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Reviewed, UniProtKB/Swiss-Prot Q6DV14 (PRDX1_GECJA)

Last modified November 25, 2008. Version 32. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Peroxiredoxin-1
    EC=1.11.1.15
Gene names
Name: PRDX1
ORF Names: GekBS014P
OrganismGecko japonicus (Japanese gecko)
Taxonomic identifier146911 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataScleroglossaGekkotaGekkonidaeGekkoninaeGekko

Protein attributes

Sequence length199 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (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' + H(2)O + ROH.

Subunit structure

Homodimer; disulfide-linked, upon oxidation By similarity.

Subcellular location

CytoplasmBy 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.

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.

Sequence similarities

Belongs to the ahpC/TSA family.

Contains 1 thioredoxin domain.

Ontologies

Keywords

   Cellular componentCytoplasm
   DomainRedox-active center
   Molecular functionAntioxidant
Oxidoreductase
Peroxidase
   PTMPhosphoprotein

Gene Ontology (GO)

   Biological processcell redox homeostasis

Inferred from electronic annotation. Source: InterPro

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionperoxiredoxin activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 199199Peroxiredoxin-1
PRO_0000256854

Regions

Domain6 – 165160Thioredoxin

Sites

Active site521Cysteine sulfenic acid (-SOH) intermediate By similarity

Amino acid modifications

Modified residue901Phosphothreonine By similarity
Modified residue1941Phosphotyrosine By similarity
Disulfide bond52Interchain (with C-173); in linked form By similarity
Disulfide bond173Interchain (with C-52); in linked form By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6DV14-1 [UniParc].

Last modified August 16, 2004. Version 1.
Checksum: 6AB33FB90907C318

FASTA19922,348
        10         20         30         40         50         60 
MSSGNAYIGK LAPDFQATAV MPDGQFKEIK LSDYKGKYVV LFFYPLDFTF VCPTEIIAFS 

        70         80         90        100        110        120 
DRSEEFRKIN CEVIGASVDS HFCHLAWINT PKKQGGLGSM HIPLVSDTKR VIAKDYGILK 

       130        140        150        160        170        180 
EDEGISYRGL FIIDDKGTLR QITINDLPVG RSVDETLRLV QAFQFTDKHG EVCPAGWQPG 

       190 
SDTIKPDVQK SKEYFSKHK 

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References

[1]"Analysis of expressed sequence tags and cloning of full length cDNA from brain and spinal cord cDNA library in Gecko."
Ding F., Liu Y., Gu X., Tan X., Shen A., Zhang H., Liu M., Jiang M., Yang H.
Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain and Spinal cord.

Cross-references

Sequence databases

AY626813 mRNA. Translation: AAT85554.1.
AY641835 mRNA. Translation: AAT68217.1.

3D structure databases

SMRQ6DV14. Positions 3-198.
ModBaseSearch...

Phylogenomic databases

HOVERGENQ6DV14.

Family and domain databases

InterProIPR000866. AhpC-TSA.
IPR012335. Thioredoxin_fold.
[Graphical view]
Gene3DG3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
PfamPF00578. AhpC-TSA. 1 hit.
[Graphical view]
PROSITEPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePRDX1_GECJA
AccessionPrimary (citable) accession number: Q6DV14
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: August 16, 2004
Last modified: November 25, 2008
This is version 32 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents