ID   MEP3_TRIRU              Reviewed;         633 AA.
AC   Q6WIH8;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Extracellular metalloproteinase 3;
DE            EC=3.4.24.-;
DE   AltName: Full=Fungalysin MEP3;
DE   Flags: Precursor;
GN   Name=MEP3;
OS   Trichophyton rubrum (Athlete's foot fungus) (Epidermophyton rubrum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=5551;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION BY MASS SPECTROMETRY, AND
RP   SUBCELLULAR LOCATION.
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).
RN   [2]
RP   INDUCTION.
RX   PubMed=19098130; DOI=10.1128/ec.00208-08;
RA   Zaugg C., Monod M., Weber J., Harshman K., Pradervand S., Thomas J.,
RA   Bueno M., Giddey K., Staib P.;
RT   "Gene expression profiling in the human pathogenic dermatophyte
RT   Trichophyton rubrum during growth on proteins.";
RL   Eukaryot. Cell 8:241-250(2009).
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:14766908}.
CC   -!- INDUCTION: Expression is strongly increased during growth on protein-
CC       rich medium. Expressed at even higher levels when keratin is present in
CC       the protein-rich medium. {ECO:0000269|PubMed:19098130}.
CC   -!- SIMILARITY: Belongs to the peptidase M36 family. {ECO:0000305}.
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DR   EMBL; AY283569; AAQ21094.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6WIH8; -.
DR   SMR; Q6WIH8; -.
DR   MEROPS; M36.001; -.
DR   PRIDE; Q6WIH8; -.
DR   VEuPathDB; FungiDB:TERG_03248; -.
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..246
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000380852"
FT   CHAIN           247..633
FT                   /note="Extracellular metalloproteinase 3"
FT                   /id="PRO_0000380853"
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        410
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        480
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        622
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   633 AA;  69341 MW;  8091FE269A666279 CRC64;
     MHGLLLAGLL ALPMNVLAYP AEQHASNVLS RRGVDIESFR LPLKAKYMDS EATAQKIQAM
     SFSKDDDYVS TATKLVKSTF PKSTFRVVDD HYIGTNGIGH VHFKQTAHGL DIDNSDFNVN
     IGRDGKVFSF GNSFFTGEIP KENPMVKRAF SDPVKALKGA VKALNLPVKS DNAKPKTIAG
     KESFEFMGTT GALSAPKANL VYLQKEDGTL ALTWKVETDV GDNWLLTYVD AHNSETVHNV
     VDYVASAEYK VFAWGLNDPT EGNPTSIRDP WTDASPYTWN SDGMSKYPTT RGNNAIAQDN
     PTGGSTYINN YRPQSPNLIF SYPWSPTATP PSSYKDFSIT QLFYTTNRYH DLLYSFGFNE
     AAGNFQVNNG NKGGKGNDFA IVNAQDGSGT NNANFATPPD GSPGRMRMYN WTTARPNRDG
     CLEAGIVIHE YTHGLSNRLC GGPANSACLN ALESGGMGEG WGDFYATAIR LKPRDTKNTN
     YSMGAWAANN PKGIRAYLYS TNLQTNPYMY TSVNSLREVH QIGTVWASML YDLMWALIEA
     HGGTYSANPV FRNGVPQDGR HLSMKLVMDG MALQPCNPNF VQARDAILDA DRALTNSANK
     CTIWKAFAKR GLGYGAKYDA RNRTGSNKLP PGC