ID   VM1B_BOTLC              Reviewed;           9 AA.
AC   P0DJJ6;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2012, sequence version 1.
DT   03-AUG-2022, entry version 20.
DE   RecName: Full=Snake venom metalloproteinase BleucMP;
DE            Short=SVMP;
DE            EC=3.4.24.-;
DE   Flags: Fragment;
OS   Bothrops leucurus (Whitetail lancehead).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX   NCBI_TaxID=157295;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBUNIT, ACTIVITY REGULATION, MASS
RP   SPECTROMETRY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=21130897; DOI=10.1016/j.cbpc.2010.11.008;
RA   Gomes M.S., de Queiroz M.R., Mamede C.C., Mendes M.M., Hamaguchi A.,
RA   Homsi-Brandeburgo M.I., Sousa M.V., Aquino E.N., Castro M.S.,
RA   de Oliveira F., Rodrigues V.M.;
RT   "Purification and functional characterization of a new metalloproteinase
RT   (BleucMP) from Bothrops leucurus snake venom.";
RL   Comp. Biochem. Physiol. 153:290-300(2011).
CC   -!- FUNCTION: Snake venom zinc metalloprotease that has fibrino(geno)lytic
CC       activities. Hydrolyzes the alpha-chain (FGA) and more slowly the beta-
CC       chain of fibrinogen (FGB), without affecting the gamma-chain.
CC       Preferentially hydrolyzes the beta-chain (FGB) of fibrin. In vivo,
CC       shows a low edema-inducing effect. This action may be attributed to
CC       degradation of proteins in the cell membrane and consequent release of
CC       inflammatory mediators and leukocyte infiltrate.
CC       {ECO:0000269|PubMed:21130897}.
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: Inhibited by EDTA and 1,10-phenanthroline. Not
CC       inhibited by beta-mercaptoethanol, benzamidine and aprotinin.
CC       {ECO:0000269|PubMed:21130897}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:21130897}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- PTM: Contains 7 disulfide bonds.
CC   -!- MASS SPECTROMETRY: Mass=23057.54; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:21130897};
CC   -!- MISCELLANEOUS: Is devoid of coagulant activities on bovine plasma. In
CC       vivo, does not induce hemorrhage on mice back skin when 50 ug of enzyme
CC       are intradermally injected (PubMed:21130897).
CC       {ECO:0000305|PubMed:21130897}.
CC   -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-I
CC       subfamily. {ECO:0000305}.
CC   -!- CAUTION: If fragments identified by mass spectrometry (and not included
CC       in this entry) are taken into account for comparison, this protein is
CC       71% identical to the metalloproteinase from the same venom
CC       leucurolysin-A (AC P84907). {ECO:0000305|PubMed:21130897}.
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DR   GO; GO:0005576; C:extracellular region; TAS:UniProtKB.
DR   GO; GO:0043655; C:host extracellular space; TAS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IDA:UniProtKB.
DR   GO; GO:0008237; F:metallopeptidase activity; IDA:UniProtKB.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0044485; P:envenomation resulting in fibrinogenolysis in another organism; IDA:UniProtKB.
DR   GO; GO:0044484; P:envenomation resulting in fibrinolysis in another organism; IDA:UniProtKB.
DR   GO; GO:0044398; P:envenomation resulting in induction of edema in another organism; IDA:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Fibrinogenolytic toxin;
KW   Fibrinolytic toxin; Hemostasis impairing toxin; Hydrolase; Metal-binding;
KW   Metalloprotease; Protease; Secreted; Toxin; Zinc.
FT   CHAIN           <1..>9
FT                   /note="Snake venom metalloproteinase BleucMP"
FT                   /id="PRO_0000418552"
FT   NON_TER         1
FT   NON_TER         9
SQ   SEQUENCE   9 AA;  1096 MW;  58177B1879D5A1A7 CRC64;
     TLTSFGEWR