| Primary Identifier | IPR006629 | Type | Domain |
| Short Name | LITAF |
| description | LITAF (LPS-induced TNF-activating factor) (also known as SIMPLE; smallintegral membrane protein of the late endosome) is an endosome-associatedintegral membrane protein important for multivesicular body (MVB) sorting. Itis a monotypic membrane protein with both termini exposed to the cytoplasm andis anchored to membranes via an in-plane helical membrane anchor, presentwithin the highly conserved C-terminal region known as the 'LITAF domain' or'SIMPLE-like domain'. The LITAF domain consists of conserved cysteinesseparated by a 22 residue hydrophobic region. LITAF domains are foundthroughout the eukaryotes, suggesting ancient conserved functions, withmultiple 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 cysteineresidues. Consistent with a protein domain that resides in close proximity tomembranes, specific residues within the LITAF domain interact withphosphoethanolamine (PE) head groups. The anchoring-region of the LITAF domainis likely to embed into the cytosolic-facing monolayer of the membrane bilayerby adopting an amphipathic character []. |
