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UniProtKB/Swiss-Prot entry P32119


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

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Entry information
Entry name PRDX2_HUMAN
Primary accession number P32119
Secondary accession numbers P31945 P32118 P35701 Q6FHG4 Q92763 Q9UC23
Integrated into Swiss-Prot on October 1, 1993
Sequence was last modified on January 23, 2007 (Sequence version 5)
Annotations were last modified on    November 25, 2008 (Entry version 106)
Name and origin of the protein
Protein name Peroxiredoxin-2
Synonyms EC 1.11.1.15
Thioredoxin peroxidase 1
Thioredoxin-dependent peroxide reductase 1
Thiol-specific antioxidant protein
TSA
PRP
Natural killer cell-enhancing factor B
NKEF-B
Gene name
Name: PRDX2
Synonyms: NKEFB, TDPX1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
DOI=10.1016/0378-1119(94)90558-4; PubMed=8144038 [NCBI, ExPASy, EBI, Israel, Japan]
Lim Y.-S., Cha M.-K., Kim H.-K., Kim I.-H.;
"The thiol-specific antioxidant protein from human brain: gene cloning and analysis of conserved cysteine regions.";
Gene 140:279-284(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1007/BF00188176; PubMed=8026862 [NCBI, ExPASy, EBI, Israel, Japan]
Shau H., Butterfield L.H., Chiu R., Kim A.;
"Cloning and sequence analysis of candidate human natural killer-enhancing factor genes.";
Immunogenetics 40:129-134(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.;
"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLU-153.
NIEHS SNPs program;
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Hypothalamus, and Lung;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 8-24, AND CATALYTIC ACTIVITY.
TISSUE=Erythrocyte;
DOI=10.1006/bbrc.1995.2856; PubMed=8554614 [NCBI, ExPASy, EBI, Israel, Japan]
Cha M.-K., Kim I.-H.;
"Thioredoxin-linked peroxidase from human red blood cell: evidence for the existence of thioredoxin and thioredoxin reductase in human red blood cell.";
Biochem. Biophys. Res. Commun. 217:900-907(1995).
[7]
PROTEIN SEQUENCE OF 17-26; 93-103 AND 120-129.
TISSUE=Erythrocyte;
PubMed=8313871 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Plasma and red blood cell protein maps: update 1993.";
Electrophoresis 14:1223-1231(1993).
[8]
PROTEIN SEQUENCE OF 17-26; 111-135 AND 140-157.
TISSUE=Colon carcinoma;
DOI=10.1002/elps.1150180344; PubMed=9150948 [NCBI, ExPASy, EBI, Israel, Japan]
Ji H., Reid G.E., Moritz R.L., Eddes J.S., Burgess A.W., Simpson R.J.;
"A two-dimensional gel database of human colon carcinoma proteins.";
Electrophoresis 18:605-613(1997).
[9]
PROTEIN SEQUENCE OF 17-25; 140-150 AND 163-185.
TISSUE=Keratinocyte;
DOI=10.1002/elps.11501301199; PubMed=1286667 [NCBI, ExPASy, EBI, Israel, Japan]
Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J.;
"Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes.";
Electrophoresis 13:960-969(1992).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 35-198.
Oberbaeumer I.;
Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
[11]
PROTEIN SEQUENCE OF 68-109 AND 140-150, AND MASS SPECTROMETRY.
TISSUE=Brain, and Cajal-Retzius cell;
Lubec G., Vishwanath V.;
Submitted (MAR-2007) to UniProtKB.
[12]
OVEROXIDATION AT CYS-51.
DOI=10.1074/jbc.M106585200; PubMed=11904290 [NCBI, ExPASy, EBI, Israel, Japan]
Rabilloud T., Heller M., Gasnier F., Luche S., Rey C., Aebersold R., Benahmed M., Louisot P., Lunardi J.;
"Proteomics analysis of cellular response to oxidative stress. Evidence for in vivo overoxidation of peroxiredoxins at their active site.";
J. Biol. Chem. 277:19396-19401(2002).
[13]
RETROREDUCTION OF CYS-51, AND MASS SPECTROMETRY.
DOI=10.1074/jbc.M305161200; PubMed=12853451 [NCBI, ExPASy, EBI, Israel, Japan]
Chevallet M., Wagner E., Luche S., van Dorsselaer A., Leize-Wagner E., Rabilloud T.;
"Regeneration of peroxiredoxins during recovery after oxidative stress: only some overoxidized peroxiredoxins can be reduced during recovery after oxidative stress.";
J. Biol. Chem. 278:37146-37153(2003).
[14]
INTERACTION WITH TIPIN.
DOI=10.1016/j.jmb.2006.10.097; PubMed=17141802 [NCBI, ExPASy, EBI, Israel, Japan]
Gotter A.L., Suppa C., Emanuel B.S.;
"Mammalian TIMELESS and Tipin are evolutionarily conserved replication fork-associated factors.";
J. Mol. Biol. 366:36-52(2007).
[15]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-198.
DOI=10.1016/S0969-2126(00)00147-7; PubMed=10873855 [NCBI, ExPASy, EBI, Israel, Japan]
Schroeder E., Littlechild J.A., Lebedev A.A., Errington N., Vagin A.A., Isupov M.N.;
"Crystal structure of decameric 2-Cys peroxiredoxin from human erythrocytes at 1.7 A resolution.";
Structure 8:605-615(2000).
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' + H2O + ROH.
  • SUBUNIT: 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.
  • MISCELLANEOUS: 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.
  • SIMILARITY: Belongs to the ahpC/TSA family.
  • SIMILARITY: Contains 1 thioredoxin domain.
  • WEB RESOURCE: Name=NIEHS SNPs; URL="http://egp.gs.washington.edu/data/prdx2/";.
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
Z22548; CAA80269.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L19185; AAA50465.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR450356; CAG29352.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR541789; CAG46588.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ231563; ABB02182.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC000452; AAH00452.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC003022; AAH03022.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC039428; AAH39428.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X82321; CAA57764.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR I68897; I68897.
RefSeq NP_005800.3; -.
UniGene Hs.432121
3D structure databases
PDB
1QMV; X-ray; 1.70 A; A/B/C/D/E/F/G/H/I/J=2-198.[ExPASy / RCSB / EBI]
PDBsum 1QMV; -.
SMR P32119; 2-197, 3-198.
ModBase P32119.
Protein family/group databases
PeroxiBase 4475; Hs2CysPrx02.
PTM databases
PhosphoSite P32119; -.
2D gel databases
SWISS-2DPAGE P32119; -.
Aarhus/Ghent-2DPAGE 6116; IEF.
Cornea-2DPAGE P32119; -.
DOSAC-COBS-2DPAGE P32119; -.
OGP P32119; -.
REPRODUCTION-2DPAGE IPI00027350; -.
Organism-specific databases
H-InvDB HIX0014805; -.
HGNC HGNC:9353; PRDX2.
GenAtlas PRDX2.
HPA CAB008713; -.
MIM 600538; gene. [NCBI / EBI]
PharmGKB PA33723; -.
GeneCards P32119.
Gene expression databases
ArrayExpress P32119; -.
CleanEx HS_PRDX2; -.
GermOnline ENSG00000167815; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (traceable author statement from UniProtKB).
GO:0008379; Molecular function: thioredoxin peroxidase activity (inferred from direct assay from UniProtKB).
GO:0006916; Biological process: anti-apoptosis (traceable author statement from UniProtKB).
GO:0045454; Biological process: cell redox homeostasis (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006979; Biological process: response to oxidative stress (inferred from mutant phenotype from UniProtKB).
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).
ProtoNet P32119.
Genome annotation databases
Ensembl ENSG00000167815; Homo sapiens. [Contig view]
GeneID 7001; -.
KEGG hsa:7001; -.
NMPDR fig|9606.3.peg.15783; -.
Phylogenomic databases
HOGENOM P32119; -.
HOVERGEN P32119; -.
Other
LinkHub P32119; -.
NextBio 27342; -.
SOURCE PRDX2; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Antioxidant; Cytoplasm; Direct protein sequencing; Oxidoreductase; Peroxidase; Polymorphism; Redox-active center.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   198  197     Peroxiredoxin-2. PRO_0000135080
DOMAIN   6   164  159     Thioredoxin. 
ACT_SITE   51    51        Cysteine sulfenic acid (-SOH) intermediate. 
MOD_RES   2     2        N-acetylalanine (By similarity). 
DISULFID   51    51        Interchain (with C-172); in linked form (By similarity). 
DISULFID   172   172        Interchain (with C-51); in linked form (By similarity). 
VARIANT   153   153  1     D -> E. VAR_025051 [3D]
CONFLICT   59    66        SNRAEDFR -> TTVKRTSA (in Ref. 1; CAA80269). 
CONFLICT   82    82        T -> N (in Ref. 2; AAA50465). 
CONFLICT   105   105        A -> G (in Ref. 2; AAA50465). 
CONFLICT   120   120        T -> N (in Ref. 1; CAA80269). 
CONFLICT   126   127        YR -> TT (in Ref. 7; AA sequence). 
CONFLICT   175   175        G -> A (in Ref. 1; CAA80269). 
CONFLICT   180   180        S -> R (in Ref. 1; CAA80269). 
TURN   4     5  2      
TURN   8     9  2      
STRAND   16    21  6      
TURN   22    23  2      
STRAND   24    29  6      
HELIX   30    33  4      
TURN   34    35  2      
STRAND   37    42  6      
TURN   46    47  2      
HELIX   50    60  11      
TURN   61    61  1      
HELIX   62    66  5      
TURN   67    69  3      
STRAND   70    76  7      
HELIX   80    87  8      
TURN   88    88  1      
HELIX   91    93  3      
TURN   94    94  1      
STRAND   103   105  3      
TURN   107   108  2      
HELIX   110   114  5      
TURN   115   116  2      
TURN   120   123  4      
STRAND   127   132  6      
TURN   134   135  2      
STRAND   137   144  8      
TURN   146   147  2      
HELIX   152   168  17      
TURN   174   175  2      
TURN   178   179  2      
HELIX   187   198  12      
Sequence information
Length: 198 AA [This is the length of the unprocessed precursor] Molecular weight: 21892 Da [This is the MW of the unprocessed precursor] CRC64: 1AC781D908B32B46 [This is a checksum on the sequence]
        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 

P32119 in FASTA format

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