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Database: UniProt
Entry: P30044
LinkDB: P30044
Original site: P30044 
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   02-DEC-2020, entry version 214.
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   SMR; P30044; -.
DR   BioGRID; 117352; 134.
DR   IntAct; P30044; 41.
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   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; 423 antibodies.
DR   DNASU; 25824; -.
DR   Ensembl; ENST00000265462; ENSP00000265462; ENSG00000126432. [P30044-1]
DR   Ensembl; ENST00000347941; ENSP00000335363; ENSG00000126432. [P30044-4]
DR   Ensembl; ENST00000352435; ENSP00000335334; ENSG00000126432. [P30044-3]
DR   GeneID; 25824; -.
DR   KEGG; hsa:25824; -.
DR   UCSC; uc001nzu.4; human. [P30044-1]
DR   CTD; 25824; -.
DR   DisGeNET; 25824; -.
DR   EuPathDB; HostDB:ENSG00000126432.13; -.
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   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-MONOMER; -.
DR   BRENDA; 1.11.1.15; 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   SIGNOR; P30044; -.
DR   BioGRID-ORCS; 25824; 9 hits in 850 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 209 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   Gene3D; 3.40.30.10; -; 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; Polymorphism; Redox-active center;
KW   Reference proteome; 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:0000244|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:0000244|PDB:3MNG"
FT   HELIX           72..74
FT                   /evidence="ECO:0000244|PDB:2VL9"
FT   STRAND          75..77
FT                   /evidence="ECO:0000244|PDB:3MNG"
FT   HELIX           78..81
FT                   /evidence="ECO:0000244|PDB:3MNG"
FT   TURN            82..84
FT                   /evidence="ECO:0000244|PDB:3MNG"
FT   STRAND          85..91
FT                   /evidence="ECO:0000244|PDB:3MNG"
FT   HELIX           98..102
FT                   /evidence="ECO:0000244|PDB:3MNG"
FT   HELIX           104..110
FT                   /evidence="ECO:0000244|PDB:3MNG"
FT   HELIX           112..116
FT                   /evidence="ECO:0000244|PDB:3MNG"
FT   TURN            117..119
FT                   /evidence="ECO:0000244|PDB:3MNG"
FT   STRAND          122..129
FT                   /evidence="ECO:0000244|PDB:3MNG"
FT   HELIX           131..140
FT                   /evidence="ECO:0000244|PDB:3MNG"
FT   TURN            144..146
FT                   /evidence="ECO:0000244|PDB:3MNG"
FT   STRAND          148..151
FT                   /evidence="ECO:0000244|PDB:3MNG"
FT   HELIX           156..161
FT                   /evidence="ECO:0000244|PDB:3MNG"
FT   HELIX           167..169
FT                   /evidence="ECO:0000244|PDB:4MMM"
FT   HELIX           170..173
FT                   /evidence="ECO:0000244|PDB:3MNG"
FT   STRAND          181..186
FT                   /evidence="ECO:0000244|PDB:3MNG"
FT   STRAND          189..195
FT                   /evidence="ECO:0000244|PDB:3MNG"
FT   STRAND          199..203
FT                   /evidence="ECO:0000244|PDB:4MMM"
FT   HELIX           207..213
FT                   /evidence="ECO:0000244|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
//
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