The catalytic subunit of pseutarin C, a group C prothrombin activator from the venom of Pseudonaja textilis, is structurally similar to mammalian blood coagulation factor Xa. Export

@article{citeulike:699519, abstract = {Pseutarin C, a group C prothrombin activator from Pseudonaja textilis venom, is a large protein complex consisting of catalytic and nonenzymatic subunits, which are functionally similar to the mammalian FXa-FVa complex. Here, we present the complete cDNA sequence of the catalytic subunit of pseutarin C. The cDNA of the catalytic subunit encodes a protein of 449 amino acids, which includes a 22-residue signal peptide, 18-residue propeptide and a mature protein of 409 amino acids. The deduced amino acid sequence shows 74-83\% identity to group D prothrombin activators from snake venom and approximately 42\% identity to mammalian FX and has identical domain structure. The precursor of the catalytic subunit of pseutarin C has several unique features.The activation peptide of the catalytic subunit of pseutarin C is significantly smaller (27 as compared to 52 residues in mammalian FX) and does not contain any glycosylation sites. Unlike coagulation FXa, Ser52 and Asn45 of the light and heavy chains are O- and N-glycosylated in pseutarin C catalytic sub-unit. There is a 12-residue insertion in pseutarin C catalytic sub-unit close to the region that is implicated in binding to FVa. This is the first sequence of the catalytic subunit of a group C prothrombin activator.}, address = {Protein Science Laboratory, Department of Biological Sciences, Faculty of Science, National University of Singapore, Singapore 117 543.}, author = {Rao, V. S. and Swarup, S. and Manjunatha Kini, R.}, citeulike-article-id = {699519}, citeulike-linkout-0 = {http://dx.doi.org/10.1267/THRO04090509}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/15351847}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=15351847}, doi = {10.1267/THRO04090509}, issn = {0340-6245}, journal = {Thromb Haemost}, keywords = {behe, blood-clotting, cooption, ic, id}, month = {September}, number = {3}, pages = {509--521}, posted-at = {2006-06-18 03:33:38}, priority = {2}, title = {The catalytic subunit of pseutarin C, a group C prothrombin activator from the venom of Pseudonaja textilis, is structurally similar to mammalian blood coagulation factor Xa.}, url = {http://dx.doi.org/10.1267/THRO04090509}, volume = {92}, year = {2004} }

TY - JOUR ID - citeulike:699519 L3 - citeulike-article-id:699519 N2 - Pseutarin C, a group C prothrombin activator from Pseudonaja textilis venom, is a large protein complex consisting of catalytic and nonenzymatic subunits, which are functionally similar to the mammalian FXa-FVa complex. Here, we present the complete cDNA sequence of the catalytic subunit of pseutarin C. The cDNA of the catalytic subunit encodes a protein of 449 amino acids, which includes a 22-residue signal peptide, 18-residue propeptide and a mature protein of 409 amino acids. The deduced amino acid sequence shows 74-83% identity to group D prothrombin activators from snake venom and approximately 42% identity to mammalian FX and has identical domain structure. The precursor of the catalytic subunit of pseutarin C has several unique features.The activation peptide of the catalytic subunit of pseutarin C is significantly smaller (27 as compared to 52 residues in mammalian FX) and does not contain any glycosylation sites. Unlike coagulation FXa, Ser52 and Asn45 of the light and heavy chains are O- and N-glycosylated in pseutarin C catalytic sub-unit. There is a 12-residue insertion in pseutarin C catalytic sub-unit close to the region that is implicated in binding to FVa. This is the first sequence of the catalytic subunit of a group C prothrombin activator. IS - 3 JF - Thromb Haemost SN - 0340-6245 AD - Protein Science Laboratory, Department of Biological Sciences, Faculty of Science, National University of Singapore, Singapore 117 543. EP - 521 TI - The catalytic subunit of pseutarin C, a group C prothrombin activator from the venom of Pseudonaja textilis, is structurally similar to mammalian blood coagulation factor Xa. VL - 92 SP - 509 KW - behe KW - blood-clotting KW - cooption KW - ic KW - id AU - Rao, VS AU - Swarup, S AU - Manjunatha Kini, R PY - 2004/09// UR - http://dx.doi.org/10.1267/THRO04090509 ER -