Type I collagen is a member of group I collagen (fibrillar forming collagen). Trimers of one alpha 2(I) and two alpha 1(I) chains. Expressed in bones. Contains mostly 4-hydroxyproline. Proline residues at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. Contains 3-hydroxyproline at a few sites. This modification occurs on the first proline residue in the sequence motif Gly-Pro-Hyp, where Hyp is 4-hydroxyproline. Lysine residues at the third position of the tripeptide repeating unit (G-X-Y) are 5-hydroxylated in some or all of the chains. O-glycosylated on hydroxylated lysine residues. The O-linked glycan consists of a Glc-Gal disaccharide. These protein fragments were extracted from an ancient pelvis bone collected in Newburgh, New York, USA and estimated to be around 11255 years old. Belongs to the fibrillar collagen family.