ID   VSP2_AGKCO              Reviewed;         234 AA.
AC   P82981;
DT   03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Thrombin-like enzyme contortrixobin;
DE            Short=SVTLE;
DE            EC=3.4.21.-;
DE   AltName: Full=Fibrinogen-clotting enzyme;
DE   AltName: Full=Snake venom serine protease;
DE            Short=SVSP;
DE   AltName: Full=Venombin B;
OS   Agkistrodon contortrix contortrix (Southern copperhead).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Agkistrodon.
OX   NCBI_TaxID=8713 {ECO:0000305};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, ACTIVITY REGULATION, MASS SPECTROMETRY, AND
RP   DISULFIDE BONDS.
RC   TISSUE=Venom;
RX   PubMed=10956019; DOI=10.1021/bi000145i;
RA   Amiconi G., Amoresano A., Boumis G., Brancaccio A., De Cristofaro R.,
RA   De Pascalis A., Di Girolamo S., Maras B., Scaloni A.;
RT   "A novel venombin B from Agkistrodon contortrix contortrix: evidence for
RT   recognition properties in the surface around the primary specificity pocket
RT   different from thrombin.";
RL   Biochemistry 39:10294-10308(2000).
CC   -!- FUNCTION: Thrombin-like snake venom serine protease that cleaves beta
CC       chain of fibrinogen (FGB), releasing fibrinopeptide B. Has a coagulant
CC       activity activating blood coagulation factors V (F5) and XIII (F13A1).
CC       {ECO:0000269|PubMed:10956019}.
CC   -!- ACTIVITY REGULATION: Strongly inhibited by diisopropylfluorophosphate
CC       (DFP) and to a lesser extent by PMSF, benzamidine and 4,6-diamidino-2-
CC       phenylindole. Low inhibition by hirudin. {ECO:0000269|PubMed:10956019}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- PTM: Not glycosylated.
CC   -!- MASS SPECTROMETRY: Mass=25400.7; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:10956019};
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR   AlphaFoldDB; P82981; -.
DR   SMR; P82981; -.
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   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.
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..234
FT                   /note="Thrombin-like enzyme contortrixobin"
FT                   /id="PRO_0000088727"
FT   DOMAIN          1..225
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        41
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        86
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        180
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   DISULFID        7..139
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT                   ECO:0000269|PubMed:10956019"
FT   DISULFID        26..42
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT                   ECO:0000269|PubMed:10956019"
FT   DISULFID        74..232
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT                   ECO:0000269|PubMed:10956019"
FT   DISULFID        118..186
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT                   ECO:0000269|PubMed:10956019"
FT   DISULFID        150..165
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT                   ECO:0000269|PubMed:10956019"
FT   DISULFID        176..201
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT                   ECO:0000269|PubMed:10956019"
FT   VARIANT         234
FT                   /note="P -> D"
FT                   /evidence="ECO:0000269|PubMed:10956019"
SQ   SEQUENCE   234 AA;  25413 MW;  CD2A97BBF9383B0F CRC64;
     VVGGDECNIN EHRFLVAIFN SNGFVCSGTL INQEWVLTAA HCDSTDFQIK LGAHSKKVLN
     EDEQIRNPKE KFICPNKKND EVLDKDIMLI KLDSRVSNSE HIAPLSLPSS PPSVGSVCHI
     MGWGSITPIE VTFPDVPHCA YINLLDDAAC QPGYPEVLPE YRTLCAGILE GGKDTCNYDS
     GGPLICNGQF QGIVSYGAHP CGQSLKPGIY TKVFDYNDWI QSIIAGNTAA TCPP