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UniProtKB/Swiss-Prot entry Q9BGI3


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

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Entry information
Entry name PRDX2_BOVIN
Primary accession number Q9BGI3
Secondary accession number Q3T0L0
Integrated into Swiss-Prot on August 2, 2002
Sequence was last modified on June 1, 2001 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 47)
Name and origin of the protein
Protein name Peroxiredoxin-2
Synonym EC 1.11.1.15
Gene name
Name: PRDX2
From
Bos taurus (Bovine) [TaxID: 9913] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
Leyens G., Donnay I., Knoops B.;
"Cloning of 4 new bovine peroxiredoxins, and screening of the complete peroxiredoxin family in different bovine tissues.";
Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Crossbred X Angus;
TISSUE=Ileum;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
Comments
  • FUNCTION: Involved in redox regulation of the cell. Reduces peroxides with reducing equivalents provided through the thioredoxin system. It is not able to receive electrons 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).
  • CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.
  • SUBUNIT: Homodimer; disulfide-linked, upon oxidation. Interacts with TIPIN (By similarity).
  • SUBCELLULAR LOCATION: Cytoplasm (By similarity).
  • 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
AF305562; AAG53659.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC102351; AAI02352.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_777188.1; -.
UniGene Bt.2689
3D structure databases
HSSP P32119; 1QMV. [HSSP ENTRY / PDB]
SMR Q9BGI3; 7-199.
ModBase Q9BGI3.
Protein family/group databases
PeroxiBase 4473; Bt2CysPrx02.
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 Q9BGI3.
Genome annotation databases
Ensembl ENSBTAG00000012062; Bos taurus. [Contig view]
GeneID 286793; -.
KEGG bta:286793; -.
Phylogenomic databases
HOVERGEN Q9BGI3; -.
Other
ProtoNet Q9BGI3.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Antioxidant; Cytoplasm; Oxidoreductase; Peroxidase; Redox-active center.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   199  199     Peroxiredoxin-2. PRO_0000135079
DOMAIN   7   165  159     Thioredoxin. 
ACT_SITE   52    52        Cysteine sulfenic acid (-SOH) intermediate (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: 21946 Da [This is the MW of the unprocessed precursor] CRC64: 5F256CE54090E2DE [This is a checksum on the sequence]
        10         20         30         40         50         60 
MACVCKAHVG KPAPEFQATA VVDGAFKEVK LSDYKGKYVV LFFYPLDFTF VCPTEIVAFS 

        70         80         90        100        110        120 
DRAAEFHKLN CEVLGVSVDS QFTHLAWINT PRKEGGLGPL NIPLLADVTR KLSSDYGVLK 

       130        140        150        160        170        180 
EDEGIAYRGL FVIDGKGVLR QVTINDLPVG RSVDEALRLV QAFQYTDEHG EVCPAGWTPG 

       190 
SDTIKPNVDD SKEYFSKHN 

Q9BGI3 in FASTA format

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