Summary: Tropomyosin like
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This family is a set of eukaryotic tropomyosins. Within the yeast Tmp1 and Tmp2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpmlp spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis . The family also contains higher eukaryote Tmp3 members.
Leung PS, Chen YC, Gershwin ME, Wong SH, Kwan HS, Chu KH;, J Allergy Clin Immunol. 1998;102:847-852.: Identification and molecular characterization of Charybdis feriatus tropomyosin, the major crab allergen. PUBMED:9819304 EPMC:9819304
Saarne T, Kaiser L, Rasool O, Huecas S, van Hage-Hamsten M, Gafvelin G;, Int Arch Allergy Immunol. 2003;130:258-265.: Cloning and characterisation of two IgE-binding proteins, homologous to tropomyosin and alpha-tubulin, from the mite Lepidoglyphus destructor. PUBMED:12740526 EPMC:12740526
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This tab holds annotation information from the InterPro database.
InterPro entry IPR000533
Tropomyosins [PUBMED:3606587], are a family of closely related proteins present in muscle and non-muscle cells. In striated muscle, tropomyosin mediate the interactions between the troponin complex and actin so as to regulate muscle contraction [PUBMED:12690456]. The role of tropomyosin in smooth muscle and non-muscle tissues is not clear. Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites [PUBMED:6993480]. There are multiple cell-specific isoforms, created by differential splicing of the messenger RNA from one gene, but the proportions of the isoforms vary between different cell types. Muscle isoforms of tropomyosin are characterised by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
This entry represents tropomyosin (Tmp) 1, 2 and 3. Within the yeast Tmp1 and Tmp2, biochemical and sequence analyses indicate that Tpm2 spans four actin monomers along a filament, whereas Tpm1 spans five. Despite its shorter length, Tpm2 can compete with Tpm1 for binding to F-actin. Over-expression of Tpm2 in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis [PUBMED:7844152].
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|Number in seed:||41|
|Number in full:||292|
|Average length of the domain:||117.90 aa|
|Average identity of full alignment:||33 %|
|Average coverage of the sequence by the domain:||58.23 %|
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build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||2|
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