Reviewed, UniProtKB/Swiss-Prot Q13162 (PRDX4_HUMAN)

Names and origin

Protein names

Recommended name:
    Peroxiredoxin-4
    EC=1.11.1.15
Alternative name(s):
    Prx-IV
    Thioredoxin peroxidase AO372
    Thioredoxin-dependent peroxide reductase A0372
    Antioxidant enzyme AOE372
      Short name=AOE37-2

Gene names

Name:

PRDX4

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	271 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (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 structure	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. Irreversibly inactivated by overoxidation of Cys-124 (to Cys-SO3H) upon oxidative stress.
Sequence similarities	Belongs to the ahpC/TSA family. Contains 1 thioredoxin domain.

Ontologies

Keywords
Cellular component	Cytoplasm
Domain	Redox-active center
Molecular function	Antioxidant Oxidoreductase Peroxidase
PTM	Disulfide bond
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	I-kappaB phosphorylation Ref.1 Traceable author statement. Source: ProtInc cell redox homeostasis Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	thioredoxin peroxidase activity Ref.1 Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 271

271

Peroxiredoxin-4

PRO_0000135098

Regions

Domain

79 – 237

159

Thioredoxin

Compositional bias

20 – 30

11

Poly-Leu

Sites

Active site

124

1

Cysteine sulfenic acid (-SOH) intermediate By similarity

Amino acid modifications

Disulfide bond

124

Interchain (with C-245); in linked form By similarity

Disulfide bond

245

Interchain (with C-124); in linked form By similarity

Experimental info

Sequence conflict

12

1

P → S in CAG46469. Ref.3

Sequence conflict

51

1

C → Y in CAG46469. Ref.3

Secondary structure

1

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271

Helix Strand Turn

Details...

Beta strand

89 – 94

6

Beta strand

97 – 102

6

Helix

103 – 106

4

Beta strand

109 – 115

7

Helix

123 – 133

11

Helix

135 – 139

5

Turn

140 – 142

3

Beta strand

143 – 151

9

Helix

153 – 160

8

Helix

164 – 166

3

Beta strand

176 – 178

3

Helix

183 – 187

5

Turn

193 – 195

3

Beta strand

196 – 198

3

Beta strand

200 – 205

6

Beta strand

209 – 217

9

Helix

225 – 241

17

Turn

260 – 262

3

Helix

263 – 267

5

Sequences

	Sequence		Length	Mass (Da)
	Q13162-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 7E56B580049FC60F	FASTA	271	30,540
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Regulatory role for a novel human thioredoxin peroxidase in NF-kappaB activation." Jin D.-Y., Chae H.Z., Rhee S.G., Jeang K.-T. J. Biol. Chem. 272:30952-30961(1997) [PubMed: 9388242] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[4]	Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 46-66; 81-99; 140-164; 174-208; 213-223 AND 231-263, MASS SPECTROMETRY. Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[5]	"A method for detection of overoxidation of cysteines: peroxiredoxins are oxidized in vivo at the active-site cysteine during oxidative stress." Wagner E., Luche S., Penna L., Chevallet M., van Dorsselaer A., Leize-Wagner E., Rabilloud T. Biochem. J. 366:777-785(2002) [PubMed: 12059788] [Abstract] Cited for: OVEROXIDATION AT CYS-124.
[6]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

U25182 mRNA. Translation: AAB95175.1.
CR541668 mRNA. Translation: CAG46469.1.
CR541705 mRNA. Translation: CAG46506.1.
BC003609 mRNA. Translation: AAH03609.1.
BC007107 mRNA. Translation: AAH07107.1.
BC016770 mRNA. Translation: AAH16770.1.

IPI

IPI00011937.

PIR

G01790.

RefSeq

NP_006397.1.

UniGene

Hs.83383

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2PN8	X-ray	1.80	A/B/C/D/E/F/G/H/I/J	84-271	[»]

ModBase

Search...

Protein family/group databases

PeroxiBase

4530. Hs2CysPrx04.

2-D gel databases

OGP

Q13162.

REPRODUCTION-2DPAGE

IPI00011937.

Proteomic databases

PeptideAtlas

Q13162.

PRIDE

Q13162.

Genome annotation databases

Ensembl

ENSG00000123131. Homo sapiens. [Contig view]

GeneID

10549.

KEGG

hsa:10549.

NMPDR

fig|9606.3.peg.32551.

Organism-specific databases

GeneCards

GC0XP023592.

H-InvDB

HIX0016701.

HGNC

HGNC:17169. PRDX4.

HPA

CAB008659.

MIM

606506. gene.

PharmGKB

PA33725.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

Q13162.

HOVERGEN

Q13162.

OMA

Q13162. AINTEVV.

Enzyme and pathway databases

BRENDA

1.11.1.15. 247.

Gene expression databases

ArrayExpress

Q13162.

Bgee

Q13162.

CleanEx

HS_PRDX4.

GermOnline

ENSG00000123131. Homo sapiens.

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...

Other Resources

NextBio

40013.

SOURCE

Search...

Entry information

Entry name

PRDX4_HUMAN

Accession

Primary (citable) accession number: Q13162
Secondary accession number(s): Q6FHT3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	November 1, 1996
Last modified:	June 16, 2009
This is version 91 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)