ID   VMP02_EULPE             Reviewed;         410 AA.
AC   B5AJT3;
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 2;
DE            Short=EpMP2;
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; EU853178; ACF60598.1; -; mRNA.
DR   AlphaFoldDB; B5AJT3; -.
DR   SMR; B5AJT3; -.
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   Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW   Secreted; Signal; Toxin; Zinc; Zymogen.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..410
FT                   /note="Venom metalloproteinase 2"
FT                   /id="PRO_0000423027"
FT   DOMAIN          214..410
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   ACT_SITE        366
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT                   ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         365
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         369
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         375
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        112
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        231
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        292
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        307
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        403
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   410 AA;  46611 MW;  912A2B8DFC54C95D CRC64;
     MDTFILTYSI LFLALFIESI HSRYSRVAEH IRTRKRPDKE LTEEEFKLVF HRSSTEEIDY
     DFVNLTTEIT EIERKVLFTI DDKDYHLKLT RASSSVIPSG TLIRSAILWT DNQTHFHDED
     STDEHWGSSH IYEDLDKMAT FLLRDDDDFT RYDGVFGGGK DMKVVGSLPA RLVNIYGANY
     HFIYYANGSV SDVILNGAKQ VVGSANTQAG LNNFYPKLLV LVDYTLFKIL NKSYEETIRY
     LAIFWNAVDM KFKKFETPKI NIIITGIIVP KNEGALKHVY DARIKSDMQK VNATKIITNS
     EHFFGANFST ESYFDNYDAT FTMASLNDLE GQTGLAYIGA ICKNNHNNAY VKDSGVFSGV
     LAAAHELGHL LASDHDEDVG CPGEINYNTR LTGTIMAEYR NNNVSKFIWS