ID   MEP2_TRIEQ              Reviewed;         609 AA.
AC   A7UKW1;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 35.
DE   RecName: Full=Extracellular metalloproteinase 2;
DE            EC=3.4.24.-;
DE   AltName: Full=Fungalysin MEP2;
DE   Flags: Precursor; Fragment;
GN   Name=MEP2;
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   Brown J.T., Preuett B.L., Abdel-Rahman S.M.;
RT   "Comparing putative pathogenicity factors between Trichophyton tonsurans
RT   and Trichophyton equinum.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
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; EU076576; ABU50386.1; -; Genomic_DNA.
DR   AlphaFoldDB; A7UKW1; -.
DR   SMR; A7UKW1; -.
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   3: Inferred from homology;
KW   Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW   Secreted; Signal; Virulence; Zinc; Zymogen.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..244
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000380840"
FT   CHAIN           245..>609
FT                   /note="Extracellular metalloproteinase 2"
FT                   /id="PRO_0000380841"
FT   ACT_SITE        430
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         429
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         433
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   CARBOHYD        270
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   NON_TER         609
SQ   SEQUENCE   609 AA;  67288 MW;  B7D0AEBCDCCBC3EE CRC64;
     MHGLLLAGLA AALPLGVAGL PARQQSGLSP RGIDINPYRF ASMAKYSEHK ATSQMVHSFS
     YSKDDDYVAT ATKLVKSTFP NMTFRTVKDH YIGTNGIGHV HFKQTAHGID IDNADFNVNI
     GRDGKVFTFG NSFYEGEMPK TNPLTKRDFA DPVKALHGAI KTLKLPVKPQ SAKAMPMKEA
     ETFMFEGTSG ALSEPMAKLV YIQKDGKLHL TWRVETDVGD NWLLSYVDSK ETETVHNVVD
     YVASADYKVF AWGLNDPTEG QPTMIKDPWN TTGSGSPFTW HGDGEMDYTV TRGNNIAAQD
     NPSGGGQWEN NYRPESPELS FVYEYNEQME PEQYKDFAIT QLFYTTNTFH DLLYSFGFTE
     EAGNFQMNNN GKGGEGNDFA ICNAQDGSGT NNANFATPPD GQNGRMRMYT WTTAQPSRDG
     DLEAGIVIHE YAHGLSNRLC GGPANSNCLS ELEAGGMGEG WGDFYATAIR LKQDDTRETD
     YTMGEWAANM EGGIREYPYF TNMQTNPYTY DDVEGMSEVH GIGTVWATIL YDVLWNLIDE
     HGMSKNIMPK FVNGAPSDGR NLAMKLVLDG MTLMPCNPNF VQARDAIIDA DQALTNGQNK
     CALMKAFSK