v5.1.0.3
Cicer data from the Legume Information System
| Type | Domain |
| Description | LITAF (LPS-induced TNF-activating factor) (also known as SIMPLE; small integral membrane protein of the late endosome) is an endosome-associatedintegral membrane protein important for multivesicular body (MVB) sorting. It is a monotypic membrane protein with both termini exposed to the cytoplasm andis anchored to membranes via an in-plane helical membrane anchor, present within the highly conserved C-terminal region known as the 'LITAF domain' or'SIMPLE-like domain'. The LITAF domain consists of conserved cysteines separated by a 22 residue hydrophobic region. LITAF domains are foundthroughout the eukaryotes, suggesting ancient conserved functions, with multiple instances of expansion, especially in the metazoa [, ].The LITAF domain consists of five β-sheets, three N-terminal and two C- terminal to the predicted hydrophobic anchor region and is stabilized by thecoordination of a zinc atom by two pairs of evolutionarily conserved cysteine residues. Consistent with a protein domain that resides in close proximity tomembranes, specific residues within the LITAF domain interact with phosphoethanolamine (PE) head groups. The anchoring-region of the LITAF domainis likely to embed into the cytosolic-facing monolayer of the membrane bilayer by adopting an amphipathic character []. |
| Short Name | LITAF |