|FAIM3||FAIM3 (Fas apoptotic inhibitory molecule 3), TOSO|
|Molecule Type||Antigen Expression||Molecular Weight|
Min / Max
|Non-lineage Restricted Molecule|
Type 1 glycoprotein
|FAIM3 is expressed in lymph nodes, peripheral blood leukocytes, lung, thymus and kidney. It is very week in spleen, liver, heart and salivary gland. Expression is in lymphoid cell lines such as Jurkat cells but not expression is detected in nonhematopoietic cell lines.|
|MOLECULAR FAMILY NAME|
FAIM3 is a single-pass type-1 390 aa glycoprotein. It contains an extracellular domain which contains an Ig-like domain and 2 cysteines, a transmembrane domain and a cytoplasmic domain which contains an acidic domain and a proline-rich domain.
POST-TRANSCRIPTIONAL MODIFICATION: No information.
POST-TRANSLATIONAL MODIFICATION: No information.
|LIGANDS AND MOLECULES ASSOCIATED WITH FAIM3: No information.|
|Faim3 may play a role in the immune system processes. It protects cell from FAS-, TNF-α and FADD-induced apoptosis without increasing expresssion of the inhibitors of apoptosis BCL2 and BCLXL. It seems to activate an inhibitory pathway that prevents CASP8 activation following FAS stimulation, rather than blocking apoptotic signals downstream. FAIM3 may inhibit FAS-induced apoptosis by preventing CASP8 processing through CFLAR up-regulation. The Ig-like domain is required for the anti-apoptotic ability. Mutational analysis established that the Ig domain and transmembrane domain, but not the cytoplasmic domain, are required for the inhibition of FAS-induced apoptotis and an increased in FAIM3 expression is responsible for the temporary FAS resistance in T cells.|
BIOCHEMICAL ACTIVITY: No information.
DISEASE RELEVANCE AND FUNCTION OF FAIM3 IN INTACT ANIMAL: No information.
PROTEINS AND DNA ELEMENTS WHICH REGULATE TRANSCRIPTION OF FAIM3: No information.
SUBSTRATES: No information.
ENZYMES WHICH MODIFY FAIM3: No information.
Database accession numbers
Revised June 25, 2008