ID   VSP1_PROEL              Reviewed;         233 AA.
AC   P84788;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=Thrombin-like enzyme elegaxobin-1;
DE            Short=SVTLE;
DE            EC=3.4.21.-;
DE   AltName: Full=Elegaxobin I;
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:12076650};
RX   PubMed=12076650; DOI=10.1016/s0041-0101(02)00092-2;
RA   Oyama E., Takahashi H.;
RT   "Amino acid sequence of a thrombin like enzyme, elegaxobin, from the venom
RT   of Trimeresurus elegans (Sakishima-habu).";
RL   Toxicon 40:959-970(2002).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 1-10, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Venom {ECO:0000269|PubMed:10708800};
RX   PubMed=10708800; DOI=10.1016/s0041-0101(99)00220-2;
RA   Oyama E., Takahashi H.;
RT   "Purification and characterization of a thrombin-like enzyme, elegaxobin,
RT   from the venom of Trimeresurus elegans (Sakishima-habu).";
RL   Toxicon 38:1087-1100(2000).
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. Incubation with human fibrinogen alpha and
CC       beta resulted in cleavage of both fibrinogen chains but generated
CC       neither fibrinopeptide A nor fibrinopeptide B. Promotes clotting of
CC       rabbit fibrinogen, but not bovine or human fibrinogen.
CC       {ECO:0000269|PubMed:10708800}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10708800,
CC       ECO:0000269|PubMed:12076650}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:10708800, ECO:0000269|PubMed:12076650}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR   AlphaFoldDB; P84788; -.
DR   SMR; P84788; -.
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   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; Hemostasis impairing toxin; Hydrolase; Protease; Secreted;
KW   Serine protease; Toxin.
FT   CHAIN           1..233
FT                   /note="Thrombin-like enzyme elegaxobin-1"
FT                   /id="PRO_0000227535"
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   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;  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