ID   MEP4_ARTGP              Reviewed;         642 AA.
AC   E4UUL6;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 1.
DT   03-AUG-2022, entry version 39.
DE   RecName: Full=Extracellular metalloproteinase 4;
DE            EC=3.4.24.-;
DE   AltName: Full=Elastinolytic metalloproteinase MEP4;
DE   AltName: Full=Fungalysin MEP4;
DE   Flags: Precursor;
GN   Name=MEP4; ORFNames=MGYG_03984;
OS   Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum
OS   gypseum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Nannizzia.
OX   NCBI_TaxID=535722;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4604 / CBS 118893;
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 that allows assimilation of
CC       proteinaceous substrates and probably acts as a virulence factor.
CC       {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:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M36 family. {ECO:0000305}.
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DR   EMBL; DS989824; EFR00983.1; -; Genomic_DNA.
DR   RefSeq; XP_003173813.1; XM_003173765.1.
DR   AlphaFoldDB; E4UUL6; -.
DR   SMR; E4UUL6; -.
DR   MEROPS; M36.001; -.
DR   EnsemblFungi; EFR00983; EFR00983; MGYG_03984.
DR   GeneID; 10029097; -.
DR   eggNOG; ENOG502QTDC; Eukaryota.
DR   HOGENOM; CLU_012703_3_0_1; -.
DR   InParanoid; E4UUL6; -.
DR   OMA; IRKDSYT; -.
DR   OrthoDB; 1136823at2759; -.
DR   Proteomes; UP000002669; 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; Zinc; Zymogen.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..253
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407166"
FT   CHAIN           254..642
FT                   /note="Extracellular metalloproteinase 4"
FT                   /id="PRO_0000407167"
FT   REGION          49..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        437
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         436
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         440
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   CARBOHYD        419
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        509
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        602
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   642 AA;  70359 MW;  6190BAC2BE701358 CRC64;
     MHGLLLAGLL ALPLNVLAHP TESHSSGISR RAIDITSYRL PQISKYTKSD SLTGQDGQSF
     TASSADADTS SGDYVSTATN WLKKTLPNAS YRLVNDHYIG DSGIGHVHFR QTAHGIDIDN
     TDFNVNIGRD GKVFSFGNSF YDGEIPKANP MVKRDFSDPV DALHGAIQTL NIPVTAKPEN
     VKAKPVEGKE SFKFEGTSGA LSDPKAQLVY LQKDGGLVLS WKVETDVGDN WLLSYVDAND
     KGKVHSVVDY VSAAAYEVYP WGINDPTEGK RSTIHVPWFK TQSVDWHIDG KNWYPTTRGN
     NAIAQENPTG QREYENNYRP KSPLFIFKYP YSEAMSPPSS YRDASITQLF YTTNVFHDVL
     YILGFNEKAG NFQTNNWNKG GLGGDYAILN SQDGSGVNNA NFATPPDGEP GRMRMYNWNA
     STPERDGCFE AGIVIHEYTH GVSNRLTGGP ANSRCLAALE SGGMGEGWSD FFATAIRLKN
     GDTRATDYTM GEWASNRPNG IRKYRYSTNL TTNPHMYVDA DGLTSVHAIG TIWASMLYEM
     LWNLIDKHGK GDVSKVKPTL KNGVPTDGRH LAMKIVLDGM ALQPCLPNFV QARDAIIDAD
     KNLTGGSNKC EIWKAFAKRG LGVGAVYNPS KRTGSNELPA GC