Group:MUZIC:Enigma Family: Difference between revisions

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==Enigma family: PDZ/LIM-domain proteins of the cytoskeleton==

Three member proteins have extensively been described and characterized within this subfamily: '''Enigma''' protein, '''Enigma Homologue''' (ENH) protein and '''ZASP/Cypher/Oracle''' (ZASP<ref>PMID:10427098</ref> being the human orthologue of cypher<ref>PMID:10391924</ref> in mouse, also identified by independent researchers as oracle<ref>PMID:10727866</ref>). The family name - ''Enigma'' - possibly was inspired by the intricately complicated splice isoforms identified in the ~~each~~ member ~~protein with~~ redundant, indinstinct functions. Didactically, protein members of the enigma subfamily typically possess within their structure: '''(1)''' an N-terminal PDZ domain (named after first three proteins where it was initially characterized i.e. '''P'''SD 95, '''D'''isc large protein and '''Z'''onula Occludens 1), and '''(2)''' three C-terminal LIM domains (a domain named after first three proteins where it was identified '''L'''in-11, '''I'''sl1 and '''M'''ec-3)<ref>PMID:20042479</ref>. The member proteins have all been located to the mammalian muscle cells, some specific to the heart and skeletal muscle Z-disk. They interact via their PDZ domains with motor protein components of the Z-disk and also recruit signalling molecules via their LIM domains or internal motifs, for example ''ZM motif'' (ZASP-like motif which is sandwiched between the PDZ- and LIM-domains in ZASP)<ref>doi:10.1161/CIRCRESAHA.110.225615</ref>. These interactions via their PDZ- and LIM-domains suggest roles important for targeting/sustaining interacting protein complexes within the myofibrillar sarcomere for a physiologically functional muscle.

Three member proteins have extensively been described and characterized within this subfamily: '''Enigma''' protein, '''Enigma Homologue''' (ENH) protein and '''ZASP/Cypher/Oracle''' (ZASP<ref>PMID:10427098</ref> being the human orthologue of cypher<ref>PMID:10391924</ref> in mouse, also identified by independent researchers as oracle<ref>PMID:10727866</ref>). The family name - ''Enigma'' - possibly was inspired by the intricately complicated splice isoforms identified in the first member, a common feature in all member proteins, as well as their redundant, indinstinct functions in the cytoskeleton. Didactically, protein members of the enigma subfamily typically possess within their structure: '''(1)''' an N-terminal PDZ domain (named after first three proteins where it was initially characterized i.e. '''P'''SD 95, '''D'''isc large protein and '''Z'''onula Occludens 1), and '''(2)''' three C-terminal LIM domains (a domain named after first three proteins where it was identified '''L'''in-11, '''I'''sl1 and '''M'''ec-3)<ref>PMID:20042479</ref>. The member proteins have all been located to the mammalian muscle cells, some specific to the heart and skeletal muscle Z-disk. They interact via their PDZ domains with motor protein components of the Z-disk and also recruit signalling molecules via their LIM domains or internal motifs, for example ''ZM motif'' (ZASP-like motif which is sandwiched between the PDZ- and LIM-domains in ZASP)<ref>doi:10.1161/CIRCRESAHA.110.225615</ref>. These interactions via their PDZ- and LIM-domains suggest roles important for targeting/sustaining interacting protein complexes within the myofibrillar sarcomere for a physiologically functional muscle.

==Sequence annotation and domain organization==

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 ==Enigma family: PDZ/LIM-domain proteins of the cytoskeleton==
-Three member proteins have extensively been described and characterized within this subfamily: '''Enigma''' protein, '''Enigma Homologue''' (ENH) protein and '''ZASP/Cypher/Oracle''' (ZASP<ref>PMID:10427098</ref> being the human orthologue of cypher<ref>PMID:10391924</ref> in mouse, also identified by independent researchers as oracle<ref>PMID:10727866</ref>). The family name - ''Enigma'' - possibly was inspired by the intricately complicated splice isoforms identified in the each member protein with redundant, indinstinct functions. Didactically, protein members of the enigma subfamily typically possess within their structure: '''(1)''' an N-terminal PDZ domain (named after first three proteins where it was initially characterized i.e. '''P'''SD 95, '''D'''isc large protein and '''Z'''onula Occludens 1), and '''(2)''' three C-terminal LIM domains (a domain named after first three proteins where it was identified '''L'''in-11, '''I'''sl1 and '''M'''ec-3)<ref>PMID:20042479</ref>. The member proteins have all been located to the mammalian muscle cells, some specific to the heart and skeletal muscle Z-disk. They interact via their PDZ domains with motor protein components of the Z-disk and also recruit signalling molecules via their LIM domains or internal motifs, for example ''ZM motif'' (ZASP-like motif which is sandwiched between the PDZ- and LIM-domains in ZASP)<ref>doi:10.1161/CIRCRESAHA.110.225615</ref>. These interactions via their PDZ- and LIM-domains suggest roles important for targeting/sustaining interacting protein complexes within the myofibrillar sarcomere for a physiologically functional muscle.
+Three member proteins have extensively been described and characterized within this subfamily: '''Enigma''' protein, '''Enigma Homologue''' (ENH) protein and '''ZASP/Cypher/Oracle''' (ZASP<ref>PMID:10427098</ref> being the human orthologue of cypher<ref>PMID:10391924</ref> in mouse, also identified by independent researchers as oracle<ref>PMID:10727866</ref>). The family name - ''Enigma'' - possibly was inspired by the intricately complicated splice isoforms identified in the first member, a common feature in all member proteins, as well as their redundant, indinstinct functions in the cytoskeleton. Didactically, protein members of the enigma subfamily typically possess within their structure: '''(1)''' an N-terminal PDZ domain (named after first three proteins where it was initially characterized i.e. '''P'''SD 95, '''D'''isc large protein and '''Z'''onula Occludens 1), and '''(2)''' three C-terminal LIM domains (a domain named after first three proteins where it was identified '''L'''in-11, '''I'''sl1 and '''M'''ec-3)<ref>PMID:20042479</ref>. The member proteins have all been located to the mammalian muscle cells, some specific to the heart and skeletal muscle Z-disk. They interact via their PDZ domains with motor protein components of the Z-disk and also recruit signalling molecules via their LIM domains or internal motifs, for example ''ZM motif'' (ZASP-like motif which is sandwiched between the PDZ- and LIM-domains in ZASP)<ref>doi:10.1161/CIRCRESAHA.110.225615</ref>. These interactions via their PDZ- and LIM-domains suggest roles important for targeting/sustaining interacting protein complexes within the myofibrillar sarcomere for a physiologically functional muscle.
 ==Sequence annotation and domain organization==