ID   PERE_HUMAN              Reviewed;         715 AA.
AC   P11678; Q4TVP3;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   24-JAN-2024, entry version 213.
DE   RecName: Full=Eosinophil peroxidase;
DE            Short=EPO;
DE            EC=1.11.1.7;
DE   Contains:
DE     RecName: Full=Eosinophil peroxidase light chain;
DE   Contains:
DE     RecName: Full=Eosinophil peroxidase heavy chain;
DE   Flags: Precursor;
GN   Name=EPX; Synonyms=EPER, EPO, EPP;
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 [GENOMIC DNA].
RC   TISSUE=Placenta;
RX   PubMed=2550461; DOI=10.1016/s0021-9258(19)84781-6;
RA   Sakamaki K., Tomonaga M., Tsukui K., Nagata S.;
RT   "Molecular cloning and characterization of a chromosomal gene for human
RT   eosinophil peroxidase.";
RL   J. Biol. Chem. 264:16828-16836(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS MET-40; HIS-122; GLU-249;
RP   ARG-276; LEU-292; PRO-326; LEU-358; HIS-364; THR-441; GLN-496 AND TYR-572.
RG   NIEHS SNPs program;
RL   Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 13-715, AND PROTEIN SEQUENCE OF 140-187 AND
RP   251-288.
RC   TISSUE=Blood;
RX   PubMed=2541222; DOI=10.1084/jem.169.5.1757;
RA   Ten R.M., Pease L.R., McKean D.J., Bell M.P., Gleich G.J.;
RT   "Molecular cloning of the human eosinophil peroxidase. Evidence for the
RT   existence of a peroxidase multigene family.";
RL   J. Exp. Med. 169:1757-1769(1989).
RN   [4]
RP   COVALENT HEME ATTACHMENT, AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Blood;
RX   PubMed=10358043; DOI=10.1074/jbc.274.24.16953;
RA   Oxvig C., Thomsen A.R., Overgaard M.T., Sorensen E.S., Hoejrup P.,
RA   Bjerrum M.J., Gleich G.J., Sottrup-Jensen L.;
RT   "Biochemical evidence for heme linkage through esters with Asp-93 and Glu-
RT   241 in human eosinophil peroxidase. The ester with Asp-93 is only partially
RT   formed in vivo.";
RL   J. Biol. Chem. 274:16953-16958(1999).
RN   [5]
RP   FUNCTION.
RX   PubMed=12540536; DOI=10.1128/iai.71.2.605-613.2003;
RA   Borelli V., Vita F., Shankar S., Soranzo M.R., Banfi E., Scialino G.,
RA   Brochetta C., Zabucchi G.;
RT   "Human eosinophil peroxidase induces surface alteration, killing, and lysis
RT   of Mycobacterium tuberculosis.";
RL   Infect. Immun. 71:605-613(2003).
RN   [6]
RP   FUNCTION, AND NITRATION AT TYR-488.
RX   PubMed=18694936; DOI=10.1074/jbc.m801196200;
RA   Ulrich M., Petre A., Youhnovski N., Proemm F., Schirle M., Schumm M.,
RA   Pero R.S., Doyle A., Checkel J., Kita H., Thiyagarajan N., Acharya K.R.,
RA   Schmid-Grendelmeier P., Simon H.-U., Schwarz H., Tsutsui M., Shimokawa H.,
RA   Bellon G., Lee J.J., Przybylski M., Doering G.;
RT   "Post-translational tyrosine nitration of eosinophil granule toxins
RT   mediated by eosinophil peroxidase.";
RL   J. Biol. Chem. 283:28629-28640(2008).
RN   [7]
RP   VARIANT EPXD HIS-286.
RX   PubMed=7809065; DOI=10.1073/pnas.91.26.12496;
RA   Romano M., Patriarca P., Melo C., Baralle F.E., Dri P.;
RT   "Hereditary eosinophil peroxidase deficiency: immunochemical and
RT   spectroscopic studies and evidence for a compound heterozygosity of the
RT   defect.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:12496-12500(1994).
RN   [8]
RP   VARIANTS HIS-326; LEU-326 AND LEU-358.
RX   PubMed=14657871; DOI=10.1016/j.jaci.2003.08.051;
RA   Nakamura H., Miyagawa K., Ogino K., Endo T., Imai T., Ozasa K.,
RA   Motohashi Y., Matsuzaki I., Sasahara S., Hatta K., Eboshida A.;
RT   "High contribution contrast between the genes of eosinophil peroxidase and
RT   IL-4 receptor alpha-chain in Japanese cedar pollinosis.";
RL   J. Allergy Clin. Immunol. 112:1127-1131(2003).
CC   -!- FUNCTION: Mediates tyrosine nitration of secondary granule proteins in
CC       mature resting eosinophils. Shows significant inhibitory activity
CC       towards Mycobacterium tuberculosis H37Rv by inducing bacterial
CC       fragmentation and lysis. {ECO:0000269|PubMed:12540536,
CC       ECO:0000269|PubMed:18694936}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2
CC         H2O; Xref=Rhea:RHEA:56136, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:139520, ChEBI:CHEBI:139521; EC=1.11.1.7;
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00298};
CC       Note=Binds 1 Ca(2+) ion per heterodimer. {ECO:0000255|PROSITE-
CC       ProRule:PRU00298};
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC       Note=Binds 1 heme b (iron(II)-protoporphyrin IX) covalently through
CC       ester linkages to hydroxylated methyl groups formed auto-catalytically
CC       with hydrogen peroxide at the heme C-1 and C-5 positions. The ester
CC       linkage to Asp-232 was observed in 30% of the chains.;
CC   -!- SUBUNIT: Tetramer of two light chains and two heavy chains.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic granule. Note=Cytoplasmic granules of
CC       eosinophils.
CC   -!- DISEASE: Eosinophil peroxidase deficiency (EPXD) [MIM:261500]: A rare
CC       abnormality without clinical symptoms characterized by decreased or
CC       absent peroxidase activity and decreased volume of the granule matrix
CC       in eosinophils. {ECO:0000269|PubMed:7809065}. Note=The disease is
CC       caused by variants affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the peroxidase family. XPO subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00298}.
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/epx/";
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DR   EMBL; M29913; AAA58458.1; -; Genomic_DNA.
DR   EMBL; M29904; AAA58458.1; JOINED; Genomic_DNA.
DR   EMBL; M29905; AAA58458.1; JOINED; Genomic_DNA.
DR   EMBL; M29906; AAA58458.1; JOINED; Genomic_DNA.
DR   EMBL; M29907; AAA58458.1; JOINED; Genomic_DNA.
DR   EMBL; M29908; AAA58458.1; JOINED; Genomic_DNA.
DR   EMBL; M29909; AAA58458.1; JOINED; Genomic_DNA.
DR   EMBL; M29910; AAA58458.1; JOINED; Genomic_DNA.
DR   EMBL; M29911; AAA58458.1; JOINED; Genomic_DNA.
DR   EMBL; M29912; AAA58458.1; JOINED; Genomic_DNA.
DR   EMBL; DQ054598; AAY43126.1; -; Genomic_DNA.
DR   EMBL; X14346; CAA32530.1; -; mRNA.
DR   CCDS; CCDS11602.1; -.
DR   PIR; A34408; A34408.
DR   RefSeq; NP_000493.1; NM_000502.5.
DR   AlphaFoldDB; P11678; -.
DR   SMR; P11678; -.
DR   BioGRID; 113893; 14.
DR   IntAct; P11678; 4.
DR   STRING; 9606.ENSP00000225371; -.
DR   BindingDB; P11678; -.
DR   ChEMBL; CHEMBL2438; -.
DR   DrugBank; DB01065; Melatonin.
DR   PeroxiBase; 3317; HsEPO.
DR   GlyConnect; 1208; 4 N-Linked glycans (1 site).
DR   GlyCosmos; P11678; 6 sites, 4 glycans.
DR   GlyGen; P11678; 6 sites, 4 N-linked glycans (1 site).
DR   iPTMnet; P11678; -.
DR   PhosphoSitePlus; P11678; -.
DR   BioMuta; EPX; -.
DR   DMDM; 1352738; -.
DR   EPD; P11678; -.
DR   jPOST; P11678; -.
DR   MassIVE; P11678; -.
DR   PaxDb; 9606-ENSP00000225371; -.
DR   PeptideAtlas; P11678; -.
DR   ProteomicsDB; 52797; -.
DR   Pumba; P11678; -.
DR   TopDownProteomics; P11678; -.
DR   Antibodypedia; 30927; 412 antibodies from 28 providers.
DR   DNASU; 8288; -.
DR   Ensembl; ENST00000225371.6; ENSP00000225371.5; ENSG00000121053.6.
DR   GeneID; 8288; -.
DR   KEGG; hsa:8288; -.
DR   MANE-Select; ENST00000225371.6; ENSP00000225371.5; NM_000502.6; NP_000493.1.
DR   UCSC; uc002ivq.4; human.
DR   AGR; HGNC:3423; -.
DR   CTD; 8288; -.
DR   DisGeNET; 8288; -.
DR   GeneCards; EPX; -.
DR   HGNC; HGNC:3423; EPX.
DR   HPA; ENSG00000121053; Tissue enriched (bone).
DR   MalaCards; EPX; -.
DR   MIM; 131399; gene.
DR   MIM; 261500; phenotype.
DR   neXtProt; NX_P11678; -.
DR   OpenTargets; ENSG00000121053; -.
DR   PharmGKB; PA27841; -.
DR   VEuPathDB; HostDB:ENSG00000121053; -.
DR   eggNOG; KOG2408; Eukaryota.
DR   GeneTree; ENSGT00940000156009; -.
DR   HOGENOM; CLU_006087_1_1_1; -.
DR   InParanoid; P11678; -.
DR   OMA; PRWNGDK; -.
DR   OrthoDB; 4560at2759; -.
DR   PhylomeDB; P11678; -.
DR   TreeFam; TF314316; -.
DR   PathwayCommons; P11678; -.
DR   Reactome; R-HSA-6798695; Neutrophil degranulation.
DR   SignaLink; P11678; -.
DR   SIGNOR; P11678; -.
DR   BioGRID-ORCS; 8288; 30 hits in 1153 CRISPR screens.
DR   ChiTaRS; EPX; human.
DR   GeneWiki; Eosinophil_peroxidase; -.
DR   GenomeRNAi; 8288; -.
DR   Pharos; P11678; Tchem.
DR   PRO; PR:P11678; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; P11678; Protein.
DR   Bgee; ENSG00000121053; Expressed in male germ line stem cell (sensu Vertebrata) in testis and 78 other cell types or tissues.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0140825; F:lactoperoxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004601; F:peroxidase activity; IBA:GO_Central.
DR   GO; GO:0042742; P:defense response to bacterium; IBA:GO_Central.
DR   GO; GO:0002215; P:defense response to nematode; IEA:Ensembl.
DR   GO; GO:0072677; P:eosinophil migration; IEA:Ensembl.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0032693; P:negative regulation of interleukin-10 production; IEA:Ensembl.
DR   GO; GO:0032714; P:negative regulation of interleukin-5 production; IEA:Ensembl.
DR   GO; GO:0010936; P:negative regulation of macrophage cytokine production; IEA:Ensembl.
DR   GO; GO:0032753; P:positive regulation of interleukin-4 production; IEA:Ensembl.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   CDD; cd09824; myeloperoxidase_like; 1.
DR   Gene3D; 1.10.640.10; Haem peroxidase domain superfamily, animal type; 1.
DR   InterPro; IPR019791; Haem_peroxidase_animal.
DR   InterPro; IPR010255; Haem_peroxidase_sf.
DR   InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR   PANTHER; PTHR11475:SF63; EOSINOPHIL PEROXIDASE; 1.
DR   PANTHER; PTHR11475; OXIDASE/PEROXIDASE; 1.
DR   Pfam; PF03098; An_peroxidase; 1.
DR   PRINTS; PR00457; ANPEROXIDASE.
DR   SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR   PROSITE; PS00435; PEROXIDASE_1; 1.
DR   PROSITE; PS50292; PEROXIDASE_3; 1.
DR   Genevisible; P11678; HS.
PE   1: Evidence at protein level;
KW   Calcium; Direct protein sequencing; Disease variant; Disulfide bond;
KW   Glycoprotein; Heme; Hydrogen peroxide; Iron; Metal-binding; Nitration;
KW   Oxidoreductase; Peroxidase; Reference proteome; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   PROPEP          18..139
FT                   /evidence="ECO:0000269|PubMed:2541222"
FT                   /id="PRO_0000023639"
FT   CHAIN           140..250
FT                   /note="Eosinophil peroxidase light chain"
FT                   /id="PRO_0000023640"
FT   CHAIN           251..715
FT                   /note="Eosinophil peroxidase heavy chain"
FT                   /id="PRO_0000023641"
FT   ACT_SITE        233
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT   BINDING         232
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /note="covalent; partial"
FT   BINDING         234
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT   BINDING         306
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT   BINDING         308
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT   BINDING         310
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT   BINDING         312
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT   BINDING         380
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /note="covalent"
FT   BINDING         474
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT   SITE            377
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT   MOD_RES         488
FT                   /note="3'-nitrotyrosine"
FT                   /evidence="ECO:0000269|PubMed:18694936"
FT   CARBOHYD        52
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        113
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        327
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        363
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        700
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        708
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        141..152
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT   DISULFID        253..263
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT   DISULFID        257..281
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT   DISULFID        359..370
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT   DISULFID        578..635
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT   DISULFID        676..701
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT   VARIANT         35
FT                   /note="V -> I (in dbSNP:rs34553736)"
FT                   /id="VAR_050485"
FT   VARIANT         40
FT                   /note="I -> M (in dbSNP:rs11079339)"
FT                   /evidence="ECO:0000269|Ref.2"
FT                   /id="VAR_025138"
FT   VARIANT         122
FT                   /note="Q -> H (in dbSNP:rs11652709)"
FT                   /evidence="ECO:0000269|Ref.2"
FT                   /id="VAR_025139"
FT   VARIANT         249
FT                   /note="A -> E (in dbSNP:rs35896669)"
FT                   /evidence="ECO:0000269|Ref.2"
FT                   /id="VAR_025140"
FT   VARIANT         276
FT                   /note="K -> R (in dbSNP:rs35074452)"
FT                   /evidence="ECO:0000269|Ref.2"
FT                   /id="VAR_025141"
FT   VARIANT         286
FT                   /note="R -> H (in EPXD; dbSNP:rs121434566)"
FT                   /evidence="ECO:0000269|PubMed:7809065"
FT                   /id="VAR_015376"
FT   VARIANT         292
FT                   /note="P -> L (in dbSNP:rs33971258)"
FT                   /evidence="ECO:0000269|Ref.2"
FT                   /id="VAR_025142"
FT   VARIANT         326
FT                   /note="R -> H (in dbSNP:rs35832094)"
FT                   /evidence="ECO:0000269|PubMed:14657871"
FT                   /id="VAR_060197"
FT   VARIANT         326
FT                   /note="R -> L"
FT                   /evidence="ECO:0000269|PubMed:14657871"
FT                   /id="VAR_060198"
FT   VARIANT         326
FT                   /note="R -> P (in dbSNP:rs35832094)"
FT                   /evidence="ECO:0000269|Ref.2"
FT                   /id="VAR_025143"
FT   VARIANT         358
FT                   /note="P -> L (probable risk factor for Japanese cedar
FT                   pollinosis; dbSNP:rs35135976)"
FT                   /evidence="ECO:0000269|PubMed:14657871, ECO:0000269|Ref.2"
FT                   /id="VAR_025144"
FT   VARIANT         364
FT                   /note="R -> H (in dbSNP:rs35232062)"
FT                   /evidence="ECO:0000269|Ref.2"
FT                   /id="VAR_025145"
FT   VARIANT         441
FT                   /note="K -> T (in dbSNP:rs35750729)"
FT                   /evidence="ECO:0000269|Ref.2"
FT                   /id="VAR_025146"
FT   VARIANT         458
FT                   /note="V -> M (in dbSNP:rs34817773)"
FT                   /id="VAR_050486"
FT   VARIANT         496
FT                   /note="H -> Q (in dbSNP:rs33955150)"
FT                   /evidence="ECO:0000269|Ref.2"
FT                   /id="VAR_025147"
FT   VARIANT         572
FT                   /note="N -> Y (in dbSNP:rs2302311)"
FT                   /evidence="ECO:0000269|Ref.2"
FT                   /id="VAR_020031"
FT   CONFLICT        13..18
FT                   /note="TLVLAQ -> EFRGQD (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        21
FT                   /note="E -> Q (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        113
FT                   /note="N -> I (in Ref. 3; CAA32530)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        163
FT                   /note="S -> C (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        645..660
FT                   /note="RDGDRFWWQKRGVFTK -> ETETGSGGRTRCFHQ (in Ref. 3; AA
FT                   sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   715 AA;  81040 MW;  CEB4E689A6C46374 CRC64;
     MHLLPALAGV LATLVLAQPC EGTDPASPGA VETSVLRDCI AEAKLLVDAA YNWTQKSIKQ
     RLRSGSASPM DLLSYFKQPV AATRTVVRAA DYMHVALGLL EEKLQPQRSG PFNVTDVLTE
     PQLRLLSQAS GCALRDQAER CSDKYRTITG RCNNKRRPLL GASNQALARW LPAEYEDGLS
     LPFGWTPSRR RNGFLLPLVR AVSNQIVRFP NERLTSDRGR ALMFMQWGQF IDHDLDFSPE
     SPARVAFTAG VDCERTCAQL PPCFPIKIPP NDPRIKNQRD CIPFFRSAPS CPQNKNRVRN
     QINALTSFVD ASMVYGSEVS LSLRLRNRTN YLGLLAINQR FQDNGRALLP FDNLHDDPCL
     LTNRSARIPC FLAGDTRSTE TPKLAAMHTL FMREHNRLAT ELRRLNPRWN GDKLYNEARK
     IMGAMVQIIT YRDFLPLVLG KARARRTLGH YRGYCSNVDP RVANVFTLAF RFGHTMLQPF
     MFRLDSQYRA SAPNSHVPLS SAFFASWRIV YEGGIDPILR GLMATPAKLN RQDAMLVDEL
     RDRLFRQVRR IGLDLAALNM QRSRDHGLPG YNAWRRFCGL SQPRNLAQLS RVLKNQDLAR
     KFLNLYGTPD NIDIWIGAIA EPLLPGARVG PLLACLFENQ FRRARDGDRF WWQKRGVFTK
     RQRKALSRIS LSRIICDNTG ITTVSRDIFR ANIYPRGFVN CSRIPRLNLS AWRGT
//