MEP3_TRISD
ID MEP3_TRISD Reviewed; 391 AA.
AC A1XIM1;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=Extracellular metalloproteinase 3;
DE EC=3.4.24.-;
DE AltName: Full=Fungalysin MEP3;
DE Flags: Precursor; Fragment;
GN Name=MEP3;
OS Trichophyton soudanense.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=69891;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION BY MASS SPECTROMETRY, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=LAU 228, and LAU 556;
RX PubMed=17156126; DOI=10.1111/j.1574-6968.2006.00541.x;
RA Giddey K., Favre B., Quadroni M., Monod M.;
RT "Closely related dermatophyte species produce different patterns of
RT secreted proteins.";
RL FEMS Microbiol. Lett. 267:95-101(2007).
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:17156126}.
CC -!- SIMILARITY: Belongs to the peptidase M36 family. {ECO:0000305}.
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DR EMBL; DQ384951; ABL84986.1; -; Genomic_DNA.
DR EMBL; DQ409178; ABL84990.1; -; Genomic_DNA.
DR AlphaFoldDB; A1XIM1; -.
DR SMR; A1XIM1; -.
DR MEROPS; M36.001; -.
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; IPR001842; Peptidase_M36.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR Pfam; PF02128; Peptidase_M36; 1.
DR PRINTS; PR00999; FUNGALYSIN.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Secreted; Virulence; Zinc; Zymogen.
FT PROPEP <1..9
FT /evidence="ECO:0000250"
FT /id="PRO_0000380854"
FT CHAIN 10..>391
FT /note="Extracellular metalloproteinase 3"
FT /id="PRO_0000380855"
FT ACT_SITE 193
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 192
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 385
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT NON_TER 1
FT NON_TER 391
SQ SEQUENCE 391 AA; 42980 MW; 10A0E630FFF877C2 CRC64;
HNVVDYVASA EYKVFAWGLN DPTEGNPTSI RDPWTDASPY TWNSDGMSKY PTTRGNNAIA
QDNPTGGSTY INNYRPQSPN LIFSYPWSPT ATPPSSYKDF SITQLFYTTN RYHDLLYSFG
FNEAAGNFQV NNGNKGGKGN DFAIVNAQDG SGTNNANFAT PPDGSPGRMR MYNWTTARPN
RDGCLEAGIV IHEYTHGLSN RLCGGPANSA CLNALESGGM GEGWGDFYAT AIRLKPRDTK
NTNYSMGAWA ANNPKGIRAY LYSTNLQTNP YMYTSVNSLR EVHQIGTVWA SMLYDLMWAL
IEAHGGTYSA NPVFRNGVPQ DGRHLSMKLV MDGMALQPCN PNFVQARDAI LDADRALTNS
ANKCTIWKAF AKRGLGYGAK YDARNRTGSN K
