[2] LIM is a protein interaction domain that is involved in binding to many structurally and functionally diverse partners.

[1] The LIM domain appeared in eukaryotes sometime prior to the most recent common ancestor of plants, fungi, amoeba and animals.

These LIM domains have divergent amino acid sequences apart from certain key residues involved in zinc binding, which facilitate the formation of a stable protein core and tertiary fold.

The sequence variation between different LIM domains may be due to the evolution of novel binding sites for diverse partners on top of the conserved stable core.

LIM-domain containing proteins have been shown to play roles in cytoskeletal organization, organ development, regulation of plant cell development, cell lineage specification, and regulation of gene transcription.

[6] LIM proteins are also implicated in a variety of heart and muscle conditions, oncogenesis, neurological disorders and other diseases.

However a large subset of LIM proteins are recruited to actin cytoskeletal structures that are under a mechanical load.

Direct force-activated F-actin binding by LIM recruits LIM domain proteins to stressed cytoskeletal networks[7] and is an example of a mechanosensing mechanism by which cytoskeletal tension governs mechanical homeostasis,[8] nuclear localization,[9] gene expression, and other cellular physiology.

The LIM superclass of genes have been classified into 14 classes: ABLIM, CRP, ENIGMA, EPLIN, LASP, LHX, LMO, LIMK, LMO7, MICAL, PXN, PINCH, TES, and ZYX.

Some versions show fusions to an inactive P-loop NTPase at their N-terminus and a single transmembrane helix.

[6] The subclasses for these domains are LIM-homeodomain transcription factors, LMO proteins, and LIM kinases.

[4][6] The nervous system relies on the LIM domain type for differentiation of neurotransmitter biosynthetic pathways.

[4] These proteins focus on overall development of multiple cell types as well as oncogenesis and transcriptional regulation.

[6] These are considered adaptor proteins related to adhesion plaques that regulate cell shape and spreading through distinct LIM-mediated protein-protein interactions.

[6] Zyxin has a variety of bind partners such as CRP, α-actinin, proto-oncogene Vav, p130, and members of Ena/VASP family of proteins.

[4] It is responsible for effecting specific muscle adherens junctions and mechanosensory functions of touch receptor neurons.

[4] The protein sequence in the LIM domains are linked with very short interdomain peptides and c-terminal extension with high amounts of positive charges.