ID   MEP1_ARTBE              Reviewed;         635 AA.
AC   Q6WIH5;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=Extracellular metalloproteinase 1;
DE            EC=3.4.24.-;
DE   AltName: Full=Fungalysin MEP1;
DE   Flags: Precursor;
GN   Name=MEP1;
OS   Arthroderma benhamiae (Trichophyton mentagrophytes).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=63400;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=14766908; DOI=10.1099/mic.0.26690-0;
RA   Jousson O., Lechenne B., Bontems O., Capoccia S., Mignon B., Barblan J.,
RA   Quadroni M., Monod M.;
RT   "Multiplication of an ancestral gene encoding secreted fungalysin preceded
RT   species differentiation in the dermatophytes Trichophyton and
RT   Microsporum.";
RL   Microbiology 150:301-310(2004).
CC   -!- FUNCTION: Secreted metalloproteinase probably acting as a virulence
CC       factor. {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M36 family. {ECO:0000305}.
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DR   EMBL; AY283572; AAQ21097.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6WIH5; -.
DR   SMR; Q6WIH5; -.
DR   MEROPS; M36.001; -.
DR   PHI-base; PHI:4970; -.
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   3: Inferred from homology;
KW   Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW   Secreted; Signal; Virulence; Zinc; Zymogen.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..246
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000380832"
FT   CHAIN           247..635
FT                   /note="Extracellular metalloproteinase 1"
FT                   /id="PRO_0000380833"
FT   ACT_SITE        431
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         430
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         434
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   CARBOHYD        287
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        475
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        594
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        623
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   635 AA;  69989 MW;  F7E66B493271375E CRC64;
     MHGLLLAAGL LSLPLHVLAH PQPSTSTSLA GRAGAVDLNE FRVAHRSSYT SHDEMKKLPS
     IASFRQGTYL EVATELVKQT MPNMEFRLVD DHYVGDSGIG HVRFRQTMHG IDIDNSDFNV
     NVGKNGKVLS HGNSFYTGPA PASNPMVKRD FIDPMQALNG VRKALNLPVK ADGAHVENMS
     EHKVMFKGTS GALSDPTAKL CYMAKEDGSL ALTWRVETDI GDNWLLSYMD AKESSKVHNV
     VDYVAHATFQ VYKWGLADPT EGKRDILTNP WNLKTSPLTW LADGKTNFTA TRGNNAIAQY
     NPDGGNDYEN NYRPSPKNLK FEYPYSPDMN PPKTYIDASV TQLFYTSNVC HDLYYMLGFN
     EKAGNFQVNN RGQGGKGNDY VILNAQDGSG TNNANFATPP DGQPGRMRAY IWTRANPPRD
     ASFEAGTIIH EYTHGLSNRL CGGPANSRCL NALESGGMGE GWGDFYATAV RLKPNDTRKT
     NYVKGGWVNN SPKGVRMYPY STDMNVNPLV YTSNNKLNEV HAIGTVWCTM LYEVLWNLID
     KHGKNDGPVP VFENGVPNDG KYLAMKLVMD GMAIQPCNPN FVQARDAILD ADMNLTKGAN
     KCEIWKGFAK RGLGVGAKFD PKNRTGSNQV PNECK