VM1B1_BOTAT
ID VM1B1_BOTAT Reviewed; 24 AA.
AC P0DJE1;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 1.
DT 03-AUG-2022, entry version 27.
DE RecName: Full=Snake venom metalloproteinase Batx-1;
DE Short=SVMP;
DE EC=3.4.24.-;
DE AltName: Full=Batx-I;
DE Flags: Fragment;
OS Bothrops atrox (Barba amarilla) (Fer-de-lance).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX NCBI_TaxID=8725;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, ACTIVITY REGULATION, TOXIC DOSE, AND MASS
RP SPECTROMETRY.
RC STRAIN=Colombia; TISSUE=Venom;
RX PubMed=20600221; DOI=10.1016/j.toxicon.2010.06.016;
RA Patino A.C., Pereanez J.A., Nunez V., Benjumea D.M., Fernandez M.,
RA Rucavado A., Sanz L., Calvete J.J.;
RT "Isolation and biological characterization of Batx-I, a weak hemorrhagic
RT and fibrinogenolytic PI metalloproteinase from Colombian Bothrops atrox
RT venom.";
RL Toxicon 56:936-943(2010).
CC -!- FUNCTION: Zinc metalloproteinase that exhits a weak hemorrhagic
CC activity. Degrades preferentially the Aalpha- (FGA) and Bbeta-chains
CC (FGB) of fibrinogen, and partially degrades gamma-chain (FGG) at higher
CC concentration. Induces a mild myotoxicity, but lacks coagulant activity
CC on human plasma or bovin fibrinogen and defibrinating activity.
CC {ECO:0000269|PubMed:20600221}.
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 o-phenanthroline, but not
CC inhibited by PMSF, pepstatin A, and aprotinin.
CC {ECO:0000269|PubMed:20600221}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- PTM: The N-terminus is blocked.
CC -!- PTM: Contains 3 disulfide bonds. {ECO:0000250}.
CC -!- MASS SPECTROMETRY: Mass=23296.2; Method=Electrospray; Note=Average
CC mass.; Evidence={ECO:0000269|PubMed:20600221};
CC -!- TOXIC DOSE: The minimal hemorrhagic dose is 0.85 mg/kg by intradermal
CC injection into mice. {ECO:0000269|PubMed:20600221}.
CC -!- MISCELLANEOUS: Accounts for about 45% of venom proteins.
CC {ECO:0000305|PubMed:20600221}.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-I
CC subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P0DJE1; -.
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 Calcium; Direct protein sequencing; Disulfide bond; Fibrinogenolytic toxin;
KW Hemorrhagic toxin; Hemostasis impairing toxin; Hydrolase; Metal-binding;
KW Metalloprotease; Myotoxin; Protease; Secreted; Toxin; Zinc.
FT CHAIN <1..>24
FT /note="Snake venom metalloproteinase Batx-1"
FT /id="PRO_0000415927"
FT DOMAIN <1..>24
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 3
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT NON_TER 1
FT NON_TER 24
SQ SEQUENCE 24 AA; 2752 MW; C64409119B34C680 CRC64;
YIELAVVADH GIFTKYNSNL NTIR
