ID PRDX5_HUMAN Reviewed; 214 AA. AC P30044; A6NC19; A6NG06; B7ZLJ4; B7ZVW3; Q14CK0; Q6IAF2; Q9UBU5; AC Q9UJU4; Q9UKX4; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 11-JAN-2011, sequence version 4. DT 04-MAR-2015, entry version 162. DE RecName: Full=Peroxiredoxin-5, mitochondrial; DE EC=1.11.1.15; 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 reductase; DE Flags: Precursor; GN Name=PRDX5; Synonyms=ACR1; ORFNames=SBBI10; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MITOCHONDRIAL), AND VARIANT RP 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., RA Krutilina R., Oei S.L., Griesenbeck J., Buchlow G., Tomilin N.; RT "A novel human DNA-binding protein with sequence similarity to a RT subfamily of redox proteins which is able to repress RNA-polymerase- RT III-driven 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), AND RP CHARACTERIZATION. 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 RP OF 54-90, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, CHARACTERIZATION, RP AND VARIANT 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 RT antioxidant enzyme of the peroxiredoxin family."; RL J. Biol. Chem. 274:30451-30458(1999). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CYTOPLASMIC+PEROXISOMAL), AND RP VARIANT 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], MUTAGENESIS, AND CHARACTERIZATION. 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 RP 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 RP 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., RA Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., RA Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., RA Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.; RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal RT axis 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 RP VARIANT 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., RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S., RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., RA 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 RP 4), 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 RT project: 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 RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., RA Walther T.C., 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., RA Buerckstuemmer T., 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., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [17] 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., RA 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 [18] 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 RT with an intramolecular disulfide bond confirm the proposed enzymatic RT mechanism for atypical 2-Cys peroxiredoxins."; RL Arch. Biochem. Biophys. 477:98-104(2008). RN [19] 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 [20] 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., RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., RA Vogelstein B., Kinzler K.W., Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal RT cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: Reduces hydrogen peroxide and alkyl hydroperoxides with CC reducing equivalents provided through the thioredoxin system. CC Involved in intracellular redox signaling. CC -!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH. CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:20643143}. CC -!- SUBCELLULAR LOCATION: Isoform Mitochondrial: Mitochondrion. CC -!- SUBCELLULAR LOCATION: Isoform Cytoplasmic+peroxisomal: Cytoplasm. CC Peroxisome. 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 Note=No experimental confirmation available.; CC Name=4; CC IsoId=P30044-4; Sequence=VSP_046682; CC Note=Produced by alternative splicing.; CC -!- TISSUE SPECIFICITY: Widely expressed. CC {ECO:0000269|PubMed:10521424}. CC -!- SIMILARITY: Belongs to the peroxiredoxin 2 family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 thioredoxin domain. {ECO:0000255|PROSITE- CC ProRule:PRU00691}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF17200.1; Type=Frameshift; Positions=14, 30; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/prdx5/"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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. DR RefSeq; NP_857634.1; NM_181651.2. DR RefSeq; NP_857635.1; NM_181652.2. DR UniGene; Hs.502823; -. 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 ProteinModelPortal; P30044; -. DR SMR; P30044; 54-214. DR BioGrid; 117352; 34. DR IntAct; P30044; 5. DR MINT; MINT-5002532; -. DR STRING; 9606.ENSP00000265462; -. DR DrugBank; DB00995; Auranofin. DR PeroxiBase; 4448; HsPrxV. DR PhosphoSite; P30044; -. DR DMDM; 317373539; -. DR OGP; P30044; -. DR REPRODUCTION-2DPAGE; IPI00759663; -. DR SWISS-2DPAGE; P30044; -. DR UCD-2DPAGE; P30044; -. DR MaxQB; P30044; -. DR PaxDb; P30044; -. DR PRIDE; P30044; -. 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.3; human. [P30044-1] DR CTD; 25824; -. DR GeneCards; GC11P064085; -. DR HGNC; HGNC:9355; PRDX5. DR HPA; CAB008661; -. DR HPA; HPA037915; -. DR HPA; HPA037916; -. DR MIM; 606583; gene. DR neXtProt; NX_P30044; -. DR PharmGKB; PA33726; -. DR eggNOG; COG0678; -. DR GeneTree; ENSGT00390000018173; -. DR HOGENOM; HOG000255884; -. DR HOVERGEN; HBG053675; -. DR InParanoid; P30044; -. DR KO; K11187; -. DR OMA; KAWGEST; -. DR OrthoDB; EOG77Q4XX; -. DR PhylomeDB; P30044; -. DR TreeFam; TF105182; -. DR Reactome; REACT_172715; Detoxification of Reactive Oxygen Species. DR ChiTaRS; PRDX5; human. DR EvolutionaryTrace; P30044; -. DR GeneWiki; PRDX5; -. DR GenomeRNAi; 25824; -. DR NextBio; 35462441; -. DR PRO; PR:P30044; -. DR Proteomes; UP000005640; Chromosome 11. DR Bgee; P30044; -. DR CleanEx; HS_PRDX5; -. DR ExpressionAtlas; P30044; baseline and differential. DR Genevestigator; P30044; -. 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:0005615; C:extracellular space; IDA:UniProtKB. DR GO; GO:0070062; C:extracellular vesicular exosome; IDA: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:0046983; F:protein dimerization activity; IDA:UniProtKB. DR GO; GO:0005102; F:receptor binding; IPI:UniProtKB. DR GO; GO:0001016; F:RNA polymerase III regulatory region DNA binding; IDA:UniProtKB. 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:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:GOC. DR GO; GO:0051354; P:negative regulation of oxidoreductase activity; IDA:UniProtKB. DR GO; GO:0016480; P:negative regulation of transcription from RNA polymerase III promoter; 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 GO; GO:0000302; P:response to reactive oxygen species; TAS:Reactome. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR013740; Redoxin. DR InterPro; IPR012336; Thioredoxin-like_fold. 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; KW Alternative splicing; Antioxidant; Complete proteome; Cytoplasm; KW Direct protein sequencing; Disulfide bond; Mitochondrion; KW Oxidoreductase; Peroxidase; Peroxisome; Polymorphism; KW Redox-active center; Reference proteome; Transit peptide. FT TRANSIT 1 52 Mitochondrion. {ECO:0000255}. FT CHAIN 53 214 Peroxiredoxin-5, mitochondrial. FT /FTId=PRO_0000023793. FT DOMAIN 56 214 Thioredoxin. {ECO:0000255|PROSITE- FT ProRule:PRU00691}. FT MOTIF 212 214 Microbody targeting signal. FT {ECO:0000250}. FT ACT_SITE 100 100 Cysteine sulfenic acid (-SOH) FT intermediate. FT {ECO:0000305|PubMed:20643143}. FT MOD_RES 75 75 N6-acetyllysine. FT {ECO:0000250|UniProtKB:P99029}. FT MOD_RES 83 83 N6-acetyllysine; alternate. FT {ECO:0000269|PubMed:19608861}. FT MOD_RES 83 83 N6-succinyllysine; alternate. FT {ECO:0000250|UniProtKB:P99029}. FT MOD_RES 116 116 N6-succinyllysine. FT {ECO:0000250|UniProtKB:P99029}. FT DISULFID 100 204 Redox-active. {ECO:0000255|PROSITE- FT ProRule:PRU00691, FT ECO:0000269|PubMed:18489898}. FT VAR_SEQ 1 52 Missing (in isoform FT Cytoplasmic+peroxisomal). FT {ECO:0000303|PubMed:10514471, FT ECO:0000303|PubMed:10679306, FT ECO:0000303|PubMed:10931946, FT ECO:0000303|Ref.6}. FT /FTId=VSP_018829. FT VAR_SEQ 57 145 Missing (in isoform 4). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_046682. FT VAR_SEQ 102 145 Missing (in isoform 3). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_045783. FT VARIANT 33 33 Y -> C (in dbSNP:rs7938623). FT {ECO:0000269|PubMed:10095767, FT ECO:0000269|PubMed:10521424, FT ECO:0000269|PubMed:10679306, FT ECO:0000269|PubMed:15489334, FT ECO:0000269|Ref.10, ECO:0000269|Ref.7, FT ECO:0000269|Ref.9}. FT /FTId=VAR_025049. FT VARIANT 157 157 F -> L (in a breast cancer sample; FT somatic mutation). FT {ECO:0000269|PubMed:16959974}. FT /FTId=VAR_036406. FT MUTAGEN 100 100 C->S: Complete loss of activity. FT {ECO:0000269|PubMed:10751410}. FT MUTAGEN 125 125 C->S: No change in activity. FT {ECO:0000269|PubMed:10751410}. FT MUTAGEN 204 204 C->S: Complete loss of activity. FT {ECO:0000269|PubMed:10751410}. FT CONFLICT 141 141 H -> T (in Ref. 4; AAF04856). FT {ECO:0000305}. FT STRAND 66 68 {ECO:0000244|PDB:3MNG}. FT HELIX 72 74 {ECO:0000244|PDB:2VL9}. FT STRAND 75 77 {ECO:0000244|PDB:3MNG}. FT HELIX 78 81 {ECO:0000244|PDB:3MNG}. FT TURN 82 84 {ECO:0000244|PDB:3MNG}. FT STRAND 85 91 {ECO:0000244|PDB:3MNG}. FT HELIX 98 102 {ECO:0000244|PDB:3MNG}. FT HELIX 104 110 {ECO:0000244|PDB:3MNG}. FT HELIX 112 116 {ECO:0000244|PDB:3MNG}. FT TURN 117 119 {ECO:0000244|PDB:3MNG}. FT STRAND 122 129 {ECO:0000244|PDB:3MNG}. FT HELIX 131 140 {ECO:0000244|PDB:3MNG}. FT TURN 144 146 {ECO:0000244|PDB:3MNG}. FT STRAND 148 151 {ECO:0000244|PDB:3MNG}. FT HELIX 156 161 {ECO:0000244|PDB:3MNG}. FT HELIX 167 169 {ECO:0000244|PDB:4MMM}. FT HELIX 170 173 {ECO:0000244|PDB:3MNG}. FT STRAND 181 186 {ECO:0000244|PDB:3MNG}. FT STRAND 189 195 {ECO:0000244|PDB:3MNG}. FT STRAND 199 203 {ECO:0000244|PDB:4MMM}. FT HELIX 207 213 {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 //