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Literature summary for 2.3.1.24 extracted from

  • Mizutani, Y.; Kihara, A.; Igarashi, Y.
    Mammalian Lass6 and its related family members regulate synthesis of specific ceramides (2005), Biochem. J., 390, 263-271 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.3.1.24

Cloned(Commentary)

Cloned (Comment) Organism
DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic tree, recombinant expression of HA-tagged enzyme in HEK-293T cells Mus musculus
DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic tree, recombinant expression of HA-tagged enzyme in HEK-293T cells, and recombinant expression of C-terminally GFP-tagged Lass6 Mus musculus

Protein Variants

Protein Variants Comment Organism
additional information no loss of activity is observed for the unglycosylated mutant (HA-tagged Lass6-N18Q) when compared with either the glycosylated mutant HA-tagged Lass6-N285Q or the glycosylated wild-type Lass6 Mus musculus
N18Q site-directed mutagenesis, a glycosylation site mutant Mus musculus
N285Q site-directed mutagenesis, a putative glycosylation site mutant Mus musculus

Localization

Localization Comment Organism GeneOntology No. Textmining
endoplasmic reticulum membrane the C-terminus of Lass6 is exposed to the cytosolic side of the endoplasmic reticulum membrane Mus musculus 5789
-

Organism

Organism UniProt Comment Textmining
Mus musculus Q8C172
-
-
Mus musculus Q9D6K9
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein Asn18, but not Asn285, of Lass6 is glycosylated, deglycosylation of Lass6 with PNGase F (N-glycosidase F). Lass6 is modified by N-glycosylation of a high-mannose and/or hybrid type. N-glycosylation is not essential for the dihydroceramide synthase activity of Lass6 Mus musculus
glycoprotein the N-glycosylation of Lass5 appears as two bands, deglycosylation of Lass5 with PNGase F (N-glycosidase F) Mus musculus

Source Tissue

Source Tissue Comment Organism Textmining
brain
-
 Mus musculus
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kidney
-
 Mus musculus
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kidney high expression level Mus musculus
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additional information isozymes mRNAs for Lass2, Lass4, Lass5 and Lass6 are found to be mostly ubiquitous, although no expression is detected in muscle for any of these. No expression of Lass6 is observed in heart, muscle, spleen or stomach. Lass6 is most highly expressed in kidney, followed by brain Mus musculus
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additional information isozymes mRNAs for Lass2, Lass4, Lass5 and Lass6 are found to be mostly ubiquitous, although no expression is detected in muscle for any of these. The highest expression of Lass5 is in testis, and the expression in kidney is also high Mus musculus
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testis high expression level Mus musculus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information both Lass5- and Lass6-overproducing cells exhibit high dihydroceramide synthesis activity using C16:0- and C14:0-CoAs and low activity with C12:0- and C18:0-CoAs. On the other hand, whereas the Lass5-overproducing cells demonstrates significant C18:1-ceramide synthesis, the Lass6-overproducing cells do not show any such increase. Recombinant Lass6 produces shorter ceramide species (C14:0- and C16:0-ceramides) in transgenic HEK-293T cells Mus musculus ?
-
 ?
additional information both Lass5- and Lass6-overproducing cells exhibit high dihydroceramide synthesis activity using C16:0- and C14:0-CoAs and low activity with C12:0- and C18:0-CoAs. On the other hand, whereas the Lass5-overproducing cells demonstrates significant C18:1-ceramide synthesis, the Lass6-overproducing cells do not show any such increase. The recombinant Lass5 shows a preference for C16 substrates in transgenic HEK-293T cells Mus musculus ?
-
 ?
sphingosine + lauroyl-CoA low activity Mus musculus N-lauroylsphingosine + CoA
-
 ?
sphingosine + myristoyl-CoA
-
 Mus musculus N-myristoylsphingosine + CoA
-
 ?
sphingosine + oleoyl-CoA low activity Mus musculus N-oleoylsphingosine + CoA
-
 ?
sphingosine + palmitoyl-CoA
-
 Mus musculus N-palmitoylsphingosine + CoA
-
 ?
sphingosine + stearoyl-CoA low activity Mus musculus N-stearoylsphingosine + CoA
-
 ?

Subunits

Subunits Comment Organism
? x * 44800, SDS-PAGE Mus musculus

Synonyms

Synonyms Comment Organism
LASS5
-
 Mus musculus
Lass6
-
 Mus musculus
trh1-like
-
 Mus musculus
trh4
-
 Mus musculus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Mus musculus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Mus musculus

General Information

General Information Comment Organism
evolution Lass proteins are known to contain a TLC [TRAM/Lag1p/ CLN8 (ceroid-lipofuscinoses, neuronal 8)] homology domain with the Lag1 motif. Lass family members Lass2, Lass4 and Lass5, but not Lass1, also contain a HOX (homeobox) domain Mus musculus
evolution murine Lass6 is a member of the mouse Lass family. It exhibits the highest identity with Lass5 (61.7% identity and 68.2% similarity) and the lowest identity with Lass1 (16.0% identity and 27.4%similarity). Lass proteins are known to contain a TLC [TRAM/Lag1p/ CLN8 (ceroid-lipofuscinoses, neuronal 8)] homology domain with the Lag1 motif. Lass family members Lass2, Lass4 and Lass5, but not Lass1, also contain a HOX (homeobox) domain Mus musculus
additional information the N-terminus is essential for catalytic activity Mus musculus