Evolutionary origin of numerous kringles in human and simian apolipoprotein(a).
Human apolipoprotein(a) has a great size heterogeneity and consists of 38 kringle domains in the amino terminal and a serine protease domain in the carboxyl terminal. All but one kringle of apolipoprotein(a) are homologous to the fourth kringle of plasminogen. However, the 38th kringle resembles the fifth kringle of plasminogen and its seems to have been deleted in simian species. The phylogenetic trees suggest that an ancestral apolipoprotein(a) may have started with a duplicate of a plasminogen type protein. It also implies that deletion of the three kringles in the amino terminus followed, and that one of the remaining two kringles was duplicated in both human and simian species and the other was processed by a deletion in simian species after species separation. Thus, the number of kringles in other mammals not yet studied may vary considerably from species to species.
Ikeo
K
K
DNA Research Center, National Institute of Genetics, Mishima, Japan.
Takahashi
K
K
Gojobori
T
T
D000818:Animals; D001054:Apolipoproteins A / Q000737:chemistry* / Q000235:genetics; D005075:Biological Evolution; D002896:Chromosomes, Human, Pair 6; D006801:Humans; D008253:Macaca mulatta; D010958:Plasminogen / Q000737:chemistry / Q000235:genetics; D011487:Protein Conformation
D001054:Apolipoproteins A; D010958:Plasminogen