MEP_ASPNC
ID MEP_ASPNC Reviewed; 631 AA.
AC A2Q7V4;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Extracellular metalloproteinase mep;
DE EC=3.4.24.-;
DE AltName: Full=Elastinolytic metalloproteinase mep;
DE AltName: Full=Fungalysin mep;
DE Flags: Precursor;
GN Name=mep; ORFNames=An01g02070;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
CC -!- FUNCTION: Secreted metalloproteinase that allows assimilation of
CC proteinaceous substrates. {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; AM269955; CAK43577.1; -; Genomic_DNA.
DR RefSeq; XP_001388645.1; XM_001388608.1.
DR AlphaFoldDB; A2Q7V4; -.
DR SMR; A2Q7V4; -.
DR MEROPS; M36.001; -.
DR PaxDb; A2Q7V4; -.
DR GeneID; 4977749; -.
DR KEGG; ang:ANI_1_2332014; -.
DR VEuPathDB; FungiDB:An01g02070; -.
DR HOGENOM; CLU_012703_3_0_1; -.
DR Proteomes; UP000006706; Chromosome 2R.
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 3: Inferred from homology;
KW Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..241
FT /evidence="ECO:0000250"
FT /id="PRO_0000407178"
FT CHAIN 242..631
FT /note="Extracellular metalloproteinase mep"
FT /id="PRO_5000219322"
FT ACT_SITE 426
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 425
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
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 CARBOHYD 282
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 332
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 364
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 470
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 505
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 631 AA; 69153 MW; BF13EDD95535B863 CRC64;
MHGLRLVCSI GTLPLVILAY PAASLHTTSA AVDLDSLRLT SNSEYVNSVH VDTNRSVAVS
AEEHYTDTAA RLVQNIVPGA SFRLIDDHFV GDNGVAHVYF RQTLHGIDID NADFNVNIGK
DGLVLSFGHS FFTGALPSSH LDNTNVLSPE AALRGARDAI QLPLTIDNVS TEAAEGRNEY
IFREAVGAVS DPKAKLVYLV KPEGTLALTW RIETDMYEHW LLTYIDAETT TVHGVVDYVA
DATYQVYPWG TNDPAEGHRT IVTDPWDLSA SAYTWISDGR DNYTTTRGNN AIAHWNPTGG
GSYLYNLRPS DPNLNFQWPY SPNMSPPRSY INASIVQLFY TANAYHDLLY TLGFTESAGN
FQWNNSAHGG RDKDYVILNA QDGSGFSNAN FATPPDGIPG RMRMYIWIES TPSRDGSFDA
GIVIHEYTHG VSNRLTGGSH NAGCLSALES GGMGEGWGDF MATAIRIKPN DTRTTSYTMG
AWADNDKCGV RDYPYSTSFT ENPLNYTSVN TMNGVHAIGT VWATMLYEVL WNLIDKYGKN
DGSRPVFRNG VPTDGKYLMM KLVVDGMALQ PCNPNFVQAR DAILDADIVL TGGKNRCEIW
RGFAKRGLGQ GAAHSSLNWM RRGSTLLPTG C
