LamGLaminin G domain |
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| SMART accession number: | SM00282 |
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| Description: | |
| Interpro abstract (IPR001791): | Laminins are large heterotrimeric glycoproteins involved in basement membrane function (PUBMED:15037599). The laminin globular (G) domain can be found in one to several copies in various laminin family members, including a large number of extracellular proteins. The C-terminus of the laminin alpha chain contains a tandem repeat of five laminin G domains, which are critical for heparin-binding and cell attachment activity (PUBMED:10747011). Laminin alpha4 is distributed in a variety of tissues including peripheral nerves, dorsal root ganglion, skeletal muscle and capillaries; in the neuromuscular junction, it is required for synaptic specialisation (PUBMED:15823034). The structure of the laminin-G domain has been predicted to resemble that of pentraxin (PUBMED:9480764). Laminin G domains can vary in their function, and a variety of binding functions have been ascribed to different LamG modules. For example, the laminin alpha1 and alpha2 chains each have five C-teminal laminin G domains, where only domains LG4 and LG5 contain binding sites for heparin, sulphatides and the cell surface receptor dystroglycan (PUBMED:10747011). Laminin G-containing proteins appear to have a wide variety of roles in cell adhesion, signalling, migration, assembly and differentiation. Proteins with laminin-G domains include:
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| Family alignment: |
There are 4181 LamG domains in 1857 proteins in SMART's nrdb database.
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- Evolution (species in which this domain is found)
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- Disease (disease genes where sequence variants are found in this domain)
- Metabolism (metabolic pathways involving proteins which contain this domain)
- Structure (3D structures containing this domain)
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