VSPTL_BOTAL
ID VSPTL_BOTAL Reviewed; 233 AA.
AC Q6IWF1;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Snake venom serine protease BthaTL;
DE Short=SVSP;
DE EC=3.4.21.-;
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], AND 3D-STRUCTURE MODELING.
RC TISSUE=Venom gland;
RX PubMed=16716626; DOI=10.1016/j.cbpb.2006.03.010;
RA Vitorino-Cardoso A.F., Pereira Ramos O.H., Homsi-Brandeburgo M.I.,
RA Selistre-de-Araujo H.S.;
RT "Insights into the substrate specificity of a novel snake venom serine
RT peptidase by molecular modeling.";
RL Comp. Biochem. Physiol. 144B:334-342(2006).
CC -!- FUNCTION: Snake venom serine protease that may act in the hemostasis
CC system of the prey. {ECO:0000250}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR EMBL; AY618559; AAT40141.1; -; mRNA.
DR AlphaFoldDB; Q6IWF1; -.
DR SMR; Q6IWF1; -.
DR MEROPS; S01.456; -.
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; 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 2: Evidence at transcript level;
KW Disulfide bond; Hemostasis impairing toxin; Hydrolase; Protease; Secreted;
KW Serine protease; Toxin.
FT CHAIN 1..233
FT /note="Snake venom serine protease BthaTL"
FT /id="PRO_5000093473"
FT DOMAIN 1..224
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 40
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 85
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 179
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT DISULFID 7..138
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 25..41
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 73..231
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 117..185
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 149..164
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 175..200
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 233 AA; 25630 MW; 3033B90DC90BC49B CRC64;
VIGGDECDIN EHRFLAFLYP GRFFCSGTLI NQEWVLTVAH CDTISMRIYL GLHTRSVPND
DEEIRYPMEK FKCPNRKRSY IKDKDIMLIR LNRPVNDSPH IAPLSLPSNP PSVGSVCHVM
GWGTTSPSKA TYPDVPHCAN INLVNDTMCH GAYNGLPVTS RKFCAGVLQG GIDTCVGDSG
GPLICNGQFQ GIVSWGGKVC ARLPRPALYT KVFEYLPWIQ SIIAGNTTAT CPL
