ID MEP5_TRIRU Reviewed; 633 AA.
AC Q8NIH1;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 22-FEB-2023, entry version 62.
DE RecName: Full=Extracellular metalloproteinase 5;
DE EC=3.4.24.-;
DE AltName: Full=Fungalysin MEP5;
DE Flags: Precursor;
GN Name=MEP5;
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:0000269|PubMed:14766908}.
CC -!- SIMILARITY: Belongs to the peptidase M36 family. {ECO:0000305}.
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DR EMBL; AF407190; AAN03641.1; -; mRNA.
DR EMBL; AF407189; AAN03640.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8NIH1; -.
DR SMR; Q8NIH1; -.
DR MEROPS; M36.001; -.
DR GlyCosmos; Q8NIH1; 3 sites, No reported glycans.
DR VEuPathDB; FungiDB:TERG_02213; -.
DR OrthoDB; 2786251at2759; -.
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 1: Evidence at protein level;
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_0000380878"
FT CHAIN 246..633
FT /note="Extracellular metalloproteinase 5"
FT /id="PRO_0000380879"
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 285
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; 69779 MW; 4DDFD7D8A01E92B6 CRC64;
MHGLLLAAAG LLSLPLHVVA HPQPSTSLAG RGVDLDAYRM ADRSSYMSSD DMKLKQPAIA
SLSGGNYVDT ATEVVKRMMP GMTFRMADDH YVGESGISHL YFRQTMHGMD IDNADFNVNI
GKDGKVLSFG HSFYTGPAPD RAPVEKRDFS GPMRAFHGAC KALNLPINAD KATIQTMNEH
EVMFVGTSGA MSDPQGKLCY MAKEDGTLAL TWRVETDMGD NWLLSYVDAK ETDKVHNVVD
YVSHATYQVY RWPIPDPTEG KREIVENPWN LKTSPFTWIS DGKTNYTTTR GNNAIAQANF
DGGEDYLNNY RPNSKNLKFE YPYAPNMSPP KSYIDASVTQ LFYSANIVHD LYYMLGFTEK
AGNFQVNNHG QGGKGNDFVI LNAQDGSGTN NANFATPPDG KPGRMRVYIW TKAKPARDSS
FEAGTVIHEY THGLSNRLCG GPANSGCLNG MESGGMGEGW GDFFATAIRL KPNDNRNANY
VHGEWVNNSP KGNRLYPYST NLQTNPLVYT SCNKYNEVHA IGTVWCSILY EVLWNLIDKH
GKNDGPTPVF ENGVPNDGKY LAMKLVLDGM AIQPCKPTFV QARDAIIDAD MNLTKGSNKC
ELWKAFAKRG LGVGAKYDPK NRTGSKAVPK ECQ
//
