ID   VMPA2_LOXIN             Reviewed;         256 AA.
AC   C9D7R2;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   03-NOV-2009, sequence version 1.
DT   03-AUG-2022, entry version 41.
DE   RecName: Full=Astacin-like metalloprotease toxin 2;
DE            EC=3.4.24.-;
DE   AltName: Full=Loxosceles astacin-like protease 2;
DE            Short=LALP2;
DE   Flags: Precursor;
OS   Loxosceles intermedia (Brown spider).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Araneomorphae; Haplogynae; Scytodoidea; Sicariidae; Loxosceles.
OX   NCBI_TaxID=58218;
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; GQ227490; ACV52010.1; -; mRNA.
DR   AlphaFoldDB; C9D7R2; -.
DR   SMR; C9D7R2; -.
DR   PRIDE; C9D7R2; -.
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.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW   Secreted; Signal; Toxin; Zinc.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   PROPEP          25..52
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5000522737"
FT   CHAIN           53..256
FT                   /note="Astacin-like metalloprotease toxin 2"
FT                   /id="PRO_5000522738"
FT   DOMAIN          53..250
FT                   /note="Peptidase M12A"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   ACT_SITE        145
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   BINDING         144
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   BINDING         148
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   BINDING         154
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   DISULFID        94..249
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   DISULFID        117..136
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
SQ   SEQUENCE   256 AA;  29204 MW;  400E9947EB1E2B0B CRC64;
     MIPDVGFLVL LTGALFICIK AAPATTDVDP TFEGRIVMEG DILIREEQLT ERNAIALENM
     RWPDATIVYK LTGWYALFPG DIKKAMRHIE ENTCIKFKAR SNEEGYVKIY KGEKESCFAD
     IGYFASEQRL SLGSGCKIFG RILHEMGHTI GLFHEHTRPD RDNYITVHED NIRPGSKRNY
     RKTPSYMTRV IGPFDYDSIM IYGETAGSRD PMHLKSMEAN KPGVTLISSR YKDRLTDLDI
     KKINTLYNCP GKEKFS