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UniProtKB/Swiss-Prot entry Q9JKY1


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

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Entry information
Entry name PRDX1_CRIGR
Primary accession number Q9JKY1
Secondary accession numbers None
Integrated into Swiss-Prot on October 31, 2006
Sequence was last modified on October 1, 2000 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 44)
Name and origin of the protein
Protein name Peroxiredoxin-1
Synonyms EC 1.11.1.15
Thioredoxin peroxidase 2
TPX-2
Gene name
Name: PRDX1
Synonyms: TDPX2
From
Cricetulus griseus (Chinese hamster) [TaxID: 10029] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Cricetidae; Cricetinae; Cricetulus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, INDUCTION, AND FUNCTION.
TISSUE=Ovary;
DOI=10.1042/BJ20021354; PubMed=12519079 [NCBI, ExPASy, EBI, Israel, Japan]
Chang K.N., Lee T.C., Tam M.F., Chen Y.C., Lee L.W., Lee S.Y., Lin P.J., Huang R.N.;
"Identification of galectin I and thioredoxin peroxidase II as two arsenic-binding proteins in Chinese hamster ovary cells.";
Biochem. J. 371:495-503(2003).
Comments
  • FUNCTION: Involved in redox regulation of the cell. Reduces peroxides with reducing equivalents provided through the thioredoxin system but not from glutaredoxin. May play an important role in eliminating peroxides generated during metabolism. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H(2)O(2) (By similarity).
  • CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.
  • SUBUNIT: Homodimer; disulfide-linked, upon oxidation (By similarity). May form heterodimers with AOP2 (By similarity).
  • SUBCELLULAR LOCATION: Cytoplasm (By similarity). Melanosome (By similarity).
  • INDUCTION: Up-regulated upon exposure to arsenate.
  • MISCELLANEOUS: The active site is the redox-active Cys-52 oxidized to Cys-SOH. Cys-SOH rapidly reacts with Cys-173-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: Inactivated upon oxidative stress by overoxidation of Cys-52 to Cys-SO(2)H and Cys-SO(3)H. Cys-SO(2)H is retroreduced to Cys-SOH after removal of H(2)O(2), while Cys-SO(3)H may be irreversibly oxidized (By similarity).
  • SIMILARITY: Belongs to the ahpC/TSA 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
AF221841; AAF32369.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
HSSP Q63716; 1QQ2. [HSSP ENTRY / PDB]
SMR Q9JKY1; 3-175.
ModBase Q9JKY1.
Ontologies
GO
GO:0042470; Cellular component: melanosome (inferred from electronic annotation from UniProtKB-SubCell).
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).
BLOCKS Q9JKY1.
ProtoNet Q9JKY1.
Phylogenomic databases
HOVERGEN Q9JKY1; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Antioxidant; Cytoplasm; Direct protein sequencing; Oxidoreductase; Peroxidase; Phosphoprotein; Redox-active center.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   199  199     Peroxiredoxin-1. PRO_0000256852
DOMAIN   6   165  160     Thioredoxin. 
ACT_SITE   52    52        Cysteine sulfenic acid (-SOH) intermediate (By similarity). 
MOD_RES   10    10        Phosphotyrosine (By similarity). 
MOD_RES   90    90        Phosphothreonine (By similarity). 
MOD_RES   183   183        Phosphothreonine (By similarity). 
MOD_RES   194   194        Phosphotyrosine (By similarity). 
DISULFID   52    52        Interchain (with C-173); in linked form (By similarity). 
DISULFID   173   173        Interchain (with C-52); in linked form (By similarity). 
Sequence information
Length: 199 AA [This is the length of the unprocessed precursor] Molecular weight: 22263 Da [This is the MW of the unprocessed precursor] CRC64: CDA6E8015E1A055E [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSSGNAKIGY PAPNFKATAV MPDGQFRDIC LSEYRGKYVV FFFYPLDFTF VCPTEIIAFS 

        70         80         90        100        110        120 
DRAEEFKKLN CQVIGASVDS HFCHLAWINT PKKQGGLGPM NIPLVSDPKR TIAQDYGVLK 

       130        140        150        160        170        180 
ADEGISFRGL FIIDDKGILR QITINDLPVG RSVDEILRLV QAFQFTDKHG EVCPAGWKPG 

       190 
SDTIKPDVQK SKEYFSKQK 

Q9JKY1 in FASTA format

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