ID   VMXP_PROSR              Reviewed;          28 AA.
AC   P85006;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 39.
DE   RecName: Full=50 kDa venom protease;
DE            EC=3.4.24.-;
DE   AltName: Full=Snake venom metalloproteinase;
DE            Short=SVMP;
DE   Flags: Fragments;
OS   Proatheris superciliaris (Lowland swamp viper).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Viperinae; Proatheris.
OX   NCBI_TaxID=110218;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Venom {ECO:0000269|PubMed:16112700};
RX   PubMed=16112700; DOI=10.1016/j.toxicon.2005.06.011;
RA   Laing G.D., Compton S.J., Ramachandran R., Fuller G.L.J., Wilkinson M.C.,
RA   Wagstaff S.C., Watson S.P., Kamiguti A.S., Theakston R.D.G., Senis Y.A.;
RT   "Characterization of a novel protein from Proatheris superciliaris venom:
RT   proatherocytin, a 34-kDa platelet receptor PAR1 agonist.";
RL   Toxicon 46:490-499(2005).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P30431};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P30431};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16112700}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:16112700}.
CC   -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; P85006; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Metal-binding; Metalloprotease;
KW   Protease; Secreted; Toxin; Zinc.
FT   CHAIN           <1..>28
FT                   /note="50 kDa venom protease"
FT                   /id="PRO_0000253947"
FT   NON_CONS        11..12
FT                   /evidence="ECO:0000303|PubMed:16112700"
FT   NON_CONS        20..21
FT                   /evidence="ECO:0000303|PubMed:16112700"
FT   NON_TER         1
FT                   /evidence="ECO:0000303|PubMed:16112700"
FT   NON_TER         28
FT                   /evidence="ECO:0000303|PubMed:16112700"
SQ   SEQUENCE   28 AA;  2970 MW;  1B94F5DA88F84F2E CRC64;
     ASDVTLNSFA EDVTVGECCD CVDLTTVY