ID   VSP3_CRODO              Reviewed;          81 AA.
AC   C0HK19;
DT   30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2016, sequence version 1.
DT   03-AUG-2022, entry version 11.
DE   RecName: Full=Thrombin-like enzyme collinein-3 {ECO:0000303|Ref.1};
DE            Short=SVTLE collinein-3 {ECO:0000303|Ref.1};
DE            EC=3.4.21.- {ECO:0000250|UniProtKB:A0A0S4FKT4};
DE   AltName: Full=Fibrinogen-clotting enzyme {ECO:0000250|UniProtKB:Q9PSN3};
DE   AltName: Full=Snake venom serine protease {ECO:0000303|Ref.1};
DE            Short=SVSP {ECO:0000303|Ref.1};
DE   Flags: Fragments;
OS   Crotalus durissus collilineatus (Brazilian rattlesnake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX   NCBI_TaxID=221569 {ECO:0000303|Ref.1};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom {ECO:0000303|Ref.1};
RA   Boldrini-France J., Cologna C.T., de Pauw E., Quinton L., Arantes E.C.;
RT   "Identification of new serine protease isoforms from Crotalus durissus
RT   collilineatus venom.";
RL   Submitted (APR-2016) to UniProtKB.
CC   -!- FUNCTION: Thrombin-like snake venom serine protease.
CC       {ECO:0000250|UniProtKB:A0A0S4FKT4}.
CC   -!- SUBUNIT: Monomer. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.1}.
CC   -!- TISSUE SPECIFICITY: Expressed by the vanom gland. {ECO:0000305|Ref.1}.
CC   -!- MASS SPECTROMETRY: Mass=29765; Method=MALDI;
CC       Evidence={ECO:0000269|Ref.1};
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000305}.
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DR   AlphaFoldDB; C0HK19; -.
DR   SMR; C0HK19; -.
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; -; 1.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001254; Trypsin_dom.
DR   Pfam; PF00089; Trypsin; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Fibrinogenolytic toxin;
KW   Hemostasis impairing toxin; Hydrolase; Protease; Secreted; Serine protease;
KW   Toxin.
FT   CHAIN           <1..>81
FT                   /note="Thrombin-like enzyme collinein-3"
FT                   /evidence="ECO:0000269|Ref.1"
FT                   /id="PRO_0000438331"
FT   ACT_SITE        4
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        36..?
FT                   /evidence="ECO:0000250|UniProtKB:Q9PSN3"
FT   DISULFID        ?..40
FT                   /evidence="ECO:0000250|UniProtKB:Q9PSN3"
FT   DISULFID        51..68
FT                   /evidence="ECO:0000250|UniProtKB:Q9PSN3"
FT   DISULFID        79..?
FT                   /evidence="ECO:0000250|UniProtKB:Q9PSN3"
FT   NON_CONS        37..38
FT                   /evidence="ECO:0000303|Ref.1"
FT   NON_TER         1
FT                   /evidence="ECO:0000303|Ref.1"
FT   NON_TER         81
FT                   /evidence="ECO:0000303|Ref.1"
SQ   SEQUENCE   81 AA;  8964 MW;  3F17B86474EAA746 CRC64;
     WDKDIMLIRL NKPVSYSEHI APLSLPSSPP IVGSVCRPHC ANINLLDYEV CRTAHPQFRL
     PATSRILCAG VLEGGIDTCH R