InterPro : IPR000533

Name  Tropomyosin Short Name  Tropomyosin
Type  Family Description  Tropomyosins [], 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 []. 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 []. 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 [].
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Proteins

InterPro protein domain ID --> Contigs

 

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4 Publications

First Author Title Year Journal Volume Pages
MacLeod AR Genetic origin of diversity of human cytoskeletal tropomyosins. 1987 Bioessays 6 208-12
Lewis WG The amino acid sequence of rabbit cardiac tropomyosin. 1980 J Biol Chem 255 6854-9
Wolska BM The role of tropomyosin in the regulation of myocardial contraction and relaxation. 2003 Pflugers Arch 446 1-8
Drees B Tropomyosin is essential in yeast, yet the TPM1 and TPM2 products perform distinct functions. 1995 J Cell Biol 128 383-92



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)