The amino-terminal domain of thrombomodulin and pancreatic stone protein are homologous with lectins.
Amino acid sequence alignment of the amino-terminal of thrombomodulin and pancreatic stone protein with the hepatic asialoglycoprotein receptor shows that these proteins are homologous. From the known disulfide bridge pattern of other proteins belonging to the same family two disulfide bonds can be predicted. The homology raises the question whether the amino-terminal part of thrombomodulin and the pancreatic protein binds carbohydrate or perhaps like tetranectin have a specific affinity for other proteins.
Petersen
T E
TE
Department of Molecular Biology and Plant Physiology, University of Aarhus, Denmark.
D000595:Amino Acid Sequence; D000818:Animals; D037263:Asialoglycoprotein Receptor; D002135:Calcium-Binding Proteins / Q000235:genetics*; D006801:Humans; D051847:Lithostathine; D008969:Molecular Sequence Data; D009419:Nerve Tissue Proteins; D010750:Phosphoproteins / Q000235:genetics*; D011956:Receptors, Cell Surface / Q000235:genetics*; D011971:Receptors, Immunologic / Q000235:genetics*; D018179:Receptors, Thrombin; D012689:Sequence Homology, Nucleic Acid; D013045:Species Specificity; D013917:Thrombin / Q000378:metabolism*
D037263:Asialoglycoprotein Receptor; D002135:Calcium-Binding Proteins; D051847:Lithostathine; D009419:Nerve Tissue Proteins; D010750:Phosphoproteins; C497617:REG1A protein, human; D011956:Receptors, Cell Surface; D011971:Receptors, Immunologic; D018179:Receptors, Thrombin; D013917:Thrombin