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 22-FEB-2023, entry version 60.
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 GlyCosmos; Q8J0D5; 2 sites, No reported glycans.
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 CDD; cd09596; M36; 1.
DR Gene3D; 3.10.170.10; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR InterPro; IPR011096; FTP_domain.
DR InterPro; IPR001842; Peptidase_M36.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR33478; EXTRACELLULAR METALLOPROTEINASE MEP; 1.
DR PANTHER; PTHR33478:SF1; EXTRACELLULAR METALLOPROTEINASE MEP; 1.
DR Pfam; PF07504; FTP; 1.
DR Pfam; PF02128; Peptidase_M36; 1.
DR PRINTS; PR00999; FUNGALYSIN.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
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
//
