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