MEP3_ARTGP
ID MEP3_ARTGP Reviewed; 633 AA.
AC E4V5B2; Q75UE7;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Extracellular metalloproteinase 3;
DE EC=3.4.24.-;
DE AltName: Full=Elastinolytic metalloproteinase MEP3;
DE AltName: Full=Fungalysin MEP3;
DE Flags: Precursor;
GN Name=MEP3; ORFNames=MGYG_08200;
OS Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum
OS gypseum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Nannizzia.
OX NCBI_TaxID=535722;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=VUT-4004;
RA Kano R., Hasegawa A.;
RT "Arthroderma gypseum metalloprotease MEP gene, complete.";
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4604 / CBS 118893;
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
CC -!- FUNCTION: Secreted metalloproteinase that allows assimilation of
CC proteinaceous substrates and probably acts as a virulence factor.
CC {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; AB126166; BAD01605.1; -; mRNA.
DR EMBL; DS989829; EFR05186.1; -; Genomic_DNA.
DR RefSeq; XP_003170021.1; XM_003169973.1.
DR AlphaFoldDB; E4V5B2; -.
DR SMR; E4V5B2; -.
DR MEROPS; M36.001; -.
DR PRIDE; E4V5B2; -.
DR EnsemblFungi; EFR05186; EFR05186; MGYG_08200.
DR GeneID; 10025256; -.
DR eggNOG; ENOG502QTDC; Eukaryota.
DR HOGENOM; CLU_012703_3_0_1; -.
DR InParanoid; E4V5B2; -.
DR OMA; WALIEAH; -.
DR OrthoDB; 1136823at2759; -.
DR Proteomes; UP000002669; Unassembled WGS sequence.
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; IPR011096; FTP_domain.
DR InterPro; IPR001842; Peptidase_M36.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR Pfam; PF07504; FTP; 1.
DR Pfam; PF02128; Peptidase_M36; 1.
DR PRINTS; PR00999; FUNGALYSIN.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..246
FT /evidence="ECO:0000250"
FT /id="PRO_0000407164"
FT CHAIN 247..633
FT /note="Extracellular metalloproteinase 3"
FT /id="PRO_0000407165"
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 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 410
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 480
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 622
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 110
FT /note="L -> P (in Ref. 1; BAD01605)"
FT /evidence="ECO:0000305"
FT CONFLICT 402
FT /note="Q -> S (in Ref. 1; BAD01605)"
FT /evidence="ECO:0000305"
FT CONFLICT 447
FT /note="A -> G (in Ref. 1; BAD01605)"
FT /evidence="ECO:0000305"
FT CONFLICT 476
FT /note="T -> A (in Ref. 1; BAD01605)"
FT /evidence="ECO:0000305"
FT CONFLICT 502
FT /note="S -> N (in Ref. 1; BAD01605)"
FT /evidence="ECO:0000305"
FT CONFLICT 522
FT /note="I -> Y (in Ref. 1; BAD01605)"
FT /evidence="ECO:0000305"
FT CONFLICT 528
FT /note="S -> T (in Ref. 1; BAD01605)"
FT /evidence="ECO:0000305"
FT CONFLICT 532
FT /note="E -> D (in Ref. 1; BAD01605)"
FT /evidence="ECO:0000305"
FT CONFLICT 628
FT /note="Q -> K (in Ref. 1; BAD01605)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 633 AA; 69329 MW; CC3CEBC18779817F CRC64;
MHGLLLAGLL ALPMNVLAHP AEHHASNVLS RRGVDIDSFR LPLKAKYMDN EAAAEKIQAL
SFTKDDDYVS TATKLVKSTF PKSTFRVVDD HYIGTNGIGH VHFKQTAHGL DIDNSDFNVN
IDRDGKVFSF GNSFFTGEIP KENPMVKRAF SDPVKALKGA VKALSLPVKS DNAKAKNVAG
KETVEFMGTS GALSAPKAKL VYLQKDDGTL ALTWRVETDV GENWLLSYVD ANNSETVHNV
VDYVASAEYK VFAWGLNDPT EGNPTSIRDP WTDASPYTWN SDGNTKYPTT RGNNAIAQDN
PTGGSQYLNN YRPQSPNLIF SYPWSATATP PSSYKDFSIT QLFYTTNRFH DLLYSFGFNE
AAGNFQVNNG NKGGRGNDFA IVNAQDGSGT NNANFATPPD GQPGRMRMYN WTTARPNRDG
CLEAGIVIHE YAHGLSNRLC GGPANSACLN ALESGGMGEG WGDFYATAIR LKPRDTKNTN
YSMGAWAANN PKGIRAYLYS TSLQTNPYMY TSVNSLREVH QIGTVWASML YELMWALIEA
HGNTYSANPV FRNGVPQDGR HLAMKLVMDG MALQPCNPNF VQARDAIIDA DRALTNSANK
CTIWKAFAKR GLGYGAKYDS RNRTGSNQLP PGC
