ID   VMPA4_LOXLA             Reviewed;         114 AA.
AC   P0DM61;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   16-OCT-2013, sequence version 1.
DT   03-AUG-2022, entry version 19.
DE   RecName: Full=Astacin-like metalloprotease toxin 4;
DE            EC=3.4.24.-;
DE   AltName: Full=Loxosceles astacin-like protease 4;
DE            Short=LALP4;
DE   Flags: Fragment;
OS   Loxosceles laeta (South American recluse spider) (Scytodes laeta).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Araneomorphae; Haplogynae; Scytodoidea; Sicariidae; Loxosceles.
OX   NCBI_TaxID=58217;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=19879318; DOI=10.1016/j.biochi.2009.10.003;
RA   Trevisan-Silva D., Gremski L.H., Chaim O.M., da Silveira R.B.,
RA   Meissner G.O., Mangili O.C., Barbaro K.C., Gremski W., Veiga S.S.,
RA   Senff-Ribeiro A.;
RT   "Astacin-like metalloproteases are a gene family of toxins present in the
RT   venom of different species of the brown spider (genus Loxosceles).";
RL   Biochimie 92:21-32(2010).
CC   -!- FUNCTION: Zinc metalloprotease. Provoques deadhesion of endothelial
CC       cells from cell cultures, and also degradation of fibronectin,
CC       fibrinogen and gelatin in vitro. Its role in the venom is not fully
CC       understood but it might act as a spreading factor that facilitates
CC       diffusion of other venom toxins. Alternatively, it might be involved in
CC       the proteolytic processing of other venom toxins or it might play a
CC       role in extra-oral digestion of prey (By similarity). {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU01211};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|PROSITE-
CC       ProRule:PRU01211};
CC   -!- ACTIVITY REGULATION: Inhibited by 1,10-phenanthroline. {ECO:0000250}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
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DR   EMBL; GR277667; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; P0DM61; -.
DR   SMR; P0DM61; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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; IPR001506; Peptidase_M12A.
DR   InterPro; IPR006026; Peptidase_Metallo.
DR   Pfam; PF01400; Astacin; 1.
DR   PRINTS; PR00480; ASTACIN.
DR   SMART; SM00235; ZnMc; 1.
DR   PROSITE; PS51864; ASTACIN; 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..>114
FT                   /note="Astacin-like metalloprotease toxin 4"
FT                   /id="PRO_0000423640"
FT   DOMAIN          <1..>114
FT                   /note="Peptidase M12A"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   ACT_SITE        47
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   BINDING         46
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   BINDING         50
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   BINDING         56
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   CARBOHYD        88
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        17..38
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   NON_TER         1
FT   NON_TER         114
SQ   SEQUENCE   114 AA;  13048 MW;  079CF04957859558 CRC64;
     RETNENDYVD IHKGDKCYSR VGKSFNGGPQ PLSLGKGCTD FGTILHELGH SVGFNHEHSR
     SDRDEYLIVH KENVLSGYER DFEKLWENKT RTIGDFDYDS IMLYGLLCLF KGSV