ID MEP5_ARTBE Reviewed; 633 AA.
AC Q6WIH6;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 22-FEB-2023, entry version 49.
DE RecName: Full=Extracellular metalloproteinase 5;
DE EC=3.4.24.-;
DE AltName: Full=Fungalysin MEP5;
DE Flags: Precursor;
GN Name=MEP5;
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; AY283571; AAQ21096.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6WIH6; -.
DR SMR; Q6WIH6; -.
DR MEROPS; M36.001; -.
DR GlyCosmos; Q6WIH6; 3 sites, No reported glycans.
DR PHI-base; PHI:4974; -.
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..21
FT /evidence="ECO:0000255"
FT PROPEP 22..245
FT /evidence="ECO:0000250"
FT /id="PRO_0000380874"
FT CHAIN 246..633
FT /note="Extracellular metalloproteinase 5"
FT /id="PRO_0000380875"
FT ACT_SITE 429
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 428
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 432
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 592
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 621
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 633 AA; 69829 MW; A0E280A44B2208D1 CRC64;
MHGLLLAAAG LLSLPLHVIA HPQPSTNLAG RGVDLDAYRM ADRSSYMNSD DMKLKQPGIA
SLSGGNYVDT ATEVVKRMMP GMTFRMVDDH YVGESGISHV YFRQTMHGMD IDNSDFNVNI
GKDGKVLSFG HSFYTGPAPD KAPVEKRDFS DPMKAFHGAC KALSLPINAD KATVQTMNEH
EVMFMGTSGA MSDPQGKLCY MAKEDGTLAL TWRVETDMGD NWLLSYVDAK ETEKVHNVVD
YVSHATYQVY RRALSPDPTE GKRESIENPW NLKTSPFTWI SDGKTNYTTT RGNNAIAQAN
FDGGEDYLNN HRPNNKNLKF EYPYAPNMSP KSYIDASVTQ LFYSANMVHD LYYMLGFTEK
AGNFQVNNHG QGGKGNDFVI LNAQDGSGTN NANFATPPDG KPGRMRVYIW TKAKPARDSS
FEAGTVIHEY THGLSNRLTG GPANAGCLNG MESGGMGEGW GDFFATAIRL KPNDNRNANY
VHGEWVNNSP KGNRMYPYST SLQTNPLVYT SCNKYNEVHA IGTVWGSMLY EVLWNLIDKH
GKNDGPTPVF ENGVPKDGKY LAMKLVMDGM AIQPCKPTFV QARDAIIDAD MNLTKGSNRC
EIWKAFAKRG LGVGAKYDPK NRTGNKGLPK DCQ
//
