Cloning and characterization of a cDNA encoding murine coagulation factor X. 1998

Z Liang, and A Cooper, and M E DeFord, and P Carmeliet, and D Collen, and F J Castellino, and E D Rosen
Department of Chemistry and Biochemistry and the Center for Transgene Research, University of Notre Dame, Indiana 46556, USA.

The cDNA encoding murine coagulation factor X (fX) was isolated and reconstructed from a lambdaZap cDNA library generated from murine liver mRNA. The cDNA contains 1486 bases starting at the 5'-translation initiation codon. It includes an open reading frame of 1443 nucleotides, followed by an 18 residue 3' nontranslated sequence downstream of the first stop codon. and a 3' poly(A) tail. The translation product is composed of a 40-amino acid signal/propeptide region followed by a 441-residue mature protein. The latter is highly homologous to that of human and rat fX. All protein domains of human and rat fX are strictly conserved in mouse fX. The cDNA coding for mouse fX has been expressed in human embryonic kidney 293 cells and generates fX activity measured in a clotting assay using human fX-deficient plasma.

UI MeSH Term Description Entries
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D002460 Cell Line Established cell cultures that have the potential to propagate indefinitely. Cell Lines,Line, Cell,Lines, Cell
D003001 Cloning, Molecular The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells. Molecular Cloning
D005170 Factor X Storage-stable glycoprotein blood coagulation factor that can be activated to factor Xa by both the intrinsic and extrinsic pathways. A deficiency of factor X, sometimes called Stuart-Prower factor deficiency, may lead to a systemic coagulation disorder. Autoprothrombin III,Coagulation Factor X,Stuart Factor,Stuart-Prower Factor,Blood Coagulation Factor X,Factor 10,Factor Ten,Stuart Prower Factor,Factor X, Coagulation
D005171 Factor X Deficiency Blood coagulation disorder usually inherited as an autosomal recessive trait, though it can be acquired. It is characterized by defective activity in both the intrinsic and extrinsic pathways, impaired thromboplastin time, and impaired prothrombin consumption. Deficiency, Factor 10,Deficiency, Factor Ten,Deficiency, Factor X,Deficiency, Stuart-Prower,Deficiency, Stuart-Prower Factor,Factor 10 Deficiency,Factor Ten Deficiency,Stuart-Prower Deficiency,Stuart-Prower Factor Deficiency,Deficiencies, Factor 10,Deficiencies, Factor Ten,Deficiencies, Factor X,Deficiency, Stuart Prower,Deficiency, Stuart Prower Factor,Factor 10 Deficiencies,Factor Ten Deficiencies,Factor X Deficiencies,Stuart Prower Deficiency,Stuart Prower Factor Deficiency,Ten Deficiencies, Factor
D005815 Genetic Code The meaning ascribed to the BASE SEQUENCE with respect to how it is translated into AMINO ACID SEQUENCE. The start, stop, and order of amino acids of a protein is specified by consecutive triplets of nucleotides called codons (CODON). Code, Genetic,Codes, Genetic,Genetic Codes
D006487 Hemostasis The process which spontaneously arrests the flow of BLOOD from vessels carrying blood under pressure. It is accomplished by contraction of the vessels, adhesion and aggregation of formed blood elements (eg. ERYTHROCYTE AGGREGATION), and the process of BLOOD COAGULATION. Hemostases
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia

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