[1]	NUCLEOTIDE SEQUENCE [MRNA]. Knoops B., Cherif H.; "Cloning and characterization of baboon AOEB166/PRDX5."; Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.

Comments

FUNCTION: Reduces hydrogen peroxide and alkyl hydroperoxides with reducing equivalents provided through the thioredoxin system. Involved in intracellular redox signaling (By similarity).
CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H₂O + ROH.
SUBUNIT: Monomer (By similarity).
SUBCELLULAR LOCATION: Mitochondrion (By similarity). Cytoplasm (By similarity). Peroxisome (By similarity).

ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative initiation.

Name	Mitochondrial
Isoform ID	Q9GLW9-1
This is the isoform sequence displayed in this entry.

Name	Cytoplasmic+peroxisomal
Isoform ID	Q9GLW9-2
Features which should be applied to build the isoform sequence: VSP_018831.

SIMILARITY: Belongs to the peroxiredoxin 2 family.
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

AF110734; AAG13451.2; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P30044; 1HD2. [HSSP ENTRY / PDB]

SMR

Q9GLW9; 55-215.

ModBase

Q9GLW9.

Family and domain databases

InterPro

IPR013740; Redoxin.
IPR012335; Thioredoxin_fold.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.30.10; Thioredoxin_fold; 1.

Pfam

PF08534; Redoxin; 1.
Pfam graphical view of domain structure.

PROSITE

PS51352; THIOREDOXIN_2; 1.
PROSITE graphical view of domain structure (profiles).

BLOCKS

Q9GLW9.

Phylogenomic databases

HOVERGEN

Q9GLW9; -.

Other

Q9GLW9; -.

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

Keywords

Alternative initiation; Antioxidant; Cytoplasm; Mitochondrion; Oxidoreductase; Peroxidase; Peroxisome; Redox-active center; Transit peptide.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 53`	`53`	`Mitochondrion (Potential).`
`CHAIN`	`54 215`	`162`	`Peroxiredoxin-5, mitochondrial.`	`PRO_0000023797`
`DOMAIN`	`57 215`	`159`	`Thioredoxin.`
`MOTIF`	`213 215`	`3`	`Microbody targeting signal (By similarity).`
`ACT_SITE`	`101 101`		`Cysteine sulfenic acid (-SOH) intermediate (Potential).`
`DISULFID`	`101 205`		`Redox-active (By similarity).`
`VAR_SEQ`	`1 53`		`Missing (in isoform Cytoplasmic+peroxisomal).`	`VSP_018831`

Sequence information

Length: 215 AA [This is the length of the unprocessed precursor]

Molecular weight: 22166 Da [This is the MW of the unprocessed precursor]

CRC64: 65183A24535C1617 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGLAGVCVLR RSAGYILGGA AGQSVAATAA ARRRSEGGWA SGGVRSFSRA AAAMAPIKVG 

        70         80         90        100        110        120 
DAIPAVEVFE GEPGNKVNLA ELFKGKKGVL FGVPGAFTPG CSKTHLPGFV EQAEALKAKG 

       130        140        150        160        170        180 
VQVLACLSVN DAFVTGEWGR AHKVEGKVRL LADPTGAFGK ETDLLLDDSL VSIFGNRRLK 

       190        200        210 
RFSMVVQDGI VKALNVEPDG TGLTCSLAPS IISQL

Q9GLW9 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