Peroxiredoxin-6 - Bos taurus (Bovine)

Contribute

Send feedback

Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot O77834 (PRDX6_BOVIN)

Last modified June 16, 2009. Version 60. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data |

Customize display

text xml rdf/xml gff fasta

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein names

Recommended name:
    Peroxiredoxin-6
    EC=1.11.1.15
Alternative name(s):
    Antioxidant protein 2
    1-Cys peroxiredoxin
      Short name=1-Cys PRX
    Acidic calcium-independent phospholipase A2
      Short name=aiPLA2
    EC=3.1.1.-
    Non-selenium glutathione peroxidase
      Short name=NSGPx
    EC=1.11.1.7
    PHGPx
    Ciliary body glutathione peroxidase

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

Hide | Top

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.

Hide | Top

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. Donor + H₂O₂ = oxidized donor + 2 H₂O.
Subunit structure	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. 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.

Hide | Top

Ontologies

Keywords
Biological process	Lipid degradation
Cellular component	Cytoplasm Cytoplasmic vesicle Lysosome
Domain	Redox-active center
Molecular function	Antioxidant Hydrolase Oxidoreductase Peroxidase
PTM	Disulfide bond Phosphoprotein
Technical term	Direct protein sequencing Multifunctional enzyme
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW response to reactive oxygen species Inferred from sequence or structural similarity. Source: AgBase
Cellular component	cytoplasmic 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	hydrolase activity Inferred from electronic annotation. Source: UniProtKB-KW peroxiredoxin activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 224

223

Peroxiredoxin-6

PRO_0000135101

Regions

Domain

5 – 169

165

Thioredoxin

Sites

Active site

For phospholipase activity By similarity

Active site

Cysteine sulfenic acid (-SOH) intermediate By similarity

Amino acid modifications

Modified residue

Phosphothreonine By similarity

Modified residue

Phosphotyrosine By similarity

Disulfide bond

Interchain; in linked form By similarity

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

O77834-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 4013D59C4D9FC05E
Show »

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

« Hide

Hide | Top

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.

Hide | Top

Cross-references

Sequence databases
	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.
UniGene	Bt.49705
3D structure databases
HSSP	HSSP built from PDB template 1PRX based on UniProtKB P30041.
SMR	O77834. Positions 5-224.
ModBase	Search...
Protein family/group databases
PeroxiBase	4423. Bt1CysPrx.
Genome annotation databases
Ensembl	ENSBTAG00000004855. Bos taurus. [Contig view]
GeneID	282438.
KEGG	bta:282438.
Phylogenomic databases
HOVERGEN	O77834.
OMA	O77834. TARVVFI.
Enzyme and pathway databases
BRENDA	1.11.1.15. 251. 1.11.1.7. 251.
Family and domain databases
InterPro	IPR000866. Alkyl_hydroperoxide_Rdtase. IPR019479. Peroxiredoxin_C. IPR017936. Thioredoxin-like. IPR012335. Thioredoxin_fold. [Graphical view]
Gene3D	G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
Pfam	PF10417. 1-cysPrx_C. 1 hit. PF00578. AhpC-TSA. 1 hit. [Graphical view]
PROSITE	PS51352. THIOREDOXIN_2. 1 hit. [Graphical view]
ProtoNet	Search...

Hide | Top

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:	June 16, 2009
This is version 60 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Hide | Top

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents