The primary structure of coagulation factor IX/factor X-binding protein isolated from the venom of Trimeresurus flavoviridis. Homology with asialoglycoprotein receptors, proteoglycan core protein, tetranectin, and lymphocyte Fc epsilon receptor for immunoglobulin E.
An anticoagulant protein, factor IX/factor X-binding protein (IX/X-bp), isolated from the venom of Trimeresurus flavoviridis, binds with factor IX and factor X in the presence of Ca2+ with a 1 to 1 stoichiometry (Atoda, H., and Morita, T. (1989) J. Biochem. (Tokyo) 106, 808-813). Analysis of S-pyridylethylated IX/X-bp by sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed a 16.0-kDa band (designated the A chain) and a 15.5-kDa band (designated the B chain). These two chains were separated by reversed-phase high performance liquid chromatography, and their complete amino acid sequences were determined by sequencing of the peptides obtained after digestion with lysyl endopeptidase, chymotrypsin, and V8 protease from Staphylococcus aureus and after chemical cleavage with cyanogen bromide. The A chain had an amino-terminal sequence of Asp-Cys-Leu-Ser-Gly- and consisted of 129 residues with Mr 14,830. The B chain has an amino-terminal sequence of Asp-Cys-Pro-Ser-Asp- and consists of 123 residues of Mr 14,440. There was 47% identity between the A and the B chain. The sequence of IX/X-bp showed 25-37% identity with that of the C-type carbohydrate recognition domain-like structure of acorn barnacle lectin, human and rat asialoglycoprotein receptors, the human lymphocyte Fc epsilon receptor for immunoglobulin E, proteoglycan core protein, pancreatic stone protein, and tetranectin. The sequences of the first 18 amino acid residues of both the A and B chains were also, to a certain extent, homologous to the partial amino acid sequence of the b subunit of factor XIII, a member of the beta 2-glycoprotein I-like family. In this region, some similarity with the amino-terminal amino acid sequence of botrocetin was also observed.
Atoda
H
H
Department of Biochemistry, Meiji College of Pharmacy, Tokyo, Japan.
Hyuga
M
M
Morita
T
T
D053674:Aggrecans; D000595:Amino Acid Sequence; D000925:Anticoagulants / Q000737:chemistry*; D000944:Antigens, Differentiation, B-Lymphocyte / Q000737:chemistry*; D037263:Asialoglycoprotein Receptor; D001798:Blood Proteins / Q000737:chemistry*; D002352:Carrier Proteins / Q000737:chemistry* / Q000302:isolation & purification; D002851:Chromatography, High Pressure Liquid; D003435:Crotalid Venoms / Q000032:analysis*; D004591:Electrophoresis, Polyacrylamide Gel; D016326:Extracellular Matrix Proteins; D005164:Factor IX; D005170:Factor X; D006023:Glycoproteins / Q000737:chemistry*; D037181:Lectins, C-Type; D008969:Molecular Sequence Data; D011509:Proteoglycans; D011961:Receptors, Fc / Q000737:chemistry*; D017455:Receptors, IgE; D011971:Receptors, Immunologic / Q000737:chemistry*; D012091:Repetitive Sequences, Nucleic Acid; D030162:Reptilian Proteins; D016415:Sequence Alignment; D012689:Sequence Homology, Nucleic Acid
C508321:Acan protein, rat; D053674:Aggrecans; D000925:Anticoagulants; D000944:Antigens, Differentiation, B-Lymphocyte; D037263:Asialoglycoprotein Receptor; D001798:Blood Proteins; D002352:Carrier Proteins; D003435:Crotalid Venoms; D016326:Extracellular Matrix Proteins; D006023:Glycoproteins; D037181:Lectins, C-Type; D011509:Proteoglycans; D011961:Receptors, Fc; D017455:Receptors, IgE; D011971:Receptors, Immunologic; D030162:Reptilian Proteins; C029748:Trimeresurus venoms; C048648:tetranectin; C070302:factor IX-factor X-binding protein, Crotalinae; D005164:Factor IX; D005170:Factor X