EC 1.11.1.15
Antioxidant protein 2
1-Cys peroxiredoxin
1-Cys PRX
Acidic calcium-independent phospholipase A2
aiPLA2
EC 3.1.1.-
Non-selenium glutathione peroxidase
NSGPx
EC 1.11.1.7
PHGPx
Ciliary body glutathione peroxidase

Gene name

	Name:	PRDX6
	Synonyms:	AOP2, GPX, PHGPX

From

Bos taurus (Bovine)

[TaxID: 9913]

Taxonomy

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

Protein existence

1: Evidence at protein level;

References

[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Ocular ciliary body; DOI=10.1074/jbc.273.40.26171; PubMed=9748299 [NCBI, ExPASy, EBI, Israel, Japan] Singh A.K., Shichi H.; "A novel glutathione peroxidase in bovine eye. Sequence analysis, mRNA level, and translation."; J. Biol. Chem. 273:26171-26178(1998).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Lung; DOI=10.1074/jbc.274.30.21326; PubMed=10409692 [NCBI, ExPASy, EBI, Israel, Japan] Fisher A.B., Dodia C., Manevich Y., Chen J.-W., Feinstein S.I.; "Phospholipid hydroperoxides are substrates for non-selenium glutathione peroxidase."; J. Biol. Chem. 274:21326-21334(1999).
[3]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Oviduct; Rojas Garcia P.P., Einspanier R.; "Glutathione peroxidase in the bovine oviduct."; Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. DOI=10.1186/1471-2164-6-166; PubMed=16305752 [NCBI, ExPASy, EBI, Israel, Japan] Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.; "Characterization of 954 bovine full-CDS cDNA sequences."; BMC Genomics 6:166-166(2005).
[5]	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.
[6]	PROTEIN SEQUENCE OF 2-30. DOI=10.1016/0014-4835(90)90040-2; PubMed=2373154 [NCBI, ExPASy, EBI, Israel, Japan] Shichi H., Demar J.C.; "Non-selenium glutathione peroxidase without glutathione S-transferase activity from bovine ciliary body."; Exp. Eye Res. 50:513-520(1990).

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.
CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H₂O + ROH.
CATALYTIC ACTIVITY: Donor + H₂O₂ = oxidized donor + 2 H₂O.
SUBUNIT: Homotetramer. May interact with HTR2A. Interacts with STH (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (By similarity). Lysosome (By similarity). Cytoplasmic vesicle (By similarity). Note=And also found in lung secretory organelles (By similarity).
MISCELLANEOUS: The active site is the redox-active Cys-47 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-47 (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

AF080228; AAC63016.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF090194; AAC84043.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ243848; CAB64802.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BT020967; AAX08984.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC102172; AAI02173.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_777068.1; -.

UniGene

Bt.49705

3D structure databases

HSSP

P30041; 1PRX. [HSSP ENTRY / PDB]

SMR

O77834; 5-224.

ModBase

O77834.

Protein family/group databases

PeroxiBase

4423; Bt1CysPrx.

Ontologies

GO:0031410;	Cellular component: cytoplasmic vesicle (inferred from electronic annotation from UniProtKB-KW).
GO:0005829;	Cellular component: cytosol (inferred from sequence or structural similarity from AgBase).
GO:0005764;	Cellular component: lysosome (inferred from electronic annotation from UniProtKB-KW).
GO:0016787;	Molecular function: hydrolase activity (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:0016042;	Biological process: lipid catabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0000302;	Biological process: response to reactive oxygen species (inferred from sequence or structural similarity from AgBase).
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

ENSBTAG00000004855; Bos taurus. [Contig view]

GeneID

282438; -.

KEGG

bta:282438; -.

Phylogenomic databases

HOVERGEN

O77834; -.

Other

ProtoNet

O77834.

UniRef

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

Keywords

Antioxidant; Cytoplasm; Cytoplasmic vesicle; Direct protein sequencing; 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_0000135101`
`DOMAIN`	`5 169`	`165`	`Thioredoxin.`
`ACT_SITE`	`32 32`		`For phospholipase activity (By similarity).`
`ACT_SITE`	`47 47`		`Cysteine sulfenic acid (-SOH) intermediate (By similarity).`
`MOD_RES`	`44 44`		`Phosphothreonine (By similarity).`
`MOD_RES`	`89 89`		`Phosphotyrosine (By similarity).`
`DISULFID`	`47 47`		`Interchain; in linked form (By similarity).`

Sequence information

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

Molecular weight: 25067 Da [This is the MW of the unprocessed precursor]

CRC64: 4013D59C4D9FC05E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPGGLLLGDE APNFEANTTI GRIRFHDYLG DSWGILFSHP RDFTPVCTTE LGRAAKLAPE 

        70         80         90        100        110        120 
FAKRNVKMIA LSIDSVEDHL AWSKDINAYN GEEPTEKLPF PIIDDKNRDL AIQLGMLDPA 

       130        140        150        160        170        180 
EKDEKGMPVT ARVVFIFGPD KKLKLSILYP ATTGRNFDEI LRVIISLQLT AEKRVATPVD 

       190        200        210        220 
WKNGDSVMVL PTIPEEEAKK LFPKGVFTKE LPSGKKYLRY TPQP

O77834 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