位置:首页 > 蛋白库 > VSP_BOTBA
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2025