ID   MEP4_ARTBE              Reviewed;         643 AA.
AC   Q6WIH1;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Extracellular metalloproteinase 4;
DE            EC=3.4.24.-;
DE   AltName: Full=Fungalysin MEP4;
DE   Flags: Precursor;
GN   Name=MEP4;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY283576; AAQ21101.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6WIH1; -.
DR   SMR; Q6WIH1; -.
DR   MEROPS; M36.001; -.
DR   PHI-base; PHI:4973; -.
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..254
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000380860"
FT   CHAIN           255..643
FT                   /note="Extracellular metalloproteinase 4"
FT                   /id="PRO_0000380861"
FT   REGION          47..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        56..71
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        438
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         437
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         441
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   CARBOHYD        271
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        420
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        510
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        553
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   643 AA;  70641 MW;  BDCE89F15EC36CEE CRC64;
     MHGLLLAGLL ALPLNVLAHP TESHSSGISR RAIDITSYRL PQISKYTKSD AVPKQDDESF
     TTSSTGDDNV SSGDYVTTAT DWLKKTLPKA TYRLVNDHYI GDSGIGHVHF RQTAHGIDID
     NTDFNVNIGR DGKVFSFGNS FYDGEIPKAN PMVKRDFSDP VNALQGAIQT LNLPVTAKPE
     NVKAKPVEGK ENFKFEGTSG AFSDPKAQLV YLQKDGGLVL SWKVETDIGD NWLLTYVDAN
     KNDKVHSVVD YVSAAEYKVY PWGINDPTEG NRTSIHLPWF KTLSTDWHID GKGWYSTTRG
     NNAIAQENPT GGPEYENNYR PKSPLFIFKY PYSEAMTPPS SYRDASITQL FYTTNVYHDV
     LYILGFNEKA GNFQVNNWNK GGVGGDFAIL NSQDGSGVNN ANFATPPDGQ PGRMRMYTWN
     ASTPERDGCF EAGIVIHEYT HGVSNRLTGG PANSRCLAAL ESGGMGEGWS DFFATAIRLK
     AGDTRATDYT MGEWASNRPN GIRKYRYSTN LTTNPHMYVD ADGLTSVHAI GTIWASMLYE
     LLWNLIDKHG KGNVTKVRPV LKNGVPTDGR HLAMKLVLDG MALQPCLPNF VQARDAILDA
     DKVLTQGSNK CEIWKAFAKR GLGVGAVFNP SKRTGSNELP AGC