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VSP2_CRODO
ID   VSP2_CRODO              Reviewed;          29 AA.
AC   C0HJR6;
DT   08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT   08-JUN-2016, sequence version 1.
DT   03-AUG-2022, entry version 8.
DE   RecName: Full=Thrombin-like enzyme collinein-2 {ECO:0000303|PubMed:26227411};
DE            Short=SVTLE collinein-2 {ECO:0000303|PubMed:26227411};
DE            EC=3.4.21.- {ECO:0000250|UniProtKB:A0A0S4FKT4};
DE   AltName: Full=Fibrinogen-clotting enzyme {ECO:0000250|UniProtKB:A0A0S4FKT4};
DE   AltName: Full=Snake venom serine protease {ECO:0000303|PubMed:26227411};
DE            Short=SVSP {ECO:0000303|PubMed:26227411};
DE   Flags: Fragment;
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|PubMed:26227411};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, SUBCELLULAR LOCATION, MASS SPECTROMETRY, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Venom {ECO:0000303|PubMed:26227411};
RX   PubMed=26227411; DOI=10.1007/s00253-015-6836-2;
RA   Boldrini-Franca J., Santos Rodrigues R., Santos-Silva L.K., de Souza D.L.,
RA   Gomes M.S., Cologna C.T., de Pauw E., Quinton L., Henrique-Silva F.,
RA   de Melo Rodrigues V., Arantes E.C.;
RT   "Expression of a new serine protease from Crotalus durissus collilineatus
RT   venom in Pichia pastoris and functional comparison with the native
RT   enzyme.";
RL   Appl. Microbiol. Biotechnol. 99:9971-9986(2015).
CC   -!- FUNCTION: Thrombin-like snake venom serine protease.
CC       {ECO:0000250|UniProtKB:A0A0S4FKT4}.
CC   -!- SUBUNIT: Monomer. {ECO:0000305|PubMed:26227411}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26227411}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:26227411}.
CC   -!- MASS SPECTROMETRY: Mass=28388; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:26227411};
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; C0HJR6; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Hydrolase; Protease; Secreted;
KW   Serine protease; Toxin.
FT   CHAIN           <1..>29
FT                   /note="Thrombin-like enzyme collinein-2"
FT                   /evidence="ECO:0000269|PubMed:26227411"
FT                   /id="PRO_0000436479"
FT   DISULFID        16..?
FT                   /evidence="ECO:0000250|UniProtKB:Q9PSN3"
FT   DISULFID        27..?
FT                   /evidence="ECO:0000250|UniProtKB:Q9PSN3"
FT   NON_TER         1
FT                   /evidence="ECO:0000303|PubMed:26227411"
FT   NON_TER         29
FT                   /evidence="ECO:0000303|PubMed:26227411"
SQ   SEQUENCE   29 AA;  3040 MW;  ECC3F64804879FBC CRC64;
     TALPQLRLPA TSRILCAGVL EGGIDTCNR
 
 
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