domain:The numerous interruptions in the triple helix may make this molecule either elastic or flexible.,function:May act as a cross-bridge between fibrils and other extracellular matrix molecules. Involved in skeletal myogenesis in the developing esophagus. May play a role in organization of the pericellular matrix or the sphinteric smooth muscle.,PTM:Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.,similarity:Belongs to the fibril-associated collagens with interrupted helices (FACIT) family.,similarity:Contains 1 TSP N-terminal (TSPN) domain.,subunit:Oligomer; disulfide-linked.,tissue specificity:Localized to vascular, neuronal, mesenchymal, and some epithelial basement membrane zones in umbilical cord.,
Secreted, extracellular space, extracellular matrix .
Localized to vascular, neuronal, mesenchymal, and some epithelial basement membrane zones in umbilical cord.
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