VSP2_PROEL
ID VSP2_PROEL Reviewed; 233 AA.
AC P84787;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Thrombin-like enzyme elegaxobin-2;
DE Short=SVTLE;
DE EC=3.4.21.-;
DE AltName: Full=Elegaxobin II;
DE AltName: Full=Fibrinogen-clotting enzyme;
DE AltName: Full=Snake venom serine protease;
DE Short=SVSP;
OS Protobothrops elegans (Elegant pitviper) (Trimeresurus elegans).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Protobothrops.
OX NCBI_TaxID=88086;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Venom {ECO:0000269|PubMed:15500847};
RX PubMed=15500847; DOI=10.1016/j.toxicon.2004.07.007;
RA Oyama E., Takahashi H.;
RT "Amino acid sequence of a thrombin-like enzyme, elegaxobin II, from the
RT venom of Trimeresurus elegans (Sakishima-Habu).";
RL Toxicon 44:711-721(2004).
RN [2] {ECO:0000305}
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12676434; DOI=10.1016/s0041-0101(02)00363-x;
RA Oyama E., Takahashi H.;
RT "Purification and characterization of a thrombin-like enzyme, elegaxobin
RT II, with Lys-bradykinin releasing activity from the venom of Trimeresurus
RT elegans (Sakishima-Habu).";
RL Toxicon 41:559-568(2003).
CC -!- FUNCTION: Thrombin-like snake venom serine protease that clots rabbit
CC fibrinogen. Only the beta chain of fibrinogen (FGB) is cleaved,
CC releasing fibrinopeptide B. Human and bovine fibrinogen are unaffected.
CC Also cleaves Met-Lys and Arg-Ser bonds in heat-denatured bovine plasma
CC kininogen to release Lys-bradykinin. {ECO:0000269|PubMed:12676434}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12676434}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12676434,
CC ECO:0000269|PubMed:15500847}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:12676434, ECO:0000269|PubMed:15500847}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR AlphaFoldDB; P84787; -.
DR SMR; P84787; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0090729; F:toxin activity; IDA:UniProtKB.
DR GO; GO:0044485; P:envenomation resulting in fibrinogenolysis in another organism; IDA:UniProtKB.
DR GO; GO:0044470; P:envenomation resulting in negative regulation of blood coagulation in another organism; IDA:UniProtKB.
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; Toxin.
FT CHAIN 1..233
FT /note="Thrombin-like enzyme elegaxobin-2"
FT /id="PRO_0000227536"
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|UniProtKB:P12544"
FT ACT_SITE 85
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P12544"
FT ACT_SITE 179
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P12544"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 7..138
FT /evidence="ECO:0000250|UniProtKB:Q9PSN3,
FT ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 25..41
FT /evidence="ECO:0000250|UniProtKB:Q9PSN3,
FT ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 73..231
FT /evidence="ECO:0000250|UniProtKB:Q9PSN3,
FT ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 117..185
FT /evidence="ECO:0000250|UniProtKB:Q9PSN3,
FT ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 149..164
FT /evidence="ECO:0000250|UniProtKB:Q9PSN3,
FT ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 175..200
FT /evidence="ECO:0000250|UniProtKB:Q9PSN3,
FT ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 233 AA; 25591 MW; 33C60B6914DF2134 CRC64;
VIGGDECNIN EHPFLVLVYY DEYQCGGTLI NEEWVLTAAH CDGENMEIHL GMHSKKVPNK
DRRRRVPKEK FFCDSSKNYT KWNKDIMLIR LNRPVRKSAH IAPLSLPSSP PSVGSVCRIM
GWGTISPTEE TYPDVPHCAN INLLDYEVCR AAYPELPATS RTLCAGILEG GKDSCGGDSG
GPLICNGQFQ GIVSWGGDPC AQPHEPGSYT NVFDHLDWIK GIIAGNTDAT CPL
