VSPBH_BOTAL
ID VSPBH_BOTAL Reviewed; 260 AA.
AC P0CG03;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Thrombin-like enzyme bhalternin;
DE Short=SVTLE;
DE EC=3.4.21.-;
DE AltName: Full=Fibrinogen-clotting enzyme;
DE AltName: Full=Snake venom serine protease;
DE Short=SVSP;
DE Flags: Precursor;
OS Bothrops alternatus (Urutu) (Rhinocerophis alternatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX NCBI_TaxID=64174;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 25-43, FUNCTION, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Venom, and Venom gland;
RX PubMed=20184912; DOI=10.1016/j.toxicon.2010.02.014;
RA Costa Jde O., Fonseca K.C., Mamede C.C., Beletti M.E., Santos-Filho N.A.,
RA Soares A.M., Arantes E.C., Hirayama S.N., Selistre-de-Araujo H.S.,
RA Fonseca F., Henrique-Silva F., Penha-Silva N., de Oliveira F.;
RT "Bhalternin: functional and structural characterization of a new thrombin-
RT like enzyme from Bothrops alternatus snake venom.";
RL Toxicon 55:1365-1377(2010).
CC -!- FUNCTION: Thrombin-like snake venom serine protease that induces blood
CC clotting in vitro, defibrinogenation in vivo (by intraperitoneal
CC injection into mice), albuminolytic and fibrinogenolytic activities.
CC Preferentially cleaves the alpha chain of fibrinogen (FGA). Causes
CC hemolysis in the heart, causes apparent hyperemia and lymphocytic
CC interstitial pneumonitis in the lung, causes necrosis and inflammatory
CC infiltrate in the liver, and causes glomerular congestion in the
CC kidney. Also provokes a drastic myonecrosis.
CC {ECO:0000269|PubMed:20184912}.
CC -!- ACTIVITY REGULATION: Inhibited by benzamidine and partially inhibited
CC by EDTA. {ECO:0000269|PubMed:20184912}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.0-8.0. {ECO:0000269|PubMed:20184912};
CC Temperature dependence:
CC Optimum temperature is 30-40 degrees Celsius.
CC {ECO:0000269|PubMed:20184912};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20184912}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:20184912}.
CC -!- MISCELLANEOUS: Does not present azocaseinolytic activity
CC (PubMed:20184912). Does not provoke vascular lesions or hemorrhage.
CC {ECO:0000305|PubMed:20184912}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
CC -!- CAUTION: Lacks the typical His and Asp active sites in position 65 and
CC 112, which are replaced by an Asn and Thr residues, preventing the
CC protease activity. The sequence corresponding to the activity described
CC in PubMed:20184912 may be slightly different from the sequence shown.
CC {ECO:0000305}.
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DR AlphaFoldDB; P0CG03; -.
DR SMR; P0CG03; -.
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:0044179; P:hemolysis in another organism; 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; IPR033116; TRYPSIN_SER.
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; PS00135; TRYPSIN_SER; 1.
PE 1: Evidence at protein level;
KW Blood coagulation cascade activating toxin; Cytolysis;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Hemolysis;
KW Hemostasis impairing toxin; Hydrolase; Myotoxin; Protease; Secreted;
KW Serine protease; Signal; Toxin; Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..24
FT /evidence="ECO:0000269|PubMed:20184912"
FT /id="PRO_0000394524"
FT CHAIN 25..260
FT /note="Thrombin-like enzyme bhalternin"
FT /id="PRO_0000394525"
FT DOMAIN 25..251
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 31..165
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 50..66
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 144..212
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 176..191
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 202..227
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 260 AA; 28045 MW; 65A471F5C35E96F5 CRC64;
MVLIRVLANL LILQLSYAQK ASELVIGGDE CNINEHRSLV VLFNSSGFLC AGTLINQEWV
LTAANCDRKN IRIKLGMHSK NVTNEDEQTR VPKRSTFVSV AKTSHQTLGT RTSMLIRLKR
PVNDSPHIAP LSLPSSPPSV GSVCRVMGWG TISPTKVSYP DVPHCANINL LDYEVCREAH
GGLPATSRTL CAGILEGGKD SCQGDSGGPL ICNGQFQGIL SWGVHPCGQP HKPGVYTKVS
DYSEWIQSII AGNTDVTCPP
