MEP4_TRISD
ID MEP4_TRISD Reviewed; 392 AA.
AC A1XIM5;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Extracellular metalloproteinase 4;
DE EC=3.4.24.-;
DE AltName: Full=Fungalysin MEP4;
DE Flags: Precursor; Fragment;
GN Name=MEP4;
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 209;
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; DQ384955; ABL84993.1; -; Genomic_DNA.
DR AlphaFoldDB; A1XIM5; -.
DR SMR; A1XIM5; -.
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_0000380868"
FT CHAIN 10..>392
FT /note="Extracellular metalloproteinase 4"
FT /id="PRO_0000380869"
FT ACT_SITE 194
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 193
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 359
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 392
SQ SEQUENCE 392 AA; 43355 MW; 5957FCB91A2EE0A6 CRC64;
VHSVVDYVSA AEHQVYPWGI NDPTEGNRTT LHLPWLKTLS TDWHIDGKGW YSTTRGNNAI
AQENPTGGPE YENNYRPKSP LFIFKYPYSK AMTPPSSYRD ASITQLFYTT NVYHDVLYIL
GFNEKAGNFQ INNWNKGGVG GDYAILNSQD GSGVNNANFA TPPDGQPGRM RMYTWNASIP
ERDGCFEAGI VIHEYTHGVS NRLTGGPENS RCLAALESGG MGEGWSDFFA TAIRLKPGDT
RATDYTMGEW ASNRPNGIRK YRYSTSLTTN PHMYVDADGL TSVHAIGNIW ASMLYELLWN
LIDKHGKGDV TKIRPVLKNG VPTDGRHLAM KIVLDGMALQ PCLPNFVQAR DAILDADKNL
TQGSNKCEIW KAFAKRGLGV GAVFNLSKRT GS
