ID   MEP4_TRIRU              Reviewed;         643 AA.
AC   Q8NIJ4;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Extracellular metalloproteinase 4;
DE            EC=3.4.24.-;
DE   AltName: Full=Fungalysin MEP4;
DE   Flags: Precursor;
GN   Name=MEP4;
OS   Trichophyton rubrum (Athlete's foot fungus) (Epidermophyton rubrum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=5551;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX   PubMed=12452286; DOI=10.1078/1438-4221-00223;
RA   Monod M., Capoccia S., Lechenne B., Zaugg C., Holdom M., Jousson O.;
RT   "Secreted proteases from pathogenic fungi.";
RL   Int. J. Med. Microbiol. 292:405-419(2002).
RN   [2]
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).
RN   [3]
RP   INDUCTION.
RX   PubMed=19098130; DOI=10.1128/ec.00208-08;
RA   Zaugg C., Monod M., Weber J., Harshman K., Pradervand S., Thomas J.,
RA   Bueno M., Giddey K., Staib P.;
RT   "Gene expression profiling in the human pathogenic dermatophyte
RT   Trichophyton rubrum during growth on proteins.";
RL   Eukaryot. Cell 8:241-250(2009).
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   -!- INDUCTION: Expression is strongly increased during growth on protein-
CC       rich medium. Expressed at even higher levels when keratin is present in
CC       the protein-rich medium. {ECO:0000269|PubMed:19098130}.
CC   -!- SIMILARITY: Belongs to the peptidase M36 family. {ECO:0000305}.
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DR   EMBL; AF407192; AAN03643.1; -; mRNA.
DR   EMBL; AF407191; AAN03642.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8NIJ4; -.
DR   SMR; Q8NIJ4; -.
DR   MEROPS; M36.001; -.
DR   PRIDE; Q8NIJ4; -.
DR   VEuPathDB; FungiDB:TERG_04324; -.
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_0000380866"
FT   CHAIN           255..643
FT                   /note="Extracellular metalloproteinase 4"
FT                   /id="PRO_0000380867"
FT   REGION          47..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        54..73
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        603
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        629
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   643 AA;  70698 MW;  1A03A8CB4CC35A42 CRC64;
     MHGLMLAGLL ALPLSVLGHP TESHSSGISR RAIDITSYRL PQISKYTKSD AVPKQDGESF
     TTSSTGNDNS SSGDYVTTAT NWLKKTLPKA TYRLVKDHYI GDSGIGHVHF RQTAHGIDID
     NTDFNVNIGR DGKVFSFGNS FYDGEIPKAN PMVKRDFSDP VNALHGAIQI LNLPVTAKPE
     NVKAKPVEGK ENFKFEGTSG ALSDPKAQLV YLQKDGGLVL SWKVETDVGD NWLLTYVDAN
     KNDKVHSVVD YVSAAEYQVY PWGINDPTEG NRTTLHLPWL KTLSTDWHID GKGWYSTTRG
     NNAIAQENPT GGPEYENNYR PKSPLFIFKY PYSKAMTPPS SYRDASITQL FYTTNVYHDV
     LYILGFNEKA GNFQINNWNK GGVGGDYAIL NSQDGSGVNN ANFATPPDGQ PGRMRMYTWN
     ASIPERDGCF EAGIVIHEYT HGVSNRLTGG PENSRCLAAL ESGGMGEGWS DFFATAIRLK
     PGDTRVTDYT MGEWASNRPN GIRKYRYSTS LTTNPHMYVD ADGLTSVHAI GNIWASMLYE
     LLWNLIDKHG KGDVTKIRPV LKNGVPTDGR HLAMKIVLDG MALQPCLPNF VQARDAILDA
     DKNLTQGSNK CEIWKAFAKR GLGVGAVFNL SKRTGSNELP AGC