[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1074/jbc.272.49.30952; PubMed=9388242 [NCBI, ExPASy, EBI, Israel, Japan] Jin D.-Y., Chae H.Z., Rhee S.G., Jeang K.-T.; "Regulatory role for a novel human thioredoxin peroxidase in NF-kappaB activation."; J. Biol. Chem. 272:30952-30961(1997).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."; Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Brain; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[4]	PROTEIN SEQUENCE OF 48-66 AND 174-200, AND MASS SPECTROMETRY. TISSUE=Brain, and Cajal-Retzius cell; Lubec G., Afjehi-Sadat L.; Submitted (MAR-2007) to UniProtKB.
[5]	OVEROXIDATION AT CYS-124. DOI=10.1042/BJ20020525; PubMed=12059788 [NCBI, ExPASy, EBI, Israel, Japan] Wagner E., Luche S., Penna L., Chevallet M., van Dorsselaer A., Leize-Wagner E., Rabilloud T.; "A method for detection of overoxidation of cysteines: peroxiredoxins are oxidized in vivo at the active-site cysteine during oxidative stress."; Biochem. J. 366:777-785(2002).

Comments

FUNCTION: Probably involved in redox regulation of the cell. Regulates the activation of NF-kappa-B in the cytosol by a modulation of I-kappa-B-alpha phosphorylation.
CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H₂O + ROH.
SUBUNIT: Homodimer or heterodimer with PRDX1; disulfide-linked, upon oxidation (By similarity).
SUBCELLULAR LOCATION: Cytoplasm.
MISCELLANEOUS: The active site is the redox-active Cys-124 oxidized to Cys-SOH. Cys-SOH rapidly reacts with Cys-245-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.
MISCELLANEOUS: Irreversibly inactivated by overoxidation of Cys-124 (to Cys-SO(3)H) upon oxidative stress.
SIMILARITY: Belongs to the ahpC/TSA 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

U25182; AAB95175.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CR541668; CAG46469.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CR541705; CAG46506.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC003609; AAH03609.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC007107; AAH07107.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC016770; AAH16770.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

G01790; G01790.

NP_006397.1; -.

3D structure databases

PDB

2PN8; X-ray; 1.80 A; A/B/C/D/E/F/G/H/I/J=82-271.

[ExPASy / RCSB / EBI]

PDBsum

2PN8; -.

ModBase

Q13162.

Protein family/group databases

PeroxiBase

4530; Hs2CysPrx04.

2D gel databases

OGP

Q13162; -.

REPRODUCTION-2DPAGE

IPI00011937; -.

Organism-specific databases

HIX0016701; -.

HGNC:17169; PRDX4.

CAB008659; -.

606506; gene. [NCBI / EBI]

PharmGKB

PA33725; -.

GeneCards

Q13162.

Gene expression databases

ArrayExpress

Q13162; -.

CleanEx

HS_PRDX4; -.

GermOnline

ENSG00000123131; Homo sapiens.

Ontologies

GO:0008379;	Molecular function: thioredoxin peroxidase activity (traceable author statement from ProtInc).
GO:0007252;	Biological process: I-kappaB phosphorylation (traceable author statement from ProtInc).
QuickGo view.

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

Q13162.

Proteomic databases

PeptideAtlas

Q13162; -.

Genome annotation databases

Ensembl

ENSG00000123131; Homo sapiens. [Contig view]

GeneID

10549; -.

KEGG

hsa:10549; -.

NMPDR

fig|9606.3.peg.32551; -.

Phylogenomic databases

HOGENOM

Q13162; -.

HOVERGEN

Q13162; -.

Other

Q13162; -.

PRDX4; Homo sapiens.

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

Keywords

3D-structure; Antioxidant; Cytoplasm; Direct protein sequencing; Oxidoreductase; Peroxidase; Redox-active center.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 271`	`271`	`Peroxiredoxin-4.`	`PRO_0000135098`
`DOMAIN`	`79 237`	`159`	`Thioredoxin.`
`COMPBIAS`	`20 30`	`11`	`Poly-Leu.`
`ACT_SITE`	`124 124`		`Cysteine sulfenic acid (-SOH) intermediate (By similarity).`
`DISULFID`	`124 124`		`Interchain (with C-245); in linked form (By similarity).`
`DISULFID`	`245 245`		`Interchain (with C-124); in linked form (By similarity).`
`CONFLICT`	`12 12`		`P -> S (in Ref. 3; CAG46469).`
`CONFLICT`	`51 51`		`C -> Y (in Ref. 3; CAG46469).`
`STRAND`	`89 94`	`6`
`STRAND`	`97 102`	`6`
`HELIX`	`103 106`	`4`
`STRAND`	`109 115`	`7`
`HELIX`	`123 133`	`11`
`HELIX`	`135 139`	`5`
`TURN`	`140 142`	`3`
`STRAND`	`143 151`	`9`
`HELIX`	`153 160`	`8`
`HELIX`	`164 166`	`3`
`STRAND`	`176 178`	`3`
`HELIX`	`183 187`	`5`
`TURN`	`193 195`	`3`
`STRAND`	`196 198`	`3`
`STRAND`	`200 205`	`6`
`STRAND`	`209 217`	`9`
`HELIX`	`225 241`	`17`
`TURN`	`260 262`	`3`
`HELIX`	`263 267`	`5`

Sequence information

Length: 271 AA [This is the length of the unprocessed precursor]

Molecular weight: 30540 Da [This is the MW of the unprocessed precursor]

CRC64: 7E56B580049FC60F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MEALPLLAAT TPDHGRHRRL LLLPLLLFLL PAGAVQGWET EERPRTREEE CHFYAGGQVY 

        70         80         90        100        110        120 
PGEASRVSVA DHSLHLSKAK ISKPAPYWEG TAVIDGEFKE LKLTDYRGKY LVFFFYPLDF 

       130        140        150        160        170        180 
TFVCPTEIIA FGDRLEEFRS INTEVVACSV DSQFTHLAWI NTPRRQGGLG PIRIPLLSDL 

       190        200        210        220        230        240 
THQISKDYGV YLEDSGHTLR GLFIIDDKGI LRQITLNDLP VGRSVDETLR LVQAFQYTDK 

       250        260        270 
HGEVCPAGWK PGSETIIPDP AGKLKYFDKL N

Q13162 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	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