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SCO-spondin

SCO-Spondin is a large protein that exists in most chordates and is encoded in humans by the SSPO gene. SCO-Spondin is a glycoprotein which is over 550 kDa in size. SCO-Spondin is a matricellular protein, secreted by the subcommissural organ (SCO) located beneath the posterior commissure located at the entrance of the Sylvian aqueduct, into the cerebrospinal fluid (CSF). SCO-spondin has the binding features of an LDL-binding protein. SCO-spondin has been characterized in zebrafish, mouse, and birds.

Functions
SCO-spondin's function is incompletely characterized, but is believed to be involved in formation of Reissner's fibers (RF). This process involves a continuous deposition, aggregation and disaggregation of the SCO-spondin along the RF length. Early in development, SCO-spondin also plays a role in modulation of neural differentiation. The secretion of SCO-spondin influences the rate of RF growth, which varies considerably between species. Human SCO-spondin is poorly researched, and any role in adult human brains remains unknown. It has been observed in the fetal and infancy stages of humans. == Domains and structure ==
Domains and structure
SCO-spondin contains dozens of tandem domains, including thrombospondin-like repeat (TSR), vWF-C, EGF-like, and LDL receptor A. It also includes an elastin microfibril interface (EMI) domain at the N-terminus and a C-terminal cystine knot (CTCK) domain at the C-terminus. and protein-protein interactions, possibly suggesting a role of SCO-spondin in forming intermolecular aggregates with other CSF proteins containing this domain. the voltage gated potassium channel Kv2.1 can regulate the assembly of SCO-spondin and its bundling into the Reissner fibers. == History ==
History
SCO-spondin was first discovered in 1996 == References ==
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