Reviewed, UniProtKB/Swiss-Prot P30044 (PRDX5_HUMAN)

Names and origin

Protein names

Recommended name:
    Peroxiredoxin-5, mitochondrial
    EC=1.11.1.15
Alternative name(s):
    Prx-V
    Peroxisomal antioxidant enzyme
    PLP
    Thioredoxin reductase
    Thioredoxin peroxidase PMP20
    Antioxidant enzyme B166
      Short name=AOEB166
    TPx type VI
    Liver tissue 2D-page spot 71B
    Alu corepressor 1

Gene names

Name:	PRDX5
Synonyms:	ACR1
ORF Names:	SBBI10

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	214 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Reduces hydrogen peroxide and alkyl hydroperoxides with reducing equivalents provided through the thioredoxin system. Involved in intracellular redox signaling.
Catalytic activity	2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.
Subunit structure	Monomer.
Subcellular location	Mitochondrion. Cytoplasm. Peroxisome. Ref.3
Tissue specificity	Widely expressed. Ref.3
Sequence similarities	Belongs to the peroxiredoxin 2 family. Contains 1 thioredoxin domain.
Sequence caution	The sequence AAF17200.1 differs from that shown. Reason: Frameshift at positions 14 and 30.

Ontologies

Keywords
Cellular component	Cytoplasm Mitochondrion Peroxisome
Coding sequence diversity	Alternative initiation Polymorphism
Domain	Redox-active center Transit peptide
Molecular function	Antioxidant Oxidoreductase Peroxidase
PTM	Disulfide bond
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro cellular response to reactive oxygen species Inferred from mutant phenotype. Source: UniProtKB inflammatory response Ref.3 Traceable author statement. Source: UniProtKB negative regulation of apoptosis Inferred from mutant phenotype. Source: UniProtKB oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosolic part Inferred from direct assay. Source: UniProtKB mitochondrion Ref.3 Inferred from direct assay. Source: UniProtKB peroxisome Ref.3 Inferred from direct assay. Source: UniProtKB
Molecular function	caspase inhibitor activity Inferred from mutant phenotype. Source: UniProtKB peroxiredoxin activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]

Isoform Mitochondrial (identifier: P30044-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform Cytoplasmic+peroxisomal (identifier: P30044-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-52: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 52

52

Mitochondrion Potential

Chain

53 – 214

162

Peroxiredoxin-5, mitochondrial

PRO_0000023793

Regions

Domain

56 – 214

159

Thioredoxin

Motif

212 – 214

3

Microbody targeting signal By similarity

Sites

Active site

100

1

Cysteine sulfenic acid (-SOH) intermediate Potential

Amino acid modifications

Disulfide bond

100 ↔ 204

Redox-active

Natural variations

Alternative sequence

1 – 52

52

Missing in isoform Cytoplasmic+peroxisomal.

VSP_018829

Natural variant

33

1

C → Y: dbSNP rs7938623. Ref.10

VAR_025049

Natural variant

157

1

F → L in a breast cancer sample; somatic mutation. Ref.16

VAR_036406

Experimental info

Mutagenesis

100

1

C → S: Complete loss of activity.

Mutagenesis

125

1

C → S: No change in activity.

Mutagenesis

204

1

C → S: Complete loss of activity.

Sequence conflict

141

1

H → T in AAF04856. Ref.4

Secondary structure

1

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214

Helix Strand Turn

Details...

Beta strand

66 – 68

3

Beta strand

75 – 77

3

Helix

78 – 81

4

Turn

82 – 84

3

Beta strand

85 – 91

7

Helix

98 – 102

5

Helix

104 – 110

7

Helix

112 – 116

5

Turn

117 – 119

3

Beta strand

120 – 129

10

Helix

131 – 140

10

Turn

144 – 146

3

Beta strand

148 – 151

4

Helix

156 – 161

6

Helix

170 – 173

4

Beta strand

181 – 186

6

Beta strand

189 – 195

7

Helix

207 – 211

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform Mitochondrial [UniParc]. Last modified February 21, 2002. Version 3. Checksum: 2FF211210809823E	FASTA	214	22,026
	10 20 30 40 50 60 MGLAGVCALR RSAGYILVGG AGGQSAAAAA RRCSEGEWAS GGVRSFSRAA AAMAPIKVGD 70 80 90 100 110 120 AIPAVEVFEG EPGNKVNLAE LFKGKKGVLF GVPGAFTPGC SKTHLPGFVE QAEALKAKGV 130 140 150 160 170 180 QVVACLSVND AFVTGEWGRA HKAEGKVRLL ADPTGAFGKE TDLLLDDSLV SIFGNRRLKR 190 200 210 FSMVVQDGIV KALNVEPDGT GLTCSLAPNI ISQL
	Isoform Cytoplasmic+peroxisomal. Checksum: 370DF621012F880D	FASTA	162	17,031
	10 20 30 40 50 60 MAPIKVGDAI PAVEVFEGEP GNKVNLAELF KGKKGVLFGV PGAFTPGCSK THLPGFVEQA 70 80 90 100 110 120 EALKAKGVQV VACLSVNDAF VTGEWGRAHK AEGKVRLLAD PTGAFGKETD LLLDDSLVSI 130 140 150 160 FGNRRLKRFS MVVQDGIVKA LNVEPDGTGL TCSLAPNIIS QL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A novel human DNA-binding protein with sequence similarity to a subfamily of redox proteins which is able to repress RNA-polymerase-III-driven transcription of the Alu-family retroposons in vitro." Kropotov A., Sedova V., Ivanov V., Sazeeva N., Tomilin A., Krutilina R., Oei S.L., Griesenbeck J., Buchlow G., Tomilin N. Eur. J. Biochem. 260:336-346(1999) [PubMed: 10095767] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Characterization of human and murine PMP20 peroxisomal proteins that exhibit antioxidant activity in vitro." Yamashita H., Avraham S., Jiang S., London R., Van Veldhoven P.P., Subramani S., Rogers R.A., Avraham H. J. Biol. Chem. 274:29897-29904(1999) [PubMed: 10514471] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
[3]	"Cloning and characterization of AOEB166, a novel mammalian antioxidant enzyme of the peroxiredoxin family." Knoops B., Clippe A., Bogard C., Arsalane K., Wattiez R., Hermans C., Duconseille E., Falmagne P., Bernard A. J. Biol. Chem. 274:30451-30458(1999) [PubMed: 10521424] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 54-90, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, CHARACTERIZATION. Tissue: Lung.
[4]	"Mouse peroxiredoxin V is a thioredoxin peroxidase that inhibits p53-induced apoptosis." Zhou Y., Kok K.H., Chun A.C.S., Wong C.M., Wu H.W., Lin M.C.M., Fung P.C.W., Kung H.-F., Jin D.-Y. Biochem. Biophys. Res. Commun. 268:921-927(2000) [PubMed: 10679306] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]	"Identification of a new type of mammalian peroxiredoxin that forms an intramolecular disulfide as a reaction intermediate." Seo M.S., Kang S.W., Kim K., Baines I.C., Lee T.H., Rhee S.G. J. Biol. Chem. 275:20346-20354(2000) [PubMed: 10751410] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS, CHARACTERIZATION.
[6]	"A new type of human thiol peroxidase (Human TPx type VI)." Kim I.H., Jeong W. Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[7]	Zhang W., Li N., Wan T., Cao X. Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[8]	"Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning." Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M. , Zhou J., Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L. Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000) [PubMed: 10931946] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Adrenal gland.
[9]	"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].
[10]	NIEHS SNPs program Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT TYR-33.
[11]	"Human chromosome 11 DNA sequence and analysis including novel gene identification." Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y. Nature 440:497-500(2006) [PubMed: 16554811] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[12]	"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 and Medulla oblongata.
[13]	"Human liver protein map: a reference database established by microsequencing and gel comparison." Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F., Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R., Appel R.D., Hughes G.J. Electrophoresis 13:992-1001(1992) [PubMed: 1286669] [Abstract] Cited for: PROTEIN SEQUENCE OF 54-63. Tissue: Liver.
[14]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[15]	"Crystal structure of human peroxiredoxin 5, a novel type of mammalian peroxiredoxin at 1.5-A resolution." Declercq J.-P., Evrard C., Clippe A., Stricht D.V., Bernard A., Knoops B. J. Mol. Biol. 311:751-759(2001) [PubMed: 11518528] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
[16]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-157.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBLGenBankDDBJ

AJ249483 mRNA. Translation: CAB62210.1.
AF231705 mRNA. Translation: AAF78899.1.
AF124993 mRNA. Translation: AAF27531.1.
AF110731 mRNA. Translation: AAF03750.1.
AF197952 mRNA. Translation: AAF04856.1.
AF242525 mRNA. Translation: AAF99605.1.
AF112212 mRNA. Translation: AAF17200.1. Frameshift.
CR457203 mRNA. Translation: CAG33484.1.
DQ247769 Genomic DNA. Translation: ABB05181.1.
AP001453 Genomic DNA. No translation available.
AP003774 Genomic DNA. No translation available.
BC110983 mRNA. Translation: AAI10984.1.
BC113723 mRNA. Translation: AAI13724.1.
BC113725 mRNA. Translation: AAI13726.1.

IPI

IPI00024915.
IPI00759663.

RefSeq

NP_036226.1.
NP_857634.1.
NP_857635.1.

UniGene

Hs.502823

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1H4O	X-ray	1.95	A/B/C/D/E/F/G/H	54-214	[»]
1HD2	X-ray	1.50	A	54-214	[»]
1OC3	X-ray	2.00	A/B/C	54-214	[»]
1URM	X-ray	1.70	A	54-214	[»]
2VL2	X-ray	1.92	A/B	54-214	[»]
			C	54-214	[»]
2VL3	X-ray	1.83	A/B/C	54-214	[»]
2VL9	X-ray	2.70	A/B/C/D	54-214	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P30044. 4 interactions.

Protein family/group databases

PeroxiBase

4448. HsPrxV.

PTM databases

PhosphoSite

P30044.

2-D gel databases

SWISS-2DPAGE

P30044.

OGP

P30044.

REPRODUCTION-2DPAGE

IPI00759663.

Proteomic databases

PRIDE

P30044.

Genome annotation databases

Ensembl

ENSG00000126432. Homo sapiens. [Contig view]

GeneID

25824.

KEGG

hsa:25824.

Organism-specific databases

GeneCards

GC11P063842.

H-InvDB

HIX0021287.

HGNC

HGNC:9355. PRDX5.

HPA

CAB008661.

MIM

606583. gene.

PharmGKB

PA33726.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P30044.

HOVERGEN

P30044.

Enzyme and pathway databases

BRENDA

1.11.1.15. 247.

Gene expression databases

ArrayExpress

P30044.

Bgee

P30044.

CleanEx

HS_PRDX5.

GermOnline

ENSG00000126432. Homo sapiens.

Family and domain databases

InterPro

IPR013740. Redoxin.
IPR017936. Thioredoxin-like.
IPR012335. Thioredoxin_fold.
[Graphical view]

Gene3D

G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.

Pfam

PF08534. Redoxin. 1 hit.
[Graphical view]

PROSITE

PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00995. Auranofin.

NextBio

47091.

SOURCE

Search...

Entry information

Entry name

PRDX5_HUMAN

Accession

Primary (citable) accession number: P30044
Secondary accession number(s): Q14CK0 , Q6IAF2, Q9UBU5, Q9UJU4, Q9UKX4

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	February 21, 2002
Last modified:	June 16, 2009
This is version 101 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)