P99029 (PRDX5_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peroxiredoxin-5, mitochondrial
EC=1.11.1.15

Alternative name(s):
Antioxidant enzyme B166
Short name=AOEB166
Liver tissue 2D-page spot 2D-0014IV
PLP
Peroxiredoxin V
Short name=Prx-V
Peroxisomal antioxidant enzyme
Thioredoxin peroxidase PMP20
Thioredoxin reductase

Gene names

Name:	Prdx5
Synonyms:	Prdx6

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	210 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.
Tissue specificity	Widely expressed.
Sequence similarities	Belongs to the peroxiredoxin 2 family. Contains 1 thioredoxin domain.

Ontologies

Keywords
Cellular component	Cytoplasm Mitochondrion Peroxisome
Coding sequence diversity	Alternative initiation
Domain	Redox-active center Transit peptide
Molecular function	Antioxidant Oxidoreductase Peroxidase
PTM	Acetylation Disulfide bond
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	NADPH oxidation Inferred from electronic annotation. Source: Compara hydrogen peroxide catabolic process Inferred from sequence or structural similarity Ref.2. Source: UniProtKB negative regulation of apoptotic process Inferred from electronic annotation. Source: Compara negative regulation of oxidoreductase activity Inferred from electronic annotation. Source: Compara negative regulation of transcription from RNA polymerase III promoter Inferred from electronic annotation. Source: Compara positive regulation of collagen biosynthetic process Inferred from electronic annotation. Source: Compara reactive nitrogen species metabolic process Inferred from electronic annotation. Source: Compara regulation of apoptosis involved in tissue homeostasis Inferred from electronic annotation. Source: Compara
Cellular_component	cytoplasmic vesicle Inferred from electronic annotation. Source: Compara cytosolic part Inferred from electronic annotation. Source: Compara mitochondrion Inferred from direct assay PubMed 14651853PubMed 18614015. Source: MGI nucleus Inferred from electronic annotation. Source: Compara perinuclear region of cytoplasm Inferred from electronic annotation. Source: Compara peroxisomal matrix Inferred from sequence or structural similarity Ref.2. Source: UniProtKB
Molecular_function	RNA polymerase III regulatory region DNA binding Inferred from electronic annotation. Source: Compara antioxidant activity Inferred from sequence or structural similarity Ref.2. Source: UniProtKB cysteine-type endopeptidase inhibitor activity involved in apoptotic process Inferred from electronic annotation. Source: Compara peroxidase activity Inferred from electronic annotation. Source: UniProtKB-KW peroxynitrite reductase activity Inferred from electronic annotation. Source: Compara receptor binding Inferred from sequence or structural similarity Ref.2. Source: UniProtKB
Complete GO annotation...

Alternative products

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

Isoform Mitochondrial (identifier: P99029-1)

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: P99029-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-48: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 48	48	Mitochondrion Potential
	Chain	49 – 210	162	Peroxiredoxin-5, mitochondrial		PRO_0000023795
Regions
	Domain	52 – 210	159	Thioredoxin
	Motif	208 – 210	3	Microbody targeting signal By similarity
Sites
	Active site	96	1	Cysteine sulfenic acid (-SOH) intermediate Potential
Amino acid modifications
	Modified residue	79	1	N6-acetyllysine By similarity
	Disulfide bond	96 ↔ 200		Redox-active By similarity
Natural variations
	Alternative sequence	1 – 48	48	Missing in isoform Cytoplasmic+peroxisomal.		VSP_018830
Experimental info
	Sequence conflict	55	1	G → D AA sequence Ref.7
	Sequence conflict	83 – 102	20	GVLFG…KTHLP → VFCLESLGHLHLAVLRPTA in AAF21016. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform Mitochondrial [UniParc]. Last modified February 21, 2002. Version 2. Checksum: E944104CC468BDD8	FASTA	210	21,897
	10 20 30 40 50 60 MLQLGLRVLG CKASSVLRAS TCLAGRAGRK EAGWECGGAR SFSSSAVTMA PIKVGDAIPS 70 80 90 100 110 120 VEVFEGEPGK KVNLAELFKG KKGVLFGVPG AFTPGCSKTH LPGFVEQAGA LKAKGAQVVA 130 140 150 160 170 180 CLSVNDVFVI EEWGRAHQAE GKVRLLADPT GAFGKATDLL LDDSLVSLFG NRRLKRFSMV 190 200 210 IDNGIVKALN VEPDGTGLTC SLAPNILSQL
	Isoform Cytoplasmic+peroxisomal [UniParc]. Checksum: EE32FFB439418B21	FASTA	162	17,015
	10 20 30 40 50 60 MAPIKVGDAI PSVEVFEGEP GKKVNLAELF KGKKGVLFGV PGAFTPGCSK THLPGFVEQA 70 80 90 100 110 120 GALKAKGAQV VACLSVNDVF VIEEWGRAHQ AEGKVRLLAD PTGAFGKATD LLLDDSLVSL 130 140 150 160 FGNRRLKRFS MVIDNGIVKA LNVEPDGTGL TCSLAPNILS QL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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], CHARACTERIZATION.
[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], 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, CHARACTERIZATION. Strain: C3H/HeJ. Tissue: Lung.
[4]	"Molecular cloning and characterization of the mouse Peroxiredoxin V gene." Lee T.H., Kim S.J., Kang S.W., Lee K.K., Rhee S.G., Yu D.Y. Biochem. Biophys. Res. Commun. 270:356-362(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Kidney.
[6]	"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]. Tissue: Mammary tumor.
[7]	Sanchez J.-C., Rouge V., Frutiger S., Hughes G.J., Yan J.X., Hoogland C., Appel R.D., Binz P.-A., Hochstrasser D.F., Cowthorne M. Submitted (AUG-1998) to UniProtKB Cited for: PROTEIN SEQUENCE OF 50-61. Tissue: Liver.
[8]	Lubec G., Klug S., Kang S.U. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 72-79; 83-112 AND 145-172, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain and Hippocampus.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF197951 mRNA. Translation: AAF04855.1. AF124994 mRNA. Translation: AAF27532.1. AF110733 mRNA. Translation: AAG13450.1. AF208730, AF208729 Genomic DNA. Translation: AAF21016.1. AK002383 mRNA. Translation: BAB22058.1. AK003332 mRNA. Translation: BAB22720.1. BC008174 mRNA. Translation: AAH08174.1.
IPI	IPI00129517. IPI00759999.
PIR	JC7239.
RefSeq	NP_036151.1. NM_012021.2.
UniGene	Mm.279782.
3D structure databases
ProteinModelPortal	P99029.
SMR	P99029. Positions 50-210.
ModBase	Search...
Protein family/group databases
PeroxiBase	4453. MmPrxV.
PTM databases
PhosphoSite	P99029.
2D gel databases
REPRODUCTION-2DPAGE	P99029.
SWISS-2DPAGE	P99029.
Proteomic databases
PaxDb	P99029.
PRIDE	P99029.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000025904; ENSMUSP00000025904; ENSMUSG00000024953.
GeneID	54683.
KEGG	mmu:54683.
Organism-specific databases
CTD	25824.
MGI	MGI:1859821. Prdx5.
Phylogenomic databases
eggNOG	COG0678.
GeneTree	ENSGT00390000018173.
HOGENOM	HOG000255884.
HOVERGEN	HBG053675.
InParanoid	P99029.
KO	K11187.
OMA	VCALRRS.
OrthoDB	EOG4PZJ7W.
Gene expression databases
ArrayExpress	P99029.
Bgee	P99029.
CleanEx	MM_PRDX5. MM_PRDX6.
Genevestigator	P99029.
GermOnline	ENSMUSG00000024953. Mus musculus.
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
NextBio	311536.
SOURCE	Search...

Entry information

Entry name

PRDX5_MOUSE

Accession

Primary (citable) accession number: P99029
Secondary accession number(s): Q9QX45, Q9QZ75

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	February 21, 2002
Last modified:	April 3, 2013
This is version 121 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program