ID A6NIW5_HUMAN Unreviewed; 136 AA.
AC A6NIW5;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 2.
DT 27-MAR-2024, entry version 119.
DE RecName: Full=Peroxiredoxin-2 {ECO:0000256|ARBA:ARBA00040770};
DE EC=1.11.1.24 {ECO:0000256|ARBA:ARBA00013017};
DE AltName: Full=Thioredoxin-dependent peroxiredoxin 2 {ECO:0000256|ARBA:ARBA00042159};
GN Name=PRDX2 {ECO:0000313|EMBL:EAW84308.1,
GN ECO:0000313|Ensembl:ENSP00000334063.5};
GN ORFNames=hCG_172488 {ECO:0000313|EMBL:EAW84308.1};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000334063.5, ECO:0000313|Proteomes:UP000005640};
RN [1] {ECO:0000313|EMBL:EAW84308.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=11181995; DOI=10.1126/science.1058040;
RA Venter J.C., Adams M.D., Myers E.W., Li P.W., Mural R.J., Sutton G.G.,
RA Smith H.O., Yandell M., Evans C.A., Holt R.A., Gocayne J.D., Amanatides P.,
RA Ballew R.M., Huson D.H., Wortman J.R., Zhang Q., Kodira C.D., Zheng X.H.,
RA Chen L., Skupski M., Subramanian G., Thomas P.D., Zhang J.,
RA Gabor Miklos G.L., Nelson C., Broder S., Clark A.G., Nadeau J.,
RA McKusick V.A., Zinder N., Levine A.J., Roberts R.J., Simon M., Slayman C.,
RA Hunkapiller M., Bolanos R., Delcher A., Dew I., Fasulo D., Flanigan M.,
RA Florea L., Halpern A., Hannenhalli S., Kravitz S., Levy S., Mobarry C.,
RA Reinert K., Remington K., Abu-Threideh J., Beasley E., Biddick K.,
RA Bonazzi V., Brandon R., Cargill M., Chandramouliswaran I., Charlab R.,
RA Chaturvedi K., Deng Z., Di Francesco V., Dunn P., Eilbeck K.,
RA Evangelista C., Gabrielian A.E., Gan W., Ge W., Gong F., Gu Z., Guan P.,
RA Heiman T.J., Higgins M.E., Ji R.R., Ke Z., Ketchum K.A., Lai Z., Lei Y.,
RA Li Z., Li J., Liang Y., Lin X., Lu F., Merkulov G.V., Milshina N.,
RA Moore H.M., Naik A.K., Narayan V.A., Neelam B., Nusskern D., Rusch D.B.,
RA Salzberg S., Shao W., Shue B., Sun J., Wang Z., Wang A., Wang X., Wang J.,
RA Wei M., Wides R., Xiao C., Yan C., Yao A., Ye J., Zhan M., Zhang W.,
RA Zhang H., Zhao Q., Zheng L., Zhong F., Zhong W., Zhu S., Zhao S.,
RA Gilbert D., Baumhueter S., Spier G., Carter C., Cravchik A., Woodage T.,
RA Ali F., An H., Awe A., Baldwin D., Baden H., Barnstead M., Barrow I.,
RA Beeson K., Busam D., Carver A., Center A., Cheng M.L., Curry L.,
RA Danaher S., Davenport L., Desilets R., Dietz S., Dodson K., Doup L.,
RA Ferriera S., Garg N., Gluecksmann A., Hart B., Haynes J., Haynes C.,
RA Heiner C., Hladun S., Hostin D., Houck J., Howland T., Ibegwam C.,
RA Johnson J., Kalush F., Kline L., Koduru S., Love A., Mann F., May D.,
RA McCawley S., McIntosh T., McMullen I., Moy M., Moy L., Murphy B.,
RA Nelson K., Pfannkoch C., Pratts E., Puri V., Qureshi H., Reardon M.,
RA Rodriguez R., Rogers Y.H., Romblad D., Ruhfel B., Scott R., Sitter C.,
RA Smallwood M., Stewart E., Strong R., Suh E., Thomas R., Tint N.N., Tse S.,
RA Vech C., Wang G., Wetter J., Williams S., Williams M., Windsor S.,
RA Winn-Deen E., Wolfe K., Zaveri J., Zaveri K., Abril J.F., Guigo R.,
RA Campbell M.J., Sjolander K.V., Karlak B., Kejariwal A., Mi H., Lazareva B.,
RA Hatton T., Narechania A., Diemer K., Muruganujan A., Guo N., Sato S.,
RA Bafna V., Istrail S., Lippert R., Schwartz R., Walenz B., Yooseph S.,
RA Allen D., Basu A., Baxendale J., Blick L., Caminha M., Carnes-Stine J.,
RA Caulk P., Chiang Y.H., Coyne M., Dahlke C., Mays A., Dombroski M.,
RA Donnelly M., Ely D., Esparham S., Fosler C., Gire H., Glanowski S.,
RA Glasser K., Glodek A., Gorokhov M., Graham K., Gropman B., Harris M.,
RA Heil J., Henderson S., Hoover J., Jennings D., Jordan C., Jordan J.,
RA Kasha J., Kagan L., Kraft C., Levitsky A., Lewis M., Liu X., Lopez J.,
RA Ma D., Majoros W., McDaniel J., Murphy S., Newman M., Nguyen T., Nguyen N.,
RA Nodell M., Pan S., Peck J., Peterson M., Rowe W., Sanders R., Scott J.,
RA Simpson M., Smith T., Sprague A., Stockwell T., Turner R., Venter E.,
RA Wang M., Wen M., Wu D., Wu M., Xia A., Zandieh A., Zhu X.;
RT "The sequence of the human genome.";
RL Science 291:1304-1351(2001).
RN [2] {ECO:0000313|Ensembl:ENSP00000334063.5, ECO:0000313|Proteomes:UP000005640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [3] {ECO:0000313|EMBL:EAW84308.1}
RP NUCLEOTIDE SEQUENCE.
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0007829|PubMed:19413330}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [5] {ECO:0007829|PubMed:21269460}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Burckstummer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [6] {ECO:0007829|PubMed:22905912}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22905912; DOI=10.1021/pr300539b;
RA Rosenow A., Noben J.P., Jocken J., Kallendrusch S., Fischer-Posovszky P.,
RA Mariman E.C., Renes J.;
RT "Resveratrol-induced changes of the human adipocyte secretion profile.";
RL J. Proteome Res. 11:4733-4743(2012).
RN [7] {ECO:0007829|PubMed:24275569}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [8] {ECO:0007829|PubMed:25944712}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [9] {ECO:0000313|Ensembl:ENSP00000334063.5}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of
CC hydrogen peroxide and organic hydroperoxides to water and alcohols,
CC respectively. Plays a role in cell protection against oxidative stress
CC by detoxifying peroxides and as sensor of hydrogen peroxide-mediated
CC signaling events. Might participate in the signaling cascades of growth
CC factors and tumor necrosis factor-alpha by regulating the intracellular
CC concentrations of H(2)O(2). {ECO:0000256|ARBA:ARBA00037127}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-
CC disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA-
CC COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924,
CC ChEBI:CHEBI:50058; EC=1.11.1.24;
CC Evidence={ECO:0000256|ARBA:ARBA00000280};
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
CC {ECO:0000256|ARBA:ARBA00009796}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC018761; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471106; EAW84308.1; -; Genomic_DNA.
DR ProteomicsDB; 1293; -.
DR Antibodypedia; 3283; 643 antibodies from 45 providers.
DR Ensembl; ENST00000334482.9; ENSP00000334063.5; ENSG00000167815.12.
DR UCSC; uc060udo.1; human.
DR HGNC; HGNC:9353; PRDX2.
DR VEuPathDB; HostDB:ENSG00000167815; -.
DR GeneTree; ENSGT00940000155828; -.
DR HOGENOM; CLU_042529_21_3_1; -.
DR ChiTaRS; PRDX2; human.
DR Proteomes; UP000005640; Chromosome 19.
DR Bgee; ENSG00000167815; Expressed in lateral nuclear group of thalamus and 217 other cell types or tissues.
DR GO; GO:0016209; F:antioxidant activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd03015; PRX_Typ2cys; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR10681:SF161; PEROXIREDOXIN-2; 1.
DR PANTHER; PTHR10681; THIOREDOXIN PEROXIDASE; 1.
DR Pfam; PF00578; AhpC-TSA; 1.
DR PIRSF; PIRSF000239; AHPC; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Proteomics identification {ECO:0007829|EPD:A6NIW5,
KW ECO:0007829|MaxQB:A6NIW5};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000005640}.
FT DOMAIN 6..136
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 51
FT /note="Cysteine sulfenic acid (-SOH) intermediate; for
FT peroxidase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000239-1"
SQ SEQUENCE 136 AA; 15138 MW; 7936C66320E2EC5F CRC64;
MASGNARIGK PAPDFKATAV VDGAFKEVKL SDYKGKYVVL FFYPLDFTFV CPTEIIAFSN
RAEDFRKLGC EVLGVSVDSQ FTHLAWINTP RKEGGLGPLN IPLLADVTRR LSEDYGVLKT
DEGIAYSLSR WLEAWQ
//
