ID   MEP1_TRIRU              Reviewed;         635 AA.
AC   Q8NIB6;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Extracellular metalloproteinase 1;
DE            EC=3.4.24.-;
DE   AltName: Full=Fungalysin MEP1;
DE   Flags: Precursor;
GN   Name=MEP1;
OS   Trichophyton rubrum (Athlete's foot fungus) (Epidermophyton rubrum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=5551;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX   PubMed=12452286; DOI=10.1078/1438-4221-00223;
RA   Monod M., Capoccia S., Lechenne B., Zaugg C., Holdom M., Jousson O.;
RT   "Secreted proteases from pathogenic fungi.";
RL   Int. J. Med. Microbiol. 292:405-419(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION BY MASS SPECTROMETRY, AND
RP   SUBCELLULAR LOCATION.
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).
RN   [3]
RP   INDUCTION.
RX   PubMed=19098130; DOI=10.1128/ec.00208-08;
RA   Zaugg C., Monod M., Weber J., Harshman K., Pradervand S., Thomas J.,
RA   Bueno M., Giddey K., Staib P.;
RT   "Gene expression profiling in the human pathogenic dermatophyte
RT   Trichophyton rubrum during growth on proteins.";
RL   Eukaryot. Cell 8:241-250(2009).
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:0000269|PubMed:14766908}.
CC   -!- INDUCTION: Expression is strongly increased during growth on protein-
CC       rich medium. Expressed at even higher levels when keratin is present in
CC       the protein-rich medium. {ECO:0000269|PubMed:19098130}.
CC   -!- SIMILARITY: Belongs to the peptidase M36 family. {ECO:0000305}.
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DR   EMBL; AF407186; AAN03637.1; -; mRNA.
DR   EMBL; AF407185; AAN03636.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8NIB6; -.
DR   SMR; Q8NIB6; -.
DR   MEROPS; M36.001; -.
DR   PRIDE; Q8NIB6; -.
DR   VEuPathDB; FungiDB:TERG_02213; -.
DR   OrthoDB; 1136823at2759; -.
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   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_0000380836"
FT   CHAIN           247..635
FT                   /note="Extracellular metalloproteinase 1"
FT                   /id="PRO_0000380837"
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;  70126 MW;  EA1123969FC0DB19 CRC64;
     MHGLLLAAGL LSLPLHVLAH PQPSTSTSLA GRAGAVDLNE FRIAHRSSYT SHDEMKKLPS
     IASFRQGTYL EVATELVKQT MPNMEFRLVD DHYVGDSGIG HVRFRQTMHG IDIDNSDFNV
     NVGKDGKVLS HGNSFYTGPA PSSNPMVKRD FIDPMQALHG VRKALNLPIK ADGAHVEDMS
     EHKVMFKGTS GALSDPTAKL CYMAKEDGSL ALTWRVETDI GDNWLLSYMD AKESSKVHNV
     VDYVAHATFQ VYKWGLADPT EGKREIITNP WNLKTSPLTW LSDGHNNYTA TRGNNAIAQY
     NPDGGNDYEN NYRPSPKNLK FEYPYSPDMN PPKTYIDASV TELFYTSNIC HDLYYMLGFN
     EKAGNFQVNN RGQGGKGNDF VILNAQDGSG TNNANFATPP DGQPGRMRAY IWTRANPPRD
     ASFEAGTIIH EYTHGLSNRL CGGPANSRCL NALESGGMGE GWGDFYATAV RLKPNDTRKT
     NYVKGGWVNN SPKGVRMYPY STDMNVNPLV YTSNNKLNEV HAIGTVWCTM LYEVLWNLID
     KHGKNDGPVP IFENGVPNDG KYLAMKIVMD GMAIQPCNPN FVQARDAILD ADMNLTKGAN
     KCEIWKGFAK RGLGVGAKFD PKNRTGSTQV PNECK