ID   VMPA5_LOXGA             Reviewed;         186 AA.
AC   P0DM62;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   16-OCT-2013, sequence version 1.
DT   03-AUG-2022, entry version 20.
DE   RecName: Full=Astacin-like metalloprotease toxin 5;
DE            EC=3.4.24.-;
DE   AltName: Full=Loxosceles astacin-like protease 5;
DE            Short=LALP5;
DE   Flags: Fragment;
OS   Loxosceles gaucho (Spider).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Araneomorphae; Haplogynae; Scytodoidea; Sicariidae; Loxosceles.
OX   NCBI_TaxID=58216;
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; GR277668; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; P0DM62; -.
DR   SMR; P0DM62; -.
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   CDD; cd04280; ZnMc_astacin_like; 1.
DR   Gene3D; 3.40.390.10; -; 1.
DR   InterPro; IPR034035; Astacin-like_dom.
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..>186
FT                   /note="Astacin-like metalloprotease toxin 5"
FT                   /id="PRO_0000423641"
FT   DOMAIN          1..>186
FT                   /note="Peptidase M12A"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   ACT_SITE        93
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   BINDING         92
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   BINDING         96
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   BINDING         102
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   CARBOHYD        122
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        42..177
FT                   /evidence="ECO:0000250|UniProtKB:P07584"
FT   DISULFID        63..84
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   NON_TER         1
FT   NON_TER         186
SQ   SEQUENCE   186 AA;  21643 MW;  837D8425672F60A3 CRC64;
     NAVKYDQQLW PNGEIIYEIS PGLRQYEQLI LEAMRSYEDT TCIKFRRRFD EDDYVNIHVG
     DKCYSRVGKS FKGGPQPLSL GNGCTDFGTI LHELGHSVGF DHEHSRTDRD EYLIIHERNI
     KNGSEHNFEK LLESKTRTIG PFDYDSIMLY GSYAFSRDTE AVENHGTRRT RTPYEICHSK
     RKAELL