VSP_BOTBA
ID VSP_BOTBA Reviewed; 249 AA.
AC K4LLQ2;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 1.
DT 03-AUG-2022, entry version 26.
DE RecName: Full=Thrombin-like enzyme barnettobin;
DE Short=Bb-TLE;
DE Short=SVTLE;
DE EC=3.4.21.-;
DE AltName: Full=Snake venom serine protease;
DE Short=SVSP;
DE Flags: Precursor; Fragment;
OS Bothrops barnetti (Barnett's lancehead) (Trimeresurus barnetti).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX NCBI_TaxID=1051630;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 17-36, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION,
RP GLYCOSYLATION, AND MASS SPECTROMETRY.
RC TISSUE=Venom, and Venom gland;
RX PubMed=23578498; DOI=10.1016/j.biochi.2013.03.015;
RA Vivas-Ruiz D.E., Sandoval G.A., Mendoza J., Inga R.R., Gontijo S.,
RA Richardson M., Eble J.A., Yarleque A., Sanchez E.F.;
RT "Coagulant thrombin-like enzyme (barnettobin) from Bothrops barnetti venom:
RT molecular sequence analysis of its cDNA and biochemical properties.";
RL Biochimie 95:1476-1486(2013).
CC -!- FUNCTION: Thrombin-like snake venom serine protease that releases only
CC fibrinopeptide A from human Aalpha chain of fibrinogen (specific
CC coagulant activity was 251.7 NIH thrombin units/mg). Also shows
CC fibrino(geno)lytic activities in vitro and defibrinogenating effects in
CC vivo. {ECO:0000269|PubMed:23578498}.
CC -!- ACTIVITY REGULATION: Both coagulant and amidolytic activities are
CC inhibited by PMSF. Amidolytic activity is partially inhibited by DTT,
CC chymostatin, SBTI and TLCK, but not by heparin and EDTA.
CC {ECO:0000269|PubMed:23578498}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.0-8.0. {ECO:0000269|PubMed:23578498};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius.
CC {ECO:0000269|PubMed:23578498};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:23578498}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23578498}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC -!- PTM: Glycoprotein, contains approx. 52% carbohydrate which could be
CC removed by N-glycosidase. Glycosylation is important, since
CC deglycosylated barnettobin loses its clotting and defibrinogenating
CC effects. {ECO:0000269|PubMed:23578498}.
CC -!- MASS SPECTROMETRY: Mass=39077.948; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:23578498};
CC -!- MISCELLANEOUS: Does not degrade beta- and gamma-chains of fibrinogen
CC (FGB). Does not hydrolyze the plasmin substrate S2251 (D-Val-Leu-Lys-
CC pNA). {ECO:0000269|PubMed:23578498}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC {ECO:0000305}.
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DR EMBL; JX499027; AFV08640.1; -; mRNA.
DR AlphaFoldDB; K4LLQ2; -.
DR SMR; K4LLQ2; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
PE 1: Evidence at protein level;
KW Blood coagulation cascade activating toxin; Direct protein sequencing;
KW Disulfide bond; Fibrinogenolytic toxin; Fibrinolytic toxin; Glycoprotein;
KW Hemostasis impairing toxin; Hydrolase; Protease; Secreted; Serine protease;
KW Signal; Toxin; Zymogen.
FT SIGNAL <1..10
FT /evidence="ECO:0000250|UniProtKB:P04971"
FT PROPEP 11..16
FT /evidence="ECO:0000269|PubMed:23578498"
FT /id="PRO_0000432788"
FT CHAIN 17..249
FT /note="Thrombin-like enzyme barnettobin"
FT /id="PRO_0000432789"
FT DOMAIN 17..240
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 56
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 101
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 195
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 23..154
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 41..57
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 89..247
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 133..201
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 165..180
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 191..216
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT NON_TER 1
SQ SEQUENCE 249 AA; 27585 MW; 222EDD231E082091 CRC64;
APKELQVSYA HKSSELVIGG DECDINEHPF LAFLYSRGNF CGLTLINQEW VLTAAHCDRR
FMPIYLGIHT LSVPNDDEVI RYPKDNFICP NNNIIDEKDK DIMLIRLNRP VKNSEHIAPI
SLPSNLPSVG SVCRVMGWGS ITAPNDTFPD VPHCANINLF NDTVCHGAYK RFPVKSRTLC
AGVLQGGKDK CMGDSGGPLI CNGPFHGILF WGDDPCALPR KPALYTKGFE YPPWIQSIIA
KNTTETCPP
