Insulin-like growth factor II receptor as a multifunctional binding protein.
The primary structure of human insulin-like growth factor II receptor, predicted from the complementary DNA sequence, reveals a transmembrane receptor molecule with a large extracellular domain made up of fifteen repeat sequences and a small region homologous to the collagen-binding domain of fibronectin. The structural and biochemical features of the IGF-II receptor appear identical to those of the cation-independent mannose-6-phosphate receptor.
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002352:Carrier Proteins; D004247:DNA / Q000235:genetics; D004274:DNA, Recombinant; D006801:Humans; D008565:Membrane Proteins; D009865:Oocytes / Q000378:metabolism; D051381:Rats; D017527:Receptor, IGF Type 2; D011972:Receptor, Insulin / Q000096:biosynthesis / Q000235:genetics / Q000302:isolation & purification; D017451:Receptors, Somatomedin; D012091:Repetitive Sequences, Nucleic Acid; D012689:Sequence Homology, Nucleic Acid; D014982:Xenopus laevis
D002352:Carrier Proteins; D004274:DNA, Recombinant; D008565:Membrane Proteins; D017527:Receptor, IGF Type 2; D017451:Receptors, Somatomedin; D004247:DNA; D011972:Receptor, Insulin