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

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. 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

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Cross-references

Sequence databases

EMBL

AB220568; BAE73101.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

SMR

Q2PFL9; 4-223, 5-224.

ModBase

Q2PFL9.

Protein family/group databases

PeroxiBase

4430; Mfa1CysPrx.

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).

BLOCKS

Q2PFL9.

Phylogenomic databases

HOVERGEN

Q2PFL9; -.

Other

ProtoNet

Q2PFL9.

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_0000256860`
`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`	`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: 25011 Da [This is the MW of the unprocessed precursor]

CRC64: 21304B97BD3B5F3E [This is a checksum on the sequence]

        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

Q2PFL9 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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