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Thrombin-like enzyme elegaxobin-1 (SVTLE) (EC 3.4.21.-) (Elegaxobin I) (Fibrinogen-clotting enzyme) (Snake venom serine protease) (SVSP)

 VSP1_PROEL              Reviewed;         233 AA.
P84788;
07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
07-MAR-2006, sequence version 1.
22-NOV-2017, entry version 43.
RecName: Full=Thrombin-like enzyme elegaxobin-1;
Short=SVTLE;
EC=3.4.21.-;
AltName: Full=Elegaxobin I;
AltName: Full=Fibrinogen-clotting enzyme;
AltName: Full=Snake venom serine protease;
Short=SVSP;
Protobothrops elegans (Elegant pitviper) (Trimeresurus elegans).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata;
Toxicofera; Serpentes; Colubroidea; Viperidae; Crotalinae;
Protobothrops.
NCBI_TaxID=88086;
[1] {ECO:0000305}
PROTEIN SEQUENCE, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Venom {ECO:0000269|PubMed:12076650};
PubMed=12076650; DOI=10.1016/S0041-0101(02)00092-2;
Oyama E., Takahashi H.;
"Amino acid sequence of a thrombin like enzyme, elegaxobin, from the
venom of Trimeresurus elegans (Sakishima-habu).";
Toxicon 40:959-970(2002).
[2] {ECO:0000305}
PROTEIN SEQUENCE OF 1-10, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
TISSUE=Venom {ECO:0000269|PubMed:10708800};
PubMed=10708800; DOI=10.1016/S0041-0101(99)00220-2;
Oyama E., Takahashi H.;
"Purification and characterization of a thrombin-like enzyme,
elegaxobin, from the venom of Trimeresurus elegans (Sakishima-habu).";
Toxicon 38:1087-1100(2000).
-!- FUNCTION: Thrombin-like snake venom serine protease that clots
rabbit fibrinogen. Only the beta chain of fibrinogen (FGB) is
cleaved, releasing fibrinopeptide B. Incubation with human
fibrinogen alpha and beta resulted in cleavage of both fibrinogen
chains but generated neither fibrinopeptide A nor fibrinopeptide
B. Promotes clotting of rabbit fibrinogen, but not bovine or human
fibrinogen. {ECO:0000269|PubMed:10708800}.
-!- SUBUNIT: Monomer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10708800,
ECO:0000269|PubMed:12076650}.
-!- TISSUE SPECIFICITY: Expressed by the venom gland.
{ECO:0000269|PubMed:10708800, ECO:0000269|PubMed:12076650}.
-!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom
subfamily. {ECO:0000255|PROSITE-ProRule:PRU00274}.
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SMR; P84788; -.
HOVERGEN; HBG013304; -.
GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
GO; GO:0042730; P:fibrinolysis; IDA:UniProtKB.
GO; GO:0030195; P:negative regulation of blood coagulation; IDA:UniProtKB.
GO; GO:0009405; P:pathogenesis; IDA:UniProtKB.
CDD; cd00190; Tryp_SPc; 1.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
Pfam; PF00089; Trypsin; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF50494; SSF50494; 1.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
1: Evidence at protein level;
Blood coagulation cascade activating toxin; Direct protein sequencing;
Disulfide bond; Hemostasis impairing toxin; Hydrolase; Protease;
Secreted; Serine protease; Toxin.
CHAIN 1 233 Thrombin-like enzyme elegaxobin-1.
/FTId=PRO_0000227535.
DOMAIN 1 224 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 40 40 Charge relay system.
{ECO:0000250|UniProtKB:P12544}.
ACT_SITE 85 85 Charge relay system.
{ECO:0000250|UniProtKB:P12544}.
ACT_SITE 179 179 Charge relay system.
{ECO:0000250|UniProtKB:P12544}.
DISULFID 7 138 {ECO:0000250|UniProtKB:Q9PSN3,
ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 25 41 {ECO:0000250|UniProtKB:Q9PSN3,
ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 73 231 {ECO:0000250|UniProtKB:Q9PSN3,
ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 117 185 {ECO:0000250|UniProtKB:Q9PSN3,
ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 149 164 {ECO:0000250|UniProtKB:Q9PSN3,
ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 175 200 {ECO:0000250|UniProtKB:Q9PSN3,
ECO:0000255|PROSITE-ProRule:PRU00274}.
SEQUENCE 233 AA; 25440 MW; B93AC18E5E027E17 CRC64;
VIGGDECNIN EHPFLVLVYY DDYQCGGTLI NEEWVLTAAH CNGKNMEIYL GVHSKKVPNK
DVQRRVPKEK FFCDSSKTYT KWNKDIMLIR LDRPVRKSAH IAPLSLPSSP PSVGSVCRVM
GWGTITSPQE TYPDVPHCAK INLLDYSECR AAYPGLPPKS RTLCAGVLEG GKDTCGGDSG
GPLICNGQFQ GIVSWGGDPC AQPHEPGSYT NVFDHLDWIK GIIAGNTDAT CPL


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