Q5E947 (PRDX1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peroxiredoxin-1
EC=1.11.1.15

Gene names

Name:

PRDX1

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	199 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript 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.
Catalytic activity	2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.
Subunit structure	Homodimer; disulfide-linked, upon oxidation. 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.
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	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	regulation of NF-kappaB import into nucleus Inferred from sequence or structural similarity. Source: AgBase
Cellular component	melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell
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_0000135075
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	16	1	N6-acetyllysine By similarity
	Modified residue	27	1	N6-acetyllysine By similarity
	Modified residue	35	1	N6-acetyllysine 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)
	Q5E947 [UniParc]. Last modified March 15, 2005. Version 1. Checksum: CFEE26A9F10B0483	FASTA	199	22,210
	10 20 30 40 50 60 MSSGNAKIGH RAPQFKATAV MPDGQFKDIS LADYKGKYVV FFFYPLDFTF VCPTEIIAFS 70 80 90 100 110 120 DRAEEFKKLN CQVIGASVDS HFCHLAWINT PKKQGGLGPM NIPLISDPKR TIAQDYGVLK 130 140 150 160 170 180 ADEGISFRGL FIIDDKGILR QITINDLPVG RSVDETLRLV QAFQFTDKHG EVCPAGWKPG 190 SDTIKPDVQK SKEYFSKQK

References

[1]	"Characterization of 954 bovine full-CDS cDNA sequences." Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L. BMC Genomics 6:166-166(2005) [PubMed: 16305752] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[2]	NIH - Mammalian Gene Collection (MGC) project Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Ascending colon.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BT021073 mRNA. Translation: AAX09090.1. BC148009 mRNA. Translation: AAI48010.1.
IPI	IPI00686092.
UniGene	Bt.65324.
3D structure databases
ProteinModelPortal	Q5E947.
SMR	Q5E947. Positions 3-199.
ModBase	Search...
Protein-protein interaction databases
STRING	Q5E947.
Protein family/group databases
PeroxiBase	4494. Bt2CysPrx01.
Proteomic databases
PRIDE	Q5E947.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSBTAT00000004751; ENSBTAP00000004751; ENSBTAG00000003642.
Phylogenomic databases
eggNOG	maNOG10288.
HOVERGEN	HBG000286.
InParanoid	Q5E947.
OrthoDB	EOG4V6ZHJ.
PhylomeDB	Q5E947.
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_BOVIN

Accession

Primary (citable) accession number: Q5E947
Secondary accession number(s): A6QLL7

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 24, 2005
Last sequence update:	March 15, 2005
Last modified:	November 16, 2011
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program