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VSP48_BOTJR
ID   VSP48_BOTJR             Reviewed;          22 AA.
AC   P0DJF0;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 1.
DT   03-AUG-2022, entry version 20.
DE   RecName: Full=Thrombin-like enzyme BJ-48;
DE            Short=SVTLE BJ-48;
DE            EC=3.4.21.-;
DE   AltName: Full=Fibrinogen-clotting enzyme;
DE   AltName: Full=Snake venom serine protease;
DE            Short=SVSP;
DE   Flags: Fragment;
OS   Bothrops jararacussu (Jararacussu).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX   NCBI_TaxID=8726;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP   BIOPHYSICOCHEMICAL PROPERTIES, GLYCOSYLATION, SIALIC ACID CONTENT, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=17433397; DOI=10.1016/j.toxicon.2007.02.018;
RA   Silva-Junior F.P., Guedes H.L., Garvey L.C., Aguiar A.S., Bourguignon S.C.,
RA   Di Cera E., Giovanni-De-Simone S.;
RT   "BJ-48, a novel thrombin-like enzyme from the Bothrops jararacussu venom
RT   with high selectivity for Arg over Lys in P1: Role of N-glycosylation in
RT   thermostability and active site accessibility.";
RL   Toxicon 50:18-31(2007).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-15.
RC   TISSUE=Venom;
RX   PubMed=15994137; DOI=10.1016/j.jchromb.2005.04.018;
RA   De-Simone S.G., Correa-Netto C., Antunes O.A., De-Alencastro R.B.,
RA   Silva F.P. Jr.;
RT   "Biochemical and molecular modeling analysis of the ability of two p-
RT   aminobenzamidine-based sorbents to selectively purify serine proteases
RT   (fibrinogenases) from snake venoms.";
RL   J. Chromatogr. B 822:1-9(2005).
RN   [3]
RP   CIRCULAR DICHROISM, AND SUBUNIT.
RC   TISSUE=Venom;
RX   PubMed=18069115; DOI=10.1016/j.bpc.2007.11.002;
RA   Guedes H.L., Silva F.P. Jr., Netto C.C., de Salles C.M., Alexandre G.,
RA   Oliveira C.L., Torriani I., De Simone S.G.;
RT   "Structural characterization and low-resolution model of BJ-48, a thrombin-
RT   like enzyme from Bothrops jararacussu venom.";
RL   Biophys. Chem. 132:159-164(2008).
CC   -!- FUNCTION: Thrombin-like serine protease which cleaves specifically the
CC       Aalpha chain of human fibrinogen (FGA) to release fibrinopeptide A.
CC       Also cleaves rapidly the Bbeta chain of human fibrinogen (FGB). Is
CC       selective for Arg over Lys at position 1 of the tripeptide substrates.
CC       {ECO:0000269|PubMed:17433397}.
CC   -!- ACTIVITY REGULATION: Inhibited by aprotinin and dithiothreitol.
CC       {ECO:0000269|PubMed:17433397}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.83 mM for BApNA {ECO:0000269|PubMed:17433397};
CC         KM=0.4 mM for BAME {ECO:0000269|PubMed:17433397};
CC         KM=0.6 mM for TAME {ECO:0000269|PubMed:17433397};
CC         KM=0.3 mM for Nalpha-Tos-Gly-Pro-ME {ECO:0000269|PubMed:17433397};
CC         KM=0.36 mM for Nalpha-Tos-Gly-Pro-Arg-pNA
CC         {ECO:0000269|PubMed:17433397};
CC       pH dependence:
CC         Optimum pH is 7.5. {ECO:0000269|PubMed:17433397};
CC       Temperature dependence:
CC         Optimum temperature is 50 degrees Celsius.
CC         {ECO:0000269|PubMed:17433397};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:18069115}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- PTM: Glycosylated; required for activity. Highly glycosylated with 42%
CC       of N-linked carbohydrates composed of
CC       Fuc(1):GalN(4):GlcN(5):Gal(1):Man(2) and a high content of sialic acid
CC       residues (8-12%). {ECO:0000269|PubMed:17433397}.
CC   -!- MASS SPECTROMETRY: Mass=48036; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:17433397};
CC   -!- MISCELLANEOUS: Is inactive toward protein C, protease-activated
CC       receptor-1 or inhibitors such as hirudin and antithrombin.
CC       {ECO:0000305|PubMed:17433397}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR   AlphaFoldDB; P0DJF0; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008236; F:serine-type peptidase 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   Blood coagulation cascade activating toxin; Direct protein sequencing;
KW   Disulfide bond; Glycoprotein; Hemostasis impairing toxin; Hydrolase;
KW   Protease; Secreted; Serine protease; Sialic acid; Toxin.
FT   CHAIN           1..>22
FT                   /note="Thrombin-like enzyme BJ-48"
FT                   /id="PRO_0000416020"
FT   DOMAIN          1..>22
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        6..?
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        22..?
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   UNSURE          6
FT                   /note="Assigned by comparison with orthologs"
FT   UNSURE          22
FT                   /note="Assigned by comparison with orthologs"
FT   NON_TER         22
SQ   SEQUENCE   22 AA;  2468 MW;  98D2A3AFB4EED743 CRC64;
     VVGGDCIPQV PFLAFLYSEY FC
 
 
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