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PMID:1333192
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| Citation |
Morén, A, Ichijo, H and Miyazono, K (1992) Molecular cloning and characterization of the human and porcine transforming growth factor-beta type III receptors. Biochem. Biophys. Res. Commun. 189:356-62 |
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| Abstract |
Full-length cDNAs for the transforming growth factor-beta (TGF-beta) type III receptors were isolated from porcine uterus and human placenta cDNA libraries. The human TGF-beta type III receptor coding region encodes a protein of 849 amino acids with a single transmembrane domain and a short stretch of the intracellular domain. Potential glycosaminoglycan attachment sites were found in the extracellular domain. The overall amino acid sequence identities with those of the porcine and rat TGF-beta type III receptors were 83% and 81%, respectively. A high degree of sequence conservation was observed in the transmembrane and intracellular domains, which also have sequence similarity with human endoglin. In addition, two portions with 29 and 52 amino acids in the extracellular domain were found to be substantially similar with human endoglin. |
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| Keywords |
Amino Acid Sequence; Animals; Antigens, CD; Base Sequence; Cloning, Molecular; DNA/genetics; DNA/isolation & purification; Female; Gene Library; Humans; Membrane Glycoproteins/genetics; Molecular Sequence Data; Placenta/physiology; Polymerase Chain Reaction/methods; Pregnancy; Receptors, Cell Surface/genetics; Receptors, Cell Surface/metabolism; Receptors, Transforming Growth Factor beta; Sequence Homology, Amino Acid; Swine; Transforming Growth Factor beta/metabolism; Uterus/physiology; Vascular Cell Adhesion Molecule-1 |
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