Tropomyosin 3

Tropomyosin alpha-3 chain is a protein that in humans is encoded by the TPM3 gene.[5][6]

TPM3
Identifiers
Aliases	TPM3, CAPM1, CFTD, HEL-189, HEL-S-82p, NEM1, OK/SW-cl.5, TM-5, TM3, TM30, TM30nm, TM5, TPMsk3, TRK, hscp30, Tropomyosin 3, TPM3nu
External IDs	OMIM: 191030 MGI: 1890149 HomoloGene: 81889 GeneCards: TPM3
Gene location (Human) Chr. Chromosome 1 (human)[1] Band 1q21.3 Start 154,155,304 bp[1] End 154,194,648 bp[1]
Gene location (Mouse) Chr. Chromosome 3 (mouse)[2] Band 3|3 F1 Start 90,072,649 bp[2] End 90,100,902 bp[2]
Gene ontology Molecular function • actin binding • GO:0001948 protein binding • structural constituent of muscle • actin filament binding • molecular function Cellular component • cytoplasm • muscle thin filament tropomyosin • extracellular exosome • cytoskeleton • stress fiber • cytosol • actin filament • actin cytoskeleton Biological process • movement of cell or subcellular component • muscle filament sliding • muscle contraction • actin filament organization Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	7170	59069
Ensembl	ENSG00000143549	ENSMUSG00000027940
UniProt	P06753	P21107
RefSeq (mRNA)	NM_001043351 NM_001043352 NM_001043353 NM_001278188 NM_001278189 NM_001278190 NM_001278191 NM_152263 NM_153649 NM_001349679 NM_001364679 NM_001364680 NM_001364681 NM_001364682 NM_001364683	NM_001253738 NM_001253740 NM_001271764 NM_001293748 NM_001293749 NM_022314 NM_001357581
RefSeq (protein)	NP_001036816 NP_001036817 NP_001036818 NP_001265117 NP_001265118 NP_001265119 NP_001265120 NP_689476 NP_705935 NP_001336608 NP_001351608 NP_001351609 NP_001351610 NP_001351611 NP_001351612	NP_001240667 NP_001240669 NP_001258693 NP_001280677 NP_001280678 NP_071709 NP_001344510
Location (UCSC)	Chr 1: 154.16 – 154.19 Mb	Chr 3: 90.07 – 90.1 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

This gene encodes a member of the tropomyosin family of actin-binding proteins involved in the contractile system of striated and smooth muscles and the cytoskeleton of non-muscle cells. Tropomyosins are dimers of coiled-coil proteins that polymerize end-to-end along the major groove in most actin filaments. They provide stability to the filaments and regulate access of other actin-binding proteins. In muscle cells, they regulate muscle contraction by controlling the binding of myosin heads to the actin filament. Mutations in this gene result in autosomal dominant nemaline myopathy, and oncogenes formed by chromosomal translocations involving this locus are associated with cancer. Multiple transcript variants encoding different isoforms have been found for this gene.[6]

References

1. GRCh38: Ensembl release 89: ENSG00000143549 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000027940 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Morris CM, Hao QL, Heisterkamp N, Fitzgerald PH, Groffen J (Aug 1991). "Localization of the TRK proto-oncogene to human chromosome bands 1q23-1q24". Oncogene. 6 (6): 1093–5. PMID 1829807.
6. "Entrez Gene: TPM3 tropomyosin 3".

Further reading

• Lees-Miller JP, Helfman DM (1992). "The molecular basis for tropomyosin isoform diversity". BioEssays. 13 (9): 429–37. doi:10.1002/bies.950130902. PMID 1796905.
• Pittenger MF, Kazzaz JA, Helfman DM (1994). "Functional properties of non-muscle tropomyosin isoforms". Curr. Opin. Cell Biol. 6 (1): 96–104. doi:10.1016/0955-0674(94)90122-8. PMID 8167032.
• Gunning P, Weinberger R, Jeffrey P (1997). "Actin and tropomyosin isoforms in morphogenesis". Anat. Embryol. 195 (4): 311–5. doi:10.1007/s004290050050. PMID 9108196.
• Gunning PW, Schevzov G, Kee AJ, Hardeman EC (2006). "Tropomyosin isoforms: divining rods for actin cytoskeleton function". Trends Cell Biol. 15 (6): 333–41. doi:10.1016/j.tcb.2005.04.007. PMID 15953552.
• Rasmussen HH, van Damme J, Puype M, et al. (1993). "Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes". Electrophoresis. 13 (12): 960–9. doi:10.1002/elps.11501301199. PMID 1286667.
• Höner B, Shoeman RL, Traub P (1992). "Degradation of cytoskeletal proteins by the human immunodeficiency virus type 1 protease". Cell Biol. Int. Rep. 16 (7): 603–12. doi:10.1016/S0309-1651(06)80002-0. PMID 1516138.
• Winder SJ, Walsh MP (1990). "Smooth muscle calponin. Inhibition of actomyosin MgATPase and regulation by phosphorylation". J. Biol. Chem. 265 (17): 10148–55. PMID 2161834.
• Takahashi K, Hiwada K, Kokubu T (1988). "Vascular smooth muscle calponin. A novel troponin T-like protein". Hypertension. 11 (6 Pt 2): 620–6. doi:10.1161/01.hyp.11.6.620. PMID 2455687.
• Coulier F, Martin-Zanca D, Ernst M, Barbacid M (1989). "Mechanism of activation of the human trk oncogene". Mol. Cell. Biol. 9 (1): 15–23. doi:10.1128/mcb.9.1.15. PMC 362140. PMID 2538716.
• Martin-Zanca D, Hughes SH, Barbacid M (1986). "A human oncogene formed by the fusion of truncated tropomyosin and protein tyrosine kinase sequences". Nature. 319 (6056): 743–8. doi:10.1038/319743a0. PMID 2869410.
• Reinach FC, MacLeod AR (1986). "Tissue-specific expression of the human tropomyosin gene involved in the generation of the trk oncogene". Nature. 322 (6080): 648–50. doi:10.1038/322648a0. PMID 3018581.
• MacLeod AR, Houlker C, Reinach FC, Talbot K (1987). "The mRNA and RNA-copy pseudogenes encoding TM30nm, a human cytoskeletal tropomyosin". Nucleic Acids Res. 14 (21): 8413–26. doi:10.1093/nar/14.21.8413. PMC 311868. PMID 3024106.
• Clayton L, Reinach FC, Chumbley GM, MacLeod AR (1988). "Organization of the hTMnm gene. Implications for the evolution of muscle and non-muscle tropomyosins". J. Mol. Biol. 201 (3): 507–15. doi:10.1016/0022-2836(88)90633-X. PMID 3418707.
• MacLeod AR, Houlker C, Reinach FC, et al. (1986). "A muscle-type tropomyosin in human fibroblasts: evidence for expression by an alternative RNA splicing mechanism". Proc. Natl. Acad. Sci. U.S.A. 82 (23): 7835–9. doi:10.1073/pnas.82.23.7835. PMC 390864. PMID 3865200.
• Butti MG, Bongarzone I, Ferraresi G, et al. (1995). "A sequence analysis of the genomic regions involved in the rearrangements between TPM3 and NTRK1 genes producing TRK oncogenes in papillary thyroid carcinomas". Genomics. 28 (1): 15–24. doi:10.1006/geno.1995.1100. PMID 7590742.
• Laing NG, Wilton SD, Akkari PA, et al. (1995). "A mutation in the alpha tropomyosin gene TPM3 associated with autosomal dominant nemaline myopathy NEM1". Nat. Genet. 10 (2): 249. doi:10.1038/ng0695-249a. PMID 7663526.
• Laing NG, Wilton SD, Akkari PA, et al. (1995). "A mutation in the alpha tropomyosin gene TPM3 associated with autosomal dominant nemaline myopathy". Nat. Genet. 9 (1): 75–9. doi:10.1038/ng0195-75. PMID 7704029.
• Wilton SD, Eyre H, Akkari PA, et al. (1994). "Assignment of the human a-tropomyosin gene TPM3 to 1q22→q23 by fluorescence in situ hybridisation". Cytogenet. Cell Genet. 68 (1–2): 122–4. doi:10.1159/000133905. PMID 7956350.

External links

• GeneReviews/NCBI/NIH/UW entry on Nemaline Myopathy