Integrin Alpha 10 (ITGa10)

The predicted 1,167-amino acid human protein shares the general structure of alpha-integrin subunits, with a signal sequence, a large N-terminal extracellular domain with 7 conserved repeats, a transmembrane segment, and a short C-terminal cytoplasmic tail. Like some alpha-integrin subunits, alpha-10 also contains an approximately 200-amino acid insertion (I) domain. Camper et al. (1998) stated that the observed molecular weight of alpha-10 corresponds to the protein with carbohydrate chains attached at each of the 10 potential N-linked glycosylation sites. Coimmunoprecipitation studies indicated that alpha-10 forms a heterodimer with beta-1. Antibodies against alpha-10 immunostained the chondrocytes in human articular cartilage sections, indicating that the alpha-10/beta-1 integrin is expressed in cartilage.