Leprecan-like alpha-helical domain

Definition

This entry represents the N-terminal α-helical domain of members of the leprecan family. Members of this family include Prolyl 3-hydroxylase 1/2/3 which often have an associated C-terminal enzymatic domain [[cite:PMID:10951563], [cite:PMID:18487197], [cite:PMID:27119146]]. This domain is also found in the Cartilage-associated protein CRTAP and in the Endoplasmic reticulum protein SC65 [[cite:PMID:17055431], [cite:PMID:27119146]]. Leprecan proteins are involved in the hydroxylation of proline residues in collagen, an essential post-translational modification for the stability and assembly of collagen fibrils. Leprecan proteins 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 Leprecan proteins also exhibit growth suppressive activity and may play a role in the secretory pathway of cells. Leprecan'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.

Download CSV (5 proteins: gene, accession, name)

• CRTAP
• P3H1
• P3H2
• P3H3
• P3H4