IPR006629
LPS-induced tumour necrosis factor alpha factor
InterPro entry
Short name | LITAF |
Description
LITAF (LPS-induced TNF-activating factor) (also known as SIMPLE; small integral membrane protein of the late endosome) is an endosome-associated integral membrane protein important for multivesicular body (MVB) sorting. It is a monotypic membrane protein with both termini exposed to the cytoplasm and is 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 found throughout the eukaryotes, suggesting ancient conserved functions, with multiple instances of expansion, especially in the metazoa
[2, 1].
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 the coordination of a zinc atom by two pairs of evolutionarily conserved cysteine residues. Consistent with a protein domain that resides in close proximity to membranes, specific residues within the LITAF domain interact with phosphoethanolamine (PE) head groups. The anchoring-region of the LITAF domain is likely to embed into the cytosolic-facing monolayer of the membrane bilayer by adopting an amphipathic character
[1].
References
1.The topology, structure and PE interaction of LITAF underpin a Charcot-Marie-Tooth disease type 1C. Ho AK, Wagstaff JL, Manna PT, Wartosch L, Qamar S, Garman EF, Freund SM, Roberts RC. BMC Biol. 14, 109, (2016). View articlePMID: 27927196
2.The Charcot Marie Tooth disease protein LITAF is a zinc-binding monotopic membrane protein. Qin W, Wunderley L, Barrett AL, High S, Woodman PG. Biochem. J. 473, 3965-3978, (2016). View articlePMID: 27582497