UniProt Accession

 PRDX3_HUMAN; P30048; B2R7Z0; D3DRC9; P35690; Q0D2H1; Q13776; Q5T5V2; Q96HK4 

Genbank Protein ID

 D49396; AK313169; CR450344; BT020007; DQ298752; AL355861; CH471066; BC002685; BC007062; BC008435; BC009601; BC021691; BC022373; BC059169; BC111397 

Genbank Nucleotide ID

 BAA08389.1; BAG35987.1; CAG29340.1; AAV38810.1; ABB84468.1; CAI15802.1; EAW49399.1; AAH02685.1; AAH07062.1; AAH08435.1; AAH09601.1; AAH21691.1; AAH22373.1; AAH59169.1; AAI11398.1 

Protein Name

 Thioredoxin-dependent peroxide reductase, mitochondrial 

Protein Synonyms/Alias

 Antioxidant protein 1; AOP-1; HBC189; Peroxiredoxin III; Prx-III; Peroxiredoxin-3; Protein MER5 homolog 

Gene Name

 PRDX3 

Gene Synonyms/Alias

 AOP1 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
83	AVVNGEFKDLSLDDF	acetylation	[1]
83	AVVNGEFKDLSLDDF	ubiquitination	[2, 3, 4]
91	DLSLDDFKGKYLVLF	acetylation	[5]
91	DLSLDDFKGKYLVLF	ubiquitination	[2, 4]
149	AWINTPRKNGGLGHM	ubiquitination	[2, 3, 4, 6]
196	IDPNGVIKHLSVNDL	ubiquitination	[2, 4]
241	TPDSPTIKPSPAASK	ubiquitination	[6]
248	KPSPAASKEYFQKVN	ubiquitination	[6]
253	ASKEYFQKVNQ****	ubiquitination	[3, 6, 7]

Reference

 [1] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [3] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [4] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [5] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [6] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [7] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983] 

Functional Description

 Involved in redox regulation of the cell. Protects radical-sensitive enzymes from oxidative damage by a radical- generating system. Acts synergistically with MAP3K13 to regulate the activation of NF-kappa-B in the cytosol. 

Sequence Annotation

 DOMAIN 63 221 Thioredoxin.
 ACT_SITE 108 108 Cysteine sulfenic acid (-SOH)
 MOD_RES 91 91 N6-acetyllysine.
 MOD_RES 146 146 Phosphothreonine (Probable).
 DISULFID 108 108 Interchain (with C-229); in linked form
 DISULFID 229 229 Interchain (with C-108); in linked form  

Keyword

 Acetylation; Antioxidant; Complete proteome; Direct protein sequencing; Disulfide bond; Mitochondrion; Oxidoreductase; Peroxidase; Phosphoprotein; Polymorphism; Redox-active center; Reference proteome; Transit peptide. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 256 AA 

Protein Sequence

Gene Ontology

 GO:0005769; C:early endosome; IDA:UniProtKB.
 GO:0005739; C:mitochondrion; IDA:UniProtKB.
 GO:0008785; F:alkyl hydroperoxide reductase activity; NAS:UniProtKB.
 GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; IMP:UniProtKB.
 GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
 GO:0051920; F:peroxiredoxin activity; IEA:EC.
 GO:0042744; P:hydrogen peroxide catabolic process; IMP:UniProtKB.
 GO:0001893; P:maternal placenta development; IEA:Compara.
 GO:0007005; P:mitochondrion organization; IMP:UniProtKB.
 GO:0030099; P:myeloid cell differentiation; ISS:UniProtKB.
 GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
 GO:0033673; P:negative regulation of kinase activity; IDA:UniProtKB.
 GO:0008284; P:positive regulation of cell proliferation; IDA:UniProtKB.
 GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
 GO:0051881; P:regulation of mitochondrial membrane potential; IMP:UniProtKB.
 GO:0032496; P:response to lipopolysaccharide; ISS:UniProtKB. 

Interpro

 IPR000866; AhpC/TSA.
 IPR024706; Peroxiredoxin_AhpC-typ.
 IPR019479; Peroxiredoxin_C.
 IPR012336; Thioredoxin-like_fold. 

Pfam

 PF10417; 1-cysPrx_C
 PF00578; AhpC-TSA 

SMART

  

PROSITE

 PS51352; THIOREDOXIN_2 

PRINTS