ID   MEP3_ARTBE              Reviewed;         633 AA.
AC   Q6WIH3;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Extracellular metalloproteinase 3;
DE            EC=3.4.24.-;
DE   AltName: Full=Fungalysin MEP3;
DE   Flags: Precursor;
GN   Name=MEP3;
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], 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).
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   -!- SIMILARITY: Belongs to the peptidase M36 family. {ECO:0000305}.
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DR   EMBL; AY283574; AAQ21099.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6WIH3; -.
DR   SMR; Q6WIH3; -.
DR   MEROPS; M36.001; -.
DR   PHI-base; PHI:4972; -.
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_0000380848"
FT   CHAIN           247..633
FT                   /note="Extracellular metalloproteinase 3"
FT                   /id="PRO_0000380849"
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;  69320 MW;  4C76F0F040656A10 CRC64;
     MHGLLLAGLL ALPMNVLAHP AEQHASNVLS RRGVDIESFR LPLKAKYMDS DAAAQKIQAM
     SFSKDDDYVS TATKLVKSTF PKSTFRVVDD HYIGTNGIGH VHFKQTAHGL DIDNSDFNVN
     IGRDGKVFSF GNSFFTGEIP KENPMVKRAF SDPVKALKGA VKALNLPVKS DNAKAKTTAG
     KESFEFMGTT GALSAPKANL VYLQKEDGTL ALTWRVETDV GDNWLLTYVD AHNSETVHNV
     VDYVASAEFK VFAWGLNDPT EGNPTSIRDP WTDSSPYTWH SDGMTKYPTT RGNNAIAQDN
     PTGGSTYINN YRPQSPNLIF NYPWSPTATP PSSYKDFSIT QLFYTTNRFH DLLYSFGFNE
     AAGNFQVNNG NKGGRGNDFA IVNAQDGSGT NNANFATPPD GSPGRMRMYN WTTARPNRDG
     CLEAGIVIHE YAHGLSNRLC GGPANSGCLN ALESGGMGEG WGDFYATAIR LKPRDTKDTN
     YSMGAWAANN PKGIRAYLYS TNLQTNPYMY TSVNSLREVH QIGTVWATML YDLMWALIEA
     HGGTYSANPV FRNGVPQDGR HLAMKLVMDG MALQPCNPNF VQARDAILDA DRALTNSANK
     CTIWKAFAKR GLGYGAKYDA RNRTGSNRLP PGC