Sec14domaincontaining

Sec14domaincontaining refers to proteins that possess the Sec14 lipid-binding domain, a conserved module within the Sec14 superfamily. Members are found across eukaryotes, including fungi, plants, animals, and some protists, and the domain is typically located in the cytosol with association to membrane surfaces such as the Golgi apparatus.

These proteins function primarily as lipid transfer or lipid-binding regulators that influence membrane trafficking and phospholipid signaling. In yeast, Sec14p is essential for Golgi function and vesicle formation, acting as a lipid chaperone that modulates the availability of phosphatidylinositol and phosphatidylcholine, thereby impacting phosphoinositide metabolism and secretory processes. In other organisms, Sec14 domain-containing proteins may regulate lipid homeostasis, vesicle dynamics, and interactions with lipid kinases or trafficking factors, with functions that can vary among family members.

Structurally, most Sec14 domain-containing proteins feature a canonical Sec14 lipid-binding domain of roughly 250–320 amino acids. They are often complemented by additional domains or extensions that provide localization signals or regulatory capabilities. The Sec14-containing family is diverse in its domain architecture and tissue or cell-type expression patterns, and mammals in particular have a subset of Sec14-like proteins (often designated as SEC14L family members) with distinct roles.

As a terminology, Sec14domaincontaining serves as a functional descriptor used in annotations to identify proteins that harbor the Sec14 domain rather than as a single gene symbol. Ongoing research aims to clarify the specific lipid cargos, interaction networks, and cellular roles of individual family members across species.