ID   MEP2_TRIRU              Reviewed;         632 AA.
AC   Q8NIE3;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Extracellular metalloproteinase 2;
DE            EC=3.4.24.-;
DE   AltName: Full=Fungalysin MEP2;
DE   Flags: Precursor;
GN   Name=MEP2;
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).
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:0000250}.
CC   -!- INDUCTION: Expression is strongly increased during growth on protein-
CC       rich medium containing keratin.
CC   -!- SIMILARITY: Belongs to the peptidase M36 family. {ECO:0000305}.
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DR   EMBL; AF407188; AAN03639.1; -; mRNA.
DR   EMBL; AF407187; AAN03638.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8NIE3; -.
DR   SMR; Q8NIE3; -.
DR   MEROPS; M36.001; -.
DR   VEuPathDB; FungiDB:TERG_04809; -.
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..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..244
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000380844"
FT   CHAIN           245..632
FT                   /note="Extracellular metalloproteinase 2"
FT                   /id="PRO_0000380845"
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        270
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   632 AA;  69756 MW;  9AF9B00C7D035348 CRC64;
     MHGLLLAGLA AALPLGVAGL PARQQSGLSP RGVDINPYRF ASMAKYSEHK STSQMVHSFS
     YSKDDDYVAT ATKLVKSTFP NMTFRTVKDH YIGTNGIGHV HFKQTAHGID IDNADFNVNI
     GRDGKVFTFG NSFYEGEMPK TNPLTKRDFS DPVKALQGAI KTLKLPVKPQ SAKAMPMKEA
     ETFKFEGTSG ALSDPMAKLV YIQKDGKLHL TWRVETDVGD NWLLSYVDSK ETETVHNVVD
     YVASADYKVF AWGLNDPTEG QPTMIKDPWN TTGTGSPFTW HGDGQMDYTV TRGNNIAAQD
     NPSGGEQWEN NYRPDSPELS FVYEYSEQME PDQYKDFAIT QLFYTTNTYH DVLYALGFTE
     EAGNFQMNNN GKGGEGNDFA ICNAQDGSGT NNANFATPPD GQNGRMRMYT WTTAQPSRDG
     DLEAGIVIHE YTHGLSNRLC GGPANSNCLN ELEAGGMGEG WGDFYATAIR LKQGDTHDTD
     YTMGEWAANM KGGIREYPYS TNMQTNPYTY ADVQGMDEVH GIGTVWATIL YEVLWNLIDE
     HGMSKNIMPK FVNGAPSDGR NLAMKLVLDG MTLMPCNPNF MQARDAIIDA DQALTNGQNK
     CALMKAFSKR GLGANYKHGK NRVNNFDMPA DC