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SCS7 fatty acid alpha-hydroxylase [ Saccharomyces cerevisiae S288C ]

Gene ID: 855315, updated on 14-Nov-2024

Summary

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Official Symbol
SCS7
Official Full Name
fatty acid alpha-hydroxylase
Primary source
SGD:S000004885
Locus tag
YMR272C
See related
AllianceGenome:SGD:S000004885; FungiDB:YMR272C; VEuPathDB:YMR272C
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Saccharomyces cerevisiae S288C (strain: S288C)
Lineage
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Also known as
FAH1
Summary
Enables fatty acid 2-hydroxylase activity and sphingosine hydroxylase activity. Involved in inositol phosphoceramide metabolic process and very long-chain fatty acid metabolic process. Located in endoplasmic reticulum. Human ortholog(s) of this gene implicated in hereditary spastic paraplegia 35. Orthologous to human FA2H (fatty acid 2-hydroxylase). [provided by Alliance of Genome Resources, Nov 2024]
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Genomic context

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See SCS7 in Genome Data Viewer
Location:
chromosome: XIII
Exon count:
1
Sequence:
Chromosome: XIII; NC_001145.3 (809623..810777, complement)

Chromosome XIII - NC_001145.3Genomic Context describing neighboring genes Neighboring gene orotate phosphoribosyltransferase URA10 Neighboring gene tRNA-Gln Neighboring gene uncharacterized protein Neighboring gene Zds1p

Genomic regions, transcripts, and products

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Genomic Sequence:
NC_001145.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. Levels of SCS7/FA2H-mediated fatty acid 2-hydroxylation determine the sensitivity of cells to antitumor PM02734. Herrero AB, et al. Cancer Res, 2008 Dec 1. PMID 19047157
  2. Mass spectrometry-based profiling of phospholipids and sphingolipids in extracts from Saccharomyces cerevisiae. Guan XL, et al. Yeast, 2006 Apr 30. PMID 16652392
  3. Requirement of sphingolipid alpha-hydroxylation for fungicidal action of syringomycin E. Hama H, et al. FEBS Lett, 2000 Jul 28. PMID 10922463
  4. Synthesis of monohydroxylated inositolphosphorylceramide (IPC-C) in Saccharomyces cerevisiae requires Scs7p, a protein with both a cytochrome b5-like domain and a hydroxylase/desaturase domain. Dunn TM, et al. Yeast, 1998 Mar 15. PMID 9559540
  5. Following the flux of long-chain bases through the sphingolipid pathway in vivo using mass spectrometry. Martínez-Montañés F, et al. J Lipid Res, 2016 May. PMID 26977056, Free PMC Article

See all (86) citations in PubMed

GeneRIFs: Gene References Into Functions

Pathways from PubChem

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Interactions

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Products Interactant Other Gene Complex Source Pubs Description

General gene information

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Homology

Gene Ontology Provided by SGD

Function Evidence Code Pubs
enables 4-hydroxysphinganine ceramide fatty acyl 2-hydroxylase activity IEA
Inferred from Electronic Annotation
more info
  
enables dihydroceramide fatty acyl 2-hydroxylase activity IEA
Inferred from Electronic Annotation
more info
  
enables fatty acid 2-hydroxylase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables fatty acid 2-hydroxylase activity IEA
Inferred from Electronic Annotation
more info
  
enables fatty acid 2-hydroxylase activity IMP
Inferred from Mutant Phenotype
more info
 PubMed 
enables heme binding IEA
Inferred from Electronic Annotation
more info
  
enables iron ion binding IEA
Inferred from Electronic Annotation
more info
  
enables metal ion binding IEA
Inferred from Electronic Annotation
more info
  
enables oxidoreductase activity IEA
Inferred from Electronic Annotation
more info
  
enables sphingosine hydroxylase activity IMP
Inferred from Mutant Phenotype
more info
 PubMed 
Process Evidence Code Pubs
involved_in fatty acid biosynthetic process IEA
Inferred from Electronic Annotation
more info
  
involved_in fatty acid metabolic process IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in inositol phosphoceramide metabolic process IGI
Inferred from Genetic Interaction
more info
 PubMed 
involved_in inositol phosphoceramide metabolic process IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in lipid biosynthetic process IEA
Inferred from Electronic Annotation
more info
  
involved_in very long-chain fatty acid metabolic process IMP
Inferred from Mutant Phenotype
more info
 PubMed 
Component Evidence Code Pubs
located_in endoplasmic reticulum HDA PubMed 
is_active_in endoplasmic reticulum IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in endoplasmic reticulum IEA
Inferred from Electronic Annotation
more info
  
located_in endoplasmic reticulum membrane IEA
Inferred from Electronic Annotation
more info
  
located_in membrane IEA
Inferred from Electronic Annotation
more info
  
is_active_in membrane ISM
Inferred from Sequence Model
more info
 PubMed 

General protein information

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Preferred Names
fatty acid alpha-hydroxylase
NP_013999.1
  • Sphingolipid alpha-hydroxylase; functions in the alpha-hydroxylation of sphingolipid-associated very long chain fatty acids, has both cytochrome b5-like and hydroxylase/desaturase domains, not essential for growth

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_001145.3 Reference assembly

    Range
    809623..810777 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001182779.1 → NP_013999.1  TPA: fatty acid alpha-hydroxylase [Saccharomyces cerevisiae S288C]

    See identical proteins and their annotated locations for NP_013999.1

    Status: REVIEWED

    UniProtKB/Swiss-Prot
    D6W098, Q03529
    UniProtKB/TrEMBL
    A6ZMY7, B3LMF9, C7GTM8, C8ZFD7, G2WKY0, N1NXQ7
    Conserved Domains (2) summary
    COG5274
    Location:31 → 224
    CYB5; Cytochrome b involved in lipid metabolism [Energy production and conversion, Lipid transport and metabolism]
    cl01132
    Location:149 → 380
    FA_hydroxylase; Fatty acid hydroxylase superfamily
Nucleotide Protein
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
Q03529.1

Gene LinkOut

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