NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=CB;
TISSUE=Bursa of Fabricius;
DOI=10.1186/gb-2004-6-1-r6; PubMed=15642098 [NCBI, ExPASy, EBI, Israel, Japan]
Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P., Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P., Hayashizaki Y., Buerstedde J.-M.;
"Full-length cDNAs from chicken bursal lymphocytes to facilitate gene function analysis.";
Genome Biol. 6:RESEARCH006.1-RESEARCH006.9(2005).

Comments

FUNCTION: Involved in redox regulation of the cell. Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides. May play a role in the regulation of phospholipid turnover as well as in protection against oxidative injury (By similarity).
CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H₂O + ROH.
SUBUNIT: Homotetramer (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (By similarity). Lysosome (By similarity). Cytoplasmic vesicle (By similarity).
MISCELLANEOUS: The active site is the redox-active Cys-46 oxidized to Cys-SOH. Cys-SOH may rapidly react with a Cys-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-46 (to Cys-SO(3)H) upon oxidative stress (By similarity).
SIMILARITY: Belongs to the ahpC/TSA family. Rehydrin subfamily.
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

AJ720480; CAG32139.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_001034418.1; -.

UniGene

Gga.34325

3D structure databases

SMR

Q5ZJF4; 3-222, 4-223.

ModBase

Q5ZJF4.

Protein family/group databases

PeroxiBase

4421; Gga1CysPrx.

Ontologies

GO:0031410;	Cellular component: cytoplasmic vesicle (inferred from electronic annotation from UniProtKB-KW).
GO:0005764;	Cellular component: lysosome (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).

Genome annotation databases

Ensembl

ENSGALG00000003053; Gallus gallus. [Contig view]

GeneID

429062; -.

KEGG

gga:429062; -.

Phylogenomic databases

HOVERGEN

Q5ZJF4; -.

Other

ProtoNet

Q5ZJF4.

UniRef

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

Keywords

Antioxidant; Cytoplasm; Cytoplasmic vesicle; Hydrolase; Lipid degradation; Lysosome; Multifunctional enzyme; Oxidoreductase; Peroxidase; Phosphoprotein; Redox-active center.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed (By similarity).`
`CHAIN`	`2 224`	`223`	`Peroxiredoxin-6.`	`PRO_0000256863`
`DOMAIN`	`4 168`	`165`	`Thioredoxin.`
`ACT_SITE`	`31 31`		`For phospholipase activity (By similarity).`
`ACT_SITE`	`46 46`		`Cysteine sulfenic acid (-SOH) intermediate (By similarity).`
`MOD_RES`	`88 88`		`Phosphotyrosine (By similarity).`
`DISULFID`	`46 46`		`Interchain; in linked form (By similarity).`

Sequence information

Length: 224 AA [This is the length of the unprocessed precursor]

Molecular weight: 24977 Da [This is the MW of the unprocessed precursor]

CRC64: 4F2759FB44EC9493 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPGLLLGDEA PNFEADTTQG GIRFHDFLGD SWGILFSHPR DFTPVCTTEL GRAAKLAPEF 

        70         80         90        100        110        120 
SKRNVKMIAL SIDSVPDHLA WSKDINAYNG DQPVEKLPFP IIADKDRELA VKLGMLDPDE 

       130        140        150        160        170        180 
RDKDGMPLTA RVVFIFGPDK KLKLSILYPA TTGRNFDEIL RVVDSLQLTA YKKVATPVDW 

       190        200        210        220 
KCGDSVMVVP TLPDEEAKKL FPKGVFTKDL PSGKKYLRYT PQPE

Q5ZJF4 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