Reviewed, UniProtKB/Swiss-Prot Q6B4U9 (PRDX1_MYOLU)

Names and origin

Protein names

Recommended name:
    Peroxiredoxin-1
    EC=1.11.1.15

Gene names

Name:	PRDX1
Synonyms:	PAG

Organism

Myotis lucifugus (Little brown bat)

Taxonomic identifier

59463 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Chiroptera › Microchiroptera › Vespertilionidae › Myotis

Protein attributes

Sequence length	199 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Involved in redox regulation of the cell. Reduces peroxides with reducing equivalents provided through the thioredoxin system but not from glutaredoxin. May play an important role in eliminating peroxides generated during metabolism. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H(2)O(2) By similarity.
Catalytic activity	2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH.
Subunit structure	Homodimer; disulfide-linked, upon oxidation By similarity. May form heterodimers with AOP2 By similarity.
Subcellular location	CytoplasmBy similarity. MelanosomeBy similarity.
Tissue specificity	Detected in heart and skeletal muscle (at protein level).
Induction	Up-regulated in hearts from hiberbating bats.
Miscellaneous	The active site is the redox-active Cys-52 oxidized to Cys-SOH. Cys-SOH rapidly reacts with Cys-173-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 By similarity. Inactivated upon oxidative stress by overoxidation of Cys-52 to Cys-SO(2)H and Cys-SO(3)H. Cys-SO(2)H is retroreduced to Cys-SOH after removal of H(2)O(2), while Cys-SO(3)H may be irreversibly oxidized By similarity.
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	Phosphoprotein
Technical term	Direct protein sequencing
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	melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	peroxiredoxin activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 199	199	Peroxiredoxin-1		PRO_0000256853
Regions
	Domain	6 – 165	160	Thioredoxin
Sites
	Active site	52	1	Cysteine sulfenic acid (-SOH) intermediate By similarity
Amino acid modifications
	Modified residue	90	1	Phosphothreonine By similarity
	Modified residue	183	1	Phosphothreonine By similarity
	Modified residue	194	1	Phosphotyrosine By similarity
	Disulfide bond	52		Interchain (with C-173); in linked form By similarity
	Disulfide bond	173		Interchain (with C-52); in linked form By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6B4U9-1 [UniParc]. Last modified September 13, 2004. Version 1. Checksum: A75F3D21C40322CD	FASTA	199	22,124
	10 20 30 40 50 60 MSSGNAKIGH PAPNFKATAV MPDGQFKDIS LSDYKGKYVV FFFYPLDFTF VCPTEIIAFS 70 80 90 100 110 120 DRAEEFKKIN CQVIGASVDS HFCHLAWINT PKKQGGLGPM NIPLVSDPKR TIAQDYGVLK 130 140 150 160 170 180 ADEGISFRGL FIIDDKGILR QITVNDLPVG RSVDETLRLV QAFQFTDKHG EVCPAGWKPG 190 SDTIKPDVQK SKEYFSKQK

References

[1]

"Up-regulation of a thioredoxin peroxidase-like protein, proliferation-associated gene, in hibernating bats." Eddy S.F., McNally J.D., Storey K.B. Arch. Biochem. Biophys. 435:103-111(2005) [PubMed: 15680912] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, TISSUE SPECIFICITY, INDUCTION. Tissue: Heart.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AY680839 mRNA. Translation: AAT79401.1.
3D structure databases
SMR	Q6B4U9. Positions 3-175.
ModBase	Search...
Genome annotation databases
Ensembl	ENSMLUG00000005673. Myotis lucifugus. [Contig view]
Phylogenomic databases
HOVERGEN	Q6B4U9.
Family and domain databases
InterPro	IPR000866. AhpC-TSA. IPR012335. Thioredoxin_fold. [Graphical view]
Gene3D	G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
Pfam	PF00578. AhpC-TSA. 1 hit. [Graphical view]
PROSITE	PS51352. THIOREDOXIN_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PRDX1_MYOLU

Accession

Primary (citable) accession number: Q6B4U9

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	September 13, 2004
Last modified:	November 25, 2008
This is version 30 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)