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TSC10 3-dehydrosphinganine reductase [ Saccharomyces cerevisiae S288C ]

Gene ID: 852568, updated on 25-Apr-2024

Summary

Gene symbol
TSC10
Gene description
3-dehydrosphinganine reductase
Primary source
SGD:S000000469
Locus tag
YBR265W
See related
AllianceGenome:SGD:S000000469
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Saccharomyces cerevisiae S288C (strain: S288C)
Lineage
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Summary
Enables 3-dehydrosphinganine reductase activity. Involved in 3-keto-sphinganine metabolic process and sphingolipid biosynthetic process. Located in lipid droplet. Used to study erythrokeratodermia variabilis et progressiva 4. Human ortholog(s) of this gene implicated in erythrokeratodermia variabilis et progressiva 4 and follicular lymphoma. Orthologous to human KDSR (3-ketodihydrosphingosine reductase). [provided by Alliance of Genome Resources, Apr 2022]
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Genomic context

Location:
chromosome: II
Exon count:
1
Sequence:
Chromosome: II; NC_001134.8 (738582..739544)

Chromosome II - NC_001134.8Genomic Context describing neighboring genes Neighboring gene glycine hydroxymethyltransferase SHM1 Neighboring gene Rab family GTPase YPT10 Neighboring gene Rei1p Neighboring gene Slm6p Neighboring gene mitochondrial 54S ribosomal protein YmL37

Pathways from PubChem

Interactions

Products Interactant Other Gene Complex Source Pubs Description

General gene information

Gene Ontology Provided by SGD

Function Evidence Code Pubs
enables 3-dehydrosphinganine reductase activity IBA
Inferred from Biological aspect of Ancestor
more info
 
enables 3-dehydrosphinganine reductase activity IDA
Inferred from Direct Assay
more info
PubMed 
enables 3-dehydrosphinganine reductase activity IEA
Inferred from Electronic Annotation
more info
 
enables nucleotide binding IEA
Inferred from Electronic Annotation
more info
 
enables oxidoreductase activity IEA
Inferred from Electronic Annotation
more info
 
Process Evidence Code Pubs
involved_in 3-keto-sphinganine metabolic process IBA
Inferred from Biological aspect of Ancestor
more info
 
involved_in 3-keto-sphinganine metabolic process IDA
Inferred from Direct Assay
more info
PubMed 
involved_in 3-keto-sphinganine metabolic process IEA
Inferred from Electronic Annotation
more info
 
involved_in sphingolipid biosynthetic process IBA
Inferred from Biological aspect of Ancestor
more info
 
involved_in sphingolipid biosynthetic process IDA
Inferred from Direct Assay
more info
PubMed 
involved_in sphingolipid biosynthetic process IEA
Inferred from Electronic Annotation
more info
 
involved_in sphingolipid biosynthetic process IMP
Inferred from Mutant Phenotype
more info
PubMed 
involved_in sphingolipid metabolic process IEA
Inferred from Electronic Annotation
more info
 

General protein information

Preferred Names
3-dehydrosphinganine reductase
NP_009824.2
  • 3-ketosphinganine reductase; catalyzes the second step in phytosphingosine synthesis; essential for growth in the absence of exogenous dihydrosphingosine or phytosphingosine; localized to lipid droplets; member of short chain dehydrogenase/reductase protein family; mutations in human homolog KDSR cause recessive progressive symmetric erythrokeratoderma

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_001134.8 Reference assembly

    Range
    738582..739544
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001178613.2NP_009824.2  TPA: 3-dehydrosphinganine reductase [Saccharomyces cerevisiae S288C]

    See identical proteins and their annotated locations for NP_009824.2

    Status: REVIEWED

    UniProtKB/Swiss-Prot
    D6VQR2, P38342
    UniProtKB/TrEMBL
    A0A8H4BVF6, A6ZLK5, B3LMP6, C7GMW5, D3UF13, G2W9S0, N1P8U4
    Conserved Domains (1) summary
    cd08939
    Location:7263
    KDSR-like_SDR_c; 3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR