ID   MEP3_ARTOT              Reviewed;         633 AA.
AC   Q8J0D6;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Extracellular metalloproteinase 3;
DE            EC=3.4.24.-;
DE   AltName: Full=Fungalysin MEP3;
DE   Flags: Precursor;
GN   Name=MEP3;
OS   Arthroderma otae (Microsporum canis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX   NCBI_TaxID=63405;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=IHEM 15221;
RX   PubMed=12228297; DOI=10.1128/iai.70.10.5676-5683.2002;
RA   Brouta F., Descamps F., Monod M., Vermout S., Losson B., Mignon B.;
RT   "Secreted metalloprotease gene family of Microsporum canis.";
RL   Infect. Immun. 70:5676-5683(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION BY MASS SPECTROMETRY, AND
RP   SUBCELLULAR LOCATION.
RC   STRAIN=LAU709-03;
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   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=TIMM4092;
RX   PubMed=14985633;
RA   Yamada T., Makimura K., Hirai A., Kano R., Hasegawa A., Uchida K.,
RA   Yamaguchi H.;
RT   "Isolation of a promoter region of a secreted metalloprotease gene from
RT   Microsporum canis.";
RL   Jpn. J. Infect. Dis. 57:25-28(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; AJ490183; CAD35288.1; -; Genomic_DNA.
DR   EMBL; AB097684; BAF97795.1; -; Genomic_DNA.
DR   EMBL; AB125268; BAF97796.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8J0D6; -.
DR   SMR; Q8J0D6; -.
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   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_5000068598"
FT   CHAIN           247..633
FT                   /note="Extracellular metalloproteinase 3"
FT                   /id="PRO_5000068599"
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"
SQ   SEQUENCE   633 AA;  69377 MW;  DB61E74102A5030C CRC64;
     MHGLLLAGLL ALPMNVLAHP AEQQTSSVLS RRGVDIDSFR LPLKAKYMDS DATAQKIQAL
     SFSKEDDYVS TATKLVKSTF PKSTFRVVDD HYIGTNGIGH VHFKQTAHGL DIDNSDFNVN
     IDRDGKVFSF GNSFFTGEIP KESPMVKREF SDPVKALKGA VKALNLPVKS ENAKAKTVEG
     KESFEFQGTS GALSAPKAKL VYLQKEDGSL ALTWKVETDV GDNWLLSYVD AHDSETVHNV
     VDYVASAEFK VFAWGLNDPT EGNPTSFRDP WTASSPFTWH SDGTNKYPTT RGNNAIAQDN
     PTGGSTYLNN YRPQSANLIF NYPWTAAMTP PSSYKDFSIT QLFYTTNRYH DLLYSFGFNE
     AAGNFQVNNN NKGGKGNDFA IVNAQDGSGT NNANFATPPD GSPGRMRMYN WTTARPNRDG
     CLEAGIVIHE YTHGLSNRLC GGPANSACLN ALESGGMGEG WGDFYATAIR LKPRDTKNTN
     YSMGAWAAND PKGIRAYLYS TNLQTNPYMY TSVNNLREVH GIGTVWATML YELMWGLIEA
     HGGTYSADPV FRNGVPQDGR HLAMKIVMDG MALQPCNPNF VQARDAIIDA DRALTNGANK
     CTIWKAFAKR GLGYGAKYDP RTRTGSNQLP PGC