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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
 
 
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