ID   VSP1_BOTAN              Reviewed;         119 AA.
AC   P0DJG3;
DT   18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2012, sequence version 1.
DT   03-AUG-2022, entry version 26.
DE   RecName: Full=Thrombin-like enzyme TLBan;
DE            Short=SVTLE TLBan;
DE            EC=3.4.21.-;
DE   AltName: Full=Fibrinogen-clotting enzyme;
DE   AltName: Full=Snake venom serine protease;
DE            Short=SVSP;
DE   Flags: Fragments;
OS   Bothrocophias andianus (Andean lancehead) (Bothrops andianus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrocophias.
OX   NCBI_TaxID=1144373;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, SUBUNIT, GLYCOSYLATION, SIALIC ACID, AND MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=22155303; DOI=10.1016/j.toxicon.2011.11.018;
RA   Valeriano-Zapana J.A., Segovia-Cruz F.S., Rojas-Hualpa J.M.,
RA   Martins-de-Souza D., Ponce-Soto L.A., Marangoni S.;
RT   "Functional and structural characterization of a new serine protease with
RT   thrombin-like activity TLBan from Bothrops andianus (Andean Lancehead)
RT   snake venom.";
RL   Toxicon 59:231-240(2012).
CC   -!- FUNCTION: Thrombin-like snake venom serine protease, with high clotting
CC       activity in vitro. Has also fibrinogenolytic ability, showing a fast
CC       degradation of fibrinogen Aalpha chain (FGA), a slow degradation of
CC       Bbeta chain (FGB) and no degradation of gamma chain. Also causes
CC       platelet aggregation in platelet rich plasma (PRP) and washed platelet
CC       suspension. {ECO:0000269|PubMed:22155303}.
CC   -!- ACTIVITY REGULATION: Strongly inhibited by PMSF and slightly inhibited
CC       by EDTA and soybean trypsin inhibitor. {ECO:0000269|PubMed:22155303}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.79 M for N-alpha-benzoyl-DL-Arg-p-nitroanilide (DL-BApNA)
CC         {ECO:0000269|PubMed:22155303};
CC         Vmax=0.54 nmol/min/mg enzyme with N-alpha-benzoyl-DL-Arg-p-
CC         nitroanilide (DL-BApNA) as substrate {ECO:0000269|PubMed:22155303};
CC       pH dependence:
CC         Optimum pH is 8.0. {ECO:0000269|PubMed:22155303};
CC       Temperature dependence:
CC         Optimum temperature is 45 degrees Celsius.
CC         {ECO:0000269|PubMed:22155303};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:22155303}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- PTM: Contains both N-linked carbohydrates and sialic acid.
CC       {ECO:0000269|PubMed:22155303}.
CC   -!- MASS SPECTROMETRY: Mass=25835.65; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:22155303};
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
CC   -!- CAUTION: Ile, Leu, Gln and Lys residues were impossible to discriminate
CC       with the method employed and are all assigned by comparison with
CC       orthologs. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; P0DJG3; -.
DR   SMR; P0DJG3; -.
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   Gene3D; 2.40.10.10; -; 2.
DR   InterPro; IPR001357; BRCT_dom.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001254; Trypsin_dom.
DR   Pfam; PF00089; Trypsin; 1.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
PE   1: Evidence at protein level;
KW   Blood coagulation cascade activating toxin; Direct protein sequencing;
KW   Disulfide bond; Fibrinogenolytic toxin; Glycoprotein;
KW   Hemostasis impairing toxin; Hydrolase;
KW   Platelet aggregation activating toxin; Protease; Secreted; Serine protease;
KW   Sialic acid; Toxin.
FT   CHAIN           1..119
FT                   /note="Thrombin-like enzyme TLBan"
FT                   /id="PRO_0000416596"
FT   DOMAIN          1..112
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        40
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        59
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   DISULFID        7..?
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        25..?
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        54..118
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        91..?
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   NON_CONS        21..22
FT                   /evidence="ECO:0000305"
FT   NON_CONS        40..41
FT                   /evidence="ECO:0000305"
FT   NON_CONS        58..59
FT                   /evidence="ECO:0000305"
FT   NON_CONS        93..94
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   119 AA;  13356 MW;  C040280888C2EA1F CRC64;
     VIGGDECNIN EHPFLVALYY STFFCGMTLI NQEWVLTAAH ESEKFPKEKY FIFCPNNKDI
     MLIRLDKPVS NSEHIAPLSL PSSPPSVGSV CRKPALYTKV FDYLLWIQSI IAGNTATCP