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InterPro: IPR000533 Tropomyosin

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UniProtKB
Matches:
632 proteins
AccessionHelp IPR000533 Tropomyosin
TypeHelp Family
SignaturesHelp
InterPro annotation
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AbstractHelp

Tropomyosins [1], 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 [2]. 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 [3]. 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.

Some of the proteins in this family are allergens. Allergies are hypersensitivity reactions of the immune system to specific substances called allergens (such as pollen, stings, drugs, or food) that, in most people, result in no symptoms. A nomenclature system has been established for antigens (allergens) that cause IgE-mediated atopic allergies in humans [WHO/IUIS Allergen Nomenclature Subcommittee King T.P., Hoffmann D., Loewenstein H., Marsh D.G., Platts-Mills T.A.E., Thomas W. Bull. World Health Organ. 72:797-806(1994)]. This nomenclature system is defined by a designation that is composed of the first three letters of the genus; a space; the first letter of the species name; a space and an arabic number. In the event that two species names have identical designations, they are discriminated from one another by adding one or more letters (as necessary) to each species designation.

The allergens in this family include allergens with the following designations: Met e 1.

Structural linksHelp
SCOP: h.1.5.1 , k.31.1.1
CATH: 1.20.5.170
Database linksHelp
PDBe-motif: PS00326
PROSITE doc: PDOC00290
PANDIT: PF00261
Blocks: IPB000533

Taxonomic coverageHelp

Example proteinsHelp
A6NL28 Putative tropomyosin alpha-3 chain-like protein

P04268 Tropomyosin alpha-1 chain

P06754 Tropomyosin-1, isoforms 9A/A/B

P21107 Tropomyosin alpha-3 chain

Q22866 Tropomyosin isoforms a/b/d/f

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR000533 Tropomyosin
SWISS-MODEL
PDB Chain
ModBase
SCOP Domain
CATH Domain

PublicationsHelp
1. MacLeod AR.
Genetic origin of diversity of human cytoskeletal tropomyosins.
Bioessays 6 208-12 1987 [PubMed: 3606587]
http://dx.doi.org/10.1002/bies.950060504
2. Wolska BM, Wieczorek DM.
The role of tropomyosin in the regulation of myocardial contraction and relaxation.
Pflugers Arch. 446 1-8 2003 [PubMed: 12690456]
3. Lewis WG, Smillie LB.
The amino acid sequence of rabbit cardiac tropomyosin.
J. Biol. Chem. 255 6854-9 1980 [PubMed: 6993480]
http://intl.jbc.org/cgi/reprint/255/14/6854.pdf

Additional ReadingHelp
Greenfield NJ, Huang YJ, Palm T, Swapna GV, Monleon D, Montelione GT, Hitchcock-DeGregori SE.
Solution NMR structure and folding dynamics of the N terminus of a rat non-muscle alpha-tropomyosin in an engineered chimeric protein.
J. Mol. Biol. 312 2001 833-47 [PubMed: 11575936]
http://dx.doi.org/10.1006/jmbi.2001.4982
Greenfield NJ, Swapna GV, Huang Y, Palm T, Graboski S, Montelione GT, Hitchcock-DeGregori SE.
The structure of the carboxyl terminus of striated alpha-tropomyosin in solution reveals an unusual parallel arrangement of interacting alpha-helices.
Biochemistry 42 2003 614-9 [PubMed: 12534273]
http://dx.doi.org/10.1021/bi026989e
Greenfield NJ, Huang YJ, Swapna GV, Bhattacharya A, Rapp B, Singh A, Montelione GT, Hitchcock-DeGregori SE.
Solution NMR structure of the junction between tropomyosin molecules: implications for actin binding and regulation.
J. Mol. Biol. 364 2006 80-96 [PubMed: 16999976]
http://dx.doi.org/10.1016/j.jmb.2006.08.033
Whitby FG, Phillips GN Jr.
Crystal structure of tropomyosin at 7 Angstroms resolution.
Proteins 38 2000 49-59 [PubMed: 10651038]
http://dx.doi.org/10.1002/(SICI)1097-0134(20000101)38:1<49::AID-PROT6>3.3.CO;2-2
Brown JH, Zhou Z, Reshetnikova L, Robinson H, Yammani RD, Tobacman LS, Cohen C.
Structure of the mid-region of tropomyosin: bending and binding sites for actin.
Proc. Natl. Acad. Sci. U.S.A. 102 2005 18878-83 [PubMed: 16365313]
http://dx.doi.org/10.1073/pnas.0509269102
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