Group:MUZIC:Enigma Family: Difference between revisions
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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> which is found in mouse and also identified by independent researchers who named it 'Oracle'<ref>PMID:10727866</ref>). Didactically, protein members of the enigma subfamily typically possess within their structure: '''(1)''' an N-terminal PDZ domain (a domain which is named after the 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 domain (a domain which is named after the first three proteins where it was characterized i.e. '''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 have been suggested to be important for targeting/sustaining interacting protein complexes within the 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> which is found in mouse and also identified by independent researchers who named it 'Oracle'<ref>PMID:10727866</ref>). Didactically, protein members of the enigma subfamily typically possess within their structure: '''(1)''' an N-terminal PDZ domain (a domain which is named after the 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 domain (a domain which is named after the first three proteins where it was characterized i.e. '''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 have been suggested to be important for targeting/sustaining interacting protein complexes within the sarcomere for a physiologically functional muscle. | ||
==Sequence | ==Sequence annotation and domain organization== | ||
'''''Enigma protein''''' | '''''Enigma protein''''' | ||
alternatively referred to as PDLIM7 (PDZ and LIM domain protein 7) is the first and representative member of the Enigma subfamily. Initially characterized in human as ~49.85 kDa protein with an N-terminal PDZ domain and three C-terminal LIM domains <ref>PMID:7929196</ref>, <ref>PMID:10359609</ref>. Five alternatively spliced isoforms are presently identified [http://www.uniprot.org/uniprot/Q9NR12#section_features] | alternatively referred to as PDLIM7 (PDZ and LIM domain protein 7) is the first and representative member of the Enigma subfamily. Initially characterized in human as ~49.85 kDa, 457 amino-acid protein with an N-terminal PDZ domain and three C-terminal LIM domains <ref>PMID:7929196</ref>, <ref>PMID:10359609</ref>. Five alternatively spliced isoforms are presently identified [http://www.uniprot.org/uniprot/Q9NR12#section_features] | ||
'''''Enigma Homologue (ENH) protein''''', also referred to as PDLIM5, is | '''''Enigma Homologue (ENH) protein''''', also referred to as PDLIM5, is ~67 kDa, 596-amino-acid human ortholog of rat ENH | ||
protein <ref>PMID:10429367</ref> with four alternatively spliced isoforms (UniProtKB: Q96HC4)[http://www.uniprot.org/uniprot/Q96HC4#section_alternative]. | protein <ref>PMID:10429367</ref> with four alternatively spliced isoforms (UniProtKB: Q96HC4)[http://www.uniprot.org/uniprot/Q96HC4#section_alternative]. | ||
'''''ZASP''''', also referred to as LIM domain-binding protein 3 (LDB-3), is the 78 kDa | '''''ZASP'''''('''Z'''-disk '''a'''lternatively '''s'''pliced '''P'''DZ domain protein), also referred to as LIM domain-binding protein 3 (LDB-3), is the 78 kDa, 727-amino-acid human ortholog of cypher, independently identified in heart and skeletal | ||
muscle<ref>PMID:10427098</ref>. Five alternatively spliced isoforms of ZASP have been identified (UniProtKB: O75112)[http://www.uniprot.org/uniprot/O75112#section_features)]. ZASP contains a motif (ZASP-like motif) which has been identified to interact with the spectrin repeats of α-actinin <ref>doi:10.1016/j.yexcr.2005.12.036</ref> | muscle<ref>PMID:10427098</ref>. Five alternatively spliced isoforms of ZASP have been identified (UniProtKB: O75112)[http://www.uniprot.org/uniprot/O75112#section_features)]. ZASP contains a motif (ZASP-like motif) which has been identified to interact with the spectrin repeats of α-actinin <ref>doi:10.1016/j.yexcr.2005.12.036</ref> | ||