ID   MEP5_TRIRU              Reviewed;         633 AA.
AC   Q8NIH1;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Extracellular metalloproteinase 5;
DE            EC=3.4.24.-;
DE   AltName: Full=Fungalysin MEP5;
DE   Flags: Precursor;
GN   Name=MEP5;
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).
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   -!- SIMILARITY: Belongs to the peptidase M36 family. {ECO:0000305}.
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DR   EMBL; AF407190; AAN03641.1; -; mRNA.
DR   EMBL; AF407189; AAN03640.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8NIH1; -.
DR   SMR; Q8NIH1; -.
DR   MEROPS; M36.001; -.
DR   VEuPathDB; FungiDB:TERG_02213; -.
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..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..245
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000380878"
FT   CHAIN           246..633
FT                   /note="Extracellular metalloproteinase 5"
FT                   /id="PRO_0000380879"
FT   ACT_SITE        429
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         428
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         432
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   CARBOHYD        285
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        592
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        621
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   633 AA;  69779 MW;  4DDFD7D8A01E92B6 CRC64;
     MHGLLLAAAG LLSLPLHVVA HPQPSTSLAG RGVDLDAYRM ADRSSYMSSD DMKLKQPAIA
     SLSGGNYVDT ATEVVKRMMP GMTFRMADDH YVGESGISHL YFRQTMHGMD IDNADFNVNI
     GKDGKVLSFG HSFYTGPAPD RAPVEKRDFS GPMRAFHGAC KALNLPINAD KATIQTMNEH
     EVMFVGTSGA MSDPQGKLCY MAKEDGTLAL TWRVETDMGD NWLLSYVDAK ETDKVHNVVD
     YVSHATYQVY RWPIPDPTEG KREIVENPWN LKTSPFTWIS DGKTNYTTTR GNNAIAQANF
     DGGEDYLNNY RPNSKNLKFE YPYAPNMSPP KSYIDASVTQ LFYSANIVHD LYYMLGFTEK
     AGNFQVNNHG QGGKGNDFVI LNAQDGSGTN NANFATPPDG KPGRMRVYIW TKAKPARDSS
     FEAGTVIHEY THGLSNRLCG GPANSGCLNG MESGGMGEGW GDFFATAIRL KPNDNRNANY
     VHGEWVNNSP KGNRLYPYST NLQTNPLVYT SCNKYNEVHA IGTVWCSILY EVLWNLIDKH
     GKNDGPTPVF ENGVPNDGKY LAMKLVLDGM AIQPCKPTFV QARDAIIDAD MNLTKGSNKC
     ELWKAFAKRG LGVGAKYDPK NRTGSKAVPK ECQ