ID   PRDX4_HUMAN             Reviewed;         271 AA.
AC   Q13162; Q6FHT3;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 215.
DE   RecName: Full=Peroxiredoxin-4;
DE            EC=1.11.1.24 {ECO:0000269|PubMed:21916849, ECO:0000269|PubMed:9388242};
DE   AltName: Full=Antioxidant enzyme AOE372;
DE            Short=AOE37-2;
DE   AltName: Full=Peroxiredoxin IV;
DE            Short=Prx-IV;
DE   AltName: Full=Thioredoxin peroxidase AO372;
DE   AltName: Full=Thioredoxin-dependent peroxide reductase A0372;
DE   AltName: Full=Thioredoxin-dependent peroxiredoxin 4 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=PRDX4;
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], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP   LOCATION, AND SUBUNIT.
RX   PubMed=9388242; DOI=10.1074/jbc.272.49.30952;
RA   Jin D.-Y., Chae H.Z., Rhee S.G., Jeang K.-T.;
RT   "Regulatory role for a novel human thioredoxin peroxidase in NF-kappaB
RT   activation.";
RL   J. Biol. Chem. 272:30952-30961(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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   [4]
RP   PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 38-46.
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19892738; DOI=10.1073/pnas.0908958106;
RA   Xu G., Shin S.B., Jaffrey S.R.;
RT   "Global profiling of protease cleavage sites by chemoselective labeling of
RT   protein N-termini.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:19310-19315(2009).
RN   [5]
RP   PROTEIN SEQUENCE OF 46-66; 81-99; 140-164; 174-208; 213-223 AND 231-263,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA   Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
RL   Submitted (DEC-2008) to UniProtKB.
RN   [6]
RP   OVEROXIDATION AT CYS-124.
RX   PubMed=12059788; DOI=10.1042/bj20020525;
RA   Wagner E., Luche S., Penna L., Chevallet M., van Dorsselaer A.,
RA   Leize-Wagner E., Rabilloud T.;
RT   "A method for detection of overoxidation of cysteines: peroxiredoxins are
RT   oxidized in vivo at the active-site cysteine during oxidative stress.";
RL   Biochem. J. 366:777-785(2002).
RN   [7]
RP   SUBCELLULAR LOCATION.
RX   PubMed=18052930; DOI=10.1042/bj20071428;
RA   Tavender T.J., Sheppard A.M., Bulleid N.J.;
RT   "Peroxiredoxin IV is an endoplasmic reticulum-localized enzyme forming
RT   oligomeric complexes in human cells.";
RL   Biochem. J. 411:191-199(2008).
RN   [8]
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   [9]
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   [10]
RP   CLEAVAGE OF SIGNAL PEPTIDE [LARGE SCALE ANALYSIS] AFTER GLY-37, AND
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   [11]
RP   X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS), AND DISULFIDE BONDS.
RX   PubMed=21994946; DOI=10.1074/jbc.m111.298810;
RA   Cao Z., Tavender T.J., Roszak A.W., Cogdell R.J., Bulleid N.J.;
RT   "Crystal structure of reduced and of oxidized peroxiredoxin IV enzyme
RT   reveals a stable oxidized decamer and a non-disulfide-bonded intermediate
RT   in the catalytic cycle.";
RL   J. Biol. Chem. 286:42257-42266(2011).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS), AND CATALYTIC ACTIVITY.
RX   PubMed=21916849; DOI=10.1042/bj20110380;
RA   Wang X., Wang L., Wang X., Sun F., Wang C.C.;
RT   "Structural insights into the peroxidase activity and inactivation of human
RT   peroxiredoxin 4.";
RL   Biochem. J. 441:113-118(2012).
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. Regulates the activation of NF-kappa-B in the cytosol
CC       by a modulation of I-kappa-B-alpha phosphorylation.
CC       {ECO:0000269|PubMed:9388242}.
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:21916849, ECO:0000269|PubMed:9388242};
CC   -!- SUBUNIT: Homodimer; disulfide-linked, upon oxidation (PubMed:9388242).
CC       5 homodimers assemble to form a ring-like decamer (PubMed:21994946).
CC       Can form heterodimers with PRDX1 (PubMed:9388242).
CC       {ECO:0000269|PubMed:21994946, ECO:0000269|PubMed:9388242}.
CC   -!- INTERACTION:
CC       Q13162; P54253: ATXN1; NbExp=4; IntAct=EBI-2211957, EBI-930964;
CC       Q13162; P18428: LBP; NbExp=4; IntAct=EBI-2211957, EBI-3927059;
CC       Q13162; P07237: P4HB; NbExp=2; IntAct=EBI-2211957, EBI-395883;
CC       Q13162; P30101: PDIA3; NbExp=2; IntAct=EBI-2211957, EBI-979862;
CC       Q13162; Q15084: PDIA6; NbExp=2; IntAct=EBI-2211957, EBI-1043087;
CC       Q13162; P21731: TBXA2R; NbExp=3; IntAct=EBI-2211957, EBI-2625082;
CC       Q13162; Q8NBS9: TXNDC5; NbExp=2; IntAct=EBI-2211957, EBI-2510815;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18052930,
CC       ECO:0000269|PubMed:9388242}. Endoplasmic reticulum
CC       {ECO:0000269|PubMed:18052930}. Note=Cotranslationally translocated to
CC       and retained within the endoplasmic reticulum. A small fraction of the
CC       protein is cytoplasmic. {ECO:0000269|PubMed:18052930}.
CC   -!- PTM: The enzyme can be inactivated by further oxidation of the cysteine
CC       sulfenic acid (C(P)-SOH) to sulphinic acid (C(P)-SO2H) and sulphonic
CC       acid (C(P)-SO3H) instead of its condensation to a disulfide bond.
CC       {ECO:0000269|PubMed:12059788, ECO:0000269|PubMed:21916849}.
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 typical 2-Cys
CC       peroxiredoxin, C(R) is provided by the other dimeric subunit to form an
CC       intersubunit disulfide. The disulfide is subsequently reduced by
CC       thioredoxin. {ECO:0000305|PubMed:21994946}.
CC   -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
CC       {ECO:0000305}.
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; U25182; AAB95175.1; -; mRNA.
DR   EMBL; CR541668; CAG46469.1; -; mRNA.
DR   EMBL; CR541705; CAG46506.1; -; mRNA.
DR   EMBL; BC003609; AAH03609.1; -; mRNA.
DR   EMBL; BC007107; AAH07107.1; -; mRNA.
DR   EMBL; BC016770; AAH16770.1; -; mRNA.
DR   CCDS; CCDS14206.1; -.
DR   PIR; G01790; G01790.
DR   RefSeq; NP_006397.1; NM_006406.1.
DR   PDB; 2PN8; X-ray; 1.80 A; A/B/C/D/E/F/G/H/I/J=84-271.
DR   PDB; 3TJB; X-ray; 2.38 A; A/B/C/D/E=38-271.
DR   PDB; 3TJF; X-ray; 2.04 A; A/B/C/D/E=38-271.
DR   PDB; 3TJG; X-ray; 2.24 A; A/B/C/D/E=38-271.
DR   PDB; 3TJJ; X-ray; 1.91 A; A/B/C/D/E=38-271.
DR   PDB; 3TJK; X-ray; 2.09 A; A/B/C/D/E=38-271.
DR   PDB; 3TKP; X-ray; 2.49 A; A/B/C/D/E=38-271.
DR   PDB; 3TKQ; X-ray; 2.22 A; A/B/C/D/E=38-271.
DR   PDB; 3TKR; X-ray; 2.10 A; A/B/C/D/E/F/G/H/I/J=38-271.
DR   PDB; 3TKS; X-ray; 2.40 A; A/B/C/D/E=38-271.
DR   PDB; 4RQX; X-ray; 2.26 A; A/B/C/D/E=79-271.
DR   PDB; 5HQP; X-ray; 2.60 A; A/B=38-271.
DR   PDB; 8EKW; EM; 2.83 A; A/B/C/D/E/F/G/H/I/J=1-271.
DR   PDB; 8EKY; EM; 3.47 A; A/B/C/D/E/F/G/H/I/J=1-271.
DR   PDBsum; 2PN8; -.
DR   PDBsum; 3TJB; -.
DR   PDBsum; 3TJF; -.
DR   PDBsum; 3TJG; -.
DR   PDBsum; 3TJJ; -.
DR   PDBsum; 3TJK; -.
DR   PDBsum; 3TKP; -.
DR   PDBsum; 3TKQ; -.
DR   PDBsum; 3TKR; -.
DR   PDBsum; 3TKS; -.
DR   PDBsum; 4RQX; -.
DR   PDBsum; 5HQP; -.
DR   PDBsum; 8EKW; -.
DR   PDBsum; 8EKY; -.
DR   AlphaFoldDB; Q13162; -.
DR   EMDB; EMD-28214; -.
DR   EMDB; EMD-28217; -.
DR   SMR; Q13162; -.
DR   BioGRID; 115800; 221.
DR   IntAct; Q13162; 78.
DR   MINT; Q13162; -.
DR   STRING; 9606.ENSP00000368646; -.
DR   ChEMBL; CHEMBL4295812; -.
DR   PeroxiBase; 4530; Hs2CysPrx04.
DR   GlyGen; Q13162; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q13162; -.
DR   PhosphoSitePlus; Q13162; -.
DR   SwissPalm; Q13162; -.
DR   BioMuta; PRDX4; -.
DR   DMDM; 3024727; -.
DR   OGP; Q13162; -.
DR   REPRODUCTION-2DPAGE; IPI00011937; -.
DR   CPTAC; CPTAC-1448; -.
DR   CPTAC; CPTAC-1449; -.
DR   CPTAC; CPTAC-1450; -.
DR   CPTAC; CPTAC-1451; -.
DR   CPTAC; CPTAC-713; -.
DR   CPTAC; CPTAC-714; -.
DR   EPD; Q13162; -.
DR   jPOST; Q13162; -.
DR   MassIVE; Q13162; -.
DR   PaxDb; 9606-ENSP00000368646; -.
DR   PeptideAtlas; Q13162; -.
DR   ProteomicsDB; 59198; -.
DR   Pumba; Q13162; -.
DR   TopDownProteomics; Q13162; -.
DR   ABCD; Q13162; 2 sequenced antibodies.
DR   Antibodypedia; 3275; 524 antibodies from 38 providers.
DR   CPTC; Q13162; 5 antibodies.
DR   DNASU; 10549; -.
DR   Ensembl; ENST00000379341.9; ENSP00000368646.4; ENSG00000123131.13.
DR   GeneID; 10549; -.
DR   KEGG; hsa:10549; -.
DR   MANE-Select; ENST00000379341.9; ENSP00000368646.4; NM_006406.2; NP_006397.1.
DR   AGR; HGNC:17169; -.
DR   CTD; 10549; -.
DR   DisGeNET; 10549; -.
DR   GeneCards; PRDX4; -.
DR   HGNC; HGNC:17169; PRDX4.
DR   HPA; ENSG00000123131; Tissue enriched (pancreas).
DR   MIM; 300927; gene.
DR   neXtProt; NX_Q13162; -.
DR   OpenTargets; ENSG00000123131; -.
DR   PharmGKB; PA33725; -.
DR   VEuPathDB; HostDB:ENSG00000123131; -.
DR   eggNOG; KOG0852; Eukaryota.
DR   GeneTree; ENSGT00940000153430; -.
DR   HOGENOM; CLU_042529_21_1_1; -.
DR   InParanoid; Q13162; -.
DR   OMA; KPAPEWE; -.
DR   OrthoDB; 47465at2759; -.
DR   PhylomeDB; Q13162; -.
DR   TreeFam; TF105181; -.
DR   BRENDA; 1.11.1.24; 2681.
DR   PathwayCommons; Q13162; -.
DR   Reactome; R-HSA-6798695; Neutrophil degranulation.
DR   SignaLink; Q13162; -.
DR   BioGRID-ORCS; 10549; 21 hits in 782 CRISPR screens.
DR   ChiTaRS; PRDX4; human.
DR   EvolutionaryTrace; Q13162; -.
DR   GeneWiki; PRDX4; -.
DR   GenomeRNAi; 10549; -.
DR   Pharos; Q13162; Tbio.
DR   PRO; PR:Q13162; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   RNAct; Q13162; Protein.
DR   Bgee; ENSG00000123131; Expressed in body of pancreas and 214 other cell types or tissues.
DR   ExpressionAtlas; Q13162; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR   GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0060090; F:molecular adaptor activity; EXP:DisProt.
DR   GO; GO:0140313; F:molecular sequestering activity; IDA:DisProt.
DR   GO; GO:0008379; F:thioredoxin peroxidase activity; IBA:GO_Central.
DR   GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR   GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
DR   GO; GO:0007252; P:I-kappaB phosphorylation; TAS:ProtInc.
DR   GO; GO:0008584; P:male gonad development; IEA:Ensembl.
DR   GO; GO:2000255; P:negative regulation of male germ cell proliferation; IEA:Ensembl.
DR   GO; GO:0022417; P:protein maturation by protein folding; IEA:Ensembl.
DR   GO; GO:0006979; P:response to oxidative stress; IBA:GO_Central.
DR   GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR   CDD; cd03015; PRX_Typ2cys; 1.
DR   DisProt; DP02764; -.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR000866; AhpC/TSA.
DR   InterPro; IPR019479; Peroxiredoxin_C.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR10681:SF173; PEROXIREDOXIN-4; 1.
DR   PANTHER; PTHR10681; THIOREDOXIN PEROXIDASE; 1.
DR   Pfam; PF10417; 1-cysPrx_C; 1.
DR   Pfam; PF00578; AhpC-TSA; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
DR   UCD-2DPAGE; Q13162; -.
DR   Genevisible; Q13162; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Antioxidant; Cytoplasm; Direct protein sequencing;
KW   Disulfide bond; Endoplasmic reticulum; Oxidoreductase; Peroxidase;
KW   Redox-active center; Reference proteome; Signal.
FT   SIGNAL          1..37
FT                   /evidence="ECO:0000269|PubMed:19892738,
FT                   ECO:0007744|PubMed:25944712"
FT   CHAIN           38..271
FT                   /note="Peroxiredoxin-4"
FT                   /id="PRO_0000135098"
FT   DOMAIN          79..237
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   ACT_SITE        124
FT                   /note="Cysteine sulfenic acid (-SOH) intermediate"
FT                   /evidence="ECO:0000305|PubMed:12059788,
FT                   ECO:0000305|PubMed:21916849"
FT   DISULFID        124
FT                   /note="Interchain (with C-245); in linked form"
FT                   /evidence="ECO:0000269|PubMed:21994946,
FT                   ECO:0007744|PDB:3TJB, ECO:0007744|PDB:3TJG"
FT   DISULFID        245
FT                   /note="Interchain (with C-124); in linked form"
FT                   /evidence="ECO:0000269|PubMed:21994946,
FT                   ECO:0007744|PDB:3TJB, ECO:0007744|PDB:3TJG"
FT   CONFLICT        12
FT                   /note="P -> S (in Ref. 3; CAG46469)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        51
FT                   /note="C -> Y (in Ref. 3; CAG46469)"
FT                   /evidence="ECO:0000305"
FT   STRAND          75..78
FT                   /evidence="ECO:0007829|PDB:3TJK"
FT   STRAND          89..94
FT                   /evidence="ECO:0007829|PDB:2PN8"
FT   STRAND          97..102
FT                   /evidence="ECO:0007829|PDB:2PN8"
FT   HELIX           103..106
FT                   /evidence="ECO:0007829|PDB:2PN8"
FT   STRAND          109..115
FT                   /evidence="ECO:0007829|PDB:2PN8"
FT   HELIX           123..133
FT                   /evidence="ECO:0007829|PDB:2PN8"
FT   HELIX           135..139
FT                   /evidence="ECO:0007829|PDB:2PN8"
FT   TURN            140..142
FT                   /evidence="ECO:0007829|PDB:2PN8"
FT   STRAND          143..151
FT                   /evidence="ECO:0007829|PDB:2PN8"
FT   HELIX           153..160
FT                   /evidence="ECO:0007829|PDB:2PN8"
FT   HELIX           164..166
FT                   /evidence="ECO:0007829|PDB:2PN8"
FT   STRAND          176..178
FT                   /evidence="ECO:0007829|PDB:2PN8"
FT   STRAND          180..182
FT                   /evidence="ECO:0007829|PDB:5HQP"
FT   HELIX           183..187
FT                   /evidence="ECO:0007829|PDB:2PN8"
FT   TURN            193..195
FT                   /evidence="ECO:0007829|PDB:2PN8"
FT   STRAND          196..198
FT                   /evidence="ECO:0007829|PDB:2PN8"
FT   STRAND          200..205
FT                   /evidence="ECO:0007829|PDB:2PN8"
FT   STRAND          209..217
FT                   /evidence="ECO:0007829|PDB:2PN8"
FT   HELIX           225..241
FT                   /evidence="ECO:0007829|PDB:2PN8"
FT   STRAND          256..258
FT                   /evidence="ECO:0007829|PDB:8EKY"
FT   TURN            260..262
FT                   /evidence="ECO:0007829|PDB:2PN8"
FT   HELIX           263..267
FT                   /evidence="ECO:0007829|PDB:2PN8"
FT   TURN            268..270
FT                   /evidence="ECO:0007829|PDB:3TKS"
SQ   SEQUENCE   271 AA;  30540 MW;  7E56B580049FC60F CRC64;
     MEALPLLAAT TPDHGRHRRL LLLPLLLFLL PAGAVQGWET EERPRTREEE CHFYAGGQVY
     PGEASRVSVA DHSLHLSKAK ISKPAPYWEG TAVIDGEFKE LKLTDYRGKY LVFFFYPLDF
     TFVCPTEIIA FGDRLEEFRS INTEVVACSV DSQFTHLAWI NTPRRQGGLG PIRIPLLSDL
     THQISKDYGV YLEDSGHTLR GLFIIDDKGI LRQITLNDLP VGRSVDETLR LVQAFQYTDK
     HGEVCPAGWK PGSETIIPDP AGKLKYFDKL N
//