ID   VMP01_EULPE             Reviewed;         431 AA.
AC   B5AJT2;
DT   24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 43.
DE   RecName: Full=Venom metalloproteinase 1;
DE            Short=EpMP1;
DE   Flags: Precursor;
OS   Eulophus pennicornis (Parasitoid wasp).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Parasitoida; Chalcidoidea;
OC   Eulophidae; Eulophinae; Eulophus.
OX   NCBI_TaxID=108749;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=19320760; DOI=10.1111/j.1365-2583.2009.00864.x;
RA   Price D.R., Bell H.A., Hinchliffe G., Fitches E., Weaver R.,
RA   Gatehouse J.A.;
RT   "A venom metalloproteinase from the parasitic wasp Eulophus pennicornis is
RT   toxic towards its host, tomato moth (Lacanobia oleracae).";
RL   Insect Mol. Biol. 18:195-202(2009).
CC   -!- FUNCTION: The recombinant protein has gelatinase activity. In vivo,
CC       injection of this recombinant into fifth instar L.oleracea (host)
CC       larvae results in partial insect mortality associated with the molt to
CC       sixth instar, with surviving insects showing retarded development and
CC       growth (By similarity). {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   -!- ACTIVITY REGULATION: The gelatinase activity is inhibited by EDTA.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- DOMAIN: The N-terminal section (alone) shows no toxic effect when
CC       injected into the host. This section may function in stabilizing the
CC       catalytic part of the protein, or in directing it to specific target
CC       sites of action (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the venom
CC       metalloproteinase (M12B) family. {ECO:0000305}.
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DR   EMBL; EU853177; ACF60597.1; -; mRNA.
DR   AlphaFoldDB; B5AJT2; -.
DR   SMR; B5AJT2; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.390.10; -; 1.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001590; Peptidase_M12B.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Hydrolase; Metal-binding; Metalloprotease;
KW   Protease; Secreted; Signal; Toxin; Zinc; Zymogen.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..431
FT                   /note="Venom metalloproteinase 1"
FT                   /id="PRO_0000423026"
FT   DOMAIN          228..428
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   ACT_SITE        364
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT                   ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         363
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         367
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         373
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        64
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        113
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        148
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        187
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        414
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        340..423
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   DISULFID        379..407
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
SQ   SEQUENCE   431 AA;  48850 MW;  7B20C38A3DD1D9BC CRC64;
     MDLFILTRFI LFLSFFMKSI HCQYSESQES GHNRNAPDKE LTTEEFQLIF HQSQTVDIEY
     DFINITTEMI ETERKVSFTI DGKEYHLSLT PAASQSVLPY GTKIKSAIWW TDNDTHIHEE
     DYSDERWDSR AIYENLEIMA TILVRTENGT SYYDGVFVKY SNEGVRSLPG RLMNIYGANY
     HFVYDSNGSV YDVVLNGQDE PAVPADMASK IIFYSETPCT CRLLIIQDLL MKTSRRLSSI
     STIFWNAVNL RFRPVQHPKV NIIITGIVIA KNEAAFQHVY RARYSKNSKL VHTGRVIDNG
     RYFFGTNFDP YYDNYDASFT MASMDDPTGK GGATVIGGIC SSSNNIAYIR DVGSYSGVKV
     ATHELGHLLN GQHDSDTTCS EKINDNIYTI MAKQGSTKAS KFVWSSCTLT AFANFSKTTS
     AACLKDTYRK Q