ID   MEP4_ARTOC              Reviewed;         649 AA.
AC   C5FIK0;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 2.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=Extracellular metalloproteinase 4;
DE            EC=3.4.24.-;
DE   AltName: Full=Fungalysin MEP4;
DE   Flags: Precursor;
GN   Name=MEP4; ORFNames=MCYG_02088;
OS   Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX   NCBI_TaxID=554155;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4605 / CBS 113480;
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
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.
CC   -!- SIMILARITY: Belongs to the peptidase M36 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EEQ29269.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; DS995702; EEQ29269.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_002849154.1; XM_002849108.1.
DR   AlphaFoldDB; C5FIK0; -.
DR   SMR; C5FIK0; -.
DR   MEROPS; M36.001; -.
DR   EnsemblFungi; EEQ29269; EEQ29269; MCYG_02088.
DR   GeneID; 9229208; -.
DR   eggNOG; ENOG502QTDC; Eukaryota.
DR   HOGENOM; CLU_012703_3_0_1; -.
DR   OrthoDB; 1136823at2759; -.
DR   Proteomes; UP000002035; Unassembled WGS sequence.
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   3: Inferred from homology;
KW   Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW   Reference proteome; Secreted; Signal; Virulence; Zinc; Zymogen.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..260
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000384083"
FT   CHAIN           261..649
FT                   /note="Extracellular metalloproteinase 4"
FT                   /id="PRO_0000384084"
FT   ACT_SITE        444
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         443
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         447
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   CARBOHYD        494
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        609
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   649 AA;  71250 MW;  73651DAAC5B40C92 CRC64;
     MHGLLLAGLL ALPSNVLGHP AEPPNSVNVT HRHIDTSAYF LPQLSLYNKS EDVAEYGGDN
     ITGSSYSGGD HSASNLSSED YVTVATSLLK ATLPYASFRL IDDHYIGDSG IGHVHFRQTV
     YGIDIDNTDF NVNVGRDGKV FSYGSSFYEG EIPKANPVAK RDFSDPVNAL IGAINTLNIP
     VTAAVGEVKT TPIEGNSTYM FKGTTGALTD PTAQLVYLQK DGGLHLTWRV ETDVGDNWLL
     TYVDAKKNDQ VHGVVDYVAS AEYQVYPWGV NDPTDGERAH LYFPWFKTGS RNWHIDGRGW
     HTTTRGNNAI AQDNPSGGWE YEDNHRPTNP LLIFRYPYTQ SMTPPASYRD ASITQLFYTG
     NVYHDLLYIL GFNEKAGNFQ VNNWGKGGKG NDFTILNTQD GSGVNNANFA TPPDGQPGRM
     RMYVWDTSTP YRDGSFEAGI VIHEYTHGVS NRLTGGPANS RCLSSLESGG MGEGWSDFFA
     TVVHLKERDT RNKNYTIGEW ASGRQGGIRK YPYSTDLHTN PLMYVDADGL ESVHAIGTIW
     CTILNEVLWN LIERHGMGNV NKIKPTFKDG VPTDGRNLAM KLVLDGMALQ PCLPNFVQAR
     DAIIDADMNL TKGANRCELW KAFAKRGLGV GAAYNPEKRV GSSRVPGGC