VSP1_BOTJA
ID VSP1_BOTJA Reviewed; 237 AA.
AC P81824; Q6URK9;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 2.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Platelet-aggregating proteinase PA-BJ;
DE EC=3.4.21.-;
DE AltName: Full=Snake venom serine protease;
DE Short=SVSP;
DE Flags: Precursor; Fragment;
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 PROTEIN SEQUENCE OF 6-237, FUNCTION, AND GLYCOSYLATION AT ASN-25 AND
RP SER-28.
RC TISSUE=Venom gland;
RX PubMed=7766629; DOI=10.1021/bi00021a033;
RA Serrano S.M.T., Mentele R., Sampaio C.A.M., Fink E.;
RT "Purification, characterization, and amino acid sequence of a serine
RT proteinase, PA-BJ, with platelet-aggregating activity from the venom of
RT Bothrops jararaca.";
RL Biochemistry 34:7186-7193(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-167.
RC TISSUE=Venom;
RA Assakura M.T., Teixeira B.C., Camargo A.C.M., Serrano S.M.T.;
RT "Molecular cloning and sequence analysis of a cDNA encoding PA-BJ, a
RT platelet-aggregating serine peptidase from the venom of Bothrops
RT jararaca.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION.
RX PubMed=10908720; DOI=10.1016/s0014-5793(00)01803-2;
RA Santos B.F., Serrano S.M.T., Kuliopulos A., Niewiarowski S.;
RT "Interaction of viper venom serine peptidases with thrombin receptors on
RT human platelets.";
RL FEBS Lett. 477:199-202(2000).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND DEVELOPMENTAL STAGE.
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).
RN [5]
RP 3D-STRUCTURE MODELING.
RX PubMed=14872537; DOI=10.1002/jmr.644;
RA Maroun R.C., Serrano S.M.T.;
RT "Identification of the substrate-binding exosites of two snake venom serine
RT proteinases: molecular basis for the partition of two essential functions
RT of thrombin.";
RL J. Mol. Recognit. 17:51-61(2004).
CC -!- FUNCTION: Snake venom serine protease that induces platelet aggregation
CC through activation of protease-activated platelet receptors (PAR1/F2R
CC and PAR4/F2RL3). On F2R, the cleavage occurs at Arg41-Ser42 (like
CC thrombin cleavage), and Arg46-Asn47. In normal condition of hemostasis,
CC the cleavage of the Arg41-Ser42 bond liberates a new N-terminus that
CC functions as an agonist. However after envenomation, the cleavage of
CC Arg46-Asn47 bond degrades this potential agonist. This may explain why
CC the snake protease is less potent than thrombin in causing platelet
CC aggregation and release reaction. On F2RL3, a thrombin-like activity
CC has also been proven by calcium release from lung fibroblasts
CC transfected with this receptor. Possesses amidolytic activities.
CC {ECO:0000269|PubMed:10908720, ECO:0000269|PubMed:7766629}.
CC -!- ACTIVITY REGULATION: Inhibited by PMSF. The amidolytic activity is also
CC inhibited by benzamidine derivatives.
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 both adult and
CC newborn B.jararaca venoms. {ECO:0000269|PubMed:20146532}.
CC -!- MISCELLANEOUS: Does not have fibrinogen-clotting activity.
CC {ECO:0000305|PubMed:7766629}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR EMBL; AY363221; AAQ62580.1; -; mRNA.
DR AlphaFoldDB; P81824; -.
DR SMR; P81824; -.
DR MEROPS; S01.180; -.
DR iPTMnet; P81824; -.
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 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 Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Hemostasis impairing toxin; Hydrolase;
KW Platelet aggregation activating toxin; Protease; Secreted; Serine protease;
KW Toxin.
FT PROPEP <1..5
FT /evidence="ECO:0000250"
FT /id="PRO_0000416999"
FT CHAIN 6..237
FT /note="Platelet-aggregating proteinase PA-BJ"
FT /id="PRO_0000088732"
FT DOMAIN 6..229
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 46
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 91
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 185
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:7766629"
FT CARBOHYD 28
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:7766629"
FT DISULFID 12..144
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 31..47
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 79..236
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 123..191
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 155..170
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 181..205
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CONFLICT 18
FT /note="R -> P (in Ref. 2; AAQ62580)"
FT /evidence="ECO:0000305"
FT CONFLICT 24
FT /note="Y -> F (in Ref. 2; AAQ62580)"
FT /evidence="ECO:0000305"
FT CONFLICT 82
FT /note="R -> K (in Ref. 2; AAQ62580)"
FT /evidence="ECO:0000305"
FT CONFLICT 85
FT /note="D -> N (in Ref. 2; AAQ62580)"
FT /evidence="ECO:0000305"
FT CONFLICT 124
FT /note="Y -> L (in Ref. 2; AAQ62580)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="D -> N (in Ref. 2; AAQ62580)"
FT /evidence="ECO:0000305"
FT CONFLICT 166..167
FT /note="ST -> ID (in Ref. 2; AAQ62580)"
FT /evidence="ECO:0000305"
FT NON_TER 1
SQ SEQUENCE 237 AA; 25742 MW; F4E051D56AEC750B CRC64;
NSLVIVVGGR PCKINVHRSL VLLYNSSSLL CSGTLINQEW VLTAAHCDSK NFKMKLGVHS
IKIRNKNERT RHPKEKFICP NRKKDDVLDK DIMLIRLNRP VSNSEHIAPL SLPSSPPSVG
SVCYVMGWGK ISSTKETYPD VPHCAKINIL DHAVCRAAYT WWPATSTTLC AGILQGGKDT
CEGDSGGPLI CNGLQGIVSG GGNPCGQPRK PALYTKVFDY LPWIESIIAG TTTATCP
