ID   MEP1_ARTOT              Reviewed;         632 AA.
AC   Q8J0D5;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Extracellular metalloproteinase 1;
DE            EC=3.4.24.-;
DE   AltName: Full=Fungalysin MEP1;
DE   Flags: Precursor;
GN   Name=MEP1;
OS   Arthroderma otae (Microsporum canis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX   NCBI_TaxID=63405;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=IHEM 15221;
RX   PubMed=12228297; DOI=10.1128/iai.70.10.5676-5683.2002;
RA   Brouta F., Descamps F., Monod M., Vermout S., Losson B., Mignon B.;
RT   "Secreted metalloprotease gene family of Microsporum canis.";
RL   Infect. Immun. 70:5676-5683(2002).
RN   [2]
RP   SUBCELLULAR LOCATION, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=10206750; DOI=10.1080/02681219880000631;
RA   Mignon B., Swinnen M., Bouchara J.P., Hofinger M., Nikkels A., Pierard G.,
RA   Gerday C., Losson B.;
RT   "Purification and characterization of a 315 kDa keratinolytic subtilisin-
RT   like serine protease from Microsporum canis and evidence of its secretion
RT   in naturally infected cats.";
RL   Med. Mycol. 36:395-404(1998).
CC   -!- FUNCTION: Secreted metalloproteinase probably acting as a virulence
CC       factor. {ECO:0000250, ECO:0000269|PubMed:10206750}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- ACTIVITY REGULATION: PMSF, soybean trypsin inhibitor (SBTI) and
CC       chymostatin strongly inhibit the proteinase.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.37 mM for the synthetic substrate N-Suc-Ala-Ala-Pro-Phe-p-
CC         nitroanilid {ECO:0000269|PubMed:10206750};
CC       pH dependence:
CC         Optimum pH is 9. {ECO:0000269|PubMed:10206750};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10206750}.
CC   -!- SIMILARITY: Belongs to the peptidase M36 family. {ECO:0000305}.
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DR   EMBL; AJ490184; CAD35289.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8J0D5; -.
DR   SMR; Q8J0D5; -.
DR   MEROPS; M36.001; -.
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_5000068600"
FT   CHAIN           247..632
FT                   /note="Extracellular metalloproteinase 1"
FT                   /id="PRO_5000068601"
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        284
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        591
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   632 AA;  69770 MW;  D2FF2E8E8FABEBAF CRC64;
     MHGLLLAAGL ISLPLHVLAH PQPSSTSLAG RAVDLNEYRI GHRSSYTSND EMMKQPSIAS
     FRAGTYVEVA TEMVKQTMPN MEFRLVDDHY IGQSGIGHVR FRQTMHGIDI DNSDFNVNIG
     QDGKVLSHGN SFYTGPAPES SPVQKRDFSD PMQALHGVRK ALNLPIKAEG ATVENMSEHK
     VMFKGTSGAL SDPTAKLCYM AKEDGSLALT WRVETDIGDN WLLSYMDAKD TGKVHNVVDY
     VAHATFQVYK WGLADPTEGN REILTNPWNL QTSPLTWLAD GQNNFTATRG NNAIAQYNPD
     GGNDYENNYR PSPKNLKFEY PYSANMDPPK TYIDASVTQL FYTSNVCHDL YYMLGFNEKA
     GNFQVNNRGQ GGKGNDYVIL NAQDGSGTNN ANFATPPDGQ PGRMRAYIWT RANPPRDASF
     EAGTIIHEYT HGLSNRLCGG PANSRCLNAI ESGGMGEGWG DFYATAVRLK PKDTRKTNYV
     KGGWVNNSPK GVRMYPYSTD MSVNPLVYTS NNQLNEVHAI GTVWATMLYE LLWNLIDKHG
     KNDGPVPIFK NGIPSDGKYL AMKIVMDGMA IQPCNPNFVQ ARDAILDADK NLTKASNKCE
     IWKAFAKRGL GVGAKFDPKN RIGSNEVPKE CK