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SB0091 : Thioredoxin peroxidase 1

[ CaMP Format ]

* Basic Information

OrganismHomo sapiens (human)
Protein Namesperoxiredoxin-2 [Homo sapiens]; peroxiredoxin-2; thiol-specific antioxidant 1; thioredoxin peroxidase 1; torin; thioredoxin-dependent peroxide reductase 1; natural killer cell-enhancing factor B; epididymis secretory sperm binding protein Li 2a; Peroxiredoxin-2;; Natural killer cell-enhancing factor B; NKEF-B; PRP; Thiol-specific antioxidant protein; TSA; Thioredoxin peroxidase 1; Thioredoxin-dependent peroxide reductase 1
Gene NamesPRDX2; NKEFB, TDPX1; NKEFB; TDPX1; peroxiredoxin 2
Gene Locus19p13.2; chromosome 19
GO FunctionNot available
Entrez Protein Entrez Nucleotide Entrez Gene UniProt OMIM HGNC HPRD KEGG
NP_005800 NM_005809 7001 P32119 600538 HGNC:9353 02763 hsa:7001

* Information From OMIM

Function: To clarify the physiologic relevance of peroxiredoxins, Lee et al. (2003) generated a mouse model deficient in PRDX2, which is abundantly expressed in all types of cells. The Prdx2 -/- mice were healthy in appearance and fertile. However, they had splenomegaly caused by the congestion of red pulp with hemosiderin accumulation. Heinz bodies were detected in their peripheral blood, and morphologically abnormal cells were increased in the dense red blood cell (RBC) fractions, which contained markedly higher levels of ROS. The null mice had significantly decreased hematocrit levels, but increased reticulocyte counts and erythropoietin levels, indicative of a compensatory action to maintain hematologic homeostasis. A labeling experiment in null mice showed that a variety of RBC proteins were highly oxidized. The results suggested that Prdx -/- mice have hemolytic anemia and that peroxiredoxin II plays a major role in protecting RBCs from oxidative stress in mice.

* Structure Information

1. Primary Information

Length: 198 aa

Average Mass: 21.892 kDa

Monoisotopic Mass: 21.878 kDa

2. Domain Information

Annotated Domains: interpro / pfam / smart / prosite

Computationally Assigned Domains (Pfam+HMMER):

domain namebeginendscoree-value
Redoxin 1. 91493.00.0
C-terminal domain of 1-Cys peroxiredoxin 1. 1611951.00.0
--- cleavage 181 (inside C-terminal domain of 1-Cys peroxiredoxin 161..195) ---
--- cleavage 182 (inside C-terminal domain of 1-Cys peroxiredoxin 161..195) ---
--- cleavage 183 (inside C-terminal domain of 1-Cys peroxiredoxin 161..195) ---
--- cleavage 193 (inside C-terminal domain of 1-Cys peroxiredoxin 161..195) ---
--- cleavage 194 (inside C-terminal domain of 1-Cys peroxiredoxin 161..195) ---

3. Sequence Information

Fasta Sequence: SB0091.fasta

Amino Acid Sequence and Secondary Structures (PsiPred):

4. 3D Information

Known Structures in PDB: 1QMV (X-ray; 170 A; A/B/C/D/E/F/G/H/I/J=2-198)

* Cleavage Information

5 [sites] cleaved by Calpain 1

Source Reference: [PubMed ID: 9602152] Schroder E, Willis AC, Ponting CP, Porcine natural-killer-enhancing factor-B: oligomerisation and identification as a calpain substrate in vitro. Biochim Biophys Acta. 1998 Apr 2;1383(2):279-91.

Cleavage sites (±10aa)


Asp181 Thr

P10 P9 P8 P7 P6 P5 P4 P3 P2 P1
P1' P2' P3' P4' P5' P6' P7' P8' P9' P10'

Sequence conservation (by blast)


Thr182 Ile

P10 P9 P8 P7 P6 P5 P4 P3 P2 P1
P1' P2' P3' P4' P5' P6' P7' P8' P9' P10'

Sequence conservation (by blast)


Ile183 Lys

P10 P9 P8 P7 P6 P5 P4 P3 P2 P1
P1' P2' P3' P4' P5' P6' P7' P8' P9' P10'

Sequence conservation (by blast)


Tyr193 Phe

P10 P9 P8 P7 P6 P5 P4 P3 P2 P1
P1' P2' P3' P4' P5' P6' P7' P8' P9' P10'

Sequence conservation (by blast)


Phe194 Ser

P10 P9 P8 P7 P6 P5 P4 P3 P2 P1
P1' P2' P3' P4' P5' P6' P7' P8' P9' P10'

Sequence conservation (by blast)

* References

[PubMed ID: 24152995] Klebe S, Callahan T, Power JH, Peroxiredoxin I and II in human eyes: cellular distribution and association with pterygium and DNA damage. J Histochem Cytochem. 2014 Jan;62(1):85-96. doi: 10.1369/0022155413508409. Epub

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