VSP_BOTPC
ID VSP_BOTPC Reviewed; 250 AA.
AC U5YCR8;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 22-JAN-2014, sequence version 1.
DT 03-AUG-2022, entry version 23.
DE RecName: Full=Snake venom serine protease pictobin;
DE Short=SVSP;
DE EC=3.4.21.-;
DE Flags: Precursor; Fragment;
OS Bothrops pictus (Desert lancehead).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX NCBI_TaxID=133440;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Vivas D.E., Sandoval G.A., Inga R.R., Yarleque A., Flores E.;
RT "Molecular and biological study of the clotting enzyme from the Bothrops
RT pictus venom.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Snake venom serine protease that may impair the hemostatic
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. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC {ECO:0000305}.
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DR EMBL; KF410948; AGZ87932.1; -; mRNA.
DR AlphaFoldDB; U5YCR8; -.
DR SMR; U5YCR8; -.
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 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Hemostasis impairing toxin; Hydrolase;
KW Protease; Secreted; Serine protease; Signal; Toxin; Zymogen.
FT SIGNAL <1..11
FT /evidence="ECO:0000255"
FT PROPEP 12..17
FT /evidence="ECO:0000250"
FT /id="PRO_0000432785"
FT CHAIN 18..250
FT /note="Snake venom serine protease pictobin"
FT /id="PRO_0000432786"
FT DOMAIN 18..241
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 57
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 102
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 196
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 24..155
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 42..58
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 134..202
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 166..181
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 192..217
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT NON_TER 1
SQ SEQUENCE 250 AA; 27783 MW; 191CF26C461546C5 CRC64;
ANLLILQVSY AQKSSELVIG GDECNINEHR FLAFTYSRGF FCGGTLINQE WVLTATHCDR
IFMRIYLGLH NQSVRYDDQQ IRYPKEKYFF PCSKNFTKWD KDIMLIRLDR PVKNSEHIAP
LSLPSNPPSV GSVCRVMGWG TITAPNDTYP DVPHCANINL FNYTVCRGAY KGLPATSRTL
CAGVLQGGID TCVGDSGGPL ICNGQFQGIV FWGGDPCAQP RKPALYTKVF DHLHWILSII
AGNTTATCPP