Summary: Tropomyosin
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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 [1]. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organisation and dynamics of the cytoskeleton in non-muscle cells [2]. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes [3]. 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 [4].
Literature references
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Lewis WG, Smillie LB;, J Biol Chem. 1980;255:6854-6859.: The amino acid sequence of rabbit cardiac tropomyosin. PUBMED:6993480 EPMC:6993480
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Vindin H, Gunning P;, J Muscle Res Cell Motil. 2013;34:261-274.: Cytoskeletal tropomyosins: choreographers of actin filament functional diversity. PUBMED:23904035 EPMC:23904035
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Perry SV;, J Muscle Res Cell Motil. 2001;22:5-49.: Vertebrate tropomyosin: distribution, properties and function. PUBMED:11563548 EPMC:11563548
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MacLeod AR;, Bioessays. 1987;6:208-212.: Genetic origin of diversity of human cytoskeletal tropomyosins. PUBMED:3606587 EPMC:3606587
Internal database links
External database links
PRINTS: | PR00194 |
PROSITE: | PDOC00290 |
SCOP: | 2tma |
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 ].
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Pfam Clan
This family is a member of clan Tropomyosin-lke (CL0452), which has the following description:
The clan contains the following 3 members:
CLZ Tropomyosin Tropomyosin_1Alignments
We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...
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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.
Seed (17) |
Full (6955) |
Representative proteomes | UniProt (11108) |
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RP15 (709) |
RP35 (1692) |
RP55 (4661) |
RP75 (6861) |
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PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
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Seed (17) |
Full (6955) |
Representative proteomes | UniProt (11108) |
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RP15 (709) |
RP35 (1692) |
RP55 (4661) |
RP75 (6861) |
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Raw Stockholm | |||||||
Gzipped |
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
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Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
Seed source: | Prosite |
Previous IDs: | none |
Type: | Coiled-coil |
Sequence Ontology: | SO:0001080 |
Author: |
Finn RD |
Number in seed: | 17 |
Number in full: | 6955 |
Average length of the domain: | 206.5 aa |
Average identity of full alignment: | 63 % |
Average coverage of the sequence by the domain: | 77.69 % |
HMM information
HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
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Model details: |
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Model length: | 237 | ||||||||||||
Family (HMM) version: | 23 | ||||||||||||
Download: | download the raw HMM for this family |
Species distribution
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Structures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Tropomyosin domain has been found. There are 124 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.
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AlphaFold Structure Predictions
The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.