ID VSP1_CRODO Reviewed; 238 AA. AC A0A0S4FKT4; C0HJR5; DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot. DT 17-FEB-2016, sequence version 1. DT 06-JUL-2016, entry version 6. DE RecName: Full=Thrombin-like enzyme collinein-1 {ECO:0000303|PubMed:26227411}; DE Short=SVTLE collinein-1 {ECO:0000303|PubMed:26227411}; DE EC=3.4.21.- {ECO:0000255|PROSITE-ProRule:PRU00274, ECO:0000269|PubMed:26227411}; DE AltName: Full=Fibrinogen-clotting enzyme {ECO:0000250|UniProtKB:Q9PSN3}; DE AltName: Full=Snake venom serine protease {ECO:0000303|PubMed:26227411}; DE Short=SVSP {ECO:0000303|PubMed:26227411}; OS Crotalus durissus collilineatus (Brazilian rattlesnake). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; OC Toxicofera; Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus. OX NCBI_TaxID=221569 {ECO:0000312|EMBL:CEJ25501.1}; RN [1] {ECO:0000305} RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, ENZYME RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, MASS RP SPECTROMETRY, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Venom {ECO:0000303|PubMed:26227411}, and RC Venom gland {ECO:0000312|EMBL:CEJ25501.1}; RX PubMed=26227411; DOI=10.1007/s00253-015-6836-2; RA Boldrini-Franca J., Santos Rodrigues R., Santos-Silva L.K., RA de Souza D.L., Gomes M.S., Cologna C.T., de Pauw E., Quinton L., RA Henrique-Silva F., de Melo Rodrigues V., Arantes E.C.; RT "Expression of a new serine protease from Crotalus durissus RT collilineatus venom in Pichia pastoris and functional comparison with RT the native enzyme."; RL Appl. Microbiol. Biotechnol. 99:9971-9986(2015). CC -!- FUNCTION: Thrombin-like snake venom serine protease. Has coagulant CC activity, releasing fibrinopeptide A and B in the conversion of CC fibrinogen to fibrin. Also hydrolyzes N-p-toluensulfonyl arginine CC ester (TAME) and chromogenic artificial substrates of the blood CC coagulation cascade: S-2222 for factor Xa, S-2302 for kallikrein CC and S-2238 for thrombin. {ECO:0000269|PubMed:26227411}. CC -!- ENZYME REGULATION: Inhibited by Cu(2+) and, to a lesser extent, by CC Zn(2+) and Ba(2+). Not inhibited by Ca(2+) and Mg(2+). CC {ECO:0000269|PubMed:26227411}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=1.43 mM for TAME {ECO:0000269|PubMed:26227411}; CC Vmax=0.06 mmol/min/ug enzyme towards TAME CC {ECO:0000269|PubMed:26227411}; CC pH dependence: CC Activity is stable from pH 3.5 and 10.5. CC {ECO:0000269|PubMed:26227411}; CC Temperature dependence: CC Thermostable. Activity is stable after incubation at 100 degrees CC Celsius for 30 min. {ECO:0000269|PubMed:26227411}; 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=29474; Method=Electrospray; Range=1-238; CC Evidence={ECO:0000269|PubMed:26227411}; CC -!- SIMILARITY: Belongs to the peptidase S1 family. CC {ECO:0000255|SAAS:SAAS00559343}. CC -!- SIMILARITY: Contains 1 peptidase S1 domain. CC {ECO:0000255|RuleBase:RU363034}. 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 EMBL; LN651356; CEJ25501.1; -; mRNA. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR InterPro; IPR009003; Peptidase_S1_PA. 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; KW Secreted; Serine protease; Toxin. FT CHAIN 1 238 Thrombin-like enzyme collinein-1. FT {ECO:0000305}. FT /FTId=PRO_0000436478. FT DOMAIN 1 229 Peptidase S1. {ECO:0000255|PROSITE- FT ProRule:PRU00274}. FT ACT_SITE 43 43 Charge relay system. FT {ECO:0000255|PROSITE-ProRule:PRU00274}. FT ACT_SITE 88 88 Charge relay system. FT {ECO:0000255|PROSITE-ProRule:PRU00274}. FT ACT_SITE 184 184 Charge relay system. FT {ECO:0000255|PROSITE-ProRule:PRU00274}. FT DISULFID 7 141 {ECO:0000250|UniProtKB:Q9PSN3}. FT DISULFID 28 44 {ECO:0000255|PROSITE-ProRule:PRU00274}. FT DISULFID 78 236 {ECO:0000250|UniProtKB:Q9PSN3}. FT DISULFID 120 190 {ECO:0000255|PROSITE-ProRule:PRU00274}. FT DISULFID 152 169 {ECO:0000255|PROSITE-ProRule:PRU00274}. FT DISULFID 180 205 {ECO:0000255|PROSITE-ProRule:PRU00274}. SQ SEQUENCE 238 AA; 26664 MW; F0366AEBA3C760E3 CRC64; VIGGDECNIN EHNFLVALYE YWSQSFLCGG TLINGEWVLT AAHCDRKHIL IYVGVHDRSV QFDKEQRRFP KEKYFFNCRN NFTKWDKDIM LIRLNKPVSY SEHIAPLSLP SSPPIVGSVC RVMGWGTIKS PQETLPDVPH CANINLLDYE VCRTAHPQFR LPATIRILCA GVLEGGIDTC HRDSGGPLIC NGEFQGIVSW GDGSCAQPDK PALYSKVFDH LDWIQNIIAG SETVNCPS //