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Any constituent part of the cytoskeleton, a cellular scaffolding or skeleton that maintains cell shape, enables some cell motion (using structures such as flagella and cilia), and plays important roles in both intra-cellular transport (e.g. the movement of vesicles and organelles) and cellular division. Includes constituent parts of intermediate filaments, microfilaments, microtubules, and the microtrabecular lattice. A myosin complex containing one or more class XII myosin heavy chains and associated light chains; myosin XII contains a large tail region with two MyTH4 domains and a short region of coiled coil. A myosin complex containing one or more class XIII myosin heavy chains and associated light chains. A myosin complex containing one or more class X myosin heavy chains and associated light chains. A myosin complex containing a dimer of class XI myosin heavy chains and associated light chains. Myosin XI heavy chain sizes are similar in molecular structure to the class V myosins with 5 to 6 IQ motifs and tail regions with predicted coiled coil domains (forming dimeric molecules) and large C-terminal regions. A protein complex, formed of one or more myosin heavy chains plus associated light chains and other proteins, that functions as a molecular motor; uses the energy of ATP hydrolysis to move actin filaments or to move vesicles or other cargo on fixed actin filaments; has magnesium-ATPase activity and binds actin. Myosin classes are distinguished based on sequence features of the motor, or head, domain, but also have distinct tail regions that are believed to bind specific cargoes. The part of the cytoskeleton (the internal framework of a cell) composed of actin and associated proteins. Includes actin cytoskeleton-associated complexes. A myosin complex containing a class III myosin heavy chain and associated light chains; myosin III is monomeric myosin that serves as a link between the cytoskeleton and the signaling complex involved in phototransduction, and differs from all other myosins in having an N-terminal kinase domain. A myosin complex containing a class XVIII myosin heavy chain and associated light chains; myosin XVIII heavy chains contain an N-terminal PDZ domain. Any macromolecular complex composed of two or more polypeptide subunits, which may or may not be identical. Protein complexes may have other associated non-protein prosthetic groups, such as nucleotides, metal ions or other small molecules. A portmanteau term for myosins other than myosin II. A myosin complex containing a class XIV myosin heavy chain and associated light chains; myosin XIV heavy chains are the simplest known, containing a motor domain, no classic IQ motif and variable length tails. A myosin complex containing a class XV myosin heavy chain and associated light chains. Myosin XV is single headed, and has a large extension (1200aa) at the N-terminus of the motor domain, two IQ motifs and a tail with a similar domain structure to that of the tail of myosin VII. A myosin complex containing a class XVI myosin heavy chains and associated light chains; myosin XVI heavy chains contain ankyrin repeat. A myosin complex containing a class I myosin heavy chain and associated light chains; myosin I heavy chains are single-headed, possess tails of various lengths, and do not self-associate into bipolar filaments; myosin I complexes are involved in diverse processes related to membrane traffic and cell movement. A myosin complex containing one or more class XVII myosin heavy chains and associated light chains. A myosin complex containing one or more class VI myosin heavy chains and associated light chains. Myosin VI has a single IQ motif in the neck and a tail region with a coiled coil domain followed by a unique globular domain; a unique insertion that enables myosin VI to move towards the pointed or minus end of actin filaments. A myosin complex containing a dimer of class V myosin heavy chains and associated light chains; involved in intracellular transport. Myosin V is a dimeric molecule consisting of conserved motor domains followed by 6 IQ motifs which bind specific light chains and calmodulin. The tail domain is important for cellular localization and cargo binding and can be divided into an alpha-helical coiled coil region and a C-terminal globular region. A myosin complex containing one or more class IV myosin heavy chains and associated light chains; myosin IV is relatively uncharacterized, but is predicted to have a single motor domain, one IQ motif and a tail with a Myosin Tail Homology (myTH4) domain homologous to that in the tails of myosins VII and XV. A myosin complex containing a class IX myosin heavy chain and associated light chains. Myosin IX is monomeric with a motor domain containing an N-terminal extension and an insert in the actin binding interface, followed by four to six IQ motifs and a tail region that contains a zinc binding motif and a domain with homology to GTPase activating proteins (GAPs) of the Rho family of G-proteins. A myosin complex containing a dimer of class VIII myosin heavy chains and associated light chains. Myosin VIII is predicted to be dimeric, and contain an unusual 100-190 residue N-terminal extension prior to their motor domains, 3-4 IQ motifs, a short region (~70 residues) of predicted alpha-helical coiled coil and a C-terminal domain. A myosin complex containing a dimer of class VII myosin heavy chains and associated light chains. Myosin VII (240 kDa) is predicted to be a dimeric molecule with 5 IQ motifs and a tail region with a short stretch of coiled coil followed by two myosin-tail homology (MyTH4) domains, two talin-binding (FERM) domains and an SH3-domain.

View Gene Ontology (GO) Term

GO TERM SUMMARY
Name: unconventional myosin complex
Acc: GO:0016461
Aspect: Cellular Component
Desc: A portmanteau term for myosins other than myosin II.
Synonyms:
  • GO:0005860
  • non-muscle myosin
Proteins in PDR annotated with:
   This term: 19 [Search]
   Term or descendants: 31 [Search]


[geneontology.org]
INTERACTIVE GO GRAPH

GO:0016461 - unconventional myosin complex (interactive image map)
YRC Informatics Platform - Version 3.0
Created and Maintained by: Michael Riffle