PXDN2_CAEEL
ID PXDN2_CAEEL Reviewed; 1328 AA.
AC G5EG78;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Peroxidasin homolog pxn-2 {ECO:0000305};
DE EC=1.11.2.- {ECO:0000250|UniProtKB:Q92626};
DE Flags: Precursor;
GN Name=pxn-2 {ECO:0000312|WormBase:K09C8.5};
GN ORFNames=K09C8.5 {ECO:0000312|WormBase:K09C8.5};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND MUTAGENESIS OF HIS-739; HIS-755; GLU-853; ARG-1178 AND GLY-1314.
RX PubMed=20876652; DOI=10.1242/dev.049189;
RA Gotenstein J.R., Swale R.E., Fukuda T., Wu Z., Giurumescu C.A.,
RA Goncharov A., Jin Y., Chisholm A.D.;
RT "The C. elegans peroxidasin PXN-2 is essential for embryonic morphogenesis
RT and inhibits adult axon regeneration.";
RL Development 137:3603-3613(2010).
RN [3] {ECO:0000305}
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=25475546; DOI=10.14348/molcells.2015.2202;
RA Lee J., Bandyopadhyay J., Lee J.I., Cho I., Park D., Cho J.H.;
RT "A role for peroxidasin PXN-1 in aspects of C. elegans development.";
RL Mol. Cells 38:51-57(2015).
RN [4] {ECO:0000305}
RP DISRUPTION PHENOTYPE.
RX PubMed=26194821; DOI=10.14348/molcells.2015.0124;
RA Cho I., Hwang G.J., Cho J.H.;
RT "pxn-1 and pxn-2 May Interact Negatively during Neuronal Development and
RT Aging in C. elegans.";
RL Mol. Cells 38:729-733(2015).
RN [5] {ECO:0000305}
RP FUNCTION, AND MUTAGENESIS OF HIS-739 AND GLU-853.
RX PubMed=29440357; DOI=10.1534/genetics.118.300731;
RA Gotenstein J.R., Koo C.C., Ho T.W., Chisholm A.D.;
RT "Genetic Suppression of Basement Membrane Defects in Caenorhabditis elegans
RT by Gain of Function in Extracellular Matrix and Cell-Matrix Attachment
RT Genes.";
RL Genetics 208:1499-1512(2018).
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 (By similarity). Required for embryonic morphogenesis
CC playing a role in epidermal elongation at the twofold stage of
CC embryonic development (PubMed:20876652). Required post-embryonically
CC for basement membrane integrity and muscle-epidermal attachments, and
CC specifically in the function of basement membrane components such as
CC the type IV collagens (PubMed:20876652, PubMed:29440357). May have a
CC role in inhibiting axon regeneration (PubMed:20876652). May
CC functionally antagonize the peroxidasin pxn-1 (PubMed:20876652).
CC {ECO:0000250|UniProtKB:Q92626, ECO:0000269|PubMed:20876652,
CC ECO:0000269|PubMed:29440357}.
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 heterodimer. {ECO:0000255|PROSITE-
CC ProRule:PRU00298};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00298};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group covalently per
CC heterodimer. {ECO:0000255|PROSITE-ProRule:PRU00298};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20876652,
CC ECO:0000269|PubMed:25475546}. Secreted, extracellular space,
CC extracellular matrix, basement membrane {ECO:0000269|PubMed:20876652}.
CC Note=Localizes to the basement membrane in between the epidermis and
CC muscles. {ECO:0000269|PubMed:20876652}.
CC -!- TISSUE SPECIFICITY: Expressed in vulval muscles and in some neurons
CC including PVQ (PubMed:20876652). Expressed in the hypodermis and in
CC coelomocytes (PubMed:25475546). {ECO:0000269|PubMed:20876652,
CC ECO:0000269|PubMed:25475546}.
CC -!- DEVELOPMENTAL STAGE: Expressed in most differentiated epidermal cells
CC throughout development from embryogenesis to adulthood
CC (PubMed:20876652). In late gastrulation, expressed in epidermal
CC precursors (PubMed:20876652). {ECO:0000269|PubMed:20876652}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes no neuronal
CC defects (PubMed:26194821). Furthermore RNAi-mediated knockdown rescues
CC the neuronal defects of the pxn-1 mutant (ok785) (PubMed:26194821).
CC {ECO:0000269|PubMed:26194821}.
CC -!- SIMILARITY: Belongs to the peroxidase family. XPO subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00298}.
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DR EMBL; BX284606; CAA91999.1; -; Genomic_DNA.
DR PIR; T23007; T23007.
DR RefSeq; NP_509834.1; NM_077433.3.
DR AlphaFoldDB; G5EG78; -.
DR SMR; G5EG78; -.
DR STRING; 6239.K09C8.5; -.
DR EPD; G5EG78; -.
DR PaxDb; G5EG78; -.
DR PeptideAtlas; G5EG78; -.
DR EnsemblMetazoa; K09C8.5.1; K09C8.5.1; WBGene00004257.
DR GeneID; 181288; -.
DR KEGG; cel:CELE_K09C8.5; -.
DR CTD; 181288; -.
DR WormBase; K09C8.5; CE18882; WBGene00004257; pxn-2.
DR eggNOG; KOG0619; Eukaryota.
DR eggNOG; KOG2408; Eukaryota.
DR GeneTree; ENSGT00940000168557; -.
DR HOGENOM; CLU_006087_0_0_1; -.
DR InParanoid; G5EG78; -.
DR OMA; PCMEFER; -.
DR OrthoDB; 276568at2759; -.
DR PhylomeDB; G5EG78; -.
DR Reactome; R-CEL-209968; Thyroxine biosynthesis.
DR Reactome; R-CEL-2243919; Crosslinking of collagen fibrils.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR Reactome; R-CEL-8941413; Events associated with phagocytolytic activity of PMN cells.
DR PRO; PR:G5EG78; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00004257; Expressed in embryo and 2 other tissues.
DR GO; GO:0005604; C:basement membrane; IDA: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:0004601; F:peroxidase activity; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; IMP:WormBase.
DR GO; GO:0071711; P:basement membrane organization; IMP:WormBase.
DR GO; GO:0010172; P:embryonic body morphogenesis; IMP:WormBase.
DR GO; GO:0016203; P:muscle attachment; IMP:WormBase.
DR GO; GO:0048681; P:negative regulation of axon regeneration; IMP:WormBase.
DR GO; GO:0110011; P:regulation of basement membrane organization; IMP: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; -; 2.
DR Gene3D; 3.80.10.10; -; 2.
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 Pfam; PF03098; An_peroxidase; 1.
DR Pfam; PF07679; I-set; 2.
DR Pfam; PF13855; LRR_8; 1.
DR PRINTS; PR00457; ANPEROXIDASE.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 2.
DR SMART; SM00369; LRR_TYP; 3.
DR SMART; SM00013; LRRNT; 1.
DR SUPFAM; SSF48113; SSF48113; 1.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 2.
DR PROSITE; PS51450; LRR; 4.
DR PROSITE; PS50292; PEROXIDASE_3; 1.
PE 1: Evidence at protein level;
KW Basement membrane; Disulfide bond; Extracellular matrix; Glycoprotein;
KW Heme; Iron; Leucine-rich repeat; Metal-binding; Oxidoreductase; Peroxidase;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..1328
FT /note="Peroxidasin homolog pxn-2"
FT /id="PRO_5003476082"
FT DOMAIN 17..45
FT /note="LRRNT"
FT REPEAT 42..66
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 67..90
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 92..114
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 116..137
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 138..161
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 164..191
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT DOMAIN 346..438
FT /note="Ig-like C2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 445..532
FT /note="Ig-like C2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT REPEAT 1085..1109
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 1204..1225
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REGION 305..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1266..1297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1272..1291
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 755
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 754
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 756
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 839
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 841
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 843
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 845
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 913
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 1008
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 910
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 403
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 455
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 630
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 776
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 894
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 373..422
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 466..516
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 660..676
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT DISULFID 775..785
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT DISULFID 779..807
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT DISULFID 1111..1168
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT DISULFID 1209..1236
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT MUTAGEN 739
FT /note="H->Y: In ju436; viable with variably abnormal
FT epidermal morphology (vab phenotype) in 20% of offspring.
FT Enhances the lethality in the emb-9 b189 mutant."
FT /evidence="ECO:0000269|PubMed:20876652,
FT ECO:0000269|PubMed:29440357"
FT MUTAGEN 755
FT /note="H->A: Suppresses the lethal phenotypes and enhances
FT the variably abnormal epidermal morphology (vab phenotype)
FT of the pxn-2 ju358 mutant."
FT /evidence="ECO:0000269|PubMed:20876652"
FT MUTAGEN 853
FT /note="E->K: In ju358; 31% embryonic and 47% larval
FT lethality. Variably abnormal epidermal morphology (vab
FT phenotype) in 21% of remaining offspring. Progressive
FT detachment of body wall muscles from the epidermis during
FT larval development and defective vulval muscle attachment,
FT which results in egg-laying defects. Progressive distortion
FT of the anterior pharyngeal bulb in adults. Defective axon
FT guidance and promotes axon regrowth following injury.
FT Basement membrane defects. The nicotinic acetylcholine
FT receptor (nAChR) agonist levamisole suppresses the
FT epidermal morphology defects, but only slightly suppresses
FT the muscle detachment defects. Lethal phenotypes are
FT suppressed, but the vab phenotype is more prevalent; when
FT association with A-755. The lethality, epidermal
FT morphological and egg-laying defects are suppressed in a
FT pxn-1 mutant (ok785) background. Basement membrane defects
FT are suppressed by the let-805 ju1123 mutant."
FT /evidence="ECO:0000269|PubMed:20876652,
FT ECO:0000269|PubMed:29440357"
FT MUTAGEN 1178
FT /note="R->K: In ju328; about 2.5% embryonic and 2.5% larval
FT lethality in offspring. Variably abnormal epidermal
FT morphology (vab phenotype) in 24% of offspring."
FT /evidence="ECO:0000269|PubMed:20876652"
FT MUTAGEN 1314
FT /note="G->S: In ju379; embryonic elongation defects
FT resulting in lethality at the three-fold stage in the
FT majority of animals. About 25-30% embryonic and 30% larval
FT lethality in offspring. Variably abnormal epidermal
FT morphology (vab phenotype) in 25% of offspring."
FT /evidence="ECO:0000269|PubMed:20876652"
SQ SEQUENCE 1328 AA; 151152 MW; E0812BE92C81723A CRC64;
MLLEFLLLIG ISLSTACPSE CRCAGLDVHC EGKNLTAIPG HIPIATTNLY FSNNLLNSLS
KSNFQALPNL QYLDLSNNSI RDIEETLLDS FPGLKYLDLS WNKIRYVPKL STAPNALVSL
NLVHNEISRL DNDLVSHSPY MQTFLIQRNR IQSLPHDFFN SRMVPTLKTV KMAGNPWSCD
CRMVNVKQFA DSLFAHSNQN IFIVGKCFFP KGLRNYVFRN LSIENLECEK PEYSKTDDGM
FKMSCPNNEM EGYHYDSIFL ENNKEARHTA HFARDKDGSL LSNGQFTRNY QCAFYRQKQS
IHMQKKMQAS SSTEPPITTT TMEPMTTSTM DSMDTTESVV TMTTMPEIDT KIVFEHKQLD
TTSRDGETLE LKCEASGEPT PTITWLFEKQ KLTESRKHKL TKNGSVLKIF PFLNTDIGQY
ECVASNGEES KSHIFSVSLK ESEQPVIIDA PMDTNATIGQ QVTLRCNAKG FPVPDVVWLF
EGIRIPRRNT RYTISDNNIE LTIEKVTRHD SGVFTCQAVN SVGSAVATAN LLVGAELTEK
VDKLLDDSTI EKIAKEAKQK VEKALSSTKD QQRMDKIESP NDLSKLFKFA INLKKVDLGK
AREIYEESIR LVQMHIDNGL AFESAMISPN VSYEAVLPVS YVQTLMEKSG CQTGQFAESC
EDHCFFSKYR SYDGQCNNHE HPWWGVSEMA FMRLLPPRYE NGFNTPVGWE KGKRYNGYEV
PNARKVSRVL IGTDETTPHS HLSAMTMQWG QFIDHDLTLT APALTRHSYK EGAFCNRTCE
NADPCFNIQL EADDPKLHTG LYQKHPCMEF ERNGAACGSG ETSPIFQRVT YRDQLNLLTS
YLDASGIYGN SEEQALELRD LYSDHGLLRF DIVSGANKPY MPFEKDSDMD CRRNFSRENP
IKCFLAGDVR ANEQLGLMSM HTIFLREHNR IASRLLEVNE NWDGETIFQE TRKLIGAMLQ
HITYNAWLPK ILGKATYNTI IGEYKGYNPD VNPTIANEFA TAALRFAHTL INTHLFRFDK
DFKETKQGHL PLHNAFFAPE RLVSEGGVDP LLRGLFAAPI KMPRPDQVLN KELTEKLFNR
FHEVALDLAA LNIQRGRDHG LPSWTEYRKF CNLTVPKTWS DMKNIVQNDT VISKLQSLYG
VTENIDLWVG GVTEKRTADA LMGPTLACII ADQFKRLRDG DRFWYENEEM FSKAQLRQIK
KVTLSKIICT NGDDIDRIQR DIFVYHGNST QFYEPCESLP EINLNMWTTC CDAMCSSSST
LARNAIGGDE KAKRRKRRHH HSKKSCHDKG KRRKSGDRWN HSNDICVECM CHDGEVWCKT
NNFCKSQV
