SAMD8
Sphingomyelin synthases synthesize sphingolipids through transfer of a phosphatidyl head group on to the primary hydroxyl of ceramide. SAMD8 is an endoplasmic reticulum (ER) transferase that has no sphingomyelin synthase activity but can convert phosphatidylethanolamine (PE) and ceramide to ceramide phosphoethanolamine (CPE) albeit with low product yield. Appears to operate as a ceramide sensor to control ceramide homeostasis in the endoplasmic reticulum rather than a converter of ceramides. Seems to be critical for the integrity of the early secretory pathway. Belongs to the sphingomyelin synthase family. 2 alternatively spliced human isoforms have been reported. Note: This description may include information from UniProtKB.
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Protein type: Cell surface; Membrane protein, integral; Membrane protein, multi-pass |
Chromosomal Location of human Ortholog: 10q22.2 |
Cellular Component:
cytosol; endoplasmic reticulum; endoplasmic reticulum membrane; membrane
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Molecular Function:
ceramide cholinephosphotransferase activity; ceramide phosphoethanolamine synthase activity; sphingomyelin synthase activity
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Biological Process:
ceramide biosynthetic process; ceramide phosphoethanolamine biosynthetic process; regulation of ceramide biosynthetic process; sphingolipid biosynthetic process; sphingomyelin biosynthetic process
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Reference #:
Q96LT4
(UniProtKB)
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Alt. Names/Synonyms: Ceramide phosphoethanolamine synthase; CPE synthase; epididymis luminal protein 177; epididymis secretory sperm binding protein Li 181mP; FLJ25082; HEL-177; HEL-S-181mP; SAM domain-containing protein 8; SAMD8; SMSr; sphingomyelin synthase related; Sphingomyelin synthase-related protein 1; sterile alpha motif domain containing 8; Sterile alpha motif domain-containing protein 8
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Gene Symbols: SAMD8
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Molecular weight:
48,321 Da
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Basal Isoelectric point:
8.35
Predict pI for various phosphorylation states
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