The complete primary structure of protein kinase C--the major phorbol ester receptor.
Protein kinase C, the major phorbol ester receptor, was purified from bovine brain and through the use of oligonucleotide probes based on partial amino acid sequence, complementary DNA clones were derived from bovine brain complementary DNA libraries. Thus, the complete amino acid sequence of bovine protein kinase C was determined, revealing a domain structure. At the amino terminal is a cysteine-rich domain with an internal duplication; a putative calcium-binding domain follows, and there is at the carboxyl terminal a domain that shows substantial homology, but not identity, to sequences of other protein kinase.
D000595:Amino Acid Sequence; D000818:Animals; D001921:Brain / Q000378:metabolism; D029742:Caenorhabditis elegans Proteins; D002352:Carrier Proteins; D002417:Cattle; D004247:DNA; D008956:Models, Chemical; D014176:Protein Biosynthesis; D011493:Protein Kinase C / Q000302:isolation & purification; D012333:RNA, Messenger / Q000378:metabolism; D011955:Receptors, Drug; D011971:Receptors, Immunologic
D029742:Caenorhabditis elegans Proteins; D002352:Carrier Proteins; D012333:RNA, Messenger; D011955:Receptors, Drug; D011971:Receptors, Immunologic; C083141:phorbol ester binding protein; C027776:phorbol ester receptor; D004247:DNA; D011493:Protein Kinase C