Leprecan family TPR-like repeat region
PF23557
Definition
This entry represents the alpha-helical N-terminal alpha helical domain of members of the leprecan family. Members of this family often have an associated C-terminal enzymatic domain. The Leprecan family proteins are involved in the hydroxylation of proline residues in collagen, an essential post-translational modification for the stability and assembly of collagen fibrils. Members of this family form complexes with other enzymes to hydroxylate lysine residues in collagen alpha chains, which is crucial for the proper assembly and cross-linking of collagen fibrils in various tissues, including skin, bone, tendon, aorta, and cornea. Some family members also exhibit growth suppressive activity and may play a role in the secretory pathway of cells. The family's enzymatic activity is particularly important for the structural integrity of type I, IV, and V collagens, contributing to normal bone density and skin stability.
5 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
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