ID   MEP3_TRIEQ              Reviewed;         633 AA.
AC   B8XGR5; A1XIL9;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 35.
DE   RecName: Full=Extracellular metalloproteinase 3;
DE            EC=3.4.24.-;
DE   AltName: Full=Fungalysin MEP3;
DE   Flags: Precursor;
GN   Name=MEP3;
OS   Trichophyton equinum (Horse ringworm fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=63418;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Krishnan S.K., Preuett B.L., Abdel-Rahman S.M.;
RT   "Comparing putative pathogenicity factors between Trichophyton tonsurans
RT   and Trichophyton equinum.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 238-628, IDENTIFICATION BY MASS
RP   SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC   STRAIN=IHEM 15219, IHEM 20668, and IHEM 20669;
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; FJ348247; ACL37337.1; -; Genomic_DNA.
DR   EMBL; DQ384949; ABL84984.1; -; Genomic_DNA.
DR   EMBL; DQ409176; ABL84988.1; -; Genomic_DNA.
DR   EMBL; DQ409177; ABL84989.1; -; Genomic_DNA.
DR   AlphaFoldDB; B8XGR5; -.
DR   SMR; B8XGR5; -.
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_0000380850"
FT   CHAIN           247..633
FT                   /note="Extracellular metalloproteinase 3"
FT                   /id="PRO_0000380851"
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;  69366 MW;  A29A20F045C17284 CRC64;
     MHGLLLAGLL ALPMNVLAHP AEQHASNVLS RRGVDIESFR LPLKAKYMDS DAAAQKIQAM
     SFSKDDDYVS TATKLVKSTF PKSTFRVVDD HYTGTNGIGH VHFKQTAHGL DIDNSDFNVN
     IDRDGKVFSF 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