VSP2_DEIAC
ID VSP2_DEIAC Reviewed; 15 AA.
AC P0DJG7;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 1.
DT 03-AUG-2022, entry version 19.
DE RecName: Full=Thrombin-like enzyme acutobin-2;
DE Short=SVTLE;
DE EC=3.4.21.-;
DE AltName: Full=Acutobin II;
DE AltName: Full=Fibrinogen-clotting enzyme;
DE AltName: Full=Snake venom serine protease;
DE Short=SVSP;
DE Flags: Fragment;
OS Deinagkistrodon acutus (Hundred-pace snake) (Agkistrodon acutus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Deinagkistrodon.
OX NCBI_TaxID=36307;
RN [1]
RP PROTEIN SEQUENCE, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=18643779; DOI=10.1042/ba20080073;
RA Xin Y., Dong D., Chen D., Li R.;
RT "Structural and biological characterization of a novel acutobin-like enzyme
RT isolated from the venom of the sharp-nosed pit viper (Deinagkistrodon
RT acutus).";
RL Biotechnol. Appl. Biochem. 53:123-131(2009).
RN [2]
RP FUNCTION.
RX PubMed=17904430; DOI=10.1016/j.jchromb.2007.09.010;
RA Xin Y., Dong D., Wang T., Li R.;
RT "Affinity purification of serine proteinase from Deinagkistrodon acutus
RT venom.";
RL J. Chromatogr. B 859:111-118(2007).
CC -!- FUNCTION: Thrombin-like snake venom serine protease that has high
CC fibrinogen-clotting activity (2025 NIH units/mg) on human fibrinogen.
CC Shows esterase and amidase activities. {ECO:0000269|PubMed:17904430}.
CC -!- ACTIVITY REGULATION: Inhibited by PMSF (100%), AEBSF (100%), aprotinin
CC (50%), benzamidine (50%), guanidinium chloride (48%) and urea (66%).
CC {ECO:0000269|PubMed:18643779}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=403 uM for BAEE (at pH 7.0 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:18643779};
CC KM=68.5 nM for DL-BAPA (at pH 7.5 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:18643779};
CC Vmax=1560 nmol/sec/mg enzyme (at pH 7.0 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:18643779};
CC Vmax=490 nmol/min/mg enzyme with DL-BAPA as substrate (at pH 7.5 and
CC 37 degrees Celsius) {ECO:0000269|PubMed:18643779};
CC pH dependence:
CC Optimum pH is 9.0 (at 25 degrees Celsius).
CC {ECO:0000269|PubMed:18643779};
CC Temperature dependence:
CC Optimum temperature is 25-50 degrees Celsius (at pH 7.0).
CC {ECO:0000269|PubMed:18643779};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- PTM: Seems to be only O-glycosylated (is not affected by PNGase F which
CC only removes N-linked glycans, but is affected by TFMS that removes
CC both O- and N-linked glycans).
CC -!- MASS SPECTROMETRY: Mass=34069.5; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:18643779};
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 Disulfide bond; Glycoprotein; Hemostasis impairing toxin; Hydrolase;
KW Protease; Secreted; Serine protease; Toxin.
FT CHAIN 1..>15
FT /note="Thrombin-like enzyme acutobin-2"
FT /id="PRO_0000417008"
FT DOMAIN 1..>15
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 7..?
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT NON_TER 15
SQ SEQUENCE 15 AA; 1701 MW; 81F387D827D52FD4 CRC64;
VIGGVECDIN EHRFL
