Laminin G domain (IPR001791)
Short name: Laminin_G
- Concanavalin A-like lectin/glucanase domain (IPR013320)
- Laminin G domain (IPR001791)
Laminins are large heterotrimeric glycoproteins involved in basement membrane function [PMID: 15037599]. The Laminin G or LNS domain (for Laminin-alpha, Neurexin and Sex hormone-binding globulin) is an around 180 amino acid long domain found in a large and diverse set of extracellular proteins [PMID: 1975589, PMID: 9480764]. 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 [PMID: 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 [PMID: 15823034]. The structure of the laminin-G domain has been predicted to resemble that of pentraxin [PMID: 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 [PMID: 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:
- Vitamin K dependent protein S.
- Sex steroid binding protein SBP/SHBG.
- Drosophila proteins Slit, Crumbs, Fat.
- several proteoglycan precursors.