ID   MEP4_TRIEQ              Reviewed;         643 AA.
AC   B6VA81; A1XIM3;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   03-AUG-2022, entry version 34.
DE   RecName: Full=Extracellular metalloproteinase 4;
DE            EC=3.4.24.-;
DE   AltName: Full=Fungalysin MEP4;
DE   Flags: Precursor;
GN   Name=MEP4;
OS   Trichophyton equinum (Horse ringworm fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=63418;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Preuett B.L., Abdel-Rahman S.M.;
RT   "Comparing putative pathogenicity factors between Trichophyton tonsurans
RT   and Trichophyton equinum.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 245-636, IDENTIFICATION BY MASS
RP   SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC   STRAIN=IHEM 20668;
RX   PubMed=17156126; DOI=10.1111/j.1574-6968.2006.00541.x;
RA   Giddey K., Favre B., Quadroni M., Monod M.;
RT   "Closely related dermatophyte species produce different patterns of
RT   secreted proteins.";
RL   FEMS Microbiol. Lett. 267:95-101(2007).
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}.
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DR   EMBL; FJ356719; ACJ04074.1; -; Genomic_DNA.
DR   EMBL; DQ384953; ABL84991.1; -; Genomic_DNA.
DR   AlphaFoldDB; B6VA81; -.
DR   SMR; B6VA81; -.
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..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..254
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000380864"
FT   CHAIN           255..643
FT                   /note="Extracellular metalloproteinase 4"
FT                   /id="PRO_0000380865"
FT   REGION          47..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        56..71
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        438
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         437
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         441
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   CARBOHYD        271
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        420
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        510
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   643 AA;  70668 MW;  F1B2921B983FBB63 CRC64;
     MHGLLLAGLL ALPLNVLAHP TESHSSGISR RAIDITSYRL PQISKYTKSD AVPKQDDESF
     TTSSTGDDNV SSGDYVTTAT DWLKKTLPKA TYRLVNDHYI GDSGIGHVHF RQTAHGIDID
     NTDFNVNIGR DGKVFSFGNS FYDGEIPKAN PMVKRDFSDP VNALQVAIQT LNLPVTAKPE
     NVKAKPVEGK ENFKFEGTSG AFSDPKAQLV YLQKDGGLVP SWKVETDIGD NWLLTYVDAN
     KNDKVHSVVD YVSAAEYKVY PWGINDPTEG NRTSIHLPWF KTLSTDWHID GKGWYSTTRG
     NNAIAQENPT GGPEYENNYR PKSPLFIFKY PYSEAMTPPS SYRDASITQL FYTTNVYHDV
     LYILGFNEKA GNFQVNNWNK GGVGGDFAIL NSQDGSGVNN ANFATPPDGQ PGRMRMYTWN
     ASTPERDGCF EAGIVIHEYT HGVSNRLTGG PANSRCLAAL ESGGMGEGWS DFFATAIRLK
     AGDTRATDYT MGEWASNRPN GIRKYRYSTN LTTNPHMYVD ADGLTSVHAI GTIWASMLYE
     LLWNLIDKHG KGDVTKVRPV LKNGVPTDGR HLAMKLVLDG MALQPCLPNF VQARDAILDA
     DKVLTQGSNK CEIWKAFAKR GLGVGAVFNP SKRTGSNELP AGC