ID MEP1_ARTBE Reviewed; 635 AA.
AC Q6WIH5;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 22-FEB-2023, entry version 53.
DE RecName: Full=Extracellular metalloproteinase 1;
DE EC=3.4.24.-;
DE AltName: Full=Fungalysin MEP1;
DE Flags: Precursor;
GN Name=MEP1;
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].
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 -!- SIMILARITY: Belongs to the peptidase M36 family. {ECO:0000305}.
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DR EMBL; AY283572; AAQ21097.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6WIH5; -.
DR SMR; Q6WIH5; -.
DR MEROPS; M36.001; -.
DR GlyCosmos; Q6WIH5; 4 sites, No reported glycans.
DR PHI-base; PHI:4970; -.
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 CDD; cd09596; M36; 1.
DR Gene3D; 3.10.170.10; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR InterPro; IPR011096; FTP_domain.
DR InterPro; IPR001842; Peptidase_M36.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR33478; EXTRACELLULAR METALLOPROTEINASE MEP; 1.
DR PANTHER; PTHR33478:SF1; EXTRACELLULAR METALLOPROTEINASE MEP; 1.
DR Pfam; PF07504; FTP; 1.
DR Pfam; PF02128; Peptidase_M36; 1.
DR PRINTS; PR00999; FUNGALYSIN.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Secreted; Signal; Virulence; Zinc; Zymogen.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..246
FT /evidence="ECO:0000250"
FT /id="PRO_0000380832"
FT CHAIN 247..635
FT /note="Extracellular metalloproteinase 1"
FT /id="PRO_0000380833"
FT ACT_SITE 431
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 430
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 434
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 475
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 594
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 623
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 635 AA; 69989 MW; F7E66B493271375E CRC64;
MHGLLLAAGL LSLPLHVLAH PQPSTSTSLA GRAGAVDLNE FRVAHRSSYT SHDEMKKLPS
IASFRQGTYL EVATELVKQT MPNMEFRLVD DHYVGDSGIG HVRFRQTMHG IDIDNSDFNV
NVGKNGKVLS HGNSFYTGPA PASNPMVKRD FIDPMQALNG VRKALNLPVK ADGAHVENMS
EHKVMFKGTS GALSDPTAKL CYMAKEDGSL ALTWRVETDI GDNWLLSYMD AKESSKVHNV
VDYVAHATFQ VYKWGLADPT EGKRDILTNP WNLKTSPLTW LADGKTNFTA TRGNNAIAQY
NPDGGNDYEN NYRPSPKNLK FEYPYSPDMN PPKTYIDASV TQLFYTSNVC HDLYYMLGFN
EKAGNFQVNN RGQGGKGNDY VILNAQDGSG TNNANFATPP DGQPGRMRAY IWTRANPPRD
ASFEAGTIIH EYTHGLSNRL CGGPANSRCL NALESGGMGE GWGDFYATAV RLKPNDTRKT
NYVKGGWVNN SPKGVRMYPY STDMNVNPLV YTSNNKLNEV HAIGTVWCTM LYEVLWNLID
KHGKNDGPVP VFENGVPNDG KYLAMKLVMD GMAIQPCNPN FVQARDAILD ADMNLTKGAN
KCEIWKGFAK RGLGVGAKFD PKNRTGSNQV PNECK
//
