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Thioredoxin-dependent peroxide reductase, mitochondrial (EC 1.11.1.15) (Antioxidant protein 1) (AOP-1) (Peroxiredoxin-3) (Protein SP-22)

 PRDX3_BOVIN             Reviewed;         257 AA.
P35705; Q3SZA8;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 2.
25-OCT-2017, entry version 131.
RecName: Full=Thioredoxin-dependent peroxide reductase, mitochondrial;
EC=1.11.1.15;
AltName: Full=Antioxidant protein 1;
Short=AOP-1;
AltName: Full=Peroxiredoxin-3;
AltName: Full=Protein SP-22 {ECO:0000303|PubMed:8089078, ECO:0000303|PubMed:8912927};
Flags: Precursor;
Name=PRDX3; Synonyms=AOP1;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Adrenal medulla;
PubMed=8912927; DOI=10.3109/10425179609008449;
Hiroi T., Watabe S., Takimoto K., Yago N., Ymamoto Y., Takahashi S.Y.;
"The cDNA sequence encoding bovine SP-22, a new defence system against
reactive oxygen species in mitochondria.";
DNA Seq. 6:239-242(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Crossbred X Angus; TISSUE=Ileum;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
[3]
PROTEIN SEQUENCE OF 63-257, CLEAVAGE OF TRANSIT PEPTIDE AFTER HIS-62,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Adrenal medulla;
PubMed=8089078;
Watabe S., Kohno H., Kouyama H., Hiroi T., Yago N., Nakazawa T.;
"Purification and characterization of a substrate protein for
mitochondrial ATP-dependent protease in bovine adrenal cortex.";
J. Biochem. 115:648-654(1994).
[4]
X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 63-257 OF MUTANT SER-230, AND
SUBUNIT.
PubMed=16271889; DOI=10.1016/j.str.2005.07.021;
Cao Z., Roszak A.W., Gourlay L.J., Lindsay J.G., Isaacs N.W.;
"Bovine mitochondrial peroxiredoxin III forms a two-ring catenane.";
Structure 13:1661-1664(2005).
[5]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS), AND DISULFIDE BONDS.
PubMed=25906064; DOI=10.1371/journal.pone.0123303;
Cao Z., McGow D.P., Shepherd C., Lindsay J.G.;
"Improved catenated structures of bovine peroxiredoxin III F190L
reveal details of ring-ring interactions and a novel conformational
state.";
PLoS ONE 10:E0123303-E0123303(2015).
-!- 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.
{ECO:0000250|UniProtKB:P30048}.
-!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH.
{ECO:0000250|UniProtKB:P30048}.
-!- SUBUNIT: Homodimer; disulfide-linked, upon oxidation. 6 homodimers
assemble to form a ring-like dodecamer (PubMed:16271889,
PubMed:25906064). Interacts with NEK6 (By similarity). Interacts
with LRRK2 (By similarity). {ECO:0000250|UniProtKB:P30048,
ECO:0000269|PubMed:16271889, ECO:0000269|PubMed:25906064}.
-!- INTERACTION:
Self; NbExp=4; IntAct=EBI-15559045, EBI-15559045;
-!- SUBCELLULAR LOCATION: Mitochondrion matrix
{ECO:0000269|PubMed:8089078}.
-!- TISSUE SPECIFICITY: Predominantly expressed in adrenal cortex.
Also detected in liver, renal cortex and medulla, and adrenal
medulla (at protein level). {ECO:0000269|PubMed:8089078}.
-!- PTM: Phosphorylated by LRRK2; phosphorylation reduces perodixase
activity. {ECO:0000250|UniProtKB:P30048}.
-!- 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:0000250|UniProtKB:P30048}.
-!- 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:16271889}.
-!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1
subfamily. {ECO:0000305}.
-!- CAUTION: It is uncertain whether transit peptide cleavage occurs
after His-62 or Ala-63. Peptides have been found for both N-
termini in roughly equal amounts. {ECO:0000269|PubMed:8089078}.
-----------------------------------------------------------------------
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EMBL; D82025; BAA11511.1; -; mRNA.
EMBL; BC103009; AAI03010.1; -; mRNA.
PIR; JC2258; JC2258.
RefSeq; NP_776857.1; NM_174432.2.
UniGene; Bt.103308; -.
UniGene; Bt.62827; -.
PDB; 1ZYE; X-ray; 3.30 A; A/B/C/D/E/F/G/H/I/J/K/L=63-257.
PDB; 4MH2; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J/K/L=63-257.
PDB; 4MH3; X-ray; 2.40 A; A/B/C/D/E/F/G/H/I/J/K/L=63-257.
PDBsum; 1ZYE; -.
PDBsum; 4MH2; -.
PDBsum; 4MH3; -.
ProteinModelPortal; P35705; -.
SMR; P35705; -.
DIP; DIP-48458N; -.
STRING; 9913.ENSBTAP00000011505; -.
PeroxiBase; 4502; Bt2CysPrx03.
PaxDb; P35705; -.
PeptideAtlas; P35705; -.
PRIDE; P35705; -.
Ensembl; ENSBTAT00000011505; ENSBTAP00000011505; ENSBTAG00000008731.
GeneID; 281998; -.
KEGG; bta:281998; -.
CTD; 10935; -.
eggNOG; KOG0852; Eukaryota.
eggNOG; COG0450; LUCA.
GeneTree; ENSGT00390000004653; -.
HOGENOM; HOG000022343; -.
HOVERGEN; HBG000286; -.
InParanoid; P35705; -.
KO; K20011; -.
OMA; TAVHNGE; -.
OrthoDB; EOG091G0IE5; -.
TreeFam; TF105181; -.
Reactome; R-BTA-3299685; Detoxification of Reactive Oxygen Species.
EvolutionaryTrace; P35705; -.
Proteomes; UP000009136; Chromosome 26.
Bgee; ENSBTAG00000008731; -.
GO; GO:0005769; C:early endosome; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
GO; GO:0008385; C:IkappaB kinase complex; IEA:Ensembl.
GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
GO; GO:0043234; C:protein complex; IEA:Ensembl.
GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; IEA:Ensembl.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
GO; GO:0008379; F:thioredoxin peroxidase activity; IEA:Ensembl.
GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
GO; GO:0034614; P:cellular response to reactive oxygen species; IEA:Ensembl.
GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:Ensembl.
GO; GO:0001893; P:maternal placenta development; IEA:Ensembl.
GO; GO:0007005; P:mitochondrion organization; IEA:Ensembl.
GO; GO:0030099; P:myeloid cell differentiation; IEA:Ensembl.
GO; GO:0033673; P:negative regulation of kinase activity; IEA:Ensembl.
GO; GO:0018171; P:peptidyl-cysteine oxidation; IEA:Ensembl.
GO; GO:0008284; P:positive regulation of cell proliferation; IEA:Ensembl.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IEA:Ensembl.
GO; GO:0051881; P:regulation of mitochondrial membrane potential; IEA:Ensembl.
GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
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; Antioxidant; Complete proteome;
Direct protein sequencing; Disulfide bond; Mitochondrion;
Oxidoreductase; Peroxidase; Phosphoprotein; Redox-active center;
Reference proteome; Transit peptide.
TRANSIT 1 62 Mitochondrion.
{ECO:0000269|PubMed:8089078}.
CHAIN 63 257 Thioredoxin-dependent peroxide reductase,
mitochondrial.
/FTId=PRO_0000023781.
DOMAIN 64 222 Thioredoxin. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
ACT_SITE 109 109 Cysteine sulfenic acid (-SOH)
intermediate.
{ECO:0000269|PubMed:8089078}.
MOD_RES 84 84 N6-succinyllysine.
{ECO:0000250|UniProtKB:P20108}.
MOD_RES 92 92 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P30048}.
MOD_RES 92 92 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P20108}.
DISULFID 109 109 Interchain (with C-230); in linked form.
{ECO:0000244|PDB:4MH3,
ECO:0000269|PubMed:16271889}.
DISULFID 230 230 Interchain (with C-109); in linked form.
{ECO:0000244|PDB:4MH3,
ECO:0000269|PubMed:16271889}.
STRAND 74 79 {ECO:0000244|PDB:4MH2}.
STRAND 82 87 {ECO:0000244|PDB:4MH2}.
HELIX 88 91 {ECO:0000244|PDB:4MH2}.
STRAND 94 100 {ECO:0000244|PDB:4MH2}.
STRAND 107 109 {ECO:0000244|PDB:4MH2}.
HELIX 110 118 {ECO:0000244|PDB:4MH2}.
HELIX 120 124 {ECO:0000244|PDB:4MH2}.
TURN 125 127 {ECO:0000244|PDB:4MH2}.
STRAND 128 136 {ECO:0000244|PDB:4MH2}.
HELIX 138 145 {ECO:0000244|PDB:4MH2}.
HELIX 149 151 {ECO:0000244|PDB:4MH2}.
STRAND 158 163 {ECO:0000244|PDB:4MH2}.
HELIX 168 172 {ECO:0000244|PDB:4MH2}.
TURN 178 181 {ECO:0000244|PDB:4MH2}.
STRAND 185 190 {ECO:0000244|PDB:4MH2}.
STRAND 194 202 {ECO:0000244|PDB:4MH2}.
HELIX 210 225 {ECO:0000244|PDB:4MH2}.
SEQUENCE 257 AA; 28195 MW; F2E89EE2F172A42D CRC64;
MAATAGRLFR ASLIRHVSAI PWGISASAAL RPAASRRMCL TNALWSGSDQ AKFAFSTSSS
YHAPAVTQHA PYFKGTAVVS GEFKEISLDD FKGKYLVLFF YPLDFTFVCP TEIIAFSDKA
SEFHDVNCEV VAVSVDSHFS HLAWINTPRK NGGLGHMNIA LLSDLTKQIS RDYGVLLEGP
GLALRGLFII DPNGVIKHLS VNDLPVGRSV EETLRLVKAF QFVEAHGEVC PANWTPESPT
IKPHPTASRE YFEKVNQ


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