Reviewed, UniProtKB/Swiss-Prot Q9GLW7 (PRDX5_CERAE)

Names and origin

Protein names

Recommended name:
    Peroxiredoxin-5, mitochondrial
    EC=1.11.1.15
Alternative name(s):
    Prx-V
    Thioredoxin reductase

Gene names

Name:

PRDX5

Organism

Cercopithecus aethiops (Green monkey) (Grivet)

Taxonomic identifier

9534 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Cercopithecidae › Cercopithecinae › Chlorocebus

Protein attributes

Sequence length	215 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Reduces hydrogen peroxide and alkyl hydroperoxides with reducing equivalents provided through the thioredoxin system. Involved in intracellular redox signaling By similarity.
Catalytic activity	2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.
Subunit structure	Monomer By similarity.
Subcellular location	Mitochondrion By similarity. Cytoplasm By similarity. Peroxisome By similarity.
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	Disulfide bond
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell peroxisome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	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: Q9GLW7-1)

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: Q9GLW7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-53: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 53	53	Mitochondrion Potential
	Chain	54 – 215	162	Peroxiredoxin-5, mitochondrial		PRO_0000023790
Regions
	Domain	57 – 215	159	Thioredoxin
	Motif	213 – 215	3	Microbody targeting signal By similarity
Sites
	Active site	101	1	Cysteine sulfenic acid (-SOH) intermediate Potential
Amino acid modifications
	Disulfide bond	101 ↔ 205		Redox-active By similarity
Natural variations
	Alternative sequence	1 – 53	53	Missing in isoform Cytoplasmic+peroxisomal.		VSP_018828

Sequences

	Sequence		Length	Mass (Da)
	Isoform Mitochondrial [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 7C9E45C1B9517B78	FASTA	215	22,237
	10 20 30 40 50 60 MGLAGVCVLR RSAGYILGGA ARQSVAATAA ARRRSEGGWA SGGVRSFSRA AAAMAPIKVG 70 80 90 100 110 120 DAIPAVEVFE GEPGNKVNLA ELFKGKKGVL FGVPGAFTPG CSKTHLPGFV EQAEALKAKG 130 140 150 160 170 180 VQVLACLSVN DAFVTGEWGR AHKAEGKVRL LADPTGAFGK ETDLLLDDSL VSIFGNRRLK 190 200 210 RFSMVVQDGI VKALNVEPDG TGLTCSLAPS IISQL
	Isoform Cytoplasmic+peroxisomal. Checksum: 23A6163ABB25D9B7	FASTA	162	17,018
	10 20 30 40 50 60 MAPIKVGDAI PAVEVFEGEP GNKVNLAELF KGKKGVLFGV PGAFTPGCSK THLPGFVEQA 70 80 90 100 110 120 EALKAKGVQV LACLSVNDAF VTGEWGRAHK AEGKVRLLAD PTGAFGKETD LLLDDSLVSI 130 140 150 160 FGNRRLKRFS MVVQDGIVKA LNVEPDGTGL TCSLAPSIIS QL

References

[1]	"Cloning and characterization of COS-7 AOEB166/PRDX5." Knoops B., Cherif H. Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF110736 mRNA. Translation: AAG13453.2.
3D structure databases
HSSP	HSSP built from PDB template 1HD2 based on UniProtKB P30044.
SMR	Q9GLW7. Positions 55-215.
ModBase	Search...
Phylogenomic databases
HOVERGEN	Q9GLW7.
Enzyme and pathway databases
BRENDA	1.11.1.15. 2052.
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...

Entry information

Entry name

PRDX5_CERAE

Accession

Primary (citable) accession number: Q9GLW7

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2002
Last sequence update:	March 1, 2001
Last modified:	June 16, 2009
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)