PRDX5_HUMAN
ID PRDX5_HUMAN Reviewed; 214 AA.
AC P30044; A6NC19; A6NG06; B7ZLJ4; B7ZVW3; Q14CK0; Q6IAF2; Q9UBU5; Q9UJU4;
AC Q9UKX4;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 4.
DT 03-AUG-2022, entry version 221.
DE RecName: Full=Peroxiredoxin-5, mitochondrial;
DE EC=1.11.1.24 {ECO:0000269|PubMed:10751410};
DE AltName: Full=Alu corepressor 1;
DE AltName: Full=Antioxidant enzyme B166;
DE Short=AOEB166;
DE AltName: Full=Liver tissue 2D-page spot 71B;
DE AltName: Full=PLP;
DE AltName: Full=Peroxiredoxin V;
DE Short=Prx-V;
DE AltName: Full=Peroxisomal antioxidant enzyme;
DE AltName: Full=TPx type VI;
DE AltName: Full=Thioredoxin peroxidase PMP20;
DE AltName: Full=Thioredoxin-dependent peroxiredoxin 5 {ECO:0000305};
DE Flags: Precursor;
GN Name=PRDX5 {ECO:0000312|HGNC:HGNC:9355}; Synonyms=ACR1; ORFNames=SBBI10;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MITOCHONDRIAL), AND VARIANT CYS-33.
RX PubMed=10095767; DOI=10.1046/j.1432-1327.1999.00162.x;
RA Kropotov A., Sedova V., Ivanov V., Sazeeva N., Tomilin A., Krutilina R.,
RA Oei S.L., Griesenbeck J., Buchlow G., Tomilin N.;
RT "A novel human DNA-binding protein with sequence similarity to a subfamily
RT of redox proteins which is able to repress RNA-polymerase-III-driven
RT transcription of the Alu-family retroposons in vitro.";
RL Eur. J. Biochem. 260:336-346(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CYTOPLASMIC+PEROXISOMAL), FUNCTION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=10514471; DOI=10.1074/jbc.274.42.29897;
RA Yamashita H., Avraham S., Jiang S., London R., Van Veldhoven P.P.,
RA Subramani S., Rogers R.A., Avraham H.;
RT "Characterization of human and murine PMP20 peroxisomal proteins that
RT exhibit antioxidant activity in vitro.";
RL J. Biol. Chem. 274:29897-29904(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MITOCHONDRIAL), PROTEIN SEQUENCE OF
RP 54-90, FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND VARIANT
RP CYS-33.
RC TISSUE=Lung;
RX PubMed=10521424; DOI=10.1074/jbc.274.43.30451;
RA Knoops B., Clippe A., Bogard C., Arsalane K., Wattiez R., Hermans C.,
RA Duconseille E., Falmagne P., Bernard A.;
RT "Cloning and characterization of AOEB166, a novel mammalian antioxidant
RT enzyme of the peroxiredoxin family.";
RL J. Biol. Chem. 274:30451-30458(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CYTOPLASMIC+PEROXISOMAL), AND VARIANT
RP CYS-33.
RX PubMed=10679306; DOI=10.1006/bbrc.2000.2231;
RA Zhou Y., Kok K.H., Chun A.C.S., Wong C.M., Wu H.W., Lin M.C.M.,
RA Fung P.C.W., Kung H.-F., Jin D.-Y.;
RT "Mouse peroxiredoxin V is a thioredoxin peroxidase that inhibits p53-
RT induced apoptosis.";
RL Biochem. Biophys. Res. Commun. 268:921-927(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF
RP CYS-100; CYS-125 AND CYS-204, ACTIVE SITE, DISULFIDE BOND, AND SUBCELLULAR
RP LOCATION.
RX PubMed=10751410; DOI=10.1074/jbc.m001943200;
RA Seo M.S., Kang S.W., Kim K., Baines I.C., Lee T.H., Rhee S.G.;
RT "Identification of a new type of mammalian peroxiredoxin that forms an
RT intramolecular disulfide as a reaction intermediate.";
RL J. Biol. Chem. 275:20346-20354(2000).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CYTOPLASMIC+PEROXISOMAL).
RA Kim I.H., Jeong W.;
RT "A new type of human thiol peroxidase (Human TPx type VI).";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MITOCHONDRIAL), AND VARIANT CYS-33.
RA Zhang W., Li N., Wan T., Cao X.;
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM CYTOPLASMIC+PEROXISOMAL).
RC TISSUE=Adrenal gland;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM MITOCHONDRIAL), AND VARIANT
RP CYS-33.
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT CYS-33.
RG NIEHS SNPs program;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS MITOCHONDRIAL; 3 AND 4),
RP AND VARIANT CYS-33.
RC TISSUE=Brain, and Medulla oblongata;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [13]
RP PROTEIN SEQUENCE OF 54-63.
RC TISSUE=Liver;
RX PubMed=1286669; DOI=10.1002/elps.11501301201;
RA Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F.,
RA Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R.,
RA Appel R.D., Hughes G.J.;
RT "Human liver protein map: a reference database established by
RT microsequencing and gel comparison.";
RL Electrophoresis 13:992-1001(1992).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-83, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
RX PubMed=11518528; DOI=10.1006/jmbi.2001.4853;
RA Declercq J.-P., Evrard C., Clippe A., Stricht D.V., Bernard A., Knoops B.;
RT "Crystal structure of human peroxiredoxin 5, a novel type of mammalian
RT peroxiredoxin at 1.5-A resolution.";
RL J. Mol. Biol. 311:751-759(2001).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS) OF 54-214, AND DISULFIDE BOND.
RX PubMed=18489898; DOI=10.1016/j.abb.2008.04.036;
RA Smeets A., Marchand C., Linard D., Knoops B., Declercq J.P.;
RT "The crystal structures of oxidized forms of human peroxiredoxin 5 with an
RT intramolecular disulfide bond confirm the proposed enzymatic mechanism for
RT atypical 2-Cys peroxiredoxins.";
RL Arch. Biochem. Biophys. 477:98-104(2008).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 54-214 IN COMPLEX WITH
RP DITHIOTHREITOL, AND ACTIVE SITE.
RX PubMed=20643143; DOI=10.1016/j.jmb.2010.07.022;
RA Hall A., Parsonage D., Poole L.B., Karplus P.A.;
RT "Structural evidence that peroxiredoxin catalytic power is based on
RT transition-state stabilization.";
RL J. Mol. Biol. 402:194-209(2010).
RN [21]
RP FUNCTION, SUBCELLULAR LOCATION, PALMITOYLATION AT CYS-100, AND MUTAGENESIS
RP OF CYS-100; CYS-125 AND CYS-204.
RX PubMed=31740833; DOI=10.1038/s41589-019-0399-y;
RA Cao Y., Qiu T., Kathayat R.S., Azizi S.A., Thorne A.K., Ahn D., Fukata Y.,
RA Fukata M., Rice P.A., Dickinson B.C.;
RT "ABHD10 is an S-depalmitoylase affecting redox homeostasis through
RT peroxiredoxin-5.";
RL Nat. Chem. Biol. 15:1232-1240(2019).
RN [22]
RP VARIANT [LARGE SCALE ANALYSIS] LEU-157.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of
CC hydrogen peroxide and organic hydroperoxides to water and alcohols,
CC respectively. Plays a role in cell protection against oxidative stress
CC by detoxifying peroxides and as sensor of hydrogen peroxide-mediated
CC signaling events. {ECO:0000269|PubMed:10514471,
CC ECO:0000269|PubMed:10521424, ECO:0000269|PubMed:10751410,
CC ECO:0000269|PubMed:31740833}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-
CC disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA-
CC COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924,
CC ChEBI:CHEBI:50058; EC=1.11.1.24;
CC Evidence={ECO:0000269|PubMed:10751410};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:20643143}.
CC -!- INTERACTION:
CC P30044; P55273: CDKN2D; NbExp=3; IntAct=EBI-722161, EBI-745859;
CC P30044; Q7Z417: NUFIP2; NbExp=3; IntAct=EBI-722161, EBI-1210753;
CC P30044; P49901: SMCP; NbExp=3; IntAct=EBI-722161, EBI-750494;
CC P30044; P00441: SOD1; NbExp=10; IntAct=EBI-722161, EBI-990792;
CC -!- SUBCELLULAR LOCATION: [Isoform Mitochondrial]: Mitochondrion
CC {ECO:0000269|PubMed:10521424, ECO:0000269|PubMed:10751410,
CC ECO:0000269|PubMed:31740833}.
CC -!- SUBCELLULAR LOCATION: [Isoform Cytoplasmic+peroxisomal]: Cytoplasm
CC {ECO:0000269|PubMed:10514471, ECO:0000269|PubMed:10751410}. Peroxisome
CC matrix {ECO:0000269|PubMed:10514471, ECO:0000269|PubMed:10521424,
CC ECO:0000269|PubMed:10751410}. Note=Imported into peroxisomes via
CC peroxisomal targeting signal 1 receptor PEX5.
CC {ECO:0000269|PubMed:10514471}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=4;
CC Name=Mitochondrial;
CC IsoId=P30044-1; Sequence=Displayed;
CC Name=Cytoplasmic+peroxisomal;
CC IsoId=P30044-2; Sequence=VSP_018829;
CC Name=3;
CC IsoId=P30044-3; Sequence=VSP_045783;
CC Name=4;
CC IsoId=P30044-4; Sequence=VSP_046682;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10521424}.
CC -!- PTM: S-palmitoylated (PubMed:31740833). Palmitoylation occurs on the
CC active site, inhibiting its reactivity; therefore PRDX5 palmitoylation
CC status determines its antioxidant capacity (PubMed:31740833).
CC {ECO:0000269|PubMed:31740833}.
CC -!- PTM: [Isoform Mitochondrial]: S-palmitoylated (PubMed:31740833).
CC Depalmitoylated by ABHD10 (PubMed:31740833).
CC {ECO:0000269|PubMed:31740833}.
CC -!- MISCELLANEOUS: The active site is a conserved redox-active cysteine
CC residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic
CC attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to
CC cysteine sulfenic acid (C(P)-SOH), which then reacts with another
CC cysteine residue, the resolving cysteine (C(R)), to form a disulfide
CC bridge. The disulfide is subsequently reduced by an appropriate
CC electron donor to complete the catalytic cycle. In this atypical 2-Cys
CC Prx, C(R) is present in the same subunit to form an intramolecular
CC disulfide. The disulfide is subsequently reduced by thioredoxin.
CC {ECO:0000305|PubMed:10751410, ECO:0000305|PubMed:18489898}.
CC -!- MISCELLANEOUS: [Isoform 4]: Produced by alternative splicing.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. Prx5 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF17200.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/prdx5/";
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DR EMBL; AF231705; AAF78899.1; -; mRNA.
DR EMBL; AF124993; AAF27531.1; -; mRNA.
DR EMBL; AF110731; AAF03750.1; -; mRNA.
DR EMBL; AF197952; AAF04856.1; -; mRNA.
DR EMBL; AJ249483; CAB62210.1; -; mRNA.
DR EMBL; AF242525; AAF99605.1; -; mRNA.
DR EMBL; AF112212; AAF17200.1; ALT_FRAME; mRNA.
DR EMBL; CR457203; CAG33484.1; -; mRNA.
DR EMBL; DQ247769; ABB05181.1; -; Genomic_DNA.
DR EMBL; AP001453; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP003774; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC110983; AAI10984.1; -; mRNA.
DR EMBL; BC113723; AAI13724.1; -; mRNA.
DR EMBL; BC113725; AAI13726.1; -; mRNA.
DR EMBL; BC143849; AAI43850.1; -; mRNA.
DR EMBL; BC171733; AAI71733.1; -; mRNA.
DR CCDS; CCDS8069.1; -. [P30044-1]
DR CCDS; CCDS8070.1; -. [P30044-3]
DR CCDS; CCDS8071.1; -. [P30044-4]
DR RefSeq; NP_036226.1; NM_012094.4. [P30044-1]
DR RefSeq; NP_857634.1; NM_181651.2. [P30044-3]
DR RefSeq; NP_857635.1; NM_181652.2. [P30044-4]
DR PDB; 1H4O; X-ray; 1.95 A; A/B/C/D/E/F/G/H=54-214.
DR PDB; 1HD2; X-ray; 1.50 A; A=54-214.
DR PDB; 1OC3; X-ray; 2.00 A; A/B/C=54-214.
DR PDB; 1URM; X-ray; 1.70 A; A=54-214.
DR PDB; 2VL2; X-ray; 1.92 A; A/B/C=54-214.
DR PDB; 2VL3; X-ray; 1.83 A; A/B/C=54-214.
DR PDB; 2VL9; X-ray; 2.70 A; A/B/C/D=54-214.
DR PDB; 3MNG; X-ray; 1.45 A; A=54-214.
DR PDB; 4K7I; X-ray; 2.25 A; A/B/C=54-214.
DR PDB; 4K7N; X-ray; 2.30 A; A/B/C=54-214.
DR PDB; 4K7O; X-ray; 1.98 A; A/B/C=54-214.
DR PDB; 4MMM; X-ray; 1.47 A; A/C/E/G=54-214.
DR PDBsum; 1H4O; -.
DR PDBsum; 1HD2; -.
DR PDBsum; 1OC3; -.
DR PDBsum; 1URM; -.
DR PDBsum; 2VL2; -.
DR PDBsum; 2VL3; -.
DR PDBsum; 2VL9; -.
DR PDBsum; 3MNG; -.
DR PDBsum; 4K7I; -.
DR PDBsum; 4K7N; -.
DR PDBsum; 4K7O; -.
DR PDBsum; 4MMM; -.
DR AlphaFoldDB; P30044; -.
DR SMR; P30044; -.
DR BioGRID; 117352; 159.
DR IntAct; P30044; 45.
DR MINT; P30044; -.
DR STRING; 9606.ENSP00000265462; -.
DR ChEMBL; CHEMBL3627586; -.
DR DrugBank; DB00995; Auranofin.
DR DrugBank; DB03608; Diminazene.
DR DrugBank; DB09221; Polaprezinc.
DR PeroxiBase; 4448; HsPrxV.
DR GlyGen; P30044; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P30044; -.
DR MetOSite; P30044; -.
DR PhosphoSitePlus; P30044; -.
DR SwissPalm; P30044; -.
DR BioMuta; PRDX5; -.
DR DMDM; 317373539; -.
DR OGP; P30044; -.
DR REPRODUCTION-2DPAGE; IPI00759663; -.
DR SWISS-2DPAGE; P30044; -.
DR UCD-2DPAGE; P30044; -.
DR CPTAC; CPTAC-572; -.
DR EPD; P30044; -.
DR jPOST; P30044; -.
DR MassIVE; P30044; -.
DR MaxQB; P30044; -.
DR PaxDb; P30044; -.
DR PeptideAtlas; P30044; -.
DR PRIDE; P30044; -.
DR ProteomicsDB; 1092; -.
DR ProteomicsDB; 54624; -. [P30044-1]
DR ProteomicsDB; 54625; -. [P30044-2]
DR ProteomicsDB; 797; -.
DR TopDownProteomics; P30044-1; -. [P30044-1]
DR TopDownProteomics; P30044-2; -. [P30044-2]
DR Antibodypedia; 3276; 452 antibodies from 39 providers.
DR DNASU; 25824; -.
DR Ensembl; ENST00000265462.9; ENSP00000265462.4; ENSG00000126432.14. [P30044-1]
DR Ensembl; ENST00000347941.4; ENSP00000335363.6; ENSG00000126432.14. [P30044-4]
DR Ensembl; ENST00000352435.8; ENSP00000335334.6; ENSG00000126432.14. [P30044-3]
DR GeneID; 25824; -.
DR KEGG; hsa:25824; -.
DR MANE-Select; ENST00000265462.9; ENSP00000265462.4; NM_012094.5; NP_036226.2.
DR UCSC; uc001nzu.4; human. [P30044-1]
DR CTD; 25824; -.
DR DisGeNET; 25824; -.
DR GeneCards; PRDX5; -.
DR HGNC; HGNC:9355; PRDX5.
DR HPA; ENSG00000126432; Low tissue specificity.
DR MIM; 606583; gene.
DR neXtProt; NX_P30044; -.
DR OpenTargets; ENSG00000126432; -.
DR PharmGKB; PA33726; -.
DR VEuPathDB; HostDB:ENSG00000126432; -.
DR eggNOG; KOG0541; Eukaryota.
DR GeneTree; ENSGT00390000018173; -.
DR HOGENOM; CLU_072440_3_1_1; -.
DR InParanoid; P30044; -.
DR OMA; GYINHPK; -.
DR OrthoDB; 1281610at2759; -.
DR PhylomeDB; P30044; -.
DR TreeFam; TF105182; -.
DR BioCyc; MetaCyc:HS05016-MON; -.
DR BRENDA; 1.11.1.24; 2681.
DR PathwayCommons; P30044; -.
DR Reactome; R-HSA-3299685; Detoxification of Reactive Oxygen Species.
DR Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes. [P30044-2]
DR SignaLink; P30044; -.
DR SIGNOR; P30044; -.
DR BioGRID-ORCS; 25824; 16 hits in 1086 CRISPR screens.
DR ChiTaRS; PRDX5; human.
DR EvolutionaryTrace; P30044; -.
DR GeneWiki; PRDX5; -.
DR GenomeRNAi; 25824; -.
DR Pharos; P30044; Tbio.
DR PRO; PR:P30044; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P30044; protein.
DR Bgee; ENSG00000126432; Expressed in bronchial epithelial cell and 181 other tissues.
DR Genevisible; P30044; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005782; C:peroxisomal matrix; IDA:UniProtKB.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0016209; F:antioxidant activity; IDA:UniProtKB.
DR GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; IMP:UniProtKB.
DR GO; GO:0004601; F:peroxidase activity; IDA:UniProtKB.
DR GO; GO:0051920; F:peroxiredoxin activity; IDA:UniProtKB.
DR GO; GO:0072541; F:peroxynitrite reductase activity; IDA:UniProtKB.
DR GO; GO:0001016; F:RNA polymerase III transcription regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; EXP:Reactome.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
DR GO; GO:0034614; P:cellular response to reactive oxygen species; IMP:UniProtKB.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IDA:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; TAS:UniProtKB.
DR GO; GO:0070995; P:NADPH oxidation; IDA:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0051354; P:negative regulation of oxidoreductase activity; IDA:UniProtKB.
DR GO; GO:0016480; P:negative regulation of transcription by RNA polymerase III; IDA:UniProtKB.
DR GO; GO:0032967; P:positive regulation of collagen biosynthetic process; IDA:UniProtKB.
DR GO; GO:2001057; P:reactive nitrogen species metabolic process; IDA:UniProtKB.
DR GO; GO:0060785; P:regulation of apoptosis involved in tissue homeostasis; IDA:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; IDA:UniProtKB.
DR CDD; cd03013; PRX5_like; 1.
DR InterPro; IPR037944; PRX5-like.
DR InterPro; IPR013740; Redoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR10430; PTHR10430; 1.
DR Pfam; PF08534; Redoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative initiation; Alternative splicing;
KW Antioxidant; Cytoplasm; Direct protein sequencing; Disulfide bond;
KW Lipoprotein; Mitochondrion; Oxidoreductase; Palmitate; Peroxidase;
KW Peroxisome; Phosphoprotein; Redox-active center; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..52
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 53..214
FT /note="Peroxiredoxin-5, mitochondrial"
FT /id="PRO_0000023793"
FT DOMAIN 56..214
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT MOTIF 212..214
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000305|PubMed:10514471"
FT ACT_SITE 100
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000305|PubMed:10751410,
FT ECO:0000305|PubMed:20643143"
FT MOD_RES 75
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P99029"
FT MOD_RES 83
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 83
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P99029"
FT MOD_RES 116
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P99029"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9R063"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P99029"
FT LIPID 100
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:31740833"
FT DISULFID 100..204
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691,
FT ECO:0000269|PubMed:10751410, ECO:0000269|PubMed:18489898"
FT VAR_SEQ 1..52
FT /note="Missing (in isoform Cytoplasmic+peroxisomal)"
FT /evidence="ECO:0000303|PubMed:10514471,
FT ECO:0000303|PubMed:10679306, ECO:0000303|PubMed:10931946,
FT ECO:0000303|Ref.6"
FT /id="VSP_018829"
FT VAR_SEQ 57..145
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_046682"
FT VAR_SEQ 102..145
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_045783"
FT VARIANT 33
FT /note="Y -> C (in dbSNP:rs7938623)"
FT /evidence="ECO:0000269|PubMed:10095767,
FT ECO:0000269|PubMed:10521424, ECO:0000269|PubMed:10679306,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.10,
FT ECO:0000269|Ref.7, ECO:0000269|Ref.9"
FT /id="VAR_025049"
FT VARIANT 157
FT /note="F -> L (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036406"
FT MUTAGEN 100
FT /note="C->S: Loss of antioxidant activity. Loss of S-
FT palmitoylation."
FT /evidence="ECO:0000269|PubMed:10751410,
FT ECO:0000269|PubMed:31740833"
FT MUTAGEN 125
FT /note="C->S: No change in antioxidant activity. No change
FT in S-palmitoylation levels."
FT /evidence="ECO:0000269|PubMed:10751410,
FT ECO:0000269|PubMed:31740833"
FT MUTAGEN 204
FT /note="C->S: Loss of antioxidant activity. No change in S-
FT palmitoylation levels."
FT /evidence="ECO:0000269|PubMed:10751410,
FT ECO:0000269|PubMed:31740833"
FT CONFLICT 141
FT /note="H -> T (in Ref. 4; AAF04856)"
FT /evidence="ECO:0000305"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:3MNG"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:2VL9"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:3MNG"
FT HELIX 78..81
FT /evidence="ECO:0007829|PDB:3MNG"
FT TURN 82..84
FT /evidence="ECO:0007829|PDB:3MNG"
FT STRAND 85..91
FT /evidence="ECO:0007829|PDB:3MNG"
FT HELIX 98..102
FT /evidence="ECO:0007829|PDB:3MNG"
FT HELIX 104..110
FT /evidence="ECO:0007829|PDB:3MNG"
FT HELIX 112..116
FT /evidence="ECO:0007829|PDB:3MNG"
FT TURN 117..119
FT /evidence="ECO:0007829|PDB:3MNG"
FT STRAND 122..129
FT /evidence="ECO:0007829|PDB:3MNG"
FT HELIX 131..140
FT /evidence="ECO:0007829|PDB:3MNG"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:3MNG"
FT STRAND 148..151
FT /evidence="ECO:0007829|PDB:3MNG"
FT HELIX 156..161
FT /evidence="ECO:0007829|PDB:3MNG"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:4MMM"
FT HELIX 170..173
FT /evidence="ECO:0007829|PDB:3MNG"
FT STRAND 181..186
FT /evidence="ECO:0007829|PDB:3MNG"
FT STRAND 189..195
FT /evidence="ECO:0007829|PDB:3MNG"
FT STRAND 199..203
FT /evidence="ECO:0007829|PDB:4MMM"
FT HELIX 207..213
FT /evidence="ECO:0007829|PDB:3MNG"
SQ SEQUENCE 214 AA; 22086 MW; DA1DEB21120254EE CRC64;
MGLAGVCALR RSAGYILVGG AGGQSAAAAA RRYSEGEWAS GGVRSFSRAA AAMAPIKVGD
AIPAVEVFEG EPGNKVNLAE LFKGKKGVLF GVPGAFTPGC SKTHLPGFVE QAEALKAKGV
QVVACLSVND AFVTGEWGRA HKAEGKVRLL ADPTGAFGKE TDLLLDDSLV SIFGNRRLKR
FSMVVQDGIV KALNVEPDGT GLTCSLAPNI ISQL
