P30044 (PRDX5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peroxiredoxin-5, mitochondrial
EC=1.11.1.15

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

Gene names

Name:	PRDX5
Synonyms:	ACR1
ORF Names:	SBBI10

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › 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	Isoform Mitochondrial: Mitochondrion Ref.3. Isoform Cytoplasmic+peroxisomal: 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	Acetylation Disulfide bond
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	NADPH oxidation Inferred from direct assay Ref.5. Source: UniProtKB cellular response to reactive oxygen species Inferred from mutant phenotype PubMed 18262354. Source: UniProtKB hydrogen peroxide catabolic process Inferred from direct assay Ref.2. Source: UniProtKB inflammatory response Traceable author statement Ref.3. Source: UniProtKB negative regulation of apoptotic process Inferred from mutant phenotype PubMed 18262354. Source: UniProtKB negative regulation of oxidoreductase activity Inferred from direct assay PubMed 15280035. Source: UniProtKB negative regulation of transcription from RNA polymerase III promoter Inferred from direct assay Ref.1. Source: UniProtKB positive regulation of collagen biosynthetic process Inferred from direct assay PubMed 15276323. Source: UniProtKB reactive nitrogen species metabolic process Inferred from direct assay PubMed 15280035. Source: UniProtKB regulation of apoptosis involved in tissue homeostasis Inferred from direct assay PubMed 15276323. Source: UniProtKB
Cellular_component	cytoplasmic vesicle Inferred from direct assay Ref.1. Source: UniProtKB cytosol Inferred from direct assay PubMed 18262354. Source: UniProtKB mitochondrion Inferred from direct assay Ref.3Ref.5PubMed 18262354. Source: UniProtKB nucleus Inferred from direct assay Ref.1PubMed 15785239. Source: UniProtKB perinuclear region of cytoplasm Inferred from direct assay Ref.1. Source: UniProtKB peroxisomal matrix Inferred from direct assay Ref.2. Source: UniProtKB peroxisome Inferred from direct assay Ref.3. Source: UniProtKB
Molecular_function	RNA polymerase III regulatory region DNA binding Inferred from direct assay Ref.1. Source: UniProtKB antioxidant activity Inferred from direct assay Ref.2. Source: UniProtKB cysteine-type endopeptidase inhibitor activity involved in apoptotic process Inferred from mutant phenotype PubMed 18262354. Source: UniProtKB peroxidase activity Inferred from direct assay Ref.3. Source: UniProtKB peroxiredoxin activity Inferred from electronic annotation. Source: EC peroxynitrite reductase activity Inferred from direct assay PubMed 15280035. Source: UniProtKB protein dimerization activity Inferred from direct assay PubMed 15046979Ref.5. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 3 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.

Isoform 3 (identifier: P30044-3)

The sequence of this isoform differs from the canonical sequence as follows:
     102-145: Missing.

Note: No experimental confirmation available.

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

Modified residue

83

1

N6-acetyllysine Ref.14

Disulfide bond

100 ↔ 204

Redox-active

Natural variations

Alternative sequence

1 – 52

52

Missing in isoform Cytoplasmic+peroxisomal.

VSP_018829

Alternative sequence

102 – 145

44

Missing in isoform 3.

VSP_045783

Natural variant

33

1

Y → C. Ref.1 Ref.3 Ref.4 Ref.7 Ref.9 Ref.10 Ref.12
Corresponds to variant rs7938623 [ dbSNP | Ensembl ].

VAR_025049

Natural variant

157

1

F → L in a breast cancer sample; somatic mutation. Ref.17

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

69 – 71

3

Helix

72 – 74

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

122 – 129

8

Helix

131 – 140

10

Turn

144 – 146

3

Beta strand

148 – 151

4

Helix

156 – 161

6

Helix

167 – 169

3

Helix

170 – 173

4

Beta strand

181 – 186

6

Beta strand

189 – 195

7

Helix

207 – 213

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform Mitochondrial [UniParc]. Last modified January 11, 2011. Version 4. Checksum: DA1DEB21120254EE	FASTA	214	22,086
	10 20 30 40 50 60 MGLAGVCALR RSAGYILVGG AGGQSAAAAA RRYSEGEWAS 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 [UniParc]. 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
	Isoform 3 [UniParc]. Checksum: 29984B81B33F82C1	FASTA	170	17,454
	10 20 30 40 50 60 MGLAGVCALR RSAGYILVGG AGGQSAAAAA RRYSEGEWAS GGVRSFSRAA AAMAPIKVGD 70 80 90 100 110 120 AIPAVEVFEG EPGNKVNLAE LFKGKKGVLF GVPGAFTPGC SKVRLLADPT GAFGKETDLL 130 140 150 160 170 LDDSLVSIFG NRRLKRFSMV VQDGIVKALN VEPDGTGLTC SLAPNIISQL

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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MITOCHONDRIAL), VARIANT CYS-33.
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CYTOPLASMIC+PEROXISOMAL), 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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MITOCHONDRIAL), PROTEIN SEQUENCE OF 54-90, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, CHARACTERIZATION, VARIANT CYS-33. 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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CYTOPLASMIC+PEROXISOMAL), VARIANT CYS-33.
[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] [Europe PMC] [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] (ISOFORM CYTOPLASMIC+PEROXISOMAL).
[7]	Zhang W., Li N., Wan T., Cao X. Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MITOCHONDRIAL), VARIANT CYS-33.
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM CYTOPLASMIC+PEROXISOMAL). 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] (ISOFORM MITOCHONDRIAL), VARIANT CYS-33.
[10]	NIEHS SNPs program Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT CYS-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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS MITOCHONDRIAL AND 3), VARIANT CYS-33. 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] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 54-63. Tissue: Liver.
[14]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-83, MASS SPECTROMETRY.
[15]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]	"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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
[17]	"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] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-157.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF231705 mRNA. Translation: AAF78899.1.
AF124993 mRNA. Translation: AAF27531.1.
AF110731 mRNA. Translation: AAF03750.1.
AF197952 mRNA. Translation: AAF04856.1.
AJ249483 mRNA. Translation: CAB62210.1.
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.
BC143849 mRNA. Translation: AAI43850.1.

IPI

IPI00024915.
IPI00375306.
IPI00759663.

RefSeq

NP_036226.1. NM_012094.4.
NP_857634.1. NM_181651.2.
NP_857635.1. NM_181652.2.

UniGene

Hs.502823.

3D structure databases

PDBe
RCSB PDB
PDBj

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/C	54-214	[»]
2VL3	X-ray	1.83	A/B/C	54-214	[»]
2VL9	X-ray	2.70	A/B/C/D	54-214	[»]
3MNG	X-ray	1.45	A	54-214	[»]

ProteinModelPortal

P30044.

SMR

P30044. Positions 54-214.

ModBase

Search...

Protein-protein interaction databases

IntAct

P30044. 4 interactions.

MINT

MINT-5002532.

STRING

9606.ENSP00000265462.

Protein family/group databases

PeroxiBase

4448. HsPrxV.

PTM databases

PhosphoSite

P30044.

Polymorphism databases

DMDM

20141713.

2D gel databases

OGP

P30044.

REPRODUCTION-2DPAGE

IPI00759663.

SWISS-2DPAGE

P30044.

UCD-2DPAGE

P30044.

Proteomic databases

PaxDb

P30044.

PRIDE

P30044.

Protocols and materials databases

DNASU

25824.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000265462; ENSP00000265462; ENSG00000126432.
ENST00000352435; ENSP00000335334; ENSG00000126432.

GeneID

25824.

KEGG

hsa:25824.

UCSC

uc001nzu.3. human.

Organism-specific databases

CTD

25824.

GeneCards

GC11P064085.

HGNC

HGNC:9355. PRDX5.

HPA

CAB008661.

MIM

606583. gene.

neXtProt

NX_P30044.

PharmGKB

PA33726.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0678.

HOGENOM

HOG000255884.

HOVERGEN

HBG053675.

InParanoid

P30044.

KO

K11187.

OMA

VCALRRS.

PhylomeDB

P30044.

Gene expression databases

ArrayExpress

P30044.

Bgee

P30044.

CleanEx

HS_PRDX5.

Genevestigator

P30044.

GermOnline

ENSG00000126432. Homo sapiens.

Family and domain databases

Gene3D

3.40.30.10. 1 hit.

InterPro

IPR013740. Redoxin.
IPR012336. Thioredoxin-like_fold.
[Graphical view]

Pfam

PF08534. Redoxin. 1 hit.
[Graphical view]

SUPFAM

SSF52833. Thiordxn-like_fd. 1 hit.

PROSITE

PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

PRDX5. human.

DrugBank

DB00995. Auranofin.

EvolutionaryTrace

P30044.

GenomeRNAi

25824.

NextBio

35462534.

SOURCE

Search...

Entry information

Entry name

PRDX5_HUMAN

Accession

Primary (citable) accession number: P30044
Secondary accession number(s): A6NG06 , B7ZLJ4, Q14CK0, Q6IAF2, Q9UBU5, Q9UJU4, Q9UKX4

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	January 11, 2011
Last modified:	May 1, 2013
This is version 142 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.