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Peroxiredoxin-2 (EC 1.11.1.15) (Natural killer cell-enhancing factor B) (NKEF-B) (PRP) (Thiol-specific antioxidant protein) (TSA) (Thioredoxin peroxidase 1) (Thioredoxin-dependent peroxide reductase 1)

 PRDX2_HUMAN             Reviewed;         198 AA.
P32119; A8K0C0; P31945; P32118; P35701; Q6FHG4; Q92763; Q9UC23;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 5.
30-AUG-2017, entry version 201.
RecName: Full=Peroxiredoxin-2;
EC=1.11.1.15 {ECO:0000269|PubMed:8554614, ECO:0000269|PubMed:9497357};
AltName: Full=Natural killer cell-enhancing factor B;
Short=NKEF-B;
AltName: Full=PRP;
AltName: Full=Thiol-specific antioxidant protein;
Short=TSA;
AltName: Full=Thioredoxin peroxidase 1;
AltName: Full=Thioredoxin-dependent peroxide reductase 1;
Name=PRDX2; Synonyms=NKEFB, TDPX1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=8144038; DOI=10.1016/0378-1119(94)90558-4;
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] (ISOFORM 1).
PubMed=8026862; DOI=10.1007/BF00188176;
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] (ISOFORM 2).
TISSUE=Cerebellum;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLU-153.
NIEHS SNPs program;
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Hypothalamus, and Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[9]
PROTEIN SEQUENCE OF 8-26; 67-135 AND 140-150, AND IDENTIFICATION BY
MASS SPECTROMETRY.
TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[10]
PROTEIN SEQUENCE OF 8-24, AND CATALYTIC ACTIVITY.
TISSUE=Erythrocyte;
PubMed=8554614; DOI=10.1006/bbrc.1995.2856;
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).
[11]
PROTEIN SEQUENCE OF 17-26; 93-103 AND 120-129.
TISSUE=Erythrocyte;
PubMed=8313871; DOI=10.1002/elps.11501401183;
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).
[12]
PROTEIN SEQUENCE OF 17-26; 111-135 AND 140-157.
TISSUE=Colon carcinoma;
PubMed=9150948; DOI=10.1002/elps.1150180344;
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).
[13]
PROTEIN SEQUENCE OF 17-25; 140-150 AND 163-185.
TISSUE=Keratinocyte;
PubMed=1286667; DOI=10.1002/elps.11501301199;
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).
[14]
NUCLEOTIDE SEQUENCE [MRNA] OF 35-198 (ISOFORM 1).
Oberbaeumer I.;
Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
[15]
FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
PubMed=9497357; DOI=10.1074/jbc.273.11.6297;
Kang S.W., Chae H.Z., Seo M.S., Kim K., Baines I.C., Rhee S.G.;
"Mammalian peroxiredoxin isoforms can reduce hydrogen peroxide
generated in response to growth factors and tumor necrosis factor-
alpha.";
J. Biol. Chem. 273:6297-6302(1998).
[16]
OVEROXIDATION AT CYS-51.
PubMed=11904290; DOI=10.1074/jbc.M106585200;
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).
[17]
RETROREDUCTION OF CYS-51, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=12853451; DOI=10.1074/jbc.M305161200;
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).
[18]
INTERACTION WITH TIPIN.
PubMed=17141802; DOI=10.1016/j.jmb.2006.10.097;
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).
[19]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22905912; DOI=10.1021/pr300539b;
Rosenow A., Noben J.P., Jocken J., Kallendrusch S.,
Fischer-Posovszky P., Mariman E.C., Renes J.;
"Resveratrol-induced changes of the human adipocyte secretion
profile.";
J. Proteome Res. 11:4733-4743(2012).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112 AND THR-182, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[24]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), AND SUBUNIT.
PubMed=10873855; DOI=10.1016/S0969-2126(00)00147-7;
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).
[25]
X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 46-198, AND DISULFIDE BONDS.
PubMed=27892488; DOI=10.1038/srep37610;
Kamariah N., Sek M.F., Eisenhaber B., Eisenhaber F., Grueber G.;
"Transition steps in peroxide reduction and a molecular switch for
peroxide robustness of prokaryotic peroxiredoxins.";
Sci. Rep. 6:37610-37610(2016).
-!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction
of hydrogen peroxide and organic hydroperoxides to water and
alcohols, respectively. Plays a role in cell protection against
oxidative stress by detoxifying peroxides and as sensor of
hydrogen peroxide-mediated signaling events. Might participate in
the signaling cascades of growth factors and tumor necrosis
factor-alpha by regulating the intracellular concentrations of
H(2)O(2). {ECO:0000269|PubMed:9497357}.
-!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH.
{ECO:0000269|PubMed:8554614, ECO:0000269|PubMed:9497357}.
-!- SUBUNIT: Homodimer; disulfide-linked, upon oxidation
(PubMed:27892488). 5 homodimers assemble to form a ring-like
decamer (PubMed:27892488). Interacts with TIPIN (PubMed:17141802).
{ECO:0000269|PubMed:17141802, ECO:0000269|PubMed:27892488}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9497357}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P32119-1; Sequence=Displayed;
Name=2;
IsoId=P32119-2; Sequence=VSP_042924;
Note=No experimental confirmation available. Due to intron
retention. May be produced at very low levels due to a premature
stop codon in the mRNA, leading to nonsense-mediated mRNA
decay.;
-!- PTM: The enzyme can be inactivated by further oxidation of the
cysteine sulfenic acid (C(P)-SOH) to sulphinic acid (C(P)-SO2H)
instead of its condensation to a disulfide bond. It can be
reactivated by forming a transient disulfide bond with
sulfiredoxin SRXN1, which reduces the cysteine sulfinic acid in an
ATP- and Mg-dependent manner. {ECO:0000250|UniProtKB:Q06830,
ECO:0000269|PubMed:11904290, ECO:0000269|PubMed:12853451}.
-!- MISCELLANEOUS: The active site is a conserved redox-active
cysteine residue, the peroxidatic cysteine (C(P)), which makes the
nucleophilic attack on the peroxide substrate. The peroxide
oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which
then reacts with another cysteine residue, the resolving cysteine
(C(R)), to form a disulfide bridge. The disulfide is subsequently
reduced by an appropriate electron donor to complete the catalytic
cycle. In this typical 2-Cys peroxiredoxin, C(R) is provided by
the other dimeric subunit to form an intersubunit disulfide. The
disulfide is subsequently reduced by thioredoxin.
{ECO:0000305|PubMed:27892488}.
-!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1
subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/prdx2/";
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EMBL; Z22548; CAA80269.1; -; mRNA.
EMBL; L19185; AAA50465.1; -; mRNA.
EMBL; CR450356; CAG29352.1; -; mRNA.
EMBL; CR541789; CAG46588.1; -; mRNA.
EMBL; AK289485; BAF82174.1; -; mRNA.
EMBL; DQ231563; ABB02182.1; -; Genomic_DNA.
EMBL; AC018761; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471106; EAW84311.1; -; Genomic_DNA.
EMBL; BC000452; AAH00452.1; -; mRNA.
EMBL; BC003022; AAH03022.1; -; mRNA.
EMBL; BC039428; AAH39428.1; -; mRNA.
EMBL; X82321; CAA57764.1; -; mRNA.
CCDS; CCDS12281.1; -. [P32119-1]
PIR; I68897; I68897.
RefSeq; NP_005800.3; NM_005809.5. [P32119-1]
UniGene; Hs.432121; -.
PDB; 1QMV; X-ray; 1.70 A; A/B/C/D/E/F/G/H/I/J=2-198.
PDB; 5B8A; X-ray; 2.70 A; A/B/C/D/E/F/G/H/I/J=46-198.
PDB; 5B8B; X-ray; 3.10 A; A/B/C/D/E/F/G/H/I/J=46-163, A/B/C/D/E/F/G/H/I/J=80-198.
PDBsum; 1QMV; -.
PDBsum; 5B8A; -.
PDBsum; 5B8B; -.
ProteinModelPortal; P32119; -.
SMR; P32119; -.
BioGrid; 112860; 117.
DIP; DIP-39882N; -.
IntAct; P32119; 44.
MINT; MINT-3012817; -.
STRING; 9606.ENSP00000301522; -.
DrugBank; DB02153; 3-Sulfinoalanine.
DrugBank; DB04048; N-Carbamoyl-Alanine.
PeroxiBase; 4475; Hs2CysPrx02.
iPTMnet; P32119; -.
PhosphoSitePlus; P32119; -.
SwissPalm; P32119; -.
DMDM; 2507169; -.
DOSAC-COBS-2DPAGE; P32119; -.
OGP; P32119; -.
REPRODUCTION-2DPAGE; IPI00027350; -.
SWISS-2DPAGE; P32119; -.
UCD-2DPAGE; P32119; -.
EPD; P32119; -.
PaxDb; P32119; -.
PeptideAtlas; P32119; -.
PRIDE; P32119; -.
TopDownProteomics; P32119-1; -. [P32119-1]
DNASU; 7001; -.
Ensembl; ENST00000301522; ENSP00000301522; ENSG00000167815. [P32119-1]
GeneID; 7001; -.
KEGG; hsa:7001; -.
CTD; 7001; -.
DisGeNET; 7001; -.
GeneCards; PRDX2; -.
HGNC; HGNC:9353; PRDX2.
HPA; CAB008713; -.
MIM; 600538; gene.
neXtProt; NX_P32119; -.
OpenTargets; ENSG00000167815; -.
PharmGKB; PA33723; -.
eggNOG; KOG0852; Eukaryota.
eggNOG; COG0450; LUCA.
GeneTree; ENSGT00390000004653; -.
HOGENOM; HOG000022343; -.
HOVERGEN; HBG000286; -.
InParanoid; P32119; -.
KO; K03386; -.
OMA; FKEVKLC; -.
OrthoDB; EOG091G0IE5; -.
PhylomeDB; P32119; -.
TreeFam; TF105181; -.
BRENDA; 1.11.1.15; 2681.
Reactome; R-HSA-3299685; Detoxification of Reactive Oxygen Species.
Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes.
Reactome; R-HSA-8862803; Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's disease models.
ChiTaRS; PRDX2; human.
EvolutionaryTrace; P32119; -.
GeneWiki; Peroxiredoxin_2; -.
GenomeRNAi; 7001; -.
PRO; PR:P32119; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000167815; -.
CleanEx; HS_PRDX2; -.
ExpressionAtlas; P32119; baseline and differential.
Genevisible; P32119; HS.
GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0016209; F:antioxidant activity; IDA:UniProtKB.
GO; GO:0008379; F:thioredoxin peroxidase activity; IDA:UniProtKB.
GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
GO; GO:0034599; P:cellular response to oxidative stress; IDA:BHF-UCL.
GO; GO:0042744; P:hydrogen peroxide catabolic process; TAS:BHF-UCL.
GO; GO:0043066; P:negative regulation of apoptotic process; TAS:UniProtKB.
GO; GO:0042981; P:regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0019430; P:removal of superoxide radicals; IDA:BHF-UCL.
GO; GO:0006979; P:response to oxidative stress; IMP:UniProtKB.
InterPro; IPR000866; AhpC/TSA.
InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
InterPro; IPR019479; Peroxiredoxin_C.
InterPro; IPR033046; PRDX2.
InterPro; IPR012336; Thioredoxin-like_fold.
InterPro; IPR013766; Thioredoxin_domain.
PANTHER; PTHR10681:SF136; PTHR10681:SF136; 1.
Pfam; PF10417; 1-cysPrx_C; 1.
Pfam; PF00578; AhpC-TSA; 1.
PIRSF; PIRSF000239; AHPC; 1.
SUPFAM; SSF52833; SSF52833; 1.
PROSITE; PS51352; THIOREDOXIN_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Antioxidant;
Complete proteome; Cytoplasm; Direct protein sequencing;
Disulfide bond; Oxidoreductase; Peroxidase; Phosphoprotein;
Polymorphism; Redox-active center; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330}.
CHAIN 2 198 Peroxiredoxin-2.
/FTId=PRO_0000135080.
DOMAIN 6 164 Thioredoxin. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
ACT_SITE 51 51 Cysteine sulfenic acid (-SOH)
intermediate.
{ECO:0000305|PubMed:11904290}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330}.
MOD_RES 112 112 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 182 182 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
DISULFID 51 51 Interchain (with C-172); in linked form.
{ECO:0000244|PDB:5B8A,
ECO:0000269|PubMed:27892488}.
DISULFID 172 172 Interchain (with C-51); in linked form.
{ECO:0000244|PDB:5B8A,
ECO:0000269|PubMed:27892488}.
VAR_SEQ 87 198 INTPRKEGGLGPLNIPLLADVTRRLSEDYGVLKTDEGIAYR
GLFIIDGKGVLRQITVNDLPVGRSVDEALRLVQAFQYTDEH
GEVCPAGWKPGSDTIKPNVDDSKEYFSKHN -> YEQGPKR
EVAAKLTPSGPSSVASWPLLNLWNLRFPIVKIMETLPPKSL
RMMTVISI (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_042924.
VARIANT 153 153 D -> E (in dbSNP:rs34012472).
{ECO:0000269|Ref.5}.
/FTId=VAR_025051.
CONFLICT 59 66 SNRAEDFR -> TTVKRTSA (in Ref. 1;
CAA80269). {ECO:0000305}.
CONFLICT 82 82 T -> N (in Ref. 2; AAA50465).
{ECO:0000305}.
CONFLICT 105 105 A -> G (in Ref. 2; AAA50465).
{ECO:0000305}.
CONFLICT 120 120 T -> N (in Ref. 1; CAA80269).
{ECO:0000305}.
CONFLICT 126 127 YR -> TT (in Ref. 11; AA sequence).
{ECO:0000305}.
CONFLICT 175 175 G -> A (in Ref. 1; CAA80269).
{ECO:0000305}.
CONFLICT 180 180 S -> R (in Ref. 1; CAA80269).
{ECO:0000305}.
STRAND 16 21 {ECO:0000244|PDB:1QMV}.
STRAND 24 29 {ECO:0000244|PDB:1QMV}.
HELIX 30 33 {ECO:0000244|PDB:1QMV}.
STRAND 36 42 {ECO:0000244|PDB:1QMV}.
HELIX 50 60 {ECO:0000244|PDB:1QMV}.
HELIX 62 66 {ECO:0000244|PDB:1QMV}.
TURN 67 69 {ECO:0000244|PDB:1QMV}.
STRAND 70 78 {ECO:0000244|PDB:1QMV}.
HELIX 80 87 {ECO:0000244|PDB:1QMV}.
HELIX 91 93 {ECO:0000244|PDB:1QMV}.
STRAND 103 105 {ECO:0000244|PDB:1QMV}.
HELIX 110 114 {ECO:0000244|PDB:1QMV}.
TURN 120 122 {ECO:0000244|PDB:1QMV}.
STRAND 127 132 {ECO:0000244|PDB:1QMV}.
STRAND 136 144 {ECO:0000244|PDB:1QMV}.
HELIX 152 168 {ECO:0000244|PDB:1QMV}.
HELIX 187 197 {ECO:0000244|PDB:1QMV}.
SEQUENCE 198 AA; 21892 MW; 1AC781D908B32B46 CRC64;
MASGNARIGK PAPDFKATAV VDGAFKEVKL SDYKGKYVVL FFYPLDFTFV CPTEIIAFSN
RAEDFRKLGC EVLGVSVDSQ FTHLAWINTP RKEGGLGPLN IPLLADVTRR LSEDYGVLKT
DEGIAYRGLF IIDGKGVLRQ ITVNDLPVGR SVDEALRLVQ AFQYTDEHGE VCPAGWKPGS
DTIKPNVDDS KEYFSKHN


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