P35705 (PRDX3_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Thioredoxin-dependent peroxide reductase, mitochondrial
EC=1.11.1.15

Alternative name(s):
Antioxidant protein 1
Short name=AOP-1
Peroxiredoxin-3
Protein SP-22

Gene names

Name:	PRDX3
Synonyms:	AOP1

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	257 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in redox regulation of the cell. Protects radical-sensitive enzymes from oxidative damage by a radical-generating system.
Catalytic activity	2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.
Subunit structure	Dodecameric ring assembled from homodimeric units; disulfide-linked, upon oxidation. The rings have an approximate diameter of 150 A and a central hole of 70 A. 3-5% of the rings are interlocked by pairs. Interacts with NEK6 By similarity. Interacts with LRRK2 By similarity. Ref.4
Subcellular location	Mitochondrion.
Post-translational modification	Phosphorylated by LRRK2; phosphorylation reduces perodixase activity By similarity.
Miscellaneous	The active site is the redox-active Cys-109 oxidized to Cys-SOH. Cys-SOH rapidly reacts with Cys-230-SH of the other subunit to form an intermolecular disulfide with a concomitant homodimer formation. The enzyme may be subsequently regenerated by reduction of the disulfide by thioredoxin By similarity. Irreversibly inactivated by overoxidation of Cys-109 (to Cys-SO3H) upon oxidative stress By similarity.
Sequence similarities	Belongs to the AhpC/TSA family. Contains 1 thioredoxin domain.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Redox-active center Transit peptide
Molecular function	Antioxidant Oxidoreductase Peroxidase
PTM	Acetylation Disulfide bond Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Cellular component	mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	peroxidase activity Inferred from electronic annotation. Source: UniProtKB-KW peroxiredoxin activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 63

63

Mitochondrion By similarity

Chain

64 – 257

194

Thioredoxin-dependent peroxide reductase, mitochondrial

PRO_0000023781

Regions

Domain

64 – 222

159

Thioredoxin

Sites

Active site

109

1

Cysteine sulfenic acid (-SOH) intermediate By similarity

Amino acid modifications

Modified residue

92

1

N6-acetyllysine By similarity

Modified residue

147

1

Phosphothreonine By similarity

Disulfide bond

109

Interchain (with C-230); in linked form By similarity

Disulfide bond

230

Interchain (with C-109); in linked form By similarity

Secondary structure

1

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257

Helix Strand Turn

Details...

Beta strand

74 – 78

5

Beta strand

80 – 87

8

Helix

88 – 91

4

Beta strand

94 – 100

7

Beta strand

107 – 109

3

Helix

110 – 125

16

Beta strand

128 – 136

9

Helix

138 – 145

8

Helix

149 – 151

3

Beta strand

158 – 163

6

Helix

168 – 172

5

Turn

178 – 181

4

Beta strand

185 – 190

6

Beta strand

194 – 202

9

Helix

210 – 222

13

Sequences

	Sequence		Length	Mass (Da)
	P35705 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: F2E89EE2F172A42D	FASTA	257	28,195
	10 20 30 40 50 60 MAATAGRLFR ASLIRHVSAI PWGISASAAL RPAASRRMCL TNALWSGSDQ AKFAFSTSSS 70 80 90 100 110 120 YHAPAVTQHA PYFKGTAVVS GEFKEISLDD FKGKYLVLFF YPLDFTFVCP TEIIAFSDKA 130 140 150 160 170 180 SEFHDVNCEV VAVSVDSHFS HLAWINTPRK NGGLGHMNIA LLSDLTKQIS RDYGVLLEGP 190 200 210 220 230 240 GLALRGLFII DPNGVIKHLS VNDLPVGRSV EETLRLVKAF QFVEAHGEVC PANWTPESPT 250 IKPHPTASRE YFEKVNQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The cDNA sequence encoding bovine SP-22, a new defence system against reactive oxygen species in mitochondria." Hiroi T., Watabe S., Takimoto K., Yago N., Ymamoto Y., Takahashi S.Y. DNA Seq. 6:239-242(1996) [PubMed: 8912927] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Adrenal medulla.
[2]	NIH - Mammalian Gene Collection (MGC) project Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Crossbred X Angus. Tissue: Ileum.
[3]	"Purification and characterization of a substrate protein for mitochondrial ATP-dependent protease in bovine adrenal cortex." Watabe S., Kohno H., Kouyama H., Hiroi T., Yago N., Nakazawa T. J. Biochem. 115:648-654(1994) [PubMed: 8089078] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-257. Tissue: Adrenal medulla.
[4]	"Bovine mitochondrial peroxiredoxin III forms a two-ring catenane." Cao Z., Roszak A.W., Gourlay L.J., Lindsay J.G., Isaacs N.W. Structure 13:1661-1664(2005) [PubMed: 16271889] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 63-257 OF MUTANT SER-230, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D82025 mRNA. Translation: BAA11511.1.
BC103009 mRNA. Translation: AAI03010.1.

IPI

IPI00696824.

PIR

JC2258.

RefSeq

NP_776857.1. NM_174432.2.

UniGene

Bt.103308.
Bt.62827.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ZYE	X-ray	3.30	A/B/C/D/E/F/G/H/I/J/K/L	63-257	[»]

ProteinModelPortal

P35705.

SMR

P35705. Positions 64-254.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-48458N.

Protein family/group databases

PeroxiBase

4502. Bt2CysPrx03.

Proteomic databases

PRIDE

P35705.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSBTAT00000011505; ENSBTAP00000011505; ENSBTAG00000008731.

GeneID

281998.

KEGG

bta:281998.

Organism-specific databases

CTD

10935.

Phylogenomic databases

eggNOG

maNOG05509.

GeneTree

ENSGT00390000004653.

HOVERGEN

HBG000286.

InParanoid

P35705.

OMA

TNVLWSG.

OrthoDB

EOG4S7JQS.

PhylomeDB

P35705.

Family and domain databases

InterPro

IPR000866. AhpC/TSA.
IPR024706. Peroxiredoxin_AhpC-typ.
IPR019479. Peroxiredoxin_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]

Gene3D

G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.

KO

K03386.

Pfam

PF10417. 1-cysPrx_C. 1 hit.
PF00578. AhpC-TSA. 1 hit.
[Graphical view]

PIRSF

PIRSF000239. AHPC. 1 hit.

SUPFAM

SSF52833. Thiordxn-like_fd. 1 hit.

PROSITE

PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

PRDX3_BOVIN

Accession

Primary (citable) accession number: P35705
Secondary accession number(s): Q3SZA8

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	November 1, 1997
Last modified:	January 25, 2012
This is version 94 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program