SERPINH1

SERPINH1 (Serpin H1, better known as HSP47, also called colligin / gp46) is an endoplasmic reticulum-resident, collagen-specific molecular chaperone. Although it belongs to the serpin superfamily by fold, it is non-inhibitory and does not act as a protease inhibitor. In the ER lumen HSP47 binds specifically to the folded triple-helical region of procollagen, stabilizing the nascent triple helix, preventing local unfolding and premature aggregation, and serving as a quality-control factor in collagen biosynthesis. HSP47 accompanies procollagen from the ER to the ER-Golgi intermediate compartment/cis-Golgi, where the lower pH triggers its release; it then recycles back to the ER through its C-terminal RDEL retrieval signal. It is heat-shock inducible. Loss-of-function variants cause autosomal-recessive osteogenesis imperfecta type X (OI10), underscoring its essential role in collagen maturation.

Disorders

Relationship is the entry's genetic[].relationship_type. untyped means the entry has a genetic record for the gene but does not type it; its free-text association is shown instead.