Description

IPR026854 is a Vacuolar protein sorting-associated protein 13-like, N-terminal domain.

<p>This is the N-terminal chorein domain of VPS13 and ATG2 proteins, which is highly conserved. ATG2 proteins are involved in autophagosome assembly, playing a key role in nonvesicular lipid transfer [[cite:PUB00100863], [cite:PUB00100769], [cite:PUB00062177], [cite:PUB00100864]]. This domain has a scoop or taco shape whose concave surface is lined by hydrophobic residues which bind glycerophospholipids. This entry also includes human Bridge-like lipid transfer protein family member 3B (also known as UHRF1BP1L and SHIP164), which shares shares structural and lipid transfer properties with these proteins [[cite:PUB00101882], [cite:PUB00101861]].</p> <p>VPS13 proteins have been implicated in processes including vesicle fusion, autophagy, and actin regulation. They bind phospholipids and act as channels that mediate the transfer of lipids between membranes at organelle contact sites [[cite:PUB00100726], [cite:PUB00100766], [cite:PUB00100863]]. It has been proposed that members of this entry have the capacity to bind and likely transfer tens of glycerolipids at once. Yeast VPS13 acts at multiple cellular sites, namely the interface between mitochondria and the vacuole, on endosomes, on the nuclear-vacuole junction and the vacuole, depending on the carbon source and metabolic state. Most evidence showed that mammalian VPS13A, VPS13C and VPS13D localize at contacts between the ER and other organelles, i.e. VPS13A and VPS13D bridge the ER to mitochondria, VPS13C bridges the ER to late endosomes and lysosomes and VPS13B may localize to endosome-endosome contacts [[cite:PUB00100863], [cite:PUB00100766], [cite:PUB00100768]]. Mutations in human VPS13 proteins (VPS13A-D) cause different diseases such as Chorea-acanthocytosis, Cohen syndrome, Parkinson's disease, and spastic ataxia, respectively which suggests they have different functions [[cite:PUB00100501], [cite:PUB00100769]]. Members of this entry belong to the repeating β-groove (RBG) superfamily. These proteins share a structure made of multiple repeating modules consisting of five β-sheets followed by a loop [[cite:PUB00101861]].</p>

This description is obtained from EB-eye REST.

Associated GO terms

Unable to find any GO terms for the transcript with the identifier.

Associated Lotus transcripts 17

Co-occuring domains 1

A list of co-occurring predicted domains within the L. japonicus gene space: