ID   VMP03_EULPE             Reviewed;         407 AA.
AC   B5AJT4;
DT   24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 42.
DE   RecName: Full=Venom metalloproteinase 3;
DE            Short=EpMP3;
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], FUNCTION, BIOASSAY, ACTIVITY REGULATION, AND
RP   TISSUE SPECIFICITY.
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. {ECO:0000269|PubMed:19320760}.
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:0000269|PubMed:19320760}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:19320760}.
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 (PubMed:19320760). {ECO:0000269|PubMed:19320760}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the venom
CC       metalloproteinase (M12B) family. {ECO:0000305}.
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DR   EMBL; EU853179; ACF60599.1; -; mRNA.
DR   AlphaFoldDB; B5AJT4; -.
DR   SMR; B5AJT4; -.
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; Toxin; Zinc.
FT   CHAIN           1..407
FT                   /note="Venom metalloproteinase 3"
FT                   /id="PRO_0000423028"
FT   DOMAIN          191..405
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   ACT_SITE        341
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT                   ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         340
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         344
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         350
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        42
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        91
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        126
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        166
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        391
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        317..400
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   DISULFID        356..384
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
SQ   SEQUENCE   407 AA;  46007 MW;  F7A1ECCCB13D6BC8 CRC64;
     QYSESQESGH NRNAPDKELT TEEFQLIFHQ SQTVDIEYDF INITTEMIET ERKVSFTIDG
     KEYHLSLTPA ASQSVLPYGT KIKSAIWWTD NDTHIHEEDY SDERWDSRAI YENLEIMATI
     LVRTENGTSY YDGVFGEGIA MKVVRSLPGR LMNIYGANYH FVYDSNGSVY DVVLNGQDEP
     AVPADMAVNN FYPKLLVLVD YSLFKIFNEN FEETVKYLTI FWNAVNLRFR PVQHPKVNII
     ITGIVIAKNE AAFQHVYRAR YSKNSKLVHT GRVIDNGRYF FGTNFDPYYD NYDASFTMAS
     MDDPTGKGGA TVIGGICSSS NNIAYIRDVG SYSGVKVATH ELGHLLNGQH DSDTTCSEKI
     NDNIYTIMAK QGSTKASKFV WSSCTLTAFA NFSKTTSAAC LKDTYRK