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UniProtKB/Swiss-Prot entry Q5E947


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

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Entry information
Entry name PRDX1_BOVIN
Primary accession number Q5E947
Secondary accession number A6QLL7
Integrated into Swiss-Prot on May 24, 2005
Sequence was last modified on March 15, 2005 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 31)
Name and origin of the protein
Protein name Peroxiredoxin-1
Synonym EC 1.11.1.15
Gene name
Name: PRDX1
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 [LARGE SCALE MRNA].
DOI=10.1186/1471-2164-6-166; PubMed=16305752 [NCBI, ExPASy, EBI, Israel, Japan]
Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
"Characterization of 954 bovine full-CDS cDNA sequences.";
BMC Genomics 6:166-166(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Hereford;
TISSUE=Ascending colon;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (JUN-2007) 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 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. May form heterodimers with AOP2 (By similarity).
  • SUBCELLULAR LOCATION: Cytoplasm (By similarity). Melanosome (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
BT021073; AAX09090.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC148009; AAI48010.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
UniGene Bt.65324
3D structure databases
SMR Q5E947; 3-175.
ModBase Q5E947.
Protein family/group databases
PeroxiBase 4494; Bt2CysPrx01.
Ontologies
GO
GO:0042345; Biological process: regulation of NF-kappaB import into nucleus (inferred from sequence or structural similarity from AgBase).
GO:0006979; Biological process: response to oxidative stress (inferred from sequence or structural similarity from AgBase).
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 Q5E947.
Genome annotation databases
Ensembl ENSBTAG00000003642; Bos taurus. [Contig view]
Phylogenomic databases
HOVERGEN Q5E947; -.
Other
ProtoNet Q5E947.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Antioxidant; Cytoplasm; 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_0000135075
DOMAIN   6   165  160     Thioredoxin. 
ACT_SITE   52    52        Cysteine sulfenic acid (-SOH) intermediate (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: 22210 Da [This is the MW of the unprocessed precursor] CRC64: CFEE26A9F10B0483 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSSGNAKIGH RAPQFKATAV MPDGQFKDIS LADYKGKYVV FFFYPLDFTF VCPTEIIAFS 

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

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

       190 
SDTIKPDVQK SKEYFSKQK 

Q5E947 in FASTA format

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