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UniProtKB/Swiss-Prot entry P30044


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PRDX5_HUMAN
Primary accession number P30044
Secondary accession numbers Q14CK0 Q6IAF2 Q9UBU5 Q9UJU4 Q9UKX4
Integrated into Swiss-Prot on April 1, 1993
Sequence was last modified on February 21, 2002 (Sequence version 3)
Annotations were last modified on    November 25, 2008 (Entry version 93)
Name and origin of the protein
Protein name Peroxiredoxin-5, mitochondrial [Precursor]
Synonyms EC 1.11.1.15
Prx-V
Peroxisomal antioxidant enzyme
PLP
Thioredoxin reductase
Thioredoxin peroxidase PMP20
Antioxidant enzyme B166
AOEB166
TPx type VI
Liver tissue 2D-page spot 71B
Alu corepressor 1
Gene name
Name: PRDX5
Synonyms: ACR1
ORFNames: SBBI10
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Kim I.H., Jeong W.;
"A new type of human thiol peroxidase (Human TPx type VI).";
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1006/bbrc.2000.2231; PubMed=10679306 [NCBI, ExPASy, EBI, Israel, Japan]
Zhou Y., Kok K.H., Chun A.C.S., Wong C.M., Wu H.W., Lin M.C.M., Fung P.C.W., Kung H.-F., Jin D.-Y.;
"Mouse peroxiredoxin V is a thioredoxin peroxidase that inhibits p53-induced apoptosis.";
Biochem. Biophys. Res. Commun. 268:921-927(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
DOI=10.1074/jbc.274.42.29897; PubMed=10514471 [NCBI, ExPASy, EBI, Israel, Japan]
Yamashita H., Avraham S., Jiang S., London R., Van Veldhoven P.P., Subramani S., Rogers R.A., Avraham H.;
"Characterization of human and murine PMP20 peroxisomal proteins that exhibit antioxidant activity in vitro.";
J. Biol. Chem. 274:29897-29904(1999).
[4]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 54-90, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND CHARACTERIZATION.
TISSUE=Lung;
DOI=10.1074/jbc.274.43.30451; PubMed=10521424 [NCBI, ExPASy, EBI, Israel, Japan]
Knoops B., Clippe A., Bogard C., Arsalane K., Wattiez R., Hermans C., Duconseille E., Falmagne P., Bernard A.;
"Cloning and characterization of AOEB166, a novel mammalian antioxidant enzyme of the peroxiredoxin family.";
J. Biol. Chem. 274:30451-30458(1999).
[5]
NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS, AND CHARACTERIZATION.
DOI=10.1074/jbc.M001943200; PubMed=10751410 [NCBI, ExPASy, EBI, Israel, Japan]
Seo M.S., Kang S.W., Kim K., Baines I.C., Lee T.H., Rhee S.G.;
"Identification of a new type of mammalian peroxiredoxin that forms an intramolecular disulfide as a reaction intermediate.";
J. Biol. Chem. 275:20346-20354(2000).
[6]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=10095767 [NCBI, ExPASy, EBI, Israel, Japan]
Kropotov A., Sedova V., Ivanov V., Sazeeva N., Tomilin A., Krutilina R., Oei S.L., Griesenbeck J., Buchlow G., Tomilin N.;
"A novel human DNA-binding protein with sequence similarity to a subfamily of redox proteins which is able to repress RNA-polymerase-III-driven transcription of the Alu-family retroposons in vitro.";
Eur. J. Biochem. 260:336-346(1999).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Adrenal gland;
DOI=10.1073/pnas.160270997; PubMed=10931946 [NCBI, ExPASy, EBI, Israel, Japan]
Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.;
"Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning.";
Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
[8]
NUCLEOTIDE SEQUENCE [MRNA].
Zhang W., Li N., Wan T., Cao X.;
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT TYR-33.
NIEHS SNPs program;
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, and Medulla oblongata;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[12]
PROTEIN SEQUENCE OF 54-63.
TISSUE=Liver;
DOI=10.1002/elps.11501301201; PubMed=1286669 [NCBI, ExPASy, EBI, Israel, Japan]
Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F., Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R., Appel R.D., Hughes G.J.;
"Human liver protein map: a reference database established by microsequencing and gel comparison.";
Electrophoresis 13:992-1001(1992).
[13]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
DOI=10.1006/jmbi.2001.4853; PubMed=11518528 [NCBI, ExPASy, EBI, Israel, Japan]
Declercq J.-P., Evrard C., Clippe A., Stricht D.V., Bernard A., Knoops B.;
"Crystal structure of human peroxiredoxin 5, a novel type of mammalian peroxiredoxin at 1.5-A resolution.";
J. Mol. Biol. 311:751-759(2001).
[14]
VARIANT [LARGE SCALE ANALYSIS] LEU-157.
DOI=10.1126/science.1133427; PubMed=16959974 [NCBI, ExPASy, EBI, Israel, Japan]
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal cancers.";
Science 314:268-274(2006).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AJ249483; CAB62210.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF197952; AAF04856.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF124993; AAF27531.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF110731; AAF03750.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF231705; AAF78899.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF112212; AAF17200.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF242525; AAF99605.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR457203; CAG33484.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ247769; ABB05181.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC110983; AAI10984.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC113723; AAI13724.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC113725; AAI13726.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_036226.1; -.
NP_857634.1; -.
NP_857635.1; -.
UniGene Hs.502823
3D structure databases
PDB
1H4O; X-ray; 1.95 A; A/B/C/D/E/F/G/H=54-214.[ExPASy / RCSB / EBI]
1HD2; X-ray; 1.50 A; A=54-214.[ExPASy / RCSB / EBI]
1OC3; X-ray; 2.00 A; A/B/C=54-214.[ExPASy / RCSB / EBI]
1URM; X-ray; 1.70 A; A=54-214.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1H4O; -.
1HD2; -.
1OC3; -.
1URM; -.
ModBase P30044.
Protein-protein interaction databases
IntAct P30044; -.
Protein family/group databases
PeroxiBase 4448; HsPrxV.
PTM databases
PhosphoSite P30044; -.
2D gel databases
SWISS-2DPAGE P30044; -.
OGP P30044; -.
REPRODUCTION-2DPAGE IPI00759663; -.
Organism-specific databases
H-InvDB HIX0021287; -.
HGNC HGNC:9355; PRDX5.
GenAtlas PRDX5.
HPA CAB008661; -.
MIM 606583; gene. [NCBI / EBI]
PharmGKB PA33726; -.
GeneCards P30044.
Gene expression databases
ArrayExpress P30044; -.
CleanEx HS_PRDX5; -.
GermOnline ENSG00000126432; Homo sapiens.
Ontologies
GO
GO:0044445; Cellular component: cytosolic part (inferred from direct assay from UniProtKB).
GO:0005739; Cellular component: mitochondrion (inferred from direct assay from UniProtKB).
GO:0005777; Cellular component: peroxisome (inferred from direct assay from UniProtKB).
GO:0043027; Molecular function: caspase inhibitor activity (inferred from mutant phenotype from UniProtKB).
GO:0051920; Molecular function: peroxiredoxin activity (inferred from electronic annotation from EC).
GO:0045454; Biological process: cell redox homeostasis (inferred from electronic annotation from InterPro).
GO:0034614; Biological process: cellular response to reactive oxygen species (inferred from mutant phenotype from UniProtKB).
GO:0006954; Biological process: inflammatory response (traceable author statement from UniProtKB).
GO:0043066; Biological process: negative regulation of apoptosis (inferred from mutant phenotype from UniProtKB).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR013740; Redoxin.
IPR012335; Thioredoxin_fold.
Graphical view of domain structure.
Gene3D G3DSA:3.40.30.10; Thioredoxin_fold; 1.
Pfam PF08534; Redoxin; 1.
Pfam graphical view of domain structure.
PROSITE PS51352; THIOREDOXIN_2; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet P30044.
Genome annotation databases
Ensembl ENSG00000126432; Homo sapiens. [Contig view]
GeneID 25824; -.
KEGG hsa:25824; -.
Phylogenomic databases
HOGENOM P30044; -.
HOVERGEN P30044; -.
Other
DrugBank DB00995; Auranofin.
LinkHub P30044; -.
NextBio 47091; -.
SOURCE PRDX5; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative initiation; Antioxidant; Cytoplasm; Direct protein sequencing; Mitochondrion; Oxidoreductase; Peroxidase; Peroxisome; Polymorphism; Redox-active center; Transit peptide.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
TRANSIT   1    52  52     Mitochondrion (Potential). 
CHAIN   53   214  162     Peroxiredoxin-5, mitochondrial. PRO_0000023793
DOMAIN   56   214  159     Thioredoxin. 
MOTIF   212   214  3     Microbody targeting signal (By similarity). 
ACT_SITE   100   100        Cysteine sulfenic acid (-SOH) intermediate (Potential). 
DISULFID   100   204        Redox-active. 
VAR_SEQ   1    52        Missing (in isoform Cytoplasmic+peroxisomal). VSP_018829
VARIANT   33    33  1     C -> Y (in dbSNP:rs7938623 [NCBI]). VAR_025049 
VARIANT   157   157  1     F -> L (in a breast cancer sample; somatic mutation). VAR_036406 [3D]
MUTAGEN   100   100        C->S: Complete loss of activity. 
MUTAGEN   125   125        C->S: No change in activity. 
MUTAGEN   204   204        C->S: Complete loss of activity. 
CONFLICT   141   141        H -> T (in Ref. 2; AAF04856). 
STRAND   66    68  3      
STRAND   75    77  3      
HELIX   78    81  4      
TURN   82    84  3      
STRAND   85    91  7      
HELIX   98   102  5      
HELIX   104   110  7      
HELIX   112   116  5      
TURN   117   119  3      
STRAND   120   129  10      
HELIX   131   140  10      
TURN   144   146  3      
STRAND   148   151  4      
HELIX   156   161  6      
HELIX   170   173  4      
STRAND   181   186  6      
STRAND   189   195  7      
HELIX   207   211  5      
Sequence information
Length: 214 AA [This is the length of the unprocessed precursor] Molecular weight: 22026 Da [This is the MW of the unprocessed precursor] CRC64: 2FF211210809823E [This is a checksum on the sequence]
        10         20         30         40         50         60 
MGLAGVCALR RSAGYILVGG AGGQSAAAAA RRCSEGEWAS GGVRSFSRAA AAMAPIKVGD 

        70         80         90        100        110        120 
AIPAVEVFEG EPGNKVNLAE LFKGKKGVLF GVPGAFTPGC SKTHLPGFVE QAEALKAKGV 

       130        140        150        160        170        180 
QVVACLSVND AFVTGEWGRA HKAEGKVRLL ADPTGAFGKE TDLLLDDSLV SIFGNRRLKR 

       190        200        210 
FSMVVQDGIV KALNVEPDGT GLTCSLAPNI ISQL 

P30044 in FASTA format

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View entry in raw text format (no links)
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