ID A0A0S4FKT4_CRODO Unreviewed; 238 AA. AC A0A0S4FKT4; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Mature snake venom serine protease {ECO:0000313|EMBL:CEJ25501.1}; DE Flags: Fragment; GN Name=Collinein-1 {ECO:0000313|EMBL:CEJ25501.1}; 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:0000313|EMBL:CEJ25501.1}; RN [1] {ECO:0000313|EMBL:CEJ25501.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Venom gland {ECO:0000313|EMBL:CEJ25501.1}; RA Tripathy S.; RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CEJ25501.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Venom gland {ECO:0000313|EMBL:CEJ25501.1}; RX PubMed=26227411; DOI=10.1007/s00253-015-6836-2; RA Boldrini-Franca J., Rodrigues R.S., 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 RT collilineatus venom in Pichia pastoris and functional comparison with RT the native enzyme."; RL Appl. Microbiol. Biotechnol. 99:9971-9986(2015). CC -!- SIMILARITY: Belongs to the peptidase S1 family. CC {ECO:0000256|SAAS:SAAS00559343}. CC -!- SIMILARITY: Contains 1 peptidase S1 domain. CC {ECO:0000256|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: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 2: Evidence at transcript level; KW Disulfide bond {ECO:0000256|SAAS:SAAS00037407}; KW Hydrolase {ECO:0000313|EMBL:CEJ25501.1}; KW Protease {ECO:0000313|EMBL:CEJ25501.1}. FT DOMAIN 1 229 Peptidase S1. {ECO:0000259|PROSITE: FT PS50240}. FT NON_TER 1 1 {ECO:0000313|EMBL:CEJ25501.1}. FT NON_TER 238 238 {ECO:0000313|EMBL:CEJ25501.1}. 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 //