PRDX3_HUMAN
ID PRDX3_HUMAN Reviewed; 256 AA.
AC P30048; B2R7Z0; D3DRC9; E9PH29; P35690; Q0D2H1; Q13776; Q5T5V2; Q96HK4;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 3.
DT 03-AUG-2022, entry version 239.
DE RecName: Full=Thioredoxin-dependent peroxide reductase, mitochondrial;
DE EC=1.11.1.24 {ECO:0000269|PubMed:17707404, ECO:0000269|PubMed:19462976};
DE AltName: Full=Antioxidant protein 1;
DE Short=AOP-1;
DE AltName: Full=HBC189;
DE AltName: Full=Peroxiredoxin III;
DE Short=Prx-III;
DE AltName: Full=Peroxiredoxin-3;
DE AltName: Full=Protein MER5 homolog;
DE AltName: Full=Thioredoxin-dependent peroxiredoxin 3 {ECO:0000305};
DE Flags: Precursor;
GN Name=PRDX3; Synonyms=AOP1;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
RC TISSUE=Blood;
RX PubMed=7733872; DOI=10.1042/bj3070377;
RA Tsuji K., Copeland N.G., Jenkins N.A., Obinata M.;
RT "Mammalian antioxidant protein complements alkylhydroperoxide reductase
RT (ahpC) mutation in Escherichia coli.";
RL Biochem. J. 307:377-381(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-55; THR-218 AND
RP ILE-234.
RG NIEHS SNPs program;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow, Skeletal muscle, Testis, Urinary bladder, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP PROTEIN SEQUENCE OF 63-72 (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=1286669; DOI=10.1002/elps.11501301201;
RA Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F.,
RA Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R.,
RA Appel R.D., Hughes G.J.;
RT "Human liver protein map: a reference database established by
RT microsequencing and gel comparison.";
RL Electrophoresis 13:992-1001(1992).
RN [10]
RP PROTEIN SEQUENCE OF 74-93; 149-166 AND 171-214 (ISOFORM 1), AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [11]
RP OVEROXIDATION AT CYS-108.
RX PubMed=12059788; DOI=10.1042/bj20020525;
RA Wagner E., Luche S., Penna L., Chevallet M., van Dorsselaer A.,
RA Leize-Wagner E., Rabilloud T.;
RT "A method for detection of overoxidation of cysteines: peroxiredoxins are
RT oxidized in vivo at the active-site cysteine during oxidative stress.";
RL Biochem. J. 366:777-785(2002).
RN [12]
RP FUNCTION, AND INTERACTION WITH MAP3K13.
RX PubMed=12492477; DOI=10.1046/j.1432-1033.2003.03363.x;
RA Masaki M., Ikeda A., Shiraki E., Oka S., Kawasaki T.;
RT "Mixed lineage kinase LZK and antioxidant protein-1 activate NF-kappaB
RT synergistically.";
RL Eur. J. Biochem. 270:76-83(2003).
RN [13]
RP INTERACTION WITH RPS6KC1, AND SUBCELLULAR LOCATION.
RX PubMed=15750338;
RA Liu L., Yang C., Yuan J., Chen X., Xu J., Wei Y., Yang J., Lin G., Yu L.;
RT "RPK118, a PX domain-containing protein, interacts with peroxiredoxin-3
RT through pseudo-kinase domains.";
RL Mol. Cells 19:39-45(2005).
RN [14]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=17707404; DOI=10.1016/j.jmb.2007.07.018;
RA Cao Z., Bhella D., Lindsay J.G.;
RT "Reconstitution of the mitochondrial PrxIII antioxidant defence pathway:
RT general properties and factors affecting PrxIII activity and oligomeric
RT state.";
RL J. Mol. Biol. 372:1022-1033(2007).
RN [15]
RP CATALYTIC ACTIVITY.
RX PubMed=19462976; DOI=10.1021/bi900558g;
RA Cox A.G., Peskin A.V., Paton L.N., Winterbourn C.C., Hampton M.B.;
RT "Redox potential and peroxide reactivity of human peroxiredoxin 3.";
RL Biochemistry 48:6495-6501(2009).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-91, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [17]
RP INTERACTION WITH NEK6.
RX PubMed=20873783; DOI=10.1021/pr100562w;
RA Vaz Meirelles G., Ferreira Lanza D.C., da Silva J.C., Santana Bernachi J.,
RA Paes Leme A.F., Kobarg J.;
RT "Characterization of hNek6 interactome reveals an important role for its
RT short N-terminal domain and colocalization with proteins at the
RT centrosome.";
RL J. Proteome Res. 9:6298-6316(2010).
RN [18]
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., Buerckstuemmer 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 [19]
RP INTERACTION WITH LRRK2, PHOSPHORYLATION AT THR-146, AND MUTAGENESIS OF
RP THR-146.
RX PubMed=21850687; DOI=10.1002/humu.21582;
RA Angeles D.C., Gan B.H., Onstead L., Zhao Y., Lim K.L., Dachsel J.,
RA Melrose H., Farrer M., Wszolek Z.K., Dickson D.W., Tan E.K.;
RT "Mutations in LRRK2 increase phosphorylation of peroxiredoxin 3
RT exacerbating oxidative stress-induced neuronal death.";
RL Hum. Mutat. 32:1390-1397(2011).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
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 [21]
RP CLEAVAGE OF TRANSIT PEPTIDE [LARGE SCALE ANALYSIS] AFTER HIS-61, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
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 [22]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS), AND SUBUNIT.
RX PubMed=27238969; DOI=10.1016/j.str.2016.04.013;
RA Yewdall N.A., Venugopal H., Desfosses A., Abrishami V., Yosaatmadja Y.,
RA Hampton M.B., Gerrard J.A., Goldstone D.C., Mitra A.K., Radjainia M.;
RT "Structures of human peroxiredoxin 3 suggest self-chaperoning assembly that
RT maintains catalytic state.";
RL Structure 24:1120-1129(2016).
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 (PubMed:7733872, PubMed:17707404). Acts
CC synergistically with MAP3K13 to regulate the activation of NF-kappa-B
CC in the cytosol (PubMed:12492477). {ECO:0000269|PubMed:12492477,
CC ECO:0000269|PubMed:17707404, ECO:0000269|PubMed:7733872}.
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:0000269|PubMed:17707404, ECO:0000269|PubMed:19462976};
CC -!- SUBUNIT: Homodimer; disulfide-linked, upon oxidation. 6 homodimers
CC assemble to form a ring-like dodecamer (PubMed:17707404,
CC PubMed:27238969). Interacts with NEK6 (PubMed:20873783). Interacts with
CC LRRK2 (PubMed:21850687). Interacts with MAP3K13 (PubMed:12492477).
CC Interacts with RPS6KC1 (via PX domain) (PubMed:15750338).
CC {ECO:0000269|PubMed:12492477, ECO:0000269|PubMed:15750338,
CC ECO:0000269|PubMed:17707404, ECO:0000269|PubMed:20873783,
CC ECO:0000269|PubMed:21850687, ECO:0000269|PubMed:27238969}.
CC -!- INTERACTION:
CC P30048; Q9H8Y8: GORASP2; NbExp=6; IntAct=EBI-748336, EBI-739467;
CC P30048; Q5S007: LRRK2; NbExp=14; IntAct=EBI-748336, EBI-5323863;
CC P30048; P30048: PRDX3; NbExp=2; IntAct=EBI-748336, EBI-748336;
CC P30048; Q15935: ZNF77; NbExp=3; IntAct=EBI-748336, EBI-12840750;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P35705}.
CC Cytoplasm {ECO:0000305|PubMed:12492477}. Early endosome
CC {ECO:0000269|PubMed:15750338}. Note=Localizes to early endosomes in a
CC RPS6KC1-dependent manner. {ECO:0000269|PubMed:15750338}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P30048-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P30048-2; Sequence=VSP_054050;
CC -!- PTM: Phosphorylated by LRRK2; phosphorylation reduces perodixase
CC activity. {ECO:0000269|PubMed:21850687}.
CC -!- PTM: The enzyme can be inactivated by further oxidation of the cysteine
CC sulfenic acid (C(P)-SOH) to sulphinic acid (C(P)-SO2H) and sulphonic
CC acid (C(P)-SO3H) instead of its condensation to a disulfide bond.
CC {ECO:0000269|PubMed:12059788}.
CC -!- PTM: S-palmitoylated. {ECO:0000250|UniProtKB:P20108}.
CC -!- MISCELLANEOUS: The active site is a conserved redox-active cysteine
CC residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic
CC attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to
CC cysteine sulfenic acid (C(P)-SOH), which then reacts with another
CC cysteine residue, the resolving cysteine (C(R)), to form a disulfide
CC bridge. The disulfide is subsequently reduced by an appropriate
CC electron donor to complete the catalytic cycle. In this typical 2-Cys
CC peroxiredoxin, C(R) is provided by the other dimeric subunit to form an
CC intersubunit disulfide. The disulfide is subsequently reduced by
CC thioredoxin. {ECO:0000305|PubMed:17707404}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether transit peptide cleavage occurs after
CC His-61 or Ala-62. Peptides have been found for both N-termini.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/prdx3/";
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DR EMBL; D49396; BAA08389.1; -; mRNA.
DR EMBL; AK313169; BAG35987.1; -; mRNA.
DR EMBL; CR450344; CAG29340.1; -; mRNA.
DR EMBL; BT020007; AAV38810.1; -; mRNA.
DR EMBL; DQ298752; ABB84468.1; -; Genomic_DNA.
DR EMBL; AL355861; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471066; EAW49399.1; -; Genomic_DNA.
DR EMBL; BC002685; AAH02685.1; -; mRNA.
DR EMBL; BC007062; AAH07062.1; -; mRNA.
DR EMBL; BC008435; AAH08435.1; -; mRNA.
DR EMBL; BC009601; AAH09601.1; -; mRNA.
DR EMBL; BC021691; AAH21691.1; -; mRNA.
DR EMBL; BC022373; AAH22373.1; -; mRNA.
DR EMBL; BC059169; AAH59169.1; -; mRNA.
DR EMBL; BC111397; AAI11398.1; -; mRNA.
DR CCDS; CCDS7611.1; -. [P30048-1]
DR RefSeq; NP_001289201.1; NM_001302272.1.
DR RefSeq; NP_006784.1; NM_006793.4. [P30048-1]
DR PDB; 5JCG; X-ray; 2.80 A; A/B/C/D/E/F/G/H/I=62-256.
DR PDB; 5UCX; X-ray; 2.40 A; A/B/C/D/E/F/G/H/I=62-256.
DR PDBsum; 5JCG; -.
DR PDBsum; 5UCX; -.
DR AlphaFoldDB; P30048; -.
DR SMR; P30048; -.
DR BioGRID; 116136; 235.
DR DIP; DIP-33600N; -.
DR IntAct; P30048; 109.
DR MINT; P30048; -.
DR STRING; 9606.ENSP00000298510; -.
DR ChEMBL; CHEMBL4295742; -.
DR PeroxiBase; 4492; Hs2CysPrx03.
DR GlyGen; P30048; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P30048; -.
DR PhosphoSitePlus; P30048; -.
DR SwissPalm; P30048; -.
DR BioMuta; PRDX3; -.
DR DMDM; 2507171; -.
DR OGP; P30048; -.
DR SWISS-2DPAGE; P30048; -.
DR UCD-2DPAGE; P30048; -.
DR CPTAC; CPTAC-115; -.
DR CPTAC; CPTAC-116; -.
DR EPD; P30048; -.
DR jPOST; P30048; -.
DR MassIVE; P30048; -.
DR MaxQB; P30048; -.
DR PaxDb; P30048; -.
DR PeptideAtlas; P30048; -.
DR PRIDE; P30048; -.
DR ProteomicsDB; 20445; -.
DR ProteomicsDB; 54628; -. [P30048-1]
DR TopDownProteomics; P30048-1; -. [P30048-1]
DR Antibodypedia; 3274; 554 antibodies from 40 providers.
DR DNASU; 10935; -.
DR Ensembl; ENST00000298510.4; ENSP00000298510.2; ENSG00000165672.7. [P30048-1]
DR GeneID; 10935; -.
DR KEGG; hsa:10935; -.
DR MANE-Select; ENST00000298510.4; ENSP00000298510.2; NM_006793.5; NP_006784.1.
DR UCSC; uc001lec.5; human. [P30048-1]
DR CTD; 10935; -.
DR DisGeNET; 10935; -.
DR GeneCards; PRDX3; -.
DR HGNC; HGNC:9354; PRDX3.
DR HPA; ENSG00000165672; Low tissue specificity.
DR MIM; 604769; gene.
DR neXtProt; NX_P30048; -.
DR OpenTargets; ENSG00000165672; -.
DR PharmGKB; PA33724; -.
DR VEuPathDB; HostDB:ENSG00000165672; -.
DR eggNOG; KOG0852; Eukaryota.
DR GeneTree; ENSGT00940000153430; -.
DR HOGENOM; CLU_042529_21_0_1; -.
DR InParanoid; P30048; -.
DR OMA; WWPKDFT; -.
DR OrthoDB; 1326484at2759; -.
DR PhylomeDB; P30048; -.
DR TreeFam; TF105181; -.
DR PathwayCommons; P30048; -.
DR Reactome; R-HSA-3299685; Detoxification of Reactive Oxygen Species.
DR SignaLink; P30048; -.
DR SIGNOR; P30048; -.
DR BioGRID-ORCS; 10935; 88 hits in 1074 CRISPR screens.
DR ChiTaRS; PRDX3; human.
DR GeneWiki; PRDX3; -.
DR GenomeRNAi; 10935; -.
DR Pharos; P30048; Tbio.
DR PRO; PR:P30048; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; P30048; protein.
DR Bgee; ENSG00000165672; Expressed in adrenal tissue and 210 other tissues.
DR ExpressionAtlas; P30048; baseline and differential.
DR Genevisible; P30048; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0008785; F:alkyl hydroperoxide reductase activity; NAS:UniProtKB.
DR GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; IMP:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR GO; GO:0034599; P:cellular response to oxidative stress; IDA:ParkinsonsUK-UCL.
DR GO; GO:0034614; P:cellular response to reactive oxygen species; IMP:UniProtKB.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IDA:MGI.
DR GO; GO:0001893; P:maternal placenta development; IEA:Ensembl.
DR GO; GO:0007005; P:mitochondrion organization; IMP:UniProtKB.
DR GO; GO:0030099; P:myeloid cell differentiation; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:ParkinsonsUK-UCL.
DR GO; GO:0033673; P:negative regulation of kinase activity; IDA:UniProtKB.
DR GO; GO:0018171; P:peptidyl-cysteine oxidation; IDA:ParkinsonsUK-UCL.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
DR GO; GO:0051881; P:regulation of mitochondrial membrane potential; IMP:UniProtKB.
DR GO; GO:0042542; P:response to hydrogen peroxide; IDA:UniProtKB.
DR GO; GO:0032496; P:response to lipopolysaccharide; ISS:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; IMP:UniProtKB.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR019479; Peroxiredoxin_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF10417; 1-cysPrx_C; 1.
DR Pfam; PF00578; AhpC-TSA; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Antioxidant; Cytoplasm;
KW Direct protein sequencing; Disulfide bond; Endosome; Lipoprotein;
KW Mitochondrion; Oxidoreductase; Palmitate; Peroxidase; Phosphoprotein;
KW Redox-active center; Reference proteome; Transit peptide.
FT TRANSIT 1..61
FT /note="Mitochondrion"
FT /evidence="ECO:0007744|PubMed:25944712"
FT CHAIN 62..256
FT /note="Thioredoxin-dependent peroxide reductase,
FT mitochondrial"
FT /id="PRO_0000023782"
FT DOMAIN 63..221
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 108
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000250|UniProtKB:P35705"
FT MOD_RES 83
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P20108"
FT MOD_RES 91
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 91
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P20108"
FT MOD_RES 146
FT /note="Phosphothreonine"
FT /evidence="ECO:0000305|PubMed:21850687"
FT DISULFID 108
FT /note="Interchain (with C-229); in linked form"
FT /evidence="ECO:0000250|UniProtKB:P35705"
FT DISULFID 229
FT /note="Interchain (with C-108); in linked form"
FT /evidence="ECO:0000250|UniProtKB:P35705"
FT VAR_SEQ 51..68
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_054050"
FT VARIANT 55
FT /note="S -> R (in dbSNP:rs34698541)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_025052"
FT VARIANT 170
FT /note="R -> Q (in dbSNP:rs11554902)"
FT /id="VAR_059546"
FT VARIANT 218
FT /note="A -> T (in dbSNP:rs36064375)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_025053"
FT VARIANT 234
FT /note="T -> I (in dbSNP:rs35697338)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_025054"
FT MUTAGEN 146
FT /note="T->A: Impairs phosphorylation."
FT /evidence="ECO:0000269|PubMed:21850687"
FT CONFLICT 31
FT /note="R -> W (in Ref. 8; AAH08435)"
FT /evidence="ECO:0000305"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:5UCX"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:5UCX"
FT HELIX 87..90
FT /evidence="ECO:0007829|PDB:5UCX"
FT STRAND 93..99
FT /evidence="ECO:0007829|PDB:5UCX"
FT HELIX 107..117
FT /evidence="ECO:0007829|PDB:5UCX"
FT HELIX 119..123
FT /evidence="ECO:0007829|PDB:5UCX"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:5UCX"
FT STRAND 127..135
FT /evidence="ECO:0007829|PDB:5UCX"
FT HELIX 137..144
FT /evidence="ECO:0007829|PDB:5UCX"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:5UCX"
FT STRAND 157..162
FT /evidence="ECO:0007829|PDB:5UCX"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:5JCG"
FT HELIX 167..171
FT /evidence="ECO:0007829|PDB:5UCX"
FT TURN 177..180
FT /evidence="ECO:0007829|PDB:5UCX"
FT STRAND 184..189
FT /evidence="ECO:0007829|PDB:5UCX"
FT STRAND 193..201
FT /evidence="ECO:0007829|PDB:5UCX"
FT HELIX 209..225
FT /evidence="ECO:0007829|PDB:5UCX"
FT HELIX 244..254
FT /evidence="ECO:0007829|PDB:5UCX"
SQ SEQUENCE 256 AA; 27693 MW; 8BEB7F5E55BFE9BE CRC64;
MAAAVGRLLR ASVARHVSAI PWGISATAAL RPAACGRTSL TNLLCSGSSQ AKLFSTSSSC
HAPAVTQHAP YFKGTAVVNG EFKDLSLDDF KGKYLVLFFY PLDFTFVCPT EIVAFSDKAN
EFHDVNCEVV AVSVDSHFSH LAWINTPRKN GGLGHMNIAL LSDLTKQISR DYGVLLEGSG
LALRGLFIID PNGVIKHLSV NDLPVGRSVE ETLRLVKAFQ YVETHGEVCP ANWTPDSPTI
KPSPAASKEY FQKVNQ
