ID   VPA_BOTAT               Reviewed;          15 AA.
AC   B3A0N1;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   03-AUG-2022, entry version 18.
DE   RecName: Full=Venom prothrombin activator;
DE            Short=vPA;
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] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, COFACTOR, ACTIVITY REGULATION, SUBUNIT, AND
RP   GLYCOSYLATION.
RC   TISSUE=Venom {ECO:0000269|Ref.1};
RA   Sun D., Ding Z., Li X., Cui L., Xue Y.;
RT   "Isolation and characterization of a prothrombin-activator from Bothrops
RT   atrox venom.";
RL   Submitted (AUG-2011) to UniProtKB.
CC   -!- FUNCTION: Snake prothrombin activator that attacks the hemostatic
CC       system of prey. This protein is functionally similar to blood
CC       coagulation factor Xa (By similarity). Potent calcium-independent
CC       prothrombin activator, possesses high hemorrhagic activity along with
CC       metalloproteinase activity. Has considerably stronger activity than
CC       FXa. {ECO:0000250|UniProtKB:P82807, ECO:0000269|Ref.1}.
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000269|Ref.1};
CC       Note=Binds divalent metal cations. {ECO:0000269|Ref.1};
CC   -!- ACTIVITY REGULATION: Inhibited by EDTA, but not by PMSF. Activity is
CC       not dependent on the presence of calcium ions, phospholipids or FXa
CC       inhibitor. {ECO:0000269|Ref.1}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|Ref.1}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC   -!- PTM: N-glycosylated. {ECO:0000269|Ref.1}.
CC   -!- MISCELLANEOUS: The molecular weight was determined to be 72 kDa with an
CC       isoelectric point of 6.67. {ECO:0000269|Ref.1}.
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DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016504; F:peptidase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR014760; Serum_albumin_N.
PE   1: Evidence at protein level;
KW   Blood coagulation cascade activating toxin; Direct protein sequencing;
KW   Glycoprotein; Hemostasis impairing toxin; Hydrolase; Metal-binding;
KW   Metalloprotease; Protease; Prothrombin activator; Toxin.
FT   CHAIN           1..>15
FT                   /note="Venom prothrombin activator"
FT                   /id="PRO_0000414616"
FT   NON_TER         15
FT                   /evidence="ECO:0000303|Ref.1"
SQ   SEQUENCE   15 AA;  1614 MW;  D4E0F9B5E9E2FAD8 CRC64;
     ALVLIAFAQV LQQCP