[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Liver; Leyens G., Donnay I., Knoops B.; "Cloning of 4 new bovine peroxiredoxins, and screening of the complete peroxiredoxin family in different bovine tissues."; Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=Crossbred X Angus; TISSUE=Liver; NIH - Mammalian Gene Collection (MGC) project; Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.

Comments

FUNCTION: Probably involved in redox regulation of the cell. Regulates the activation of NF-kappa-B in the cytosol by a modulation of I-kappa-B-alpha phosphorylation (By similarity).
CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H₂O + ROH.
SUBUNIT: Homodimer or heterodimer with PRDX1; disulfide-linked, upon oxidation (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
MISCELLANEOUS: The active site is the redox-active Cys-127 oxidized to Cys-SOH. Cys-SOH rapidly reacts with Cys-248-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-127 (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

AF305563; AAG53660.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC109824; AAI09825.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_776858.1; -.

UniGene

Bt.5203

3D structure databases

HSSP

Q63716; 1QQ2. [HSSP ENTRY / PDB]

ModBase

Q9BGI2.

Protein family/group databases

PeroxiBase

4531; Bt2CysPrx04.

Ontologies

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).

Genome annotation databases

Ensembl

ENSBTAG00000006165; Bos taurus. [Contig view]

GeneID

281999; -.

KEGG

bta:281999; -.

Phylogenomic databases

HOVERGEN

Q9BGI2; -.

Other

ProtoNet

Q9BGI2.

UniRef

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

Keywords

Antioxidant; Cytoplasm; Oxidoreductase; Peroxidase; Redox-active center.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 274`	`274`	`Peroxiredoxin-4.`	`PRO_0000135097`
`DOMAIN`	`82 240`	`159`	`Thioredoxin.`
`ACT_SITE`	`127 127`		`Cysteine sulfenic acid (-SOH) intermediate (By similarity).`
`DISULFID`	`127 127`		`Interchain (with C-248); in linked form (By similarity).`
`DISULFID`	`248 248`		`Interchain (with C-127); in linked form (By similarity).`

Sequence information

Length: 274 AA [This is the length of the unprocessed precursor]

Molecular weight: 30741 Da [This is the MW of the unprocessed precursor]

CRC64: AE14176CF1C70E37 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MEAPPPPPPL PATTLAPGRS RKLLLLPLLL FLLRAEAVRG FEAEERPRTR EEECHFYAGG 

        70         80         90        100        110        120 
QVYPGEVSRV SVAEHSLHLS KAKISKPAPY WEGTAVINGE FKELKLTDYR GKYLVFFFYP 

       130        140        150        160        170        180 
LDFTFVCPTE IIAFGDRIDE FRSINTEVVA CSVDSQFTHL AWINTPRRQG GLGSINIPLL 

       190        200        210        220        230        240 
ADLNHQISKD YGVYLEDSGH TLRGLFIIDD KGILRQITLN DLPVGRSVDE TLRLVQAFQY 

       250        260        270 
TDKHGEVCPA GWKPGSETII PDPAGKLKYF DKLN

Q9BGI2 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