Q2PFL9 (PRDX6_MACFA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peroxiredoxin-6
EC=1.11.1.15

Alternative name(s):
Non-selenium glutathione peroxidase
Short name=NSGPx
EC=1.11.1.9

Gene names

Name:	PRDX6
ORF Names:	QtsA-11939

Organism

Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)

Taxonomic identifier

9541 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Cercopithecidae › Cercopithecinae › Macaca

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 transcript 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 By similarity.
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 APEX1 and STH By similarity.
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 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.

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	Multifunctional enzyme
Gene Ontology (GO)
Biological process	lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasmic membrane-bounded vesicle Inferred from electronic annotation. Source: UniProtKB-SubCell lysosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	glutathione peroxidase activity Inferred from electronic annotation. Source: EC hydrolase activity Inferred from electronic annotation. Source: UniProtKB-KW 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_0000256860
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)
	Q2PFL9 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 21304B97BD3B5F3E	FASTA	224	25,011
	10 20 30 40 50 60 MPGGLLLGDE APNFEANTTV GRIRFHDFLG DSWGILFSHP RDFTPVCTTE LGRAAKLAPE 70 80 90 100 110 120 FAKRNVKLIA LSIDSVEDHL AWSKDTNAYN CEEPTEKLPF PIIDDKNRDL AILLGMLDPA 130 140 150 160 170 180 EKDEKGMPVT ARVVFVFGPD KKLKLSILYP ATTGRNFDEI LRVVISLQLT AEKRVATPVD 190 200 210 220 WKDGDSVMVL PTIPEEEAKK LFPKGVFTKE LPSGKKYLRY TPQP

References

[1]	"Analysis of gene expression in cynomolgus monkey tissues by macaque cDNA oligo-chips." Kobayashi M., Tanuma R., Hirata M., Osada N., Kusuda J., Sugano S., Hashimoto K. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB220568 mRNA. Translation: BAE73101.1.
3D structure databases
HSSP	HSSP built from PDB template 1X0R based on UniProtKB Q9Y9L0.
ProteinModelPortal	Q2PFL9.
SMR	Q2PFL9. Positions 5-224.
ModBase	Search...
Protein family/group databases
PeroxiBase	4430. Mfa1CysPrx.
Proteomic databases
PRIDE	Q2PFL9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
HOVERGEN	HBG105234.
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.
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_MACFA

Accession

Primary (citable) accession number: Q2PFL9

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	January 23, 2007
Last modified:	November 16, 2011
This is version 43 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program