VSP2_GLOUS
ID VSP2_GLOUS Reviewed; 19 AA.
AC P0C590;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Thrombin-like enzyme calobin-2;
DE Short=SVTLE;
DE EC=3.4.21.-;
DE AltName: Full=Calobin II;
DE AltName: Full=Fibrinogen-clotting enzyme;
DE AltName: Full=Snake venom serine protease;
DE Short=SVSP;
DE Flags: Fragment;
OS Gloydius ussuriensis (Ussuri mamushi) (Gloydius blomhoffii ussuriensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Gloydius.
OX NCBI_TaxID=35671;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBUNIT, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=11024490; DOI=10.1016/s0041-0101(00)00152-5;
RA Cho S.Y., Hahn B.-S., Yang K.Y., Kim Y.S.;
RT "Purification and characterization of calobin II, a second type of
RT thrombin-like enzyme from Agkistrodon caliginosus (Korean viper).";
RL Toxicon 39:499-506(2001).
CC -!- FUNCTION: Thrombin-like snake venom serine protease that cleaves alpha-
CC chain of fibrinogen (FGA) releasing fibrinopeptide A. Has high clotting
CC activity. {ECO:0000269|PubMed:11024490}.
CC -!- ACTIVITY REGULATION: Its proteolytic activity is inhibited by PMSF and
CC TPCK. {ECO:0000269|PubMed:11024490}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8. {ECO:0000269|PubMed:11024490};
CC Temperature dependence:
CC Optimum temperature is between 20 and 40 degrees Celsius.
CC {ECO:0000269|PubMed:11024490};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11024490}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11024490}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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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 Glycoprotein; Hemostasis impairing toxin; Hydrolase; Protease; Secreted;
KW Serine protease; Toxin.
FT CHAIN 1..>19
FT /note="Thrombin-like enzyme calobin-2"
FT /id="PRO_0000295819"
FT DOMAIN 1..>19
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT NON_TER 19
SQ SEQUENCE 19 AA; 2161 MW; 49F2A2F343F39102 CRC64;
VIGGDECNIN EHRFLVAXY