VSP2_BOTJA
ID VSP2_BOTJA Reviewed; 257 AA.
AC O13069;
DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Thrombin-like enzyme KN-BJ 2;
DE Short=SVTLE;
DE EC=3.4.21.-;
DE AltName: Full=Kinin-releasing and fibrinogen-clotting serine protease 2 {ECO:0000303|PubMed:20146532};
DE Flags: Precursor;
OS Bothrops jararaca (Jararaca) (Bothrops jajaraca).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX NCBI_TaxID=8724;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND FUNCTION.
RC TISSUE=Venom, and Venom gland;
RX PubMed=9490060; DOI=10.1046/j.1432-1327.1998.2510845.x;
RA Serrano S.M.T., Hagiwara Y., Murayama N., Higuchi S., Mentele R.,
RA Sampaio C.A.M., Camargo A.C.M., Fink E.;
RT "Purification and characterization of a kinin-releasing and fibrinogen-
RT clotting serine proteinase (KN-BJ) from the venom of Bothrops jararaca, and
RT molecular cloning and sequence analysis of its cDNA.";
RL Eur. J. Biochem. 251:845-853(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, DEVELOPMENTAL STAGE, AND
RP GLYCOSYLATION.
RC TISSUE=Venom;
RX PubMed=20146532; DOI=10.1021/pr901027r;
RA Zelanis A., Tashima A.K., Rocha M.M., Furtado M.F., Camargo A.C., Ho P.L.,
RA Serrano S.M.;
RT "Analysis of the ontogenetic variation in the venom proteome/peptidome of
RT Bothrops jararaca reveals different strategies to deal with prey.";
RL J. Proteome Res. 9:2278-2291(2010).
CC -!- FUNCTION: Thrombin-like snake venom serine protease that clots
CC fibrinogen (FGA) by releasing only fibrinopeptide A. Also releases
CC bradykinin from bovine low-molecular-mass kininogen (KNG).
CC {ECO:0000269|PubMed:9490060}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- DEVELOPMENTAL STAGE: This protein seems to be found in adult B.jararaca
CC venom but not in newborn snake venom. {ECO:0000269|PubMed:20146532}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR EMBL; AB004067; BAA20283.1; -; mRNA.
DR AlphaFoldDB; O13069; -.
DR SMR; O13069; -.
DR MEROPS; S01.354; -.
DR iPTMnet; O13069; -.
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 GO; GO:0008217; P:regulation of blood pressure; 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 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; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 1: Evidence at protein level;
KW Blood coagulation cascade activating toxin; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Hemostasis impairing toxin; Hydrolase;
KW Hypotensive agent; Protease; Secreted; Serine protease; Signal; Toxin;
KW Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000250"
FT PROPEP 19..24
FT /id="PRO_0000028381"
FT CHAIN 25..257
FT /note="Thrombin-like enzyme KN-BJ 2"
FT /id="PRO_0000028382"
FT DOMAIN 25..248
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 64
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 109
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 203
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:20146532"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:20146532"
FT CARBOHYD 250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:20146532"
FT DISULFID 31..162
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 49..65
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 97..255
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 141..209
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 173..188
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 199..224
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 257 AA; 27894 MW; A9F96BFA6BDDDDE6 CRC64;
MVLIRVLANL LILQLSYAQK ASELIIGGRP CDINEHRSLA LVKYGNFQCS GTLINQEWVL
SAAHCDGEKM KIHLGVHSKK VPNKDKQTRV AKEKFFCLSS KNYTKWDKDI MLIRLDSPVK
NSAHIAPISL PSSPPIVGSV CRIMGWGTIS TSKVILSDVP HCANINLLNY TVCRAAYPEL
PATSRTLCAG ILQGGKDTCV GDSGGPLICN GQFQGIVSWG SDVCGYVLEP ALYTKVSDYT
EWINSIIAGN TTATCPP
