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1:  NP_857634Reports  peroxiredoxin 5 i...[gi:32455260] BLink, Conserved Domains, Links
LOCUS       NP_857634                170 aa            linear   PRI 23-NOV-2008
DEFINITION  peroxiredoxin 5 isoform b precursor [Homo sapiens].
ACCESSION   NP_857634
VERSION     NP_857634.1  GI:32455260
DBSOURCE    REFSEQ: accession NM_181651.1
KEYWORDS    .
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Starr,J.M., Shiels,P.G., Harris,S.E., Pattie,A., Pearce,M.S.,
            Relton,C.L. and Deary,I.J.
  TITLE     Oxidative stress, telomere length and biomarkers of physical aging
            in a cohort aged 79 years from the 1932 Scottish Mental Survey
  JOURNAL   Mech. Ageing Dev. (2008) In press
   PUBMED   18977241
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Available-Online prior to print
REFERENCE   2  (residues 1 to 170)
  AUTHORS   Smeets,A., Marchand,C., Linard,D., Knoops,B. and Declercq,J.P.
  TITLE     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
  JOURNAL   Arch. Biochem. Biophys. 477 (1), 98-104 (2008)
   PUBMED   18489898
  REMARK    GeneRIF: report here three crystal forms in which this
            intramolecular disulfide bond is indeed observed. The structures
            are characterized by the expected local unfolding of the
            peroxidatic loop, but also by the unfolding of the resolving loop
REFERENCE   3  (residues 1 to 170)
  AUTHORS   Jurkunas,U.V., Rawe,I., Bitar,M.S., Zhu,C., Harris,D.L., Colby,K.
            and Joyce,N.C.
  TITLE     Decreased expression of peroxiredoxins in Fuchs' endothelial
            dystrophy
  JOURNAL   Invest. Ophthalmol. Vis. Sci. 49 (7), 2956-2963 (2008)
   PUBMED   18378575
  REMARK    GeneRIF: Significantly decreased expression of Prx-2, -3, and -5 in
            FED may suggest an alteration in the ability of endothelial cells
            to withstand oxidant-induced damage and may be closely related to
            the pathogenesis of this disease.
REFERENCE   4  (residues 1 to 170)
  AUTHORS   De Simoni,S., Goemaere,J. and Knoops,B.
  TITLE     Silencing of peroxiredoxin 3 and peroxiredoxin 5 reveals the role
            of mitochondrial peroxiredoxins in the protection of human
            neuroblastoma SH-SY5Y cells toward MPP+
  JOURNAL   Neurosci. Lett. 433 (3), 219-224 (2008)
   PUBMED   18262354
  REMARK    GeneRIF: Our results show that mitochondrial PRDX-depleted cells
            are more prone to oxidative damages and apoptosis induced by
            MPP(+), a complex I inhibitor which provides an experimental
            paradigm of Parkinson's disease.
REFERENCE   5  (residues 1 to 170)
  AUTHORS   Avila,P.C., Kropotov,A.V., Krutilina,R., Krasnodembskay,A.,
            Tomilin,N.V. and Serikov,V.B.
  TITLE     Peroxiredoxin V contributes to antioxidant defense of lung
            epithelial cells
  JOURNAL   Lung 186 (2), 103-114 (2008)
   PUBMED   18219526
  REMARK    GeneRIF: Peroxiredoxin V (PRXV) is an important antioxidant protein
            of lung epithelial cells. Its expression in the human lung
            increases in inflammation.
REFERENCE   6  (residues 1 to 170)
  AUTHORS   Knoops,B., Clippe,A., Bogard,C., Arsalane,K., Wattiez,R.,
            Hermans,C., Duconseille,E., Falmagne,P. and Bernard,A.
  TITLE     Cloning and characterization of AOEB166, a novel mammalian
            antioxidant enzyme of the peroxiredoxin family
  JOURNAL   J. Biol. Chem. 274 (43), 30451-30458 (1999)
   PUBMED   10521424
REFERENCE   7  (residues 1 to 170)
  AUTHORS   Yamashita,H., Avraham,S., Jiang,S., London,R., Van Veldhoven,P.P.,
            Subramani,S., Rogers,R.A. and Avraham,H.
  TITLE     Characterization of human and murine PMP20 peroxisomal proteins
            that exhibit antioxidant activity in vitro
  JOURNAL   J. Biol. Chem. 274 (42), 29897-29904 (1999)
   PUBMED   10514471
REFERENCE   8  (residues 1 to 170)
  AUTHORS   Wattiez,R., Hermans,C., Bernard,A., Lesur,O. and Falmagne,P.
  TITLE     Human bronchoalveolar lavage fluid: two-dimensional gel
            electrophoresis, amino acid microsequencing and identification of
            major proteins
  JOURNAL   Electrophoresis 20 (7), 1634-1645 (1999)
   PUBMED   10424490
REFERENCE   9  (residues 1 to 170)
  AUTHORS   Kropotov,A., Sedova,V., Ivanov,V., Sazeeva,N., Tomilin,A.,
            Krutilina,R., Oei,S.L., Griesenbeck,J., Buchlow,G. and Tomilin,N.
  TITLE     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
  JOURNAL   Eur. J. Biochem. 260 (2), 336-346 (1999)
   PUBMED   10095767
REFERENCE   10 (residues 1 to 170)
  AUTHORS   Hochstrasser,D.F., Frutiger,S., Paquet,N., Bairoch,A., Ravier,F.,
            Pasquali,C., Sanchez,J.C., Tissot,J.D., Bjellqvist,B., Vargas,R. et
            al.
  TITLE     Human liver protein map: a reference database established by
            microsequencing and gel comparison
  JOURNAL   Electrophoresis 13 (12), 992-1001 (1992)
   PUBMED   1286669
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF242525.1 and BU598032.1.
            
            Summary: This gene encodes a member of the peroxiredoxin family of
            antioxidant enzymes, which reduce hydrogen peroxide and alkyl
            hydroperoxides. The encoded protein may play an antioxidant
            protective role in different tissues under normal conditions and
            during inflammatory processes. This protein interacts with
            peroxisome receptor 1. The crystal structure of this protein in its
            reduced form has been resolved to 1.5 angstrom resolution. This
            gene uses alternate in-frame translation initiation sites to
            generate mitochondrial or peroxisomal/cytoplasmic forms. Three
            transcript variants encoding distinct isoforms have been identified
            for this gene. [provided by RefSeq].
            
            Transcript Variant: This variant (2) lacks a segment in the coding
            region, which leads to a frameshift, compared to variant 1. The
            resulting isoform (b) contains a shorter and distinct C-terminus
            compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the
            Entrez Gene record to access additional publications.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13"
     Protein         1..170
                     /product="peroxiredoxin 5 isoform b precursor"
                     /EC_number="1.11.1.15"
                     /note="antioxidant enzyme B166; thioredoxin peroxidase
                     PMP20; peroxisomal antioxidant enzyme; TPx type VI; liver
                     tissue 2D-page spot 71B; Alu co-repressor 1"
                     /calculated_mol_wt=17263
     Region          1..170
                     /region_name="alternative start site"
                     /note="cytoplasmic/peroxisomal protein"
     CDS             1..170
                     /gene="PRDX5"
                     /gene_synonym="PLP"
                     /gene_synonym="ACR1"
                     /gene_synonym="B166"
                     /gene_synonym="PRXV"
                     /gene_synonym="PMP20"
                     /gene_synonym="PRDX6"
                     /gene_synonym="SBBI10"
                     /gene_synonym="AOEB166"
                     /gene_synonym="MGC117264"
                     /gene_synonym="MGC142283"
                     /gene_synonym="MGC142285"
                     /coded_by="NM_181651.1:120..632"
                     /note="isoform b precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS8070.1"
                     /db_xref="GeneID:25824"
                     /db_xref="HGNC:9355"
                     /db_xref="MIM:606583"
ORIGIN      
        1 mglagvcalr rsagyilvgg aggqsaaaaa rrcsegewas ggvrsfsraa aamapikvgd
       61 aipavevfeg epgnkvnlae lfkgkkgvlf gvpgaftpgc skvrlladpt gafgketdll
      121 lddslvsifg nrrlkrfsmv vqdgivkaln vepdgtgltc slapniisql
//

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Last update: Wed, 05 Nov 2008 Rev. 145015