ID   MEP2_ARTBE              Reviewed;         632 AA.
AC   Q6WIH2;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=Extracellular metalloproteinase 2;
DE            EC=3.4.24.-;
DE   AltName: Full=Fungalysin MEP2;
DE   Flags: Precursor;
GN   Name=MEP2;
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}.
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DR   EMBL; AY283575; AAQ21100.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6WIH2; -.
DR   SMR; Q6WIH2; -.
DR   MEROPS; M36.001; -.
DR   PHI-base; PHI:4971; -.
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_0000380842"
FT   CHAIN           245..632
FT                   /note="Extracellular metalloproteinase 2"
FT                   /id="PRO_0000380843"
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"
SQ   SEQUENCE   632 AA;  69744 MW;  3CEA9C1FE7D5232D 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 PEQFKDFAIT QLFYTTNTFH DLLYSFGFTE
     EAGNFQMNNN GKGGEGNDFA ICNAQDGSGT NNANFATPPD GQNGRMRMYT WTTAQPSRDG
     DLEAGIVIHE YAHGLSNRLC GGPANSNCLS ELEAGGMGEG WGDFYATAIR LKQDDTRETD
     YTMGEWAANM EGGIREYPYS TNMQTNPYTY ADVEGMSEVH GIGTVWATIL YDVLWNLIDE
     HGMSKNIMPK FVNGAPSDGR NLAMKLVLDG MTLMPCNPNF VQARDAIIDA DQALTNGQNK
     CALMKAFSKR GLGSNYKHGK NRVNNFDMPA DC