collagen 14 alpha-1 (undulin, COL14A1)
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Function
Structure
- homotrimer
- belongs to the fibril-associated collagens with interrupted helices (FACIT) family
- contains 8 fibronectin F3 modules
- contains 1 TSP N-terminal (TSPN) domain
- contains 2 VWFA domains
- associated with surface of interstitial collagen fibrils via COL1 domain (putative)
- COL2 domain serves as a rigid arm which sticks out from the fibril & protrudes the large N-terminal globular domain into the extracellular space, where it might interact with other matrix molecules or cell surface receptors (putative)
- large N-terminal globular interacts with other matrix molecules or cell surface receptors (putative)
- Lys at the 3rd position of the G-X-Y tripeptide repeats are hydroxylated; they bind carbohydrates
- Pro at the 3rd position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains
- may contain numerous Cys involved in intermolecular & intramolecular disulfide bonding
Compartment
Alternative splicing
named isoforms=3