; -.
KEGG rno:94167; -.
Phylogenomic databases
HOVERGEN O35244; -.
Other
NextBio 617808; -.
ProtoNet O35244.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Antioxidant; Cytoplasm; Direct protein sequencing; Hydrolase; Lipid degradation; Lysosome; Multifunctional enzyme; Oxidoreductase; Peroxidase; Phosphoprotein; Redox-active center.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom  To Length Description FTId
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   224  223     Peroxiredoxin-6. PRO_0000135104
DOMAIN   5   169  165     Thioredoxin. 
ACT_SITE   32    32        For phospholipase activity (By similarity). 
ACT_SITE   47    47        Cysteine sulfenic acid (-SOH) intermediate (By similarity). 
MOD_RES   44    44        Phosphothreonine (By similarity). 
MOD_RES   89    89        Phosphotyrosine (By similarity). 
DISULFID   47    47        Interchain; in linked form (By similarity). 
Sequence information
Length: 224 AA [This is the length of the unprocessed precursor] Molecular weight: 24819 Da [This is the MW of the unprocessed precursor] CRC64: EE41D9079A708FD9 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MPGGLLLGDE APNFEANTTI GHIRFHDFLG DSWGILFSHP RDFTPVCTTE LGRAAKLAPE 

        70         80         90        100        110        120 
FAKRNVKLIA LSIDSVEDHF AWSKDINAYN GAAPTEKLPF PIIDDKDRDL AILLGMLDPA 

       130        140        150        160        170        180 
EKDEKGMPVT ARVVFIFGPD KKLKLSILYP ATTGRNFDEI LRVVDSLQLT ASNPVATPVD 

       190        200        210        220 
WKKGESVMVL PTLPEEEAKQ LFPKGVFTKE LPSGKKYLRY TPQP 

O35244 in FASTA format

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