ID MEP2_ARTOT Reviewed; 632 AA.
AC Q8J0D4;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 22-FEB-2023, entry version 61.
DE RecName: Full=Extracellular metalloproteinase 2;
DE EC=3.4.24.-;
DE AltName: Full=Fungalysin MEP2;
DE Flags: Precursor;
GN Name=MEP2;
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].
RC STRAIN=IHEM 15221;
RX PubMed=12228297; DOI=10.1128/iai.70.10.5676-5683.2002;
RA Brouta F., Descamps F., Monod M., Vermout S., Losson B., Mignon B.;
RT "Secreted metalloprotease gene family of Microsporum canis.";
RL Infect. Immun. 70:5676-5683(2002).
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; AJ490185; CAD35290.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8J0D4; -.
DR SMR; Q8J0D4; -.
DR MEROPS; M36.001; -.
DR GlyCosmos; Q8J0D4; 1 site, 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 3: Inferred from homology;
KW Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Secreted; Signal; Virulence; Zinc; Zymogen.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..244
FT /evidence="ECO:0000250"
FT /id="PRO_5000068602"
FT CHAIN 245..632
FT /note="Extracellular metalloproteinase 2"
FT /id="PRO_5000068603"
FT REGION 294..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 430
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 429
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 433
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT CARBOHYD 270
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 632 AA; 69468 MW; F2FFC2FF8683D33E CRC64;
MHGLLLAGLA VALPLGVAGH PARPQTALSP RGIDVNAYRF TSTAKYNEHK TTSQMVQSFA
YSKDDDYVAT ATKLVKSTFP NMTFRTVKDH YIGTNGIGHV HFKQTAHDID IDNADFNVNI
GRDGKVFTFG NSFYQGEMPK TNPMVKRDYS DPVKALHGAI KTLKIPVKPE SAKAMPMDEV
ETFKFEGTSG ALSEPKAKLV YIQKDGNLHL TWRVETDVGD NWLLSYVDSK ESETVHNVVD
YVASADYKVF AFGLNDPTEG QPSMIKDPWN TTGSGSPFTW HGDGKTDYTV TRGNNVAAQD
NPSGGSQWEN NYRPDSPQLS FVYDYSDQME PEDYKDFAIT QLFYTTNTFH DVLYSLGFTE
EAGNFQVNNG NKGGKGNDFA ICNAQDGSGT NNANFATPPD GQPGRMRMYT WTTSKPKRDG
DLEAGIVIHE YTHGLSNRLC GGPANSNCLN DLEAGGMGEG WGDFYATAIR LKQGDTHDTD
YTMGEWAANQ KGGIREYPYS TNMQTNPYTY ADVKGMREVH GIGTVWATIL YDVLWNLIDD
HGMGKNVMPK MVDGVPTDGR TLAMKLVLDG MTLMPCNPNF MQARDAIIDA DMALTKGANK
CSLMKAFAKR GLGSNTKPGK GYTNNFDMPS GC
//
