ID   MEP2_ARTGP              Reviewed;         632 AA.
AC   E4UQ65;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 1.
DT   03-AUG-2022, entry version 40.
DE   RecName: Full=Extracellular metalloproteinase 2;
DE            EC=3.4.24.-;
DE   AltName: Full=Elastinolytic metalloproteinase MEP2;
DE   AltName: Full=Fungalysin MEP2;
DE   Flags: Precursor;
GN   Name=MEP2; ORFNames=MGYG_02992;
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; DS989823; EFQ99984.1; -; Genomic_DNA.
DR   RefSeq; XP_003175467.1; XM_003175419.1.
DR   AlphaFoldDB; E4UQ65; -.
DR   SMR; E4UQ65; -.
DR   MEROPS; M36.001; -.
DR   EnsemblFungi; EFQ99984; EFQ99984; MGYG_02992.
DR   GeneID; 10030775; -.
DR   eggNOG; ENOG502QTDC; Eukaryota.
DR   HOGENOM; CLU_012703_3_0_1; -.
DR   InParanoid; E4UQ65; -.
DR   OMA; NDFAICN; -.
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..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..244
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407158"
FT   CHAIN           245..632
FT                   /note="Extracellular metalloproteinase 2"
FT                   /id="PRO_0000407159"
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;  69566 MW;  3C30F0FAE2B49884 CRC64;
     MHGLLLAGLA AALPLGVAGL PARQQSGLSP RGIDINAYRF ASMAKYSEHK TTSQMVHSFS
     YSKDDDYVAT ATKLVKSTFP NMTFRTVKDH YIGTNGIGHV HFKQTAHGID IDNADFNVNI
     GRDGKVFTFG NSFFEGEMPK TNPLTKRDFS DPVKALHGAV KTLKIPVKPE SAKAMPMKEV
     ETFKFEGTSG ALSEPKAKLV YLQKDGNLHL TWRVETDVGD NWLLSYVDAK ESETVHNVVD
     YVASADYKVF AWGLNDPTEG QPTMIKDPWN TTGSGSPFTW HGDGQMDYTV TRGNNVPAQD
     NPSGGSQWEN NYRPESAELS FVYEYSEQME PEQYKDFAIT QLFYTVNTFH DVLYTLGFTE
     EAGNFQMNNN GKGGQGNDFA ICNAQDGSGT NNANFATPPD GQPGRMRMYT WTTAQPSRDG
     DLEAGIVIHE YTHGLSNRLC GGPANSNCLN ELEAGGMGEG WGDFYATAIR LKQGDTHDTD
     YTMGEWAANQ KGGIREYPYS TNMQTNPYTY ADVQGMSEVH GIGTVWATIL YDVLWNLIDE
     HGMGKNIMPK FVNGAPTDGR NLAMKLVLDG MTLMPCNPNF MQARDAIIDA DQALTNGQNK
     CALMKAFAKR GLGSNYKHGK NRVNNFDMPA GC