Difference between revisions of "Kinase Subfamily DAPK"
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[[kinase classification|Kinase Classification]]: [[Kinase_Group_CAMK|Group CAMK]]: [[Kinase_Family_DAPK|Family DAPK]]: [[Kinase_Subfamily_DAPK|Subfamily DAPK]] | [[kinase classification|Kinase Classification]]: [[Kinase_Group_CAMK|Group CAMK]]: [[Kinase_Family_DAPK|Family DAPK]]: [[Kinase_Subfamily_DAPK|Subfamily DAPK]] | ||
| − | + | ||
====Evolution==== | ====Evolution==== | ||
| + | DAPK kinases are found in animals, including sponges, but lost from a number of lineages, including Drosophila and other dipterans, Trichoplax, and Nematostella. C. elegans has a single DRAK, K11C12.4/dapk-1, while mammals have three, DAPK1-3. | ||
====Domain Structure==== | ====Domain Structure==== | ||
| − | DAPK kinases have an N-terminal kinase domain and a variable C terminal extension. The ancestral state, found in human DAPK1 and nematode K12C11.4 has ankyrin repeat region followed by ROC and COR | + | DAPK kinases have an N-terminal kinase domain and a variable C terminal extension. The ancestral state, found in human DAPK1 and nematode K12C11.4 has ankyrin repeat region followed by ROC and COR domains and a death domain. Vertebrate DAPK2 and DAPK3 lack these additional domains. Several invertebrates, including all beetles and Aplysia appear to have lost just the kinase domain. A splice isoform of human DAPK1 lacks the kinase domain <cite>Lin</cite> and causes degradation of the full-length form, and C. elegans may also have splice isoforms (isoforms c, d) that lack the kinase domain. |
====Functions==== | ====Functions==== | ||
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====References==== | ====References==== | ||
| + | <biblio> | ||
| + | #Lin pmid=19267229 | ||
| + | </biblio> | ||
Latest revision as of 20:05, 16 March 2023
Kinase Classification: Group CAMK: Family DAPK: Subfamily DAPK
Evolution
DAPK kinases are found in animals, including sponges, but lost from a number of lineages, including Drosophila and other dipterans, Trichoplax, and Nematostella. C. elegans has a single DRAK, K11C12.4/dapk-1, while mammals have three, DAPK1-3.
Domain Structure
DAPK kinases have an N-terminal kinase domain and a variable C terminal extension. The ancestral state, found in human DAPK1 and nematode K12C11.4 has ankyrin repeat region followed by ROC and COR domains and a death domain. Vertebrate DAPK2 and DAPK3 lack these additional domains. Several invertebrates, including all beetles and Aplysia appear to have lost just the kinase domain. A splice isoform of human DAPK1 lacks the kinase domain [1] and causes degradation of the full-length form, and C. elegans may also have splice isoforms (isoforms c, d) that lack the kinase domain.
