[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Adrenal medulla; PubMed=8912927 [NCBI, ExPASy, EBI, Israel, Japan] 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]	NUCLEOTIDE SEQUENCE [MRNA] OF 2-257. TISSUE=Adrenal medulla; PubMed=8089078 [NCBI, ExPASy, EBI, Israel, Japan] 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).

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: Homodimer; disulfide-linked, upon oxidation (By similarity).
SUBCELLULAR LOCATION: Mitochondrion.
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).
MISCELLANEOUS: Irreversibly inactivated by overoxidation of Cys-109 (to Cys-SO(3)H) upon oxidative stress (By similarity).
SIMILARITY: Belongs to the ahpC/TSA family.
SIMILARITY: Contains 1 thioredoxin domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

D82025; BAA11511.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC103009; AAI03010.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

JC2258; JC2258.

NP_776857.1; -.

3D structure databases

PDB

1ZYE; X-ray; 3.30 A; A/B/C/D/E/F/G/H/I/J/K/L=63-257.

[ExPASy / RCSB / EBI]

PDBsum

1ZYE; -.

ModBase

P35705.

Protein family/group databases

PeroxiBase

4502; Bt2CysPrx03.

Ontologies

GO:0005739;	Cellular component: mitochondrion (inferred from electronic annotation from UniProtKB-KW).
GO:0051920;	Molecular function: peroxiredoxin activity (inferred from electronic annotation from EC).
GO:0045454;	Biological process: cell redox homeostasis (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR000866; AhpC-TSA.
IPR012335; Thioredoxin_fold.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.30.10; Thioredoxin_fold; 1.

Pfam

PF00578; AhpC-TSA; 1.
Pfam graphical view of domain structure.

PROSITE

PS51352; THIOREDOXIN_2; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

P35705.

Genome annotation databases

Ensembl

ENSBTAG00000008731; Bos taurus. [Contig view]

GeneID

281998; -.

KEGG

bta:281998; -.

Phylogenomic databases

HOVERGEN

P35705; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Antioxidant; Mitochondrion; Oxidoreductase; Peroxidase; Redox-active center; Transit peptide.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 63`	`63`	`Mitochondrion (By similarity).`
`CHAIN`	`64 257`	`194`	`Thioredoxin-dependent peroxide reductase, mitochondrial.`	`PRO_0000023781`
`DOMAIN`	`64 222`	`159`	`Thioredoxin.`
`ACT_SITE`	`109 109`		`Cysteine sulfenic acid (-SOH) intermediate (By similarity).`
`DISULFID`	`109 109`		`Interchain (with C-230); in linked form (By similarity).`
`DISULFID`	`230 230`		`Interchain (with C-109); in linked form (By similarity).`
`STRAND`	`74 78`	`5`
`STRAND`	`80 87`	`8`
`HELIX`	`88 91`	`4`
`STRAND`	`94 100`	`7`
`STRAND`	`107 109`	`3`
`HELIX`	`110 125`	`16`
`STRAND`	`128 136`	`9`
`HELIX`	`138 145`	`8`
`HELIX`	`149 151`	`3`
`STRAND`	`158 163`	`6`
`HELIX`	`168 172`	`5`
`TURN`	`178 181`	`4`
`STRAND`	`185 190`	`6`
`STRAND`	`194 202`	`9`
`HELIX`	`210 222`	`13`

Sequence information

Length: 257 AA [This is the length of the unprocessed precursor]

Molecular weight: 28195 Da [This is the MW of the unprocessed precursor]

CRC64: F2E89EE2F172A42D [This is a checksum on the sequence]

        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

P35705 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools