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TPM4
Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments. Binds calcium. Belongs to the tropomyosin family. Detected in cardiac tissue and platelets, the form found in cardiac tissue is a higher molecular weight than the form found in platelets. Expressed at higher levels in the platelets of hypertensive patients with cardiac hypertrophy than in the platelets of hypertensive patients without cardiac hypertrophy (at protein level). 1 alternatively spliced human isoform has been reported. Note: This description may include information from UniProtKB.
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| Protein type: Motility/polarity/chemotaxis |
| Chromosomal Location of Human Ortholog: 19p13.12-p13.11 |
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Cellular Component:
cortical cytoskeleton; cytoskeleton; cytosol; muscle thin filament tropomyosin; podosome; stress fiber
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Molecular Function:
actin filament binding; calcium ion binding; identical protein binding; protein binding; protein heterodimerization activity; protein homodimerization activity; structural constituent of muscle
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Biological Process:
muscle contraction; muscle filament sliding
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Reference #:
P67936
(UniProtKB)
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Alt. Names/Synonyms: epididymis secretory protein Li 108; HEL-S-108; TM30p1; TPM4; tropomyosin 4; Tropomyosin alpha-4 chain; Tropomyosin-4
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Gene Symbols: TPM4
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Molecular weight:
28,522 Da
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Basal Isoelectric point:
4.67
Predict pI for various phosphorylation states
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CST Pathways:
Actin Dynamics
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