VSP14_BOTJA
ID VSP14_BOTJA Reviewed; 258 AA.
AC Q5W959;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Snake venom serine protease HS114 {ECO:0000303|PubMed:15876446};
DE Short=SVSP;
DE EC=3.4.21.-;
DE AltName: Full=BjSP {ECO:0000303|PubMed:30145175};
DE AltName: Full=Thrombin-like enzyme HS114 {ECO:0000305};
DE Short=SVTLE {ECO:0000305};
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].
RC TISSUE=Venom gland;
RX PubMed=15876446; DOI=10.1016/j.toxicon.2005.03.011;
RA Saguchi K., Hagiwara-Saguchi Y., Murayama N., Ohi H., Fujita Y.,
RA Camargo A.C.M., Serrano S.M.T., Higuchi S.;
RT "Molecular cloning of serine proteinases from Bothrops jararaca venom
RT gland.";
RL Toxicon 46:72-83(2005).
RN [2]
RP PROTEIN SEQUENCE OF 25-64, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION,
RP SUBCELLULAR LOCATION, GLYCOSYLATION, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND PROBABLE GLYCOSYLATION AT ASN-44.
RC TISSUE=Venom;
RX PubMed=30145175; DOI=10.1016/j.taap.2018.08.018;
RA Carone S.E.I., Menaldo D.L., Sartim M.A., Bernardes C.P., Caetano R.C.,
RA da Silva R.R., Cabral H., Barraviera B., Ferreira Junior R.S.,
RA Sampaio S.V.;
RT "BjSP, a novel serine protease from Bothrops jararaca snake venom that
RT degrades fibrinogen without forming fibrin clots.";
RL Toxicol. Appl. Pharmacol. 357:50-61(2018).
RN [3]
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).
RN [4]
RP LACK OF ACTIVITY ON POTASSIUM CHANNELS.
RX PubMed=32161292; DOI=10.1038/s41598-020-61258-x;
RA Boldrini-Franca J., Pinheiro-Junior E.L., Peigneur S., Pucca M.B.,
RA Cerni F.A., Borges R.J., Costa T.R., Carone S.E.I., Fontes M.R.M.,
RA Sampaio S.V., Arantes E.C., Tytgat J.;
RT "Beyond hemostasis: a snake venom serine protease with potassium channel
RT blocking and potential antitumor activities.";
RL Sci. Rep. 10:4476-4476(2020).
CC -!- FUNCTION: Snake venom serine protease that shows non-specific action on
CC fibrinogen (PubMed:30145175). It preferentially degrades fibrinogen
CC Aalpha (FGA), releasing fibrinopeptide A, and shows a lower activity on
CC fibrinogen Bbeta (FGB), releasing fibrinopeptide B and other uncommon
CC fibrinopeptides (PubMed:30145175). Also shows low fibrinolytic activity
CC compared to plasmin (PubMed:30145175). Has high enzymatic activity on
CC the substrates for activated protein C and factor XIa, and for thrombin
CC (PubMed:30145175). Shows a wide activity spectrum at different peptide
CC sequences, with a preferential cleavage at Lys-|-Xaa over Arg-|-Xaa
CC bonds (PubMed:30145175). {ECO:0000269|PubMed:30145175}.
CC -!- ACTIVITY REGULATION: Inhibited by benzamidine, PMSF, leupeptin, SDS and
CC DTT, but not by EDTA, and commercial antivenom.
CC {ECO:0000269|PubMed:30145175}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:30145175};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius.
CC {ECO:0000269|PubMed:30145175};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q7SZE1}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:30145175}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:30145175}.
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 -!- PTM: N-glycosylated. Contains approximately 10% carbohydrates.
CC {ECO:0000269|PubMed:30145175}.
CC -!- MISCELLANEOUS: Does not cleave fibrinogen gamma chain (FGG)
CC (PubMed:30145175). Does not form fibrin clots from fibrinogen solutions
CC (PubMed:30145175). Has no effect on aggregation of washed platelets
CC (PubMed:30145175). Has minor effects on the substrate for plasma
CC kallikrein, plasmin and factor Xa, and also on certain isolated
CC factors, such as prothrombin, factor X and protein C, not inducing the
CC formation of their activated forms (PubMed:30145175). Also shows a very
CC weak inhibitory activity on the human voltage-gated potassium channel
CC Kv10.1/KCNH1/EAG1 (9.2% current inhibition at 5 uM) (PubMed:32161292).
CC {ECO:0000269|PubMed:30145175, ECO:0000269|PubMed:32161292}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR EMBL; AB178322; BAD66928.1; -; mRNA.
DR AlphaFoldDB; Q5W959; -.
DR SMR; Q5W959; -.
DR MEROPS; S01.023; -.
DR iPTMnet; Q5W959; -.
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; Fibrinogenolytic toxin;
KW Fibrinolytic toxin; Glycoprotein; Hemostasis impairing toxin; Hydrolase;
KW Protease; Secreted; Serine protease; Signal; Toxin; Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..24
FT /evidence="ECO:0000305|PubMed:30145175"
FT /id="PRO_0000294989"
FT CHAIN 25..258
FT /note="Snake venom serine protease HS114"
FT /evidence="ECO:0000269|PubMed:30145175"
FT /id="PRO_5000051172"
FT DOMAIN 25..249
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 65
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q7SZE1"
FT ACT_SITE 110
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q7SZE1"
FT ACT_SITE 204
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q7SZE1"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:20146532,
FT ECO:0000305|PubMed:30145175"
FT DISULFID 31..163
FT /evidence="ECO:0000250|UniProtKB:Q7SZE1"
FT DISULFID 50..66
FT /evidence="ECO:0000250|UniProtKB:Q7SZE1"
FT DISULFID 98..256
FT /evidence="ECO:0000250|UniProtKB:Q7SZE1"
FT DISULFID 142..210
FT /evidence="ECO:0000250|UniProtKB:Q7SZE1"
FT DISULFID 174..189
FT /evidence="ECO:0000250|UniProtKB:Q7SZE1"
FT DISULFID 200..225
FT /evidence="ECO:0000250|UniProtKB:Q7SZE1"
SQ SEQUENCE 258 AA; 27843 MW; 5971865DB411B645 CRC64;
MVLVRVVANL LILQLSYAQK VSELVVGGDE CNINEHRSLV AIFNSTGFFC SGILLNQEWV
LTASHCDSTN FQMKIGVHSK KTLNQDEQTR NPKEKIFCPN KKNDDALDKD LMLVRLDSPV
SDSEHIAPLS LPSSPPSVGS VCRIMGWGSI TPIQKTNPDV PHCANINLLD DAVCRAAYPE
LPAEYRTLCA GVPEGGIDTC NGDSGGPLIC NGQFQGIVFY GAHPCGQAPK PGLYTKVIDY
NTWIESVIAG NTAATCPP
