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UniProtKB/Swiss-Prot entry Q6B4U9


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

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Entry information
Entry name PRDX1_MYOLU
Primary accession number Q6B4U9
Secondary accession numbers None
Integrated into Swiss-Prot on October 31, 2006
Sequence was last modified on September 13, 2004 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 28)
Name and origin of the protein
Protein name Peroxiredoxin-1
Synonym EC 1.11.1.15
Gene name
Name: PRDX1
Synonyms: PAG
From
Myotis lucifugus (Little brown bat) [TaxID: 59463] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae; Myotis.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, TISSUE SPECIFICITY, AND INDUCTION.
TISSUE=Heart;
DOI=10.1016/j.abb.2004.11.020; PubMed=15680912 [NCBI, ExPASy, EBI, Israel, Japan]
Eddy S.F., McNally J.D., Storey K.B.;
"Up-regulation of a thioredoxin peroxidase-like protein, proliferation-associated gene, in hibernating bats.";
Arch. Biochem. Biophys. 435:103-111(2005).
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).
  • TISSUE SPECIFICITY: Detected in heart and skeletal muscle (at protein level).
  • INDUCTION: Up-regulated in hearts from hiberbating bats.
  • 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
AY680839; AAT79401.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
SMR Q6B4U9; 3-175.
ModBase Q6B4U9.
Ontologies
GO
GO:0042470; Cellular component: melanosome (inferred from electronic annotation from UniProtKB-SubCell).
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 Q6B4U9.
Genome annotation databases
Ensembl ENSMLUG00000005673; Myotis lucifugus. [Contig view]
Phylogenomic databases
HOVERGEN Q6B4U9; -.
Other
ProtoNet Q6B4U9.
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_0000256853
DOMAIN   6   165  160     Thioredoxin. 
ACT_SITE   52    52        Cysteine sulfenic acid (-SOH) intermediate (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: 22124 Da [This is the MW of the unprocessed precursor] CRC64: A75F3D21C40322CD [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSSGNAKIGH PAPNFKATAV MPDGQFKDIS LSDYKGKYVV FFFYPLDFTF VCPTEIIAFS 

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

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

       190 
SDTIKPDVQK SKEYFSKQK 

Q6B4U9 in FASTA format

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