O77834 (PRDX6_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peroxiredoxin-6
EC=1.11.1.15

Alternative name(s):
1-Cys peroxiredoxin
Short name=1-Cys PRX
Acidic calcium-independent phospholipase A2
Short name=aiPLA2
EC=3.1.1.-
Antioxidant protein 2
Ciliary body glutathione peroxidase
Non-selenium glutathione peroxidase
Short name=NSGPx
EC=1.11.1.9
PHGPx

Gene names

Name:	PRDX6
Synonyms:	AOP2, GPX, PHGPX

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	224 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. Can reduce H2O2 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. 2 glutathione + H2O2 = glutathione disulfide + 2 H2O.
Subunit structure	Homotetramer. Interacts with GSTP1; mediates PRDX6 glutathionylation and regeneration. May interact with HTR2A. Interacts with STH and APEX1 By similarity. Ref.7
Subcellular location	Cytoplasm By similarity. Lysosome By similarity. Cytoplasmic vesicle By similarity. Note: Also found in lung secretory organelles By similarity.
Miscellaneous	The active site is the redox-active Cys-47 oxidized to Cys-SOH. Unlike 2-Cys peroxiredoxins, PRDX6 conserves only this peroxidatic cysteine. To regenerate and activate the enzyme, the oxidized form is directly reduced to cysteine by glutathione and not thioredoxin. Irreversibly inactivated by overoxidation of Cys-47 (to Cys-SO3H) upon oxidative stress By similarity.
Sequence similarities	Belongs to the AhpC/TSA family. Rehydrin subfamily. Contains 1 thioredoxin domain.

Ontologies

Keywords
Biological process	Lipid degradation
Cellular component	Cytoplasm Cytoplasmic vesicle Lysosome
Domain	Redox-active center
Molecular function	Antioxidant Hydrolase Oxidoreductase Peroxidase
PTM	Acetylation Disulfide bond Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological process	response to reactive oxygen species Inferred from sequence or structural similarity. Source: AgBase
Cellular component	cytoplasmic membrane-bounded vesicle Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Inferred from sequence or structural similarity. Source: AgBase lysosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	glutathione peroxidase activity Inferred from electronic annotation. Source: EC 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
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 224	223	Peroxiredoxin-6		PRO_0000135101
Regions
	Domain	5 – 169	165	Thioredoxin
Sites
	Active site	32	1	For phospholipase activity By similarity
	Active site	47	1	Cysteine sulfenic acid (-SOH) intermediate By similarity
Amino acid modifications
	Modified residue	44	1	Phosphothreonine By similarity
	Modified residue	63	1	N6-acetyllysine By similarity
	Modified residue	89	1	Phosphotyrosine By similarity
	Modified residue	209	1	N6-acetyllysine By similarity
	Disulfide bond	47		Interchain; in linked form By similarity

Sequences

	Sequence		Length	Mass (Da)
	O77834 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 4013D59C4D9FC05E	FASTA	224	25,067
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A novel glutathione peroxidase in bovine eye. Sequence analysis, mRNA level, and translation." Singh A.K., Shichi H. J. Biol. Chem. 273:26171-26178(1998) [PubMed: 9748299] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Ocular ciliary body.
[2]	"Phospholipid hydroperoxides are substrates for non-selenium glutathione peroxidase." Fisher A.B., Dodia C., Manevich Y., Chen J.-W., Feinstein S.I. J. Biol. Chem. 274:21326-21334(1999) [PubMed: 10409692] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Lung.
[3]	"Glutathione peroxidase in the bovine oviduct." Rojas Garcia P.P., Einspanier R. Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Oviduct.
[4]	"Characterization of 954 bovine full-CDS cDNA sequences." 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. BMC Genomics 6:166-166(2005) [PubMed: 16305752] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	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.
[6]	"Non-selenium glutathione peroxidase without glutathione S-transferase activity from bovine ciliary body." Shichi H., Demar J.C. Exp. Eye Res. 50:513-520(1990) [PubMed: 2373154] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-30.
[7]	"Activation of the antioxidant enzyme 1-CYS peroxiredoxin requires glutathionylation mediated by heterodimerization with pi GST." Manevich Y., Feinstein S.I., Fisher A.B. Proc. Natl. Acad. Sci. U.S.A. 101:3780-3785(2004) [PubMed: 15004285] [Abstract] Cited for: INTERACTION WITH GSTP1, ACTIVATION BY GLUTATHIONE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF080228 mRNA. Translation: AAC63016.1. AF090194 mRNA. Translation: AAC84043.1. AJ243848 mRNA. Translation: CAB64802.1. BT020967 mRNA. Translation: AAX08984.1. BC102172 mRNA. Translation: AAI02173.1.
IPI	IPI00689857.
RefSeq	NP_777068.1. NM_174643.1.
UniGene	Bt.49705.
3D structure databases
ProteinModelPortal	O77834.
SMR	O77834. Positions 5-224.
ModBase	Search...
Protein-protein interaction databases
STRING	O77834.
Protein family/group databases
PeroxiBase	4423. Bt1CysPrx.
Proteomic databases
PRIDE	O77834.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSBTAT00000006383; ENSBTAP00000006383; ENSBTAG00000004855.
GeneID	282438.
KEGG	bta:282438.
Organism-specific databases
CTD	9588.
Phylogenomic databases
eggNOG	maNOG04384.
GeneTree	ENSGT00550000074794.
HOVERGEN	HBG105234.
InParanoid	O77834.
OMA	NYPILAD.
OrthoDB	EOG4M399H.
PhylomeDB	O77834.
Enzyme and pathway databases
BRENDA	1.11.1.15. 908.
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	K11188.
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

PRDX6_BOVIN

Accession

Primary (citable) accession number: O77834
Secondary accession number(s): Q5E9F3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	January 23, 2007
Last modified:	November 16, 2011
This is version 83 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program