ID   MEP3_TRIVO              Reviewed;         391 AA.
AC   A1XIM2;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 39.
DE   RecName: Full=Extracellular metalloproteinase 3;
DE            EC=3.4.24.-;
DE   AltName: Full=Fungalysin MEP3;
DE   Flags: Precursor; Fragment;
GN   Name=MEP3;
OS   Trichophyton violaceum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=34388;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION BY MASS SPECTROMETRY, AND
RP   SUBCELLULAR LOCATION.
RC   STRAIN=LAU 819;
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:0000269|PubMed:17156126}.
CC   -!- SIMILARITY: Belongs to the peptidase M36 family. {ECO:0000305}.
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DR   EMBL; DQ384952; ABL84987.1; -; Genomic_DNA.
DR   AlphaFoldDB; A1XIM2; -.
DR   SMR; A1XIM2; -.
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; IPR001842; Peptidase_M36.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
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; Virulence; Zinc; Zymogen.
FT   PROPEP          <1..9
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000380858"
FT   CHAIN           10..>391
FT                   /note="Extracellular metalloproteinase 3"
FT                   /id="PRO_0000380859"
FT   ACT_SITE        193
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         192
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         196
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   CARBOHYD        173
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        243
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        385
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
FT   NON_TER         391
SQ   SEQUENCE   391 AA;  42980 MW;  10A0E630FFF877C2 CRC64;
     HNVVDYVASA EYKVFAWGLN DPTEGNPTSI RDPWTDASPY TWNSDGMSKY PTTRGNNAIA
     QDNPTGGSTY INNYRPQSPN LIFSYPWSPT ATPPSSYKDF SITQLFYTTN RYHDLLYSFG
     FNEAAGNFQV NNGNKGGKGN DFAIVNAQDG SGTNNANFAT PPDGSPGRMR MYNWTTARPN
     RDGCLEAGIV IHEYTHGLSN RLCGGPANSA CLNALESGGM GEGWGDFYAT AIRLKPRDTK
     NTNYSMGAWA ANNPKGIRAY LYSTNLQTNP YMYTSVNSLR EVHQIGTVWA SMLYDLMWAL
     IEAHGGTYSA NPVFRNGVPQ DGRHLSMKLV MDGMALQPCN PNFVQARDAI LDADRALTNS
     ANKCTIWKAF AKRGLGYGAK YDARNRTGSN K