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    PRDX5 peroxiredoxin 5 [ Homo sapiens (human) ]

    Gene ID: 25824, updated on 10-Dec-2024

    Summary

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    Official Symbol
    PRDX5provided by HGNC
    Official Full Name
    peroxiredoxin 5provided by HGNC
    Primary source
    HGNC:HGNC:9355
    See related
    Ensembl:ENSG00000126432 MIM:606583; AllianceGenome:HGNC:9355
    Gene type
    protein coding
    RefSeq status
    REVIEWED
    Organism
    Homo sapiens
    Lineage
    Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
    Also known as
    PLP; ACR1; B166; PRXV; PMP20; PRDX6; prx-V; SBBI10; AOEB166; HEL-S-55
    Summary
    This gene encodes a member of the peroxiredoxin family of antioxidant enzymes, which reduce hydrogen peroxide and alkyl hydroperoxides. The encoded protein interacts with peroxisome receptor 1 and plays an antioxidant protective role in different tissues under normal conditions and during inflammatory processes. The use of alternate transcription start sites is thought to result in transcript variants that use different in-frame translational start codons to generate isoforms that are targeted to the mitochondrion (isoform L) or peroxisome/cytoplasm (isoform S). Multiple related pseudogenes have been defined for this gene. [provided by RefSeq, Nov 2017]
    Expression
    Ubiquitous expression in colon (RPKM 157.0), kidney (RPKM 130.3) and 25 other tissues See more
    Orthologs
    mouse all
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    Genomic context

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    See PRDX5 in Genome Data Viewer
    Location:
    11q13.1
    Exon count:
    6
    Annotation release Status Assembly Chr Location
    RS_2024_08 current GRCh38.p14 (GCF_000001405.40) 11 NC_000011.10 (64318121..64321811)
    RS_2024_08 current T2T-CHM13v2.0 (GCF_009914755.1) 11 NC_060935.1 (64308102..64311792)
    RS_2024_09 previous assembly GRCh37.p13 (GCF_000001405.25) 11 NC_000011.9 (64085593..64089283)

    Chromosome 11 - NC_000011.10Genomic Context describing neighboring genes Neighboring gene KCNK4-CATSPERZ readthrough (NMD candidate) Neighboring gene catsper channel auxiliary subunit zeta Neighboring gene ATAC-STARR-seq lymphoblastoid silent region 3476 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 4897 Neighboring gene estrogen related receptor alpha Neighboring gene H3K4me1 hESC enhancer GRCh37_chr11:64083535-64084050 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 4898 Neighboring gene ATAC-STARR-seq lymphoblastoid silent region 3477 Neighboring gene tRNA methyltransferase activator subunit 11-2 Neighboring gene uncharacterized LOC102723878 Neighboring gene ReSE screen-validated silencer GRCh37_chr11:64092812-64092964 Neighboring gene H3K4me1 hESC enhancer GRCh37_chr11:64098506-64099028 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 4899 Neighboring gene CRISPRi-validated cis-regulatory element chr11.3041 Neighboring gene ATAC-STARR-seq lymphoblastoid silent region 3478 Neighboring gene ATAC-STARR-seq lymphoblastoid silent region 3479 Neighboring gene coiled-coil domain containing 88B Neighboring gene microRNA 7155

    Genomic regions, transcripts, and products

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    Go to nucleotide: Graphics FASTA GenBank

    Expression

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    • Project title: HPA RNA-seq normal tissues
    • Description: RNA-seq was performed of tissue samples from 95 human individuals representing 27 different tissues in order to determine tissue-specificity of all protein-coding genes
    • BioProject: PRJEB4337
    • Publication: PMID 24309898
    • Analysis date: Wed Apr 4 07:08:55 2018

    Bibliography

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    Related articles in PubMed

    1. The crystal structures of oxidized forms of human peroxiredoxin 5 with an intramolecular disulfide bond confirm the proposed enzymatic mechanism for atypical 2-Cys peroxiredoxins. Smeets A, et al. Arch Biochem Biophys, 2008 Sep 1. PMID 18489898
    2. Expression and regulation of peroxiredoxin 5 in human osteoarthritis. Wang MX, et al. FEBS Lett, 2002 Nov 6. PMID 12417342
    3. Human peroxiredoxin 5 gene organization, initial characterization of its promoter and identification of alternative forms of mRNA. Nguyên-Nhu NT, et al. Biochim Biophys Acta, 2007 Jul-Aug. PMID 17628720
    4. Knockdown of Peroxiredoxin V increased the cytotoxicity of non-thermal plasma-treated culture medium to A549 cells. Sun HN, et al. Aging (Albany NY), 2022 May 11. PMID 35546738, Free PMC Article
    5. Mitochondrial peroxiredoxin-5 as potential modulator of mitochondria-ER crosstalk in MPP+-induced cell death. De Simoni S, et al. J Neurochem, 2013 May. PMID 23216451

    See all (151) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Selenoprotein P, peroxiredoxin-5, renalase, and total antioxidant status in patients with suspected obstructive sleep apnea.
      Title: Selenoprotein P, peroxiredoxin-5, renalase, and total antioxidant status in patients with suspected obstructive sleep apnea.
    2. Identification of PRDX5 as A Target for The Treatment of Castration-Resistant Prostate Cancer.
      Title: Identification of PRDX5 as A Target for The Treatment of Castration-Resistant Prostate Cancer.
    3. [Thioredoxin-reductase in fibroblasts of human dermis in the process of aging.].
      Title: [Thioredoxin-reductase in fibroblasts of human dermis in the process of aging.].
    4. Prdx5 in the Regulation of Tuberous Sclerosis Complex Mutation-Induced Signaling Mechanisms.
      Title: Prdx5 in the Regulation of Tuberous Sclerosis Complex Mutation-Induced Signaling Mechanisms.
    5. Peroxiredoxin 5 is involved in cancer cell invasion and tumor growth of oral squamous cell carcinoma.
      Title: Peroxiredoxin 5 is involved in cancer cell invasion and tumor growth of oral squamous cell carcinoma.
    6. Knockdown of Peroxiredoxin V increased the cytotoxicity of non-thermal plasma-treated culture medium to A549 cells.
      Title: Knockdown of Peroxiredoxin V increased the cytotoxicity of non-thermal plasma-treated culture medium to A549 cells.
    7. Antioxidant enzyme peroxiredoxin 5 regulates cyst growth and ciliogenesis via modulating Plk1 stability.
      Title: Antioxidant enzyme peroxiredoxin 5 regulates cyst growth and ciliogenesis via modulating Plk1 stability.
    8. ROSmediated hypomethylation of PRDX5 promotes STAT3 binding and activates the Nrf2 signaling pathway in NSCLC.
      Title: ROS‑mediated hypomethylation of PRDX5 promotes STAT3 binding and activates the Nrf2 signaling pathway in NSCLC.
    9. Peroxiredoxins are involved in the pathogenesis of multiple sclerosis and neuromyelitis optica spectrum disorder.
      Title: Peroxiredoxins are involved in the pathogenesis of multiple sclerosis and neuromyelitis optica spectrum disorder.
    10. Peroxiredoxin 5 ameliorates obesity-induced non-alcoholic fatty liver disease through the regulation of oxidative stress and AMP-activated protein kinase signaling.
      Title: Peroxiredoxin 5 ameliorates obesity-induced non-alcoholic fatty liver disease through the regulation of oxidative stress and AMP-activated protein kinase signaling.
    Submit: New GeneRIF Correction See all GeneRIFs (55)

    Phenotypes

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    Review eQTL and phenotype association data in this region using PheGenI

    EBI GWAS Catalog

    Description
    A novel sarcoidosis risk locus for Europeans on chromosome 11q13.1.
    EBI GWAS Catalog
    Genome-wide association study in alopecia areata implicates both innate and adaptive immunity.
    EBI GWAS Catalog
    Genome-wide meta-analysis increases to 71 the number of confirmed Crohn's disease susceptibility loci.
    EBI GWAS Catalog

    Variation

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    See variants in ClinVar

    See studies and variants in dbVar

    See Variation Viewer (GRCh37.p13)

    See Variation Viewer (GRCh38)

    Pathways from PubChem

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    Interactions

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    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

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    Markers

    Homology

    Clone Names

    • MGC117264, MGC142283, MGC142285

    Gene Ontology Provided by GOA

    Function Evidence Code Pubs
    enables RNA polymerase III transcription regulatory region sequence-specific DNA binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables antioxidant activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables cysteine-type endopeptidase inhibitor activity involved in apoptotic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables identical protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables peroxidase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables peroxynitrite reductase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables signaling receptor binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables thioredoxin peroxidase activity EXP
    Inferred from Experiment
    more info
    		 PubMed 
    enables thioredoxin peroxidase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables thioredoxin peroxidase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in NADPH oxidation IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in cell redox homeostasis IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in cellular oxidant detoxification IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in cellular response to oxidative stress IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in cellular response to oxidative stress TAS
    Traceable Author Statement
    more info
    		  
    involved_in cellular response to reactive oxygen species IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in hydrogen peroxide catabolic process IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in hydrogen peroxide catabolic process IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in inflammatory response TAS
    Traceable Author Statement
    more info
    		 PubMed 
    involved_in negative regulation of apoptotic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in negative regulation of oxidoreductase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in negative regulation of transcription by RNA polymerase III IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in positive regulation of collagen biosynthetic process IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in reactive nitrogen species metabolic process IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in regulation of apoptosis involved in tissue homeostasis IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in response to oxidative stress IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    Component Evidence Code Pubs
    is_active_in cytoplasm IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in cytoplasm IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in cytoplasmic vesicle IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in cytosol IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in cytosol TAS
    Traceable Author Statement
    more info
    		  
    located_in extracellular exosome HDA PubMed 
    located_in extracellular space HDA PubMed 
    located_in intracellular membrane-bounded organelle IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in mitochondrial matrix TAS
    Traceable Author Statement
    more info
    		  
    located_in mitochondrion HTP PubMed 
    is_active_in mitochondrion IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in mitochondrion IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in nucleus IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in perinuclear region of cytoplasm IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in peroxisomal matrix IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in peroxisomal matrix IEA
    Inferred from Electronic Annotation
    more info
    		  
    is_active_in peroxisome IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in peroxisome IDA
    Inferred from Direct Assay
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    peroxiredoxin-5, mitochondrial
    Names
    Alu co-repressor 1
    TPx type VI
    antioxidant enzyme B166
    epididymis secretory protein Li 55
    liver tissue 2D-page spot 71B
    peroxiredoxin V
    peroxisomal antioxidant enzyme
    thioredoxin peroxidase PMP20
    thioredoxin reductase
    thioredoxin-dependent peroxiredoxin 5
    NP_001345440.2
    NP_001345445.1
    NP_036226.2
    NP_857634.2
    NP_857635.2

    NCBI Reference Sequences (RefSeq)

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    NEW Try the new Transcript table

    RefSeqs maintained independently of Annotated Genomes

    These reference sequences exist independently of genome builds. Explain

    These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

    mRNA and Protein(s)

    1. NM_001358511.2 → NP_001345440.2  peroxiredoxin-5, mitochondrial isoform d precursor

      Status: REVIEWED

      Description
      Transcript Variant: This variant (4) lacks an alternate in-frame exon compared to variant 1. The encoded isoform (d) is shorter than isoform L.
      Source sequence(s)
      AP001453, AP003774
      Conserved Domains (1) summary
      cd03013
      Location:57 → 167
      PRX5_like; Peroxiredoxin (PRX) family, PRX5-like subfamily; members are similar to the human protein, PRX5, a homodimeric TRX peroxidase, widely expressed in tissues and found cellularly in mitochondria, peroxisomes and the cytosol. The cellular location of PRX5 ...

    2. NM_001358516.2 → NP_001345445.1  peroxiredoxin-5, mitochondrial isoform S

      Status: REVIEWED

      Description
      Transcript Variant: This variant (5) represents use of an internal transcription start site determined in PMID:17628720 compared to variant 1. It initiates translation at an in-frame downstream start codon and encodes isoform S, which has a shorter N-terminus lacking the mitochondrial transit peptide found in isoform L.
      Source sequence(s)
      AF112212, AF124993, AF197952, AF242525, AP001453
      UniProtKB/TrEMBL
      V9HW35
      Conserved Domains (1) summary
      cd03013
      Location:6 → 160
      PRX5_like; Peroxiredoxin (PRX) family, PRX5-like subfamily; members are similar to the human protein, PRX5, a homodimeric TRX peroxidase, widely expressed in tissues and found cellularly in mitochondria, peroxisomes and the cytosol. The cellular location of PRX5 ...

    3. NM_012094.5 → NP_036226.2  peroxiredoxin-5, mitochondrial isoform L precursor

      Status: REVIEWED

      Description
      Transcript Variant: This variant (1) represents the longest transcript, and encodes the longest isoform (L).
      Source sequence(s)
      AP001453, AP003774
      Consensus CDS
      CCDS8069.1
      UniProtKB/Swiss-Prot
      A6NC19, A6NG06, B7ZLJ4, B7ZVW3, P30044, Q14CK0, Q6IAF2, Q9UBU5, Q9UJU4, Q9UKX4
      Related
      ENSP00000265462.4, ENST00000265462.9
      Conserved Domains (1) summary
      cd03013
      Location:58 → 212
      PRX5_like; Peroxiredoxin (PRX) family, PRX5-like subfamily; members are similar to the human protein, PRX5, a homodimeric TRX peroxidase, widely expressed in tissues and found cellularly in mitochondria, peroxisomes and the cytosol. The cellular location of PRX5 ...

    4. NM_181651.3 → NP_857634.2  peroxiredoxin-5, mitochondrial isoform b precursor

      Status: REVIEWED

      Description
      Transcript Variant: This variant (2) lacks an alternate in-frame exon compared to variant 1. The resulting isoform (b) is shorter than isoform L.
      Source sequence(s)
      AP001453, AP003774
      Consensus CDS
      CCDS8070.1
      Related
      ENSP00000335334.6, ENST00000352435.8
      Conserved Domains (1) summary
      cl00388
      Location:58 → 168
      Thioredoxin_like; Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold

    5. NM_181652.3 → NP_857635.2  peroxiredoxin-5, mitochondrial isoform c precursor

      Status: REVIEWED

      Description
      Transcript Variant: This variant (3) lacks two alternate in-frame exons compared to variant 1. The resulting isoform (c) is shorter than isoform L.
      Source sequence(s)
      AP001453, AP003774
      Consensus CDS
      CCDS8071.1
      Related
      ENSP00000335363.6, ENST00000347941.4
      Conserved Domains (1) summary
      cl00388
      Location:57 → 123
      Thioredoxin_like; Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold

    RefSeqs of Annotated Genomes: GCF_000001405.40-RS_2024_08

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference GRCh38.p14 Primary Assembly

    Genomic

    1. NC_000011.10 Reference GRCh38.p14 Primary Assembly

      Range
      64318121..64321811
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    Alternate T2T-CHM13v2.0

    Genomic

    1. NC_060935.1 Alternate T2T-CHM13v2.0

      Range
      64308102..64311792
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P30044.4 GenPept UniProtKB/Swiss-Prot:P30044

    Gene LinkOut

    The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.

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