Peroxiredoxin-2 - Homo sapiens (Human)

Names and origin

Protein names

Recommended name:
    Peroxiredoxin-2
    EC=1.11.1.15
Alternative name(s):
    Thioredoxin peroxidase 1
    Thioredoxin-dependent peroxide reductase 1
    Thiol-specific antioxidant protein
      Short name(s)=TSA
    PRP
    Natural killer cell-enhancing factor B
      Short name(s)=NKEF-B

Gene names

Name:	PRDX2
Synonyms:	NKEFB, TDPX1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	198 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (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' + H(2)O + ROH.
Subunit structure	Homodimer; disulfide-linked, upon oxidation. May be found as a toroid-shaped decamer composed of 5 dimers, depending on pH and calcium concentration. Interacts with TIPIN.
Subcellular location	Cytoplasm.
Miscellaneous	The active site is the redox-active Cys-51 oxidized to Cys-SOH. Cys-SOH rapidly reacts with Cys-172-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. Inactivated upon oxidative stress by overoxidation of Cys-51 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.
Sequence similarities	Belongs to the ahpC/TSA family. Contains 1 thioredoxin domain.

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Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Domain	Redox-active center
Molecular function	Antioxidant Oxidoreductase Peroxidase
PTM	Acetylation
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	anti-apoptosis Traceable author statement. Source: UniProtKB response to oxidative stress Ref.12 Inferred from mutant phenotype. Source: UniProtKB
Cellular component	cytoplasm Traceable author statement. Source: UniProtKB
Molecular function	thioredoxin peroxidase activity Ref.1 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Molecule processing

Initiator methionine

1

Removed By similarity

Chain

2 – 198

197

Peroxiredoxin-2

Regions

Domain

6 – 164

159

Thioredoxin

Sites

Active site

51

1

Cysteine sulfenic acid (-SOH) intermediate

Amino acid modifications

Modified residue

2

1

N-acetylalanine By similarity

Disulfide bond

51

Interchain (with C-172); in linked form By similarity

Disulfide bond

172

Interchain (with C-51); in linked form By similarity

Natural variations

Natural variant

153

1

D → E

Experimental info

Sequence conflict

59 – 66

8

SNRAEDFR → TTVKRTSA in CAA80269. Ref.1

Sequence conflict

82

1

T → N in AAA50465. Ref.2

Sequence conflict

105

1

A → G in AAA50465. Ref.2

Sequence conflict

120

1

T → N in CAA80269. Ref.1

Sequence conflict

126 – 127

2

YR → TT AA sequence Ref.7

Sequence conflict

175

1

G → A in CAA80269. Ref.1

Sequence conflict

180

1

S → R in CAA80269. Ref.1

Secondary structure

1

.

198

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P32119-1 [UniParc].

Last modified January 23, 2007. Version 5.
Checksum: 1AC781D908B32B46
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FASTA

198

21,892

        10         20         30         40         50         60 
MASGNARIGK PAPDFKATAV VDGAFKEVKL SDYKGKYVVL FFYPLDFTFV CPTEIIAFSN 

        70         80         90        100        110        120 
RAEDFRKLGC EVLGVSVDSQ FTHLAWINTP RKEGGLGPLN IPLLADVTRR LSEDYGVLKT 

       130        140        150        160        170        180 
DEGIAYRGLF IIDGKGVLRQ ITVNDLPVGR SVDEALRLVQ AFQYTDEHGE VCPAGWKPGS 

       190 
DTIKPNVDDS KEYFSKHN

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References

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[1]	"The thiol-specific antioxidant protein from human brain: gene cloning and analysis of conserved cysteine regions." Lim Y.-S., Cha M.-K., Kim H.-K., Kim I.-H. Gene 140:279-284(1994) [PubMed: 8144038] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[2]	"Cloning and sequence analysis of candidate human natural killer-enhancing factor genes." Shau H., Butterfield L.H., Chiu R., Kim A. Immunogenetics 40:129-134(1994) [PubMed: 8026862] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	NIEHS SNPs program Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLU-153.
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Hypothalamus and Lung.
[6]	"Thioredoxin-linked peroxidase from human red blood cell: evidence for the existence of thioredoxin and thioredoxin reductase in human red blood cell." Cha M.-K., Kim I.-H. Biochem. Biophys. Res. Commun. 217:900-907(1995) [PubMed: 8554614] [Abstract] Cited for: PROTEIN SEQUENCE OF 8-24, CATALYTIC ACTIVITY. Tissue: Erythrocyte.
[7]	"Plasma and red blood cell protein maps: update 1993." Golaz O., Hughes G.J., Frutiger S., Paquet N., Bairoch A., Pasquali C., Sanchez J.-C., Tissot J.-D., Appel R.D., Walzer C., Balant L., Hochstrasser D.F. Electrophoresis 14:1223-1231(1993) [PubMed: 8313871] [Abstract] Cited for: PROTEIN SEQUENCE OF 17-26; 93-103 AND 120-129. Tissue: Erythrocyte.
[8]	"A two-dimensional gel database of human colon carcinoma proteins." Ji H., Reid G.E., Moritz R.L., Eddes J.S., Burgess A.W., Simpson R.J. Electrophoresis 18:605-613(1997) [PubMed: 9150948] [Abstract] Cited for: PROTEIN SEQUENCE OF 17-26; 111-135 AND 140-157. Tissue: Colon carcinoma.
[9]	"Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes." Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J. Electrophoresis 13:960-969(1992) [PubMed: 1286667] [Abstract] Cited for: PROTEIN SEQUENCE OF 17-25; 140-150 AND 163-185. Tissue: Keratinocyte.
[10]	Oberbaeumer I. Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 35-198.
[11]	Lubec G., Vishwanath V. Submitted (MAR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 68-109 AND 140-150, MASS SPECTROMETRY. Tissue: Brain and Cajal-Retzius cell.
[12]	"Proteomics analysis of cellular response to oxidative stress. Evidence for in vivo overoxidation of peroxiredoxins at their active site." Rabilloud T., Heller M., Gasnier F., Luche S., Rey C., Aebersold R., Benahmed M., Louisot P., Lunardi J. J. Biol. Chem. 277:19396-19401(2002) [PubMed: 11904290] [Abstract] Cited for: OVEROXIDATION AT CYS-51.
[13]	"Regeneration of peroxiredoxins during recovery after oxidative stress: only some overoxidized peroxiredoxins can be reduced during recovery after oxidative stress." Chevallet M., Wagner E., Luche S., van Dorsselaer A., Leize-Wagner E., Rabilloud T. J. Biol. Chem. 278:37146-37153(2003) [PubMed: 12853451] [Abstract] Cited for: RETROREDUCTION OF CYS-51, MASS SPECTROMETRY.
[14]	"Mammalian TIMELESS and Tipin are evolutionarily conserved replication fork-associated factors." Gotter A.L., Suppa C., Emanuel B.S. J. Mol. Biol. 366:36-52(2007) [PubMed: 17141802] [Abstract] Cited for: INTERACTION WITH TIPIN.
[15]	"Crystal structure of decameric 2-Cys peroxiredoxin from human erythrocytes at 1.7 A resolution." Schroeder E., Littlechild J.A., Lebedev A.A., Errington N., Vagin A.A., Isupov M.N. Structure 8:605-615(2000) [PubMed: 10873855] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-198.