COL14A1
Function
Plays an adhesive role by integrating collagen bundles. It is probably associated with the surface of interstitial collagen fibrils via COL1. The COL2 domain may then serve as a rigid arm which sticks out from the fibril and protrudes the large N-terminal globular domain into the extracellular space, where it might interact with other matrix molecules or cell surface receptors (By similarity).
Post-translational modifications
Lysines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in all cases and bind carbohydrates.
Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.
May contain numerous cysteine residues involved in inter- and intramolecular disulfide bonding.
Sequence Similarities
Belongs to the fibril-associated collagens with interrupted helices (FACIT) family.
Cellular localization
- Secreted
- Extracellular space
- Extracellular matrix
Alternative names
UND, COL14A1, Collagen alpha-1(XIV) chain, Undulin