ID   MEP5_ARTBE              Reviewed;         633 AA.
AC   Q6WIH6;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=Extracellular metalloproteinase 5;
DE            EC=3.4.24.-;
DE   AltName: Full=Fungalysin MEP5;
DE   Flags: Precursor;
GN   Name=MEP5;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY283571; AAQ21096.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6WIH6; -.
DR   SMR; Q6WIH6; -.
DR   MEROPS; M36.001; -.
DR   PHI-base; PHI:4974; -.
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..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..245
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000380874"
FT   CHAIN           246..633
FT                   /note="Extracellular metalloproteinase 5"
FT                   /id="PRO_0000380875"
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        286
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;  69829 MW;  A0E280A44B2208D1 CRC64;
     MHGLLLAAAG LLSLPLHVIA HPQPSTNLAG RGVDLDAYRM ADRSSYMNSD DMKLKQPGIA
     SLSGGNYVDT ATEVVKRMMP GMTFRMVDDH YVGESGISHV YFRQTMHGMD IDNSDFNVNI
     GKDGKVLSFG HSFYTGPAPD KAPVEKRDFS DPMKAFHGAC KALSLPINAD KATVQTMNEH
     EVMFMGTSGA MSDPQGKLCY MAKEDGTLAL TWRVETDMGD NWLLSYVDAK ETEKVHNVVD
     YVSHATYQVY RRALSPDPTE GKRESIENPW NLKTSPFTWI SDGKTNYTTT RGNNAIAQAN
     FDGGEDYLNN HRPNNKNLKF EYPYAPNMSP KSYIDASVTQ LFYSANMVHD LYYMLGFTEK
     AGNFQVNNHG QGGKGNDFVI LNAQDGSGTN NANFATPPDG KPGRMRVYIW TKAKPARDSS
     FEAGTVIHEY THGLSNRLTG GPANAGCLNG MESGGMGEGW GDFFATAIRL KPNDNRNANY
     VHGEWVNNSP KGNRMYPYST SLQTNPLVYT SCNKYNEVHA IGTVWGSMLY EVLWNLIDKH
     GKNDGPTPVF ENGVPKDGKY LAMKLVMDGM AIQPCKPTFV QARDAIIDAD MNLTKGSNRC
     EIWKAFAKRG LGVGAKYDPK NRTGNKGLPK DCQ