SEC14-like protein (SEC14L)

SEC14-like proteins are a family of lipid-binding proteins characterized by the presence of a CRAL-TRIO domain, which allows them to sequester and transport small lipophilic molecules (InterPro IPR001251). These proteins play a vital role in regulating intracellular lipid trafficking and signaling, particularly involving phospholipids, cholesterol, and alpha-tocopherol (UniProt P55058). For example, SEC14L2, also known as supernatant protein factor (SPF), is essential for the conversion of squalene to lanosterol in cholesterol biosynthesis and facilitates the transport of Vitamin E (PubMed: 11514546). In the context of disease, SEC14-like proteins have been identified as key players in cancer progression, where SEC14L1 is often overexpressed and correlates with poor prognosis in prostate and breast cancers (PubMed: 25103495). Additionally, SEC14L2 has been shown to be a critical host factor for Hepatitis C virus (HCV) replication, making it a potential target for antiviral therapy (PubMed: 22438551). Therapeutic strategies targeting these proteins often focus on inhibiting their lipid-binding capacity or modulating their expression to disrupt downstream signaling pathways.

Other names

SEC14 domain-containing proteinCRAL-TRIO domain-containing proteinSupernatant protein factor familySPF familyAlpha-tocopherol transfer protein-like

SEC14-like proteins function by binding specific lipid ligands within their hydrophobic CRAL-TRIO domain, facilitating their transfer between membranes and modulating the activity of lipid-metabolizing enzymes or signaling proteins (InterPro IPR001251, PubMed: 11514546).