TPM4
Domain
The molecule is in a coiled coil structure that is formed by 2 polypeptide chains. The sequence exhibits a prominent seven-residues periodicity.
Function
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 (By similarity). Binds calcium (PubMed:1836432). Plays a role in platelet biogenesis.
Involvement in disease
Bleeding disorder, platelet-type, 25
BDPLT25
An autosomal dominant disorder characterized by increased bleeding tendency due to decreased or dysfunctional platelets. Platelet morphologic and functional defects are variable. Some individuals have normal numbers of enlarged platelets.
None
The disease is caused by variants affecting the gene represented in this entry.
Sequence Similarities
Belongs to the tropomyosin family.
Tissue Specificity
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).
Cellular localization
- Cytoplasm
- Cytoskeleton
- Associates with F-actin stress fibers.
Alternative names
Tropomyosin alpha-4 chain, TM30p1, Tropomyosin-4, TPM4