Class I myosin, motor domain
IPR036072
Definition
Class I myosins are present in a wide range of species from yeast to man, and have been implicated in actin cytoskeleton organization, cell motility, and endocytosis [[cite:PMID:18344022], [cite:PMID:27401928]]. They are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. S. cerevisiae has two class I myosins, Myo3 and Myo5, whereas S. pombe has only Myo1 PMID:11294886. Vertebrates have eight class I myosin genes, six of which encode short-tailed forms (Myo1a, b, c, d, g, and h) and two of which encode long-tailed forms (Myo1e, f) PMID:18344022. Myosin I, an unconventional myosin, does not form dimers PMID:12471888. Myosin I consist of a N-terminal motor domain, a C-terminal tail homology domain (TH1), and in some cases additional C-terminal structures that can mediate protein-protein interactions. The class 1 myosin motor domain contains motifs that are conserved across the myosin superfamily, including an actin binding cleft and a nucleotide binding pocket. When ATP is present, the motor has a low affinity for actin. Attachment to actin is accompanied by a force generating conformational change, referred to as a 'working stroke' PMID:20471271.
8 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
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