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Thioredoxin-dependent peroxide reductase, mitochondrial (EC 1.11.1.15) (Antioxidant protein 1) (AOP-1) (HBC189) (Peroxiredoxin III) (Prx-III) (Peroxiredoxin-3) (Protein MER5 homolog)

 PRDX3_HUMAN             Reviewed;         256 AA.
P30048; B2R7Z0; D3DRC9; E9PH29; P35690; Q0D2H1; Q13776; Q5T5V2;
Q96HK4;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 3.
25-OCT-2017, entry version 207.
RecName: Full=Thioredoxin-dependent peroxide reductase, mitochondrial;
EC=1.11.1.15 {ECO:0000269|PubMed:17707404, ECO:0000269|PubMed:19462976};
AltName: Full=Antioxidant protein 1;
Short=AOP-1;
AltName: Full=HBC189;
AltName: Full=Peroxiredoxin III;
Short=Prx-III;
AltName: Full=Peroxiredoxin-3;
AltName: Full=Protein MER5 homolog;
Flags: Precursor;
Name=PRDX3; Synonyms=AOP1;
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), AND FUNCTION.
TISSUE=Blood;
PubMed=7733872; DOI=10.1042/bj3070377;
Tsuji K., Copeland N.G., Jenkins N.A., Obinata M.;
"Mammalian antioxidant protein complements alkylhydroperoxide
reductase (ahpC) mutation in Escherichia coli.";
Biochem. J. 307:377-381(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-55; THR-218 AND
ILE-234.
NIEHS SNPs program;
Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Bone marrow, Skeletal muscle, Testis, Urinary bladder, and
Uterus;
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 63-72 (ISOFORM 1).
TISSUE=Liver;
PubMed=1286669; DOI=10.1002/elps.11501301201;
Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F.,
Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R.,
Appel R.D., Hughes G.J.;
"Human liver protein map: a reference database established by
microsequencing and gel comparison.";
Electrophoresis 13:992-1001(1992).
[10]
PROTEIN SEQUENCE OF 74-93; 149-166 AND 171-214 (ISOFORM 1), 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.
[11]
OVEROXIDATION AT CYS-108.
PubMed=12059788; DOI=10.1042/BJ20020525;
Wagner E., Luche S., Penna L., Chevallet M., van Dorsselaer A.,
Leize-Wagner E., Rabilloud T.;
"A method for detection of overoxidation of cysteines: peroxiredoxins
are oxidized in vivo at the active-site cysteine during oxidative
stress.";
Biochem. J. 366:777-785(2002).
[12]
FUNCTION, AND INTERACTION WITH MAP3K13.
PubMed=12492477; DOI=10.1046/j.1432-1033.2003.03363.x;
Masaki M., Ikeda A., Shiraki E., Oka S., Kawasaki T.;
"Mixed lineage kinase LZK and antioxidant protein-1 activate NF-kappaB
synergistically.";
Eur. J. Biochem. 270:76-83(2003).
[13]
FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
PubMed=17707404; DOI=10.1016/j.jmb.2007.07.018;
Cao Z., Bhella D., Lindsay J.G.;
"Reconstitution of the mitochondrial PrxIII antioxidant defence
pathway: general properties and factors affecting PrxIII activity and
oligomeric state.";
J. Mol. Biol. 372:1022-1033(2007).
[14]
CATALYTIC ACTIVITY.
PubMed=19462976; DOI=10.1021/bi900558g;
Cox A.G., Peskin A.V., Paton L.N., Winterbourn C.C., Hampton M.B.;
"Redox potential and peroxide reactivity of human peroxiredoxin 3.";
Biochemistry 48:6495-6501(2009).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-91, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[16]
INTERACTION WITH NEK6.
PubMed=20873783; DOI=10.1021/pr100562w;
Vaz Meirelles G., Ferreira Lanza D.C., da Silva J.C.,
Santana Bernachi J., Paes Leme A.F., Kobarg J.;
"Characterization of hNek6 interactome reveals an important role for
its short N-terminal domain and colocalization with proteins at the
centrosome.";
J. Proteome Res. 9:6298-6316(2010).
[17]
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).
[18]
INTERACTION WITH LRRK2, PHOSPHORYLATION AT THR-146, AND MUTAGENESIS OF
THR-146.
PubMed=21850687; DOI=10.1002/humu.21582;
Angeles D.C., Gan B.H., Onstead L., Zhao Y., Lim K.L., Dachsel J.,
Melrose H., Farrer M., Wszolek Z.K., Dickson D.W., Tan E.K.;
"Mutations in LRRK2 increase phosphorylation of peroxiredoxin 3
exacerbating oxidative stress-induced neuronal death.";
Hum. Mutat. 32:1390-1397(2011).
[19]
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).
[20]
CLEAVAGE OF TRANSIT PEPTIDE [LARGE SCALE ANALYSIS] AFTER HIS-61, AND
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).
[21]
X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS), AND SUBUNIT.
PubMed=27238969; DOI=10.1016/j.str.2016.04.013;
Yewdall N.A., Venugopal H., Desfosses A., Abrishami V.,
Yosaatmadja Y., Hampton M.B., Gerrard J.A., Goldstone D.C.,
Mitra A.K., Radjainia M.;
"Structures of human peroxiredoxin 3 suggest self-chaperoning assembly
that maintains catalytic state.";
Structure 24:1120-1129(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 (PubMed:7733872,
PubMed:17707404). Acts synergistically with MAP3K13 to regulate
the activation of NF-kappa-B in the cytosol (PubMed:12492477).
{ECO:0000269|PubMed:12492477, ECO:0000269|PubMed:17707404,
ECO:0000269|PubMed:7733872}.
-!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH.
{ECO:0000269|PubMed:17707404, ECO:0000269|PubMed:19462976}.
-!- SUBUNIT: Homodimer; disulfide-linked, upon oxidation. 6 homodimers
assemble to form a ring-like dodecamer (PubMed:17707404,
PubMed:27238969). Interacts with NEK6 (PubMed:20873783). Interacts
with LRRK2 (PubMed:21850687). Interacts with MAP3K13
(PubMed:12492477). {ECO:0000269|PubMed:12492477,
ECO:0000269|PubMed:17707404, ECO:0000269|PubMed:20873783,
ECO:0000269|PubMed:21850687, ECO:0000269|PubMed:27238969}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-748336, EBI-748336;
Q9H8Y8:GORASP2; NbExp=3; IntAct=EBI-748336, EBI-739467;
Q5S007:LRRK2; NbExp=12; IntAct=EBI-748336, EBI-5323863;
-!- SUBCELLULAR LOCATION: Mitochondrion
{ECO:0000250|UniProtKB:P35705}. Cytoplasm
{ECO:0000305|PubMed:12492477}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P30048-1; Sequence=Displayed;
Name=2;
IsoId=P30048-2; Sequence=VSP_054050;
Note=No experimental confirmation available. Gene prediction
based on EST data.;
-!- PTM: Phosphorylated by LRRK2; phosphorylation reduces perodixase
activity. {ECO:0000269|PubMed:21850687}.
-!- PTM: The enzyme can be inactivated by further oxidation of the
cysteine sulfenic acid (C(P)-SOH) to sulphinic acid (C(P)-SO2H)
and sulphonic acid (C(P)-SO3H) instead of its condensation to a
disulfide bond. {ECO:0000269|PubMed:12059788}.
-!- 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:17707404}.
-!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1
subfamily. {ECO:0000305}.
-!- CAUTION: It is uncertain whether transit peptide cleavage occurs
after His-61 or Ala-62. Peptides have been found for both N-
termini.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/prdx3/";
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EMBL; D49396; BAA08389.1; -; mRNA.
EMBL; AK313169; BAG35987.1; -; mRNA.
EMBL; CR450344; CAG29340.1; -; mRNA.
EMBL; BT020007; AAV38810.1; -; mRNA.
EMBL; DQ298752; ABB84468.1; -; Genomic_DNA.
EMBL; AL355861; CAI15802.1; -; Genomic_DNA.
EMBL; CH471066; EAW49399.1; -; Genomic_DNA.
EMBL; BC002685; AAH02685.1; -; mRNA.
EMBL; BC007062; AAH07062.1; -; mRNA.
EMBL; BC008435; AAH08435.1; -; mRNA.
EMBL; BC009601; AAH09601.1; -; mRNA.
EMBL; BC021691; AAH21691.1; -; mRNA.
EMBL; BC022373; AAH22373.1; -; mRNA.
EMBL; BC059169; AAH59169.1; -; mRNA.
EMBL; BC111397; AAI11398.1; -; mRNA.
CCDS; CCDS7611.1; -. [P30048-1]
RefSeq; NP_001289201.1; NM_001302272.1.
RefSeq; NP_006784.1; NM_006793.4. [P30048-1]
UniGene; Hs.523302; -.
PDB; 5JCG; X-ray; 2.80 A; A/B/C/D/E/F/G/H/I=62-256.
PDBsum; 5JCG; -.
ProteinModelPortal; P30048; -.
SMR; P30048; -.
BioGrid; 116136; 67.
DIP; DIP-33600N; -.
IntAct; P30048; 58.
MINT; MINT-195453; -.
STRING; 9606.ENSP00000298510; -.
PeroxiBase; 4492; Hs2CysPrx03.
iPTMnet; P30048; -.
PhosphoSitePlus; P30048; -.
SwissPalm; P30048; -.
DMDM; 2507171; -.
OGP; P30048; -.
SWISS-2DPAGE; P30048; -.
UCD-2DPAGE; P30048; -.
EPD; P30048; -.
MaxQB; P30048; -.
PaxDb; P30048; -.
PeptideAtlas; P30048; -.
PRIDE; P30048; -.
TopDownProteomics; P30048-1; -. [P30048-1]
DNASU; 10935; -.
Ensembl; ENST00000298510; ENSP00000298510; ENSG00000165672. [P30048-1]
GeneID; 10935; -.
KEGG; hsa:10935; -.
UCSC; uc001lec.5; human. [P30048-1]
CTD; 10935; -.
DisGeNET; 10935; -.
EuPathDB; HostDB:ENSG00000165672.6; -.
GeneCards; PRDX3; -.
H-InvDB; HIX0035477; -.
HGNC; HGNC:9354; PRDX3.
HPA; CAB008656; -.
HPA; HPA041488; -.
MIM; 604769; gene.
neXtProt; NX_P30048; -.
OpenTargets; ENSG00000165672; -.
PharmGKB; PA33724; -.
eggNOG; KOG0852; Eukaryota.
eggNOG; COG0450; LUCA.
GeneTree; ENSGT00390000004653; -.
HOVERGEN; HBG000286; -.
InParanoid; P30048; -.
KO; K20011; -.
OMA; TAVHNGE; -.
OrthoDB; EOG091G0IE5; -.
PhylomeDB; P30048; -.
TreeFam; TF105181; -.
Reactome; R-HSA-3299685; Detoxification of Reactive Oxygen Species.
ChiTaRS; PRDX3; human.
GeneWiki; PRDX3; -.
GenomeRNAi; 10935; -.
PRO; PR:P30048; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000165672; -.
CleanEx; HS_PRDX3; -.
Genevisible; P30048; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:ParkinsonsUK-UCL.
GO; GO:0005769; C:early endosome; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
GO; GO:0043234; C:protein complex; IDA:UniProtKB.
GO; GO:0008785; F:alkyl hydroperoxide reductase activity; NAS:UniProtKB.
GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; IMP:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0008379; F:thioredoxin peroxidase activity; IDA:ParkinsonsUK-UCL.
GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
GO; GO:0034599; P:cellular response to oxidative stress; IDA:ParkinsonsUK-UCL.
GO; GO:0034614; P:cellular response to reactive oxygen species; IMP:UniProtKB.
GO; GO:0042744; P:hydrogen peroxide catabolic process; IDA:MGI.
GO; GO:0001893; P:maternal placenta development; IEA:Ensembl.
GO; GO:0007005; P:mitochondrion organization; IMP:UniProtKB.
GO; GO:0030099; P:myeloid cell differentiation; ISS:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:ParkinsonsUK-UCL.
GO; GO:0033673; P:negative regulation of kinase activity; IDA:UniProtKB.
GO; GO:0018171; P:peptidyl-cysteine oxidation; IDA:ParkinsonsUK-UCL.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:UniProtKB.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
GO; GO:0051881; P:regulation of mitochondrial membrane potential; IMP:UniProtKB.
GO; GO:0042542; P:response to hydrogen peroxide; IDA:UniProtKB.
GO; GO:0032496; P:response to lipopolysaccharide; ISS:UniProtKB.
GO; GO:0006979; P:response to oxidative stress; IMP:UniProtKB.
InterPro; IPR000866; AhpC/TSA.
InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
InterPro; IPR019479; Peroxiredoxin_C.
InterPro; IPR036249; Thioredoxin-like_sf.
InterPro; IPR013766; Thioredoxin_domain.
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; Mitochondrion; Oxidoreductase; Peroxidase;
Phosphoprotein; Polymorphism; Redox-active center; Reference proteome;
Transit peptide.
TRANSIT 1 61 Mitochondrion.
{ECO:0000244|PubMed:25944712}.
CHAIN 62 256 Thioredoxin-dependent peroxide reductase,
mitochondrial.
/FTId=PRO_0000023782.
DOMAIN 63 221 Thioredoxin. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
ACT_SITE 108 108 Cysteine sulfenic acid (-SOH)
intermediate.
{ECO:0000250|UniProtKB:P35705}.
MOD_RES 83 83 N6-succinyllysine.
{ECO:0000250|UniProtKB:P20108}.
MOD_RES 91 91 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 91 91 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P20108}.
MOD_RES 146 146 Phosphothreonine.
{ECO:0000305|PubMed:21850687}.
DISULFID 108 108 Interchain (with C-229); in linked form.
{ECO:0000250|UniProtKB:P35705}.
DISULFID 229 229 Interchain (with C-108); in linked form.
{ECO:0000250|UniProtKB:P35705}.
VAR_SEQ 51 68 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_054050.
VARIANT 55 55 S -> R (in dbSNP:rs34698541).
{ECO:0000269|Ref.5}.
/FTId=VAR_025052.
VARIANT 170 170 R -> Q (in dbSNP:rs11554902).
/FTId=VAR_059546.
VARIANT 218 218 A -> T (in dbSNP:rs36064375).
{ECO:0000269|Ref.5}.
/FTId=VAR_025053.
VARIANT 234 234 T -> I (in dbSNP:rs35697338).
{ECO:0000269|Ref.5}.
/FTId=VAR_025054.
MUTAGEN 146 146 T->A: Impairs phosphorylation.
{ECO:0000269|PubMed:21850687}.
CONFLICT 31 31 R -> W (in Ref. 8; AAH08435).
{ECO:0000305}.
STRAND 73 78 {ECO:0000244|PDB:5JCG}.
STRAND 81 86 {ECO:0000244|PDB:5JCG}.
HELIX 87 90 {ECO:0000244|PDB:5JCG}.
STRAND 93 99 {ECO:0000244|PDB:5JCG}.
HELIX 107 117 {ECO:0000244|PDB:5JCG}.
HELIX 119 123 {ECO:0000244|PDB:5JCG}.
TURN 124 126 {ECO:0000244|PDB:5JCG}.
STRAND 127 135 {ECO:0000244|PDB:5JCG}.
HELIX 137 144 {ECO:0000244|PDB:5JCG}.
HELIX 148 150 {ECO:0000244|PDB:5JCG}.
STRAND 157 162 {ECO:0000244|PDB:5JCG}.
STRAND 164 166 {ECO:0000244|PDB:5JCG}.
HELIX 167 171 {ECO:0000244|PDB:5JCG}.
TURN 177 180 {ECO:0000244|PDB:5JCG}.
STRAND 184 189 {ECO:0000244|PDB:5JCG}.
STRAND 193 201 {ECO:0000244|PDB:5JCG}.
HELIX 209 225 {ECO:0000244|PDB:5JCG}.
TURN 244 247 {ECO:0000244|PDB:5JCG}.
HELIX 248 253 {ECO:0000244|PDB:5JCG}.
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


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