ELM_ASPFU
ID ELM_ASPFU Reviewed; 634 AA.
AC P46075; P46074; Q4WBR6;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 3.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Extracellular metalloproteinase mep;
DE EC=3.4.24.- {ECO:0000269|PubMed:24100314, ECO:0000269|PubMed:7927676, ECO:0000269|PubMed:8188335};
DE AltName: Full=AfuMep {ECO:0000303|PubMed:24100314};
DE AltName: Full=Allergen Asp f 5 {ECO:0000303|PubMed:9482698};
DE AltName: Full=Elastinolytic metalloproteinase mep;
DE AltName: Full=Fungalysin mep {ECO:0000303|PubMed:24100314};
DE AltName: Allergen=Asp f 5.0101 {ECO:0000305};
DE Flags: Precursor;
GN Name=mep; ORFNames=AFUA_8G07080;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=Delta18;
RX PubMed=7715453; DOI=10.1111/j.1365-2958.1994.tb01327.x;
RA Jaton-Ogay K., Paris S., Huerre M., Quadroni M., Falchetto R., Togni G.,
RA Latge J.-P., Monod M.;
RT "Cloning and disruption of the gene encoding an extracellular
RT metalloprotease of Aspergillus fumigatus.";
RL Mol. Microbiol. 14:917-928(1994).
RN [2]
RP SEQUENCE REVISION.
RA Sanglard D.;
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 530-542, FUNCTION,
RP AND CATALYTIC ACTIVITY.
RC STRAIN=Isolate 13;
RX PubMed=7927676; DOI=10.1128/iai.62.10.4208-4218.1994;
RA Sirakova T.D., Markaryan A., Kolattukudy P.E.;
RT "Molecular cloning and sequencing of the cDNA and gene for a novel
RT elastinolytic metalloproteinase from Aspergillus fumigatus and its
RT expression in Escherichia coli.";
RL Infect. Immun. 62:4208-4218(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
RN [5]
RP PROTEIN SEQUENCE OF 246-267, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, INDUCTION,
RP AND PTM.
RX PubMed=8188335; DOI=10.1128/iai.62.6.2149-2157.1994;
RA Markaryan A., Morozova I., Yu H., Kolattukudy P.E.;
RT "Purification and characterization of an elastinolytic metalloprotease from
RT Aspergillus fumigatus and immunoelectron microscopic evidence of secretion
RT of this enzyme by the fungus invading the murine lung.";
RL Infect. Immun. 62:2149-2157(1994).
RN [6]
RP ALLERGEN.
RX PubMed=9482698; DOI=10.1159/000023889;
RA Crameri R.;
RT "Recombinant Aspergillus fumigatus allergens: from the nucleotide sequences
RT to clinical applications.";
RL Int. Arch. Allergy Immunol. 115:99-114(1998).
RN [7]
RP INDUCTION.
RX PubMed=19564390; DOI=10.1128/iai.00425-09;
RA Bergmann A., Hartmann T., Cairns T., Bignell E.M., Krappmann S.;
RT "A regulator of Aspergillus fumigatus extracellular proteolytic activity is
RT dispensable for virulence.";
RL Infect. Immun. 77:4041-4050(2009).
RN [8]
RP INDUCTION.
RX PubMed=19564385; DOI=10.1128/iai.00426-09;
RA Sharon H., Hagag S., Osherov N.;
RT "Transcription factor PrtT controls expression of multiple secreted
RT proteases in the human pathogenic mold Aspergillus fumigatus.";
RL Infect. Immun. 77:4051-4060(2009).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 31-245 AND 246-634 IN COMPLEX WITH
RP ZINC AND CALCIUM, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION, SITE,
RP GLYCOSYLATION AT ASN-47, DISULFIDE BONDS, MUTAGENESIS OF ARG-470 AND
RP CYS-634, AND CIRCULAR DICHROISM ANALYSIS.
RX PubMed=24100314; DOI=10.1107/s0907444913017642;
RA Fernandez D., Russi S., Vendrell J., Monod M., Pallares I.;
RT "A functional and structural study of the major metalloprotease secreted by
RT the pathogenic fungus Aspergillus fumigatus.";
RL Acta Crystallogr. D 69:1946-1957(2013).
CC -!- FUNCTION: Secreted metalloproteinase that allows assimilation of
CC proteinaceous substrates and probably acts as a virulence factor (By
CC similarity). Catalyzes the hydrolysis of elastin (PubMed:7927676,
CC PubMed:8188335). Hydrolyzes azocasein, synthetic fluorigenic substrate
CC Abz-Ala-Ala-Phe-Phe-pNA, and His-Leu, Ala-Leu, Tyr-Leu, Gly-Phe, and
CC Phe-Phe peptide bonds in the B chain of insulin (PubMed:8188335).
CC {ECO:0000250, ECO:0000269|PubMed:7927676, ECO:0000269|PubMed:8188335}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:24100314};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:24100314};
CC -!- ACTIVITY REGULATION: Completely inhibited by metalloprotease inhibitors
CC EDTA, 1,10-phenanthroline, and phosphoramidon, but not by inhibitors
CC specific for serine, cysteine, and aspartate proteases, such as PMSF,
CC antipain, leupeptin, chymostatin, and pepstatin. Zn(2+) and, to a
CC lesser extent, Co(2+) reversed the inhibition of 1,10-phenanthroline.
CC {ECO:0000269|PubMed:8188335}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.5-8.0. {ECO:0000269|PubMed:8188335};
CC Temperature dependence:
CC Optimum temperature is 60 degrees Celsius against azocasein. Retains
CC 50% of the activity by incubation at 60 degrees Celsius for 1 hour.
CC {ECO:0000269|PubMed:8188335};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24100314,
CC ECO:0000269|PubMed:8188335}. Note=Secreted in the neutropenic mouse
CC lungs by invading Aspergillus fumigatus. {ECO:0000269|PubMed:8188335}.
CC -!- INDUCTION: By Zn(2+) (PubMed:8188335). Expression is controlled by the
CC prtT transcription factor (PubMed:19564390, PubMed:19564385).
CC {ECO:0000269|PubMed:19564385, ECO:0000269|PubMed:19564390,
CC ECO:0000269|PubMed:8188335}.
CC -!- PTM: Not glycosylated according to PubMed:8188335, but glycosylated
CC according to PubMed:24100314. {ECO:0000269|PubMed:24100314,
CC ECO:0000269|PubMed:8188335}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Recombinant protein
CC binds to IgE in 93% of the 54 patients tested suffering with allergic
CC bronchopulmonary aspergillosis (ABPA). Recombinant protein binds to IgE
CC in 74% of the 35 A.fumigatus-allergic patients tested without ABPA.
CC {ECO:0000269|PubMed:9482698}.
CC -!- SIMILARITY: Belongs to the peptidase M36 family. {ECO:0000305}.
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DR EMBL; Z30424; CAA83015.1; -; Genomic_DNA.
DR EMBL; L29566; AAB07708.1; -; Genomic_DNA.
DR EMBL; AAHF01000013; EAL85468.1; -; Genomic_DNA.
DR PIR; S61435; S61435.
DR RefSeq; XP_747506.1; XM_742413.1.
DR PDB; 4K90; X-ray; 1.80 A; A=246-634, B=31-245.
DR PDBsum; 4K90; -.
DR AlphaFoldDB; P46075; -.
DR SMR; P46075; -.
DR STRING; 330879.P46075; -.
DR Allergome; 3123; Asp f 5.0101.
DR Allergome; 75; Asp f 5.
DR MEROPS; M36.001; -.
DR EnsemblFungi; EAL85468; EAL85468; AFUA_8G07080.
DR GeneID; 3504960; -.
DR KEGG; afm:AFUA_8G07080; -.
DR VEuPathDB; FungiDB:Afu8g07080; -.
DR eggNOG; ENOG502QTDC; Eukaryota.
DR HOGENOM; CLU_012703_3_0_1; -.
DR InParanoid; P46075; -.
DR OMA; WALIEAH; -.
DR OrthoDB; 1136823at2759; -.
DR Proteomes; UP000002530; Chromosome 8.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.390.10; -; 1.
DR InterPro; IPR011096; FTP_domain.
DR InterPro; IPR001842; Peptidase_M36.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR Pfam; PF07504; FTP; 1.
DR Pfam; PF02128; Peptidase_M36; 1.
DR PRINTS; PR00999; FUNGALYSIN.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allergen; Calcium; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Secreted; Signal; Virulence; Zinc; Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..245
FT /evidence="ECO:0000255, ECO:0000305|PubMed:8188335"
FT /id="PRO_0000029243"
FT CHAIN 246..634
FT /note="Extracellular metalloproteinase mep"
FT /evidence="ECO:0000305|PubMed:8188335"
FT /id="PRO_0000029244"
FT ACT_SITE 430
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 245
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:24100314,
FT ECO:0007744|PDB:4K90"
FT BINDING 364
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24100314,
FT ECO:0007744|PDB:4K90"
FT BINDING 375
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24100314,
FT ECO:0007744|PDB:4K90"
FT BINDING 378
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24100314,
FT ECO:0007744|PDB:4K90"
FT BINDING 400
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24100314,
FT ECO:0007744|PDB:4K90"
FT BINDING 429
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095,
FT ECO:0000269|PubMed:24100314, ECO:0007744|PDB:4K90"
FT BINDING 433
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095,
FT ECO:0000269|PubMed:24100314, ECO:0007744|PDB:4K90"
FT BINDING 437
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:24100314,
FT ECO:0007744|PDB:4K90"
FT BINDING 438
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:24100314,
FT ECO:0007744|PDB:4K90"
FT BINDING 440
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:24100314,
FT ECO:0007744|PDB:4K90"
FT BINDING 442
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:24100314,
FT ECO:0007744|PDB:4K90"
FT BINDING 445
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:24100314,
FT ECO:0007744|PDB:4K90"
FT BINDING 459
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:24100314,
FT ECO:0007744|PDB:4K90"
FT SITE 470
FT /note="Important for proper folding of the protein and
FT catalytic activity"
FT /evidence="ECO:0000305|PubMed:24100314"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:24100314, ECO:0007744|PDB:4K90"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 448..576
FT /evidence="ECO:0000269|PubMed:24100314,
FT ECO:0007744|PDB:4K90"
FT DISULFID 601..634
FT /evidence="ECO:0000269|PubMed:24100314,
FT ECO:0007744|PDB:4K90"
FT VARIANT 137
FT /note="Q -> K (in strain: Isolate 13)"
FT VARIANT 197
FT /note="A -> P (in strain: Isolate 13)"
FT VARIANT 419
FT /note="D -> N (in strain: Isolate 13)"
FT VARIANT 448..450
FT /note="CLN -> SLY (in strain: Isolate 13)"
FT VARIANT 482
FT /note="T -> A (in strain: Isolate 13)"
FT VARIANT 529
FT /note="M -> I (in strain: Isolate 13)"
FT VARIANT 573
FT /note="L -> F (in strain: Isolate 13)"
FT VARIANT 578
FT /note="P -> A (in strain: Isolate 13)"
FT MUTAGEN 470
FT /note="R->E: Loss of secretion."
FT /evidence="ECO:0000269|PubMed:24100314"
FT MUTAGEN 470
FT /note="R->K: Normal secretion level."
FT /evidence="ECO:0000269|PubMed:24100314"
FT MUTAGEN 470
FT /note="R->S,A: Slightly increased secretion level."
FT /evidence="ECO:0000269|PubMed:24100314"
FT MUTAGEN 634
FT /note="C->A: Catalytically active against casein."
FT /evidence="ECO:0000269|PubMed:24100314"
FT CONFLICT 260..261
FT /note="EG -> PE (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 266
FT /note="I -> V (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 305
FT /note="S -> P (in Ref. 1; CAA83015)"
FT /evidence="ECO:0000305"
FT HELIX 34..37
FT /evidence="ECO:0007829|PDB:4K90"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:4K90"
FT HELIX 48..54
FT /evidence="ECO:0007829|PDB:4K90"
FT HELIX 67..78
FT /evidence="ECO:0007829|PDB:4K90"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:4K90"
FT STRAND 98..106
FT /evidence="ECO:0007829|PDB:4K90"
FT STRAND 109..120
FT /evidence="ECO:0007829|PDB:4K90"
FT STRAND 124..131
FT /evidence="ECO:0007829|PDB:4K90"
FT HELIX 142..145
FT /evidence="ECO:0007829|PDB:4K90"
FT HELIX 152..163
FT /evidence="ECO:0007829|PDB:4K90"
FT STRAND 168..175
FT /evidence="ECO:0007829|PDB:4K90"
FT STRAND 182..190
FT /evidence="ECO:0007829|PDB:4K90"
FT STRAND 196..203
FT /evidence="ECO:0007829|PDB:4K90"
FT STRAND 209..218
FT /evidence="ECO:0007829|PDB:4K90"
FT STRAND 223..231
FT /evidence="ECO:0007829|PDB:4K90"
FT HELIX 232..234
FT /evidence="ECO:0007829|PDB:4K90"
FT STRAND 236..244
FT /evidence="ECO:0007829|PDB:4K90"
FT STRAND 247..250
FT /evidence="ECO:0007829|PDB:4K90"
FT HELIX 258..260
FT /evidence="ECO:0007829|PDB:4K90"
FT STRAND 264..267
FT /evidence="ECO:0007829|PDB:4K90"
FT TURN 272..277
FT /evidence="ECO:0007829|PDB:4K90"
FT STRAND 288..299
FT /evidence="ECO:0007829|PDB:4K90"
FT HELIX 331..334
FT /evidence="ECO:0007829|PDB:4K90"
FT HELIX 335..355
FT /evidence="ECO:0007829|PDB:4K90"
FT TURN 360..363
FT /evidence="ECO:0007829|PDB:4K90"
FT STRAND 372..374
FT /evidence="ECO:0007829|PDB:4K90"
FT STRAND 380..384
FT /evidence="ECO:0007829|PDB:4K90"
FT STRAND 393..396
FT /evidence="ECO:0007829|PDB:4K90"
FT STRAND 404..408
FT /evidence="ECO:0007829|PDB:4K90"
FT STRAND 413..416
FT /evidence="ECO:0007829|PDB:4K90"
FT HELIX 420..422
FT /evidence="ECO:0007829|PDB:4K90"
FT HELIX 424..439
FT /evidence="ECO:0007829|PDB:4K90"
FT HELIX 452..470
FT /evidence="ECO:0007829|PDB:4K90"
FT HELIX 485..488
FT /evidence="ECO:0007829|PDB:4K90"
FT STRAND 494..497
FT /evidence="ECO:0007829|PDB:4K90"
FT TURN 503..505
FT /evidence="ECO:0007829|PDB:4K90"
FT HELIX 510..515
FT /evidence="ECO:0007829|PDB:4K90"
FT HELIX 519..541
FT /evidence="ECO:0007829|PDB:4K90"
FT STRAND 546..548
FT /evidence="ECO:0007829|PDB:4K90"
FT STRAND 555..558
FT /evidence="ECO:0007829|PDB:4K90"
FT HELIX 559..573
FT /evidence="ECO:0007829|PDB:4K90"
FT HELIX 580..595
FT /evidence="ECO:0007829|PDB:4K90"
FT HELIX 600..609
FT /evidence="ECO:0007829|PDB:4K90"
SQ SEQUENCE 634 AA; 68708 MW; B9F9A8D83E1FEBBF CRC64;
MRGLLLAGAL ALPASVFAHP AHQSYGLNRR TVDLNAFRLK SLAKYVNATE TVIEAPSSFA
PFKPQSYVEV ATQHVKMIAP DATFRVVDDH YVGDNGVAHV HFRQTANGLD IDNADFNVNV
GKDGKVFSYG NSFYTGQIPS SAALTKRDFS DPVTALKGTT NTLQLPITVD SASSESTEEK
ESYVFKGVSG TVSDPKAKLV YFVKDDGTLA LAWRVETDID SNWLLTYIDA KSGEEIHGVV
DYVAEADYQV YAWGINDPTE GERTVIKDPW DSVASEFTWI SDGSTNYTTS RGNNGIAQSN
PSGGSSYLNN YRPSSSSLSF KYPYSVSSSP PSSYIDASII QLFYTANIYH DLLYTLGFTE
KAGNFEYNTN GQGGLGNDYV ILNAQDGSGT NNANFATPPD GQPGRMRMYV WTESTPYRDG
SFEAGIVIHE YTHGLSNRLT GGPANSNCLN ALESGGMGEG WSDFMATAIR LKPGDKRSTD
YTMGEWASNR AGGIRQYPYS TSLSTNPLTY TSVNSLNAVH AIGTVWASML YEVLWNLIDK
HGKNDAPKPT LRDGVPTDGK YLAMKLVMDG MALQPCNPNF VQARDAILDA DTALTGGENQ
CEIWTAFAKR GLGAGAKYSS RNRVGSTEVP SGVC
