PXDN_XENTR
ID PXDN_XENTR Reviewed; 1457 AA.
AC A4IGL7; Q5HZ61;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Peroxidasin {ECO:0000250|UniProtKB:Q92626};
DE EC=1.11.2.- {ECO:0000250|UniProtKB:Q92626};
DE Contains:
DE RecName: Full=PXDN active fragment {ECO:0000250|UniProtKB:Q92626};
DE Flags: Precursor;
GN Name=pxdn {ECO:0000250|UniProtKB:Q92626}; Synonyms=pxn;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP IDENTIFICATION, AND DEVELOPMENTAL STAGE.
RX PubMed=15614763; DOI=10.1002/dvdy.20226;
RA Tindall A.J., Pownall M.E., Morris I.D., Isaacs H.V.;
RT "Xenopus tropicalis peroxidasin gene is expressed within the developing
RT neural tube and pronephric kidney.";
RL Dev. Dyn. 232:377-384(2005).
CC -!- FUNCTION: Catalyzes the two-electron oxidation of bromide by hydrogen
CC peroxide and generates hypobromite as a reactive intermediate which
CC mediates the formation of sulfilimine cross-links between methionine
CC and hydroxylysine residues within an uncross-linked collagen IV/COL4A1
CC NC1 hexamer and participates to the basement membrane integrity.
CC Moreover brominates alpha2 collagen IV chain/COL4A2 and leads to
CC bromine enrichment of the basement membranes.
CC {ECO:0000250|UniProtKB:Q92626}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O2 + L-lysyl-[collagen] + L-methionyl-[collagen] =
CC [collagen]-L-lysyl-N-S-L-methionyl-[collagen] + H(+) + 2 H2O;
CC Xref=Rhea:RHEA:66020, Rhea:RHEA-COMP:12751, Rhea:RHEA-COMP:16949,
CC Rhea:RHEA-COMP:16951, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16044, ChEBI:CHEBI:16240, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:166867; Evidence={ECO:0000250|UniProtKB:Q92626};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66021;
CC Evidence={ECO:0000250|UniProtKB:Q92626};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=bromide + H2O2 = H2O + hypobromite; Xref=Rhea:RHEA:66016,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15858, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:29250; Evidence={ECO:0000250|UniProtKB:Q92626};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66017;
CC Evidence={ECO:0000250|UniProtKB:Q92626};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hypobromite + L-lysyl-[collagen] + L-methionyl-[collagen] =
CC [collagen]-L-lysyl-N-S-L-methionyl-[collagen] + bromide + H(+) + H2O;
CC Xref=Rhea:RHEA:66024, Rhea:RHEA-COMP:12751, Rhea:RHEA-COMP:16949,
CC Rhea:RHEA-COMP:16951, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15858, ChEBI:CHEBI:16044, ChEBI:CHEBI:29250,
CC ChEBI:CHEBI:29969, ChEBI:CHEBI:166867;
CC Evidence={ECO:0000250|UniProtKB:Q92626};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66025;
CC Evidence={ECO:0000250|UniProtKB:Q92626};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=bromide + H(+) + H2O2 + L-tyrosyl-[protein] = 3-bromo-L-
CC tyrosyl-[protein] + 2 H2O; Xref=Rhea:RHEA:69360, Rhea:RHEA-
CC COMP:10136, Rhea:RHEA-COMP:17686, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15858, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:46858, ChEBI:CHEBI:183512;
CC Evidence={ECO:0000250|UniProtKB:Q92626};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69361;
CC Evidence={ECO:0000250|UniProtKB:Q92626};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hypobromite + L-tyrosyl-[protein] = 3-bromo-L-tyrosyl-
CC [protein] + H2O; Xref=Rhea:RHEA:69356, Rhea:RHEA-COMP:10136,
CC Rhea:RHEA-COMP:17686, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29250, ChEBI:CHEBI:46858, ChEBI:CHEBI:183512;
CC Evidence={ECO:0000250|UniProtKB:Q92626};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69357;
CC Evidence={ECO:0000250|UniProtKB:Q92626};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00298};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00298};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000250|UniProtKB:A5JUY8,
CC ECO:0000255|PROSITE-ProRule:PRU00298};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group covalently per
CC subunit. {ECO:0000250|UniProtKB:A5JUY8, ECO:0000255|PROSITE-
CC ProRule:PRU00298};
CC -!- SUBUNIT: Homotrimer; disulfide-linked. The homotrimer form is
CC predominant. Homooligomer; disulfide-linked. Oligomerization occurs
CC intracellularly before C-terminal proteolytic cleavage.
CC {ECO:0000250|UniProtKB:Q92626}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250|UniProtKB:Q92626}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q92626}. Cell surface
CC {ECO:0000250|UniProtKB:Q92626}. Secreted, extracellular space,
CC extracellular matrix, basement membrane {ECO:0000250|UniProtKB:Q3UQ28}.
CC Note=Enriched in the peritubular space of fibrotic kidneys. Adheres on
CC the cell surface in 'hot spots'. {ECO:0000250|UniProtKB:Q92626}.
CC -!- SUBCELLULAR LOCATION: [PXDN active fragment]: Secreted, extracellular
CC space, extracellular matrix {ECO:0000250|UniProtKB:Q92626}.
CC -!- DEVELOPMENTAL STAGE: Maternal expression is localized to the animal
CC hemisphere where it persists through early cleavage stages. Initial
CC zygotic expression is detected in the developing neural tube and
CC becomes localized to the hindbrain and midbrain. Expressed in the
CC primordium of the pronephric kidney and expression persists in the
CC pronephric tubules and duct throughout development.
CC {ECO:0000269|PubMed:15614763}.
CC -!- DOMAIN: The VWFC domain mediates the covalent links between monomers
CC throught disulfide bridges. Ig-like C2-type domains are required to
CC sulfilimine bond formation. The VWFC domain is not required for
CC trimerization. The LRR domain mediates high affinity binding to
CC laminin-1. {ECO:0000250|UniProtKB:Q92626}.
CC -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:Q92626}.
CC -!- PTM: Processed by FURIN and the proteolytic processing largely depends
CC on the peroxidase activity of PXDN (By similarity). The proteolytic
CC cleavage occurs after intracellular homotrimerization and releases into
CC the extracellular matrix a large, catalytically active fragment and a
CC smaller fragment consisting primarily of the C-terminal VWFC domain.
CC The processing enhances both peroxidase activity and sulfilimine cross-
CC links formation (By similarity). {ECO:0000250|UniProtKB:Q92626}.
CC -!- SIMILARITY: Belongs to the peroxidase family. XPO subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00298}.
CC -!- SEQUENCE CAUTION:
CC Sequence=DAA05635.1; Type=Erroneous initiation; Evidence={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; BC135155; AAI35156.1; -; mRNA.
DR EMBL; BK005589; DAA05635.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_001076815.1; NM_001083346.1.
DR AlphaFoldDB; A4IGL7; -.
DR SMR; A4IGL7; -.
DR PeroxiBase; 4051; XtPxd.
DR PRIDE; A4IGL7; -.
DR GeneID; 493201; -.
DR KEGG; xtr:493201; -.
DR CTD; 7837; -.
DR Xenbase; XB-GENE-923300; pxdn.
DR InParanoid; A4IGL7; -.
DR OrthoDB; 276568at2759; -.
DR Reactome; R-XTR-2243919; Crosslinking of collagen fibrils.
DR Proteomes; UP000008143; Chromosome 5.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0005604; C:basement membrane; ISS:UniProtKB.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0031012; C:extracellular matrix; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016684; F:oxidoreductase activity, acting on peroxide as acceptor; ISS:UniProtKB.
DR GO; GO:0004601; F:peroxidase activity; IBA:GO_Central.
DR GO; GO:0001525; P:angiogenesis; ISS:UniProtKB.
DR GO; GO:0070831; P:basement membrane assembly; ISS:UniProtKB.
DR GO; GO:0071711; P:basement membrane organization; ISS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; ISS:UniProtKB.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR GO; GO:0070207; P:protein homotrimerization; ISS:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd09826; peroxidasin_like; 1.
DR Gene3D; 1.10.640.10; -; 1.
DR Gene3D; 2.60.40.10; -; 4.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
DR InterPro; IPR019791; Haem_peroxidase_animal.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000372; LRRNT.
DR InterPro; IPR034824; Peroxidasin_peroxidase.
DR InterPro; IPR034828; Peroxidasin_vert.
DR InterPro; IPR001007; VWF_dom.
DR PANTHER; PTHR11475:SF75; PTHR11475:SF75; 3.
DR Pfam; PF03098; An_peroxidase; 1.
DR Pfam; PF07679; I-set; 4.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF00093; VWC; 1.
DR PRINTS; PR00457; ANPEROXIDASE.
DR SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 4.
DR SMART; SM00369; LRR_TYP; 5.
DR SMART; SM00082; LRRCT; 1.
DR SMART; SM00013; LRRNT; 1.
DR SMART; SM00214; VWC; 1.
DR SUPFAM; SSF48113; SSF48113; 1.
DR SUPFAM; SSF48726; SSF48726; 4.
DR PROSITE; PS50835; IG_LIKE; 4.
DR PROSITE; PS51450; LRR; 5.
DR PROSITE; PS50292; PEROXIDASE_3; 1.
DR PROSITE; PS01208; VWFC_1; 1.
DR PROSITE; PS50184; VWFC_2; 1.
PE 2: Evidence at transcript level;
KW Basement membrane; Calcium; Disulfide bond; Endoplasmic reticulum;
KW Extracellular matrix; Glycoprotein; Heme; Hydrogen peroxide;
KW Immunoglobulin domain; Iron; Leucine-rich repeat; Metal-binding;
KW Oxidoreductase; Peroxidase; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..1457
FT /note="Peroxidasin"
FT /id="PRO_0000319621"
FT CHAIN 26..1325
FT /note="PXDN active fragment"
FT /evidence="ECO:0000250|UniProtKB:Q92626"
FT /id="PRO_0000455177"
FT DOMAIN 26..53
FT /note="LRRNT"
FT REPEAT 51..74
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 75..98
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 100..122
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 123..146
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 147..170
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 172..194
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT DOMAIN 182..234
FT /note="LRRCT"
FT /evidence="ECO:0000255"
FT DOMAIN 236..324
FT /note="Ig-like C2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 332..418
FT /note="Ig-like C2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 423..510
FT /note="Ig-like C2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 515..600
FT /note="Ig-like C2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 1392..1450
FT /note="VWFC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT REGION 1304..1390
FT /note="Required in homotrimerization"
FT /evidence="ECO:0000250|UniProtKB:Q92626"
FT ACT_SITE 816
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 815
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 817
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 896
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 898
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 900
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 902
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 969
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 1063
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 966
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT SITE 1325
FT /note="Cleavage; by FURIN"
FT /evidence="ECO:0000250|UniProtKB:Q92626"
FT CARBOHYD 630
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 689
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 709
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 721
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1343
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1347
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1434
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 26..32
FT /evidence="ECO:0000250|UniProtKB:Q92626"
FT DISULFID 30..39
FT /evidence="ECO:0000250|UniProtKB:Q92626"
FT DISULFID 186..233
FT /evidence="ECO:0000250|UniProtKB:Q92626"
FT DISULFID 188..212
FT /evidence="ECO:0000250|UniProtKB:Q92626"
FT DISULFID 257..307
FT /evidence="ECO:0000250|UniProtKB:Q92626"
FT DISULFID 353..402
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 444..492
FT /evidence="ECO:0000250|UniProtKB:Q92626"
FT DISULFID 536..584
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 713..874
FT /evidence="ECO:0000250|UniProtKB:Q92626"
FT DISULFID 722..738
FT /evidence="ECO:0000250|UniProtKB:Q92626"
FT DISULFID 726
FT /note="Interchain (with C-1304); in homotrimer"
FT /evidence="ECO:0000250|UniProtKB:Q92626"
FT DISULFID 836..846
FT /evidence="ECO:0000250|UniProtKB:Q92626"
FT DISULFID 840..864
FT /evidence="ECO:0000250|UniProtKB:Q92626"
FT DISULFID 948..959
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1166..1223
FT /evidence="ECO:0000250|UniProtKB:Q92626"
FT DISULFID 1264..1290
FT /evidence="ECO:0000250|UniProtKB:Q92626"
FT DISULFID 1304
FT /note="Interchain (with C-726); in homotrimer"
FT /evidence="ECO:0000250|UniProtKB:Q92626"
SQ SEQUENCE 1457 AA; 163914 MW; 902697AA1C02311A CRC64;
MAGAGSWLYL TAGLLVVALP QLSHSCPSRC LCFRTTVRCM HLMLESVPAV PPHTTILDLR
FNRIKDIQTG AFKHLKNLNT LLLNNNQIKR IPSEAFKDLE NLKYLYLYKN EIQSIDRQAF
KGLASLEQLY LHFNQIETLE PESFNYLPKL ERLFLHNNRI THLVPGTFSQ LESMKRLRLD
SNALHCDCEI LWLADLLKIY SESGNAQAAA TCEYPRRLQG RSVSTITPSE LNCERPRITS
EPQDVDVTFG NTVYFTCRAE GNPKPEIIWL RNNNELSMKD DSRLNLLNDG TLMIQNTKET
DQGIYQCMAK NVAGEVKTHE VTLRYYGTPA TPTFVIQPQN TEVLVGESVT LECSATGQPH
PRVTWTRGDR TPLPSDPRIN ITPSGGLYIQ NVNQDDAGEY TCFATNSVET IHSTAYIIVQ
AVPQFTVVPQ DRNVFEGHTV DFHCEAQGNP KPVIAWTKGG NQLSVDRRHQ VLSSGTLRIL
RVALHDQGQY ECQAVNIVGS KSTAAQLIVQ TRVTPVFATV PNDMTVEVGT DVQIPCSSQG
DPLPIITWNK DGIQVTESGK FHISPHGYLA IRDAGLADQG RYECVARNPI GYSSVSMVLS
VLVPEVSRTG DPFVATSIIE AIATVDRAIN STRTHLFDSR PRSPGDLLAL FRYPRDPYTV
EQARAAEIFE RTLQLIQDHV QSGLMVDLNG TSYHYNDLVS PQYLNMIANL SGCATHRRIN
NCSNMCFHQK YRTHDGTCNN LQHPMWGASL TAFERLLKSV YENGFNLPRG ISGRIYNGFP
LPLPRLVSTT LIGTHTITPD EQFTHMLMQW GQFLDHDLDS TVVALSQARF SDGQDCSVVC
TNDAPCFPIM VPPNDPRVRN NARCMSMVRS SPVCGSGMTS LLMNSVYPRE QMNQLTSYID
ASNVYGSSDH ESNEIRDSAS HRGLLKQGIV QRSGKPLLPF ATGPPTECMR DENESPIPCF
LAGDHRANEQ LGLTSMHTLW FREHNRIATE LLRLNPHWDG DTIYHETRKI VGAQMQHITY
SHWLPKIFGD VGMKMLGEYK SYDPNVNAGI LNEFATAAFR FGHTLINPIL YRLDEKFEPI
PQGHVPLHRA FFSPFRIVNE GGIDPLLRGL IGVAAKMRVT SQLLNTELTE KLFSMAHAVA
LDLAALNVQR GRDHGIPPYH DFRVFCNLST VQTFDDLRNE IKNPDVREKL KRLYGSPLNI
DLFPALMVED LIPGSRLGPT LMCLLTTQFR NIRDGDRFWY ENPGVFTAAQ LTQIKQTSLA
RVLCDNGDNI TKVQHDLFRV AEFPHGYVSC KNIAKMDLRV WQDCCEDCRT RGQFSTFSNH
FRGKRSTEHS YKEDNKEPSS LLNQSVNTTC NTEQPKNLPH VNDFKEFVLD MQKTITGLRK
QIKKLESRLS NTDCTDETGE SHSTKEKWNK DACTKCECYN GHITCFVKSC PPVNCSRPQR
IEGVCCPVCT DDKIQST
