Q9JKY1 (PRDX1_CRIGR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peroxiredoxin-1
EC=1.11.1.15

Alternative name(s):
Thioredoxin peroxidase 2
Short name=TPX-2

Gene names

Name:	PRDX1
Synonyms:	TDPX2

Organism

Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)

Taxonomic identifier

10029 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Cricetidae › Cricetinae › Cricetulus

Protein attributes

Sequence length	199 AA.
Sequence status	Complete.
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 H2O2 By similarity. Reduces an intramolecular disulfide bond in GDPD5 that gates the ability to GDPD5 to drive postmitotic motor neuron differentiation By similarity. Ref.1
Catalytic activity	2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.
Subunit structure	Homodimer; disulfide-linked, upon oxidation By similarity. May form heterodimers with AOP2 By similarity. Interacts with GDPD5; forms a mixed-disulfide with GDPD5 By similarity.
Subcellular location	Cytoplasm By similarity. Melanosome By similarity.
Induction	Up-regulated upon exposure to arsenate. Ref.1
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-SO2H and Cys-SO3H. Cys-SO2H is retroreduced to Cys-SOH after removal of H2O2, while Cys-SO3H 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	Acetylation Disulfide bond Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Cellular component	melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	peroxidase activity Inferred from electronic annotation. Source: UniProtKB-KW 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_0000256852
Regions
	Domain	6 – 165	160	Thioredoxin
Sites
	Active site	52	1	Cysteine sulfenic acid (-SOH) intermediate By similarity
Amino acid modifications
	Modified residue	7	1	N6-acetyllysine By similarity
	Modified residue	10	1	Phosphotyrosine By similarity
	Modified residue	16	1	N6-acetyllysine By similarity
	Modified residue	90	1	Phosphothreonine By similarity
	Modified residue	183	1	Phosphothreonine By similarity
	Modified residue	194	1	Phosphotyrosine By similarity
	Modified residue	197	1	N6-acetyllysine 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)
	Q9JKY1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: CDA6E8015E1A055E	FASTA	199	22,263
	10 20 30 40 50 60 MSSGNAKIGY PAPNFKATAV MPDGQFRDIC LSEYRGKYVV FFFYPLDFTF VCPTEIIAFS 70 80 90 100 110 120 DRAEEFKKLN CQVIGASVDS HFCHLAWINT PKKQGGLGPM NIPLVSDPKR TIAQDYGVLK 130 140 150 160 170 180 ADEGISFRGL FIIDDKGILR QITINDLPVG RSVDEILRLV QAFQFTDKHG EVCPAGWKPG 190 SDTIKPDVQK SKEYFSKQK

References

[1]	"Identification of galectin I and thioredoxin peroxidase II as two arsenic-binding proteins in Chinese hamster ovary cells." Chang K.N., Lee T.C., Tam M.F., Chen Y.C., Lee L.W., Lee S.Y., Lin P.J., Huang R.N. Biochem. J. 371:495-503(2003) [PubMed: 12519079] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, INDUCTION, FUNCTION. Tissue: Ovary.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF221841 mRNA. Translation: AAF32369.1.
RefSeq	NP_001233694.1. NM_001246765.1.
3D structure databases
HSSP	HSSP built from PDB template 1QQ2 based on UniProtKB Q63716.
ProteinModelPortal	Q9JKY1.
SMR	Q9JKY1. Positions 3-199.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	100689332.
Phylogenomic databases
HOVERGEN	HBG000286.
Family and domain databases
InterPro	IPR000866. AhpC/TSA. IPR024706. Peroxiredoxin_AhpC-typ. IPR019479. Peroxiredoxin_C. IPR012336. Thioredoxin-like_fold. [Graphical view]
Gene3D	G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
Pfam	PF10417. 1-cysPrx_C. 1 hit. PF00578. AhpC-TSA. 1 hit. [Graphical view]
PIRSF	PIRSF000239. AHPC. 1 hit.
SUPFAM	SSF52833. Thiordxn-like_fd. 1 hit.
PROSITE	PS51352. THIOREDOXIN_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PRDX1_CRIGR

Accession

Primary (citable) accession number: Q9JKY1

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	October 1, 2000
Last modified:	January 25, 2012
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program