ID MEP4_ARTOT Reviewed; 649 AA.
AC Q6WIH4;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 22-FEB-2023, entry version 51.
DE RecName: Full=Extracellular metalloproteinase 4;
DE EC=3.4.24.-;
DE AltName: Full=Fungalysin MEP4;
DE Flags: Precursor;
GN Name=MEP4;
OS Arthroderma otae (Microsporum canis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX NCBI_TaxID=63405;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION BY MASS SPECTROMETRY, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=LAU709-03;
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; AY283573; AAQ21098.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6WIH4; -.
DR SMR; Q6WIH4; -.
DR MEROPS; M36.001; -.
DR GlyCosmos; Q6WIH4; 2 sites, No reported glycans.
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..18
FT /evidence="ECO:0000255"
FT PROPEP 19..260
FT /evidence="ECO:0000250"
FT /id="PRO_0000380862"
FT CHAIN 261..649
FT /note="Extracellular metalloproteinase 4"
FT /id="PRO_0000380863"
FT ACT_SITE 444
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 443
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 447
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT CARBOHYD 494
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 609
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 649 AA; 71250 MW; 73651DAAC5B40C92 CRC64;
MHGLLLAGLL ALPSNVLGHP AEPPNSVNVT HRHIDTSAYF LPQLSLYNKS EDVAEYGGDN
ITGSSYSGGD HSASNLSSED YVTVATSLLK ATLPYASFRL IDDHYIGDSG IGHVHFRQTV
YGIDIDNTDF NVNVGRDGKV FSYGSSFYEG EIPKANPVAK RDFSDPVNAL IGAINTLNIP
VTAAVGEVKT TPIEGNSTYM FKGTTGALTD PTAQLVYLQK DGGLHLTWRV ETDVGDNWLL
TYVDAKKNDQ VHGVVDYVAS AEYQVYPWGV NDPTDGERAH LYFPWFKTGS RNWHIDGRGW
HTTTRGNNAI AQDNPSGGWE YEDNHRPTNP LLIFRYPYTQ SMTPPASYRD ASITQLFYTG
NVYHDLLYIL GFNEKAGNFQ VNNWGKGGKG NDFTILNTQD GSGVNNANFA TPPDGQPGRM
RMYVWDTSTP YRDGSFEAGI VIHEYTHGVS NRLTGGPANS RCLSSLESGG MGEGWSDFFA
TVVHLKERDT RNKNYTIGEW ASGRQGGIRK YPYSTDLHTN PLMYVDADGL ESVHAIGTIW
CTILNEVLWN LIERHGMGNV NKIKPTFKDG VPTDGRNLAM KLVLDGMALQ PCLPNFVQAR
DAIIDADMNL TKGANRCELW KAFAKRGLGV GAAYNPEKRV GSSRVPGGC
//
