COL13A1 (collagen 13-alpha 1) is a 95 kDa member of the transmembrane group of the collagen family of proteins. It is a type II transmembrane glycoprotein that is expressed by multiple cell types, including fibroblasts, endothelial cells, and cardiac muscle. COL13A1 forms disulfide-linked homotrimers and participates in cell adhesion by binding to the integrin alpha 1 subunit, nidogen-2, and fibronectin. Human COL13A1 is 717 amino acids (aa) in length (SwissProt #:Q5TAT6). It has an N‑terminal 44 amino acid cytoplasmic region plus a 656 amino acid extracellular domain (ECD) (aa 62-717). The ECD contains four non-collagenous (NC) regions (aa 1‑121, 217-269, 442-463, and 700-717) interspersed among three collagenous (COL) domains (aa 122-216, 270-441, and 464-699). Multiple splice forms exist and typically involve deletions of 12-30 aa between aa 220-705. Proteolytic cleavage after Arg108 generates an 85-90 kDa soluble form. Over aa 109-668 (based on a human isoform [NP_542992} that shows a deletion of aa 239-260, 551-565, and 616-627), human COL13A1 shares 91% aa sequence identity with mouse COL13A1.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.