Ceramide very long chain fatty acid hydroxylase SCS7 (Q03529)

Identification
NameCeramide very long chain fatty acid hydroxylase SCS7
Synonyms
  • Ceramide VLCFA hydroxylase SCS7
  • Suppressor of calcium sensitivity 7
Gene NameSCS7
Enzyme Class
Biological Properties
General FunctionInvolved in heme binding
Specific FunctionCeramide hydroxylase involved in the alpha-hydroxylation of sphingolipid-associated very long chain fatty acids. Hydroxylates the very long chain fatty acid of ceramides at C2 and C3
Cellular LocationEndoplasmic reticulum membrane; Multi-pass membrane protein
SMPDB PathwaysNot Available
KEGG PathwaysNot Available
SMPDB ReactionsNot Available
KEGG Reactions
N-tetracosanoylsphinganine + NADPH + hydron + oxygen → NADP + water + N-(24-hydroxytetracosanoyl)sphinganine
N-hexacosanylsphinganine + NADPH + hydron + oxygen → NADP + water + N-(26-hydroxyhexacosanoyl)sphinganine
N-Tetracosanoylphytosphingosine + NADPH + hydron + oxygen → N-(24-Hydroxytetracosanoyl)phytosphingosine + NADP + water
N-Hexacosanoylphytosphingosine + NADPH + hydron + oxygen → NADP + N-(26-Hydroxyhexacosanyl)phytosphingosine + water
Metabolites
YMDB IDNameView
YMDB00426NADPHShow
YMDB00427NADPShow
YMDB00619N-tetracosanoylsphinganineShow
YMDB00620N-(24-hydroxytetracosanoyl)sphinganineShow
YMDB00621N-hexacosanylsphinganineShow
YMDB00622N-(26-hydroxyhexacosanoyl)sphinganineShow
YMDB00623N-(24-Hydroxytetracosanoyl)phytosphingosineShow
YMDB00624N-(26-Hydroxyhexacosanyl)phytosphingosineShow
YMDB00862hydronShow
YMDB00890waterShow
YMDB00900oxygenShow
YMDB00963N-TetracosanoylphytosphingosineShow
YMDB00964N-HexacosanoylphytosphingosineShow
GO Classification
Component
endoplasmic reticulum
organelle
membrane-bounded organelle
intracellular membrane-bounded organelle
Function
ion binding
cation binding
metal ion binding
transition metal ion binding
iron ion binding
oxidoreductase activity
heme binding
catalytic activity
binding
Process
membrane lipid metabolic process
sphingolipid metabolic process
monocarboxylic acid metabolic process
fatty acid metabolic process
fatty acid biosynthetic process
oxidation reduction
organic acid metabolic process
oxoacid metabolic process
carboxylic acid metabolic process
metabolic process
cellular metabolic process
lipid metabolic process
primary metabolic process
cellular lipid metabolic process
Gene Properties
Chromosome Locationchromosome 13
LocusYMR272C
Gene Sequence>1155 bp ATGTCGACTAATACTTCCAAGACTTTGGAACTGTTTTCAAAAAAGACGGTACAAGAACAC AATACTGCCAATGACTGCTGGGTCACTTATCAAAACAGAAAGATTTATGACGTGACCAGG TTTTTGAGCGAACACCCTGGTGGTGACGAGTCCATCTTGGACTATGCTGGTAAGGACATT ACTGAGATCATGAAAGACTCAGATGTGCATGAACACAGCGACTCCGCGTATGAAATCCTT GAGGACGAATATTTGATTGGTTACTTGGCAACTGACGAAGAGGCAGCGAGATTGTTGACT AACAAGAACCATAAGGTTGAAGTGCAGTTGTCAGCTGACGGTACTGAGTTTGACTCCACT ACTTTTGTAAAGGAGTTGCCCGCCGAGGAGAAACTAAGTATTGCTACGGACTACAGTAAC GACTACAAAAAGCATAAATTTTTGGATCTGAACCGTCCTTTGCTGATGCAGATTCTGCGT AGTGATTTCAAGAAAGATTTTTACGTTGACCAAATCCATAGACCAAGACATTACGGTAAG GGGTCTGCCCCGCTATTTGGTAATTTCTTGGAACCATTAACTAAAACAGCTTGGTGGGTT GTTCCAGTTGCTTGGTTGCCTGTAGTTGTGTACCACATGGGTGTTGCTTTGAAGAACATG AACCAGCTATTTGCATGTTTCTTGTTCTGTGTCGGTGTCTTTGTTTGGACTTTGATTGAA TACGGTCTTCACCGTTTCCTATTTCATTTCGATGATTGGTTACCTGAAAGTAACATCGCA TTCGCCACACATTTTCTACTACATGGTTGCCATCATTACTTGCCCATGGACAAGTACCGT TTAGTTATGCCACCTACTCTGTTCGTCATCCTTTGTGCTCCATTTTACAAGTTGGTATTT GCTCTGCTGCCACTTTATTGGGCTTACGCTGGTTTTGCTGGCGGTCTTTTCGGTTATGTC TGTTATGACGAATGTCATTTCTTCTTGCACCACTCTAAATTGCCTCCCTTCATGCGTAAG TTGAAAAAATATCACCTGGAACATCATTATAAAAACTACCAACTGGGATTTGGCGTCACA TCCTGGTTTTGGGACGAAGTTTTTGGCACCTACTTAGGCCCCGATGCCCCATTGTCCAAA ATGAAATATGAATAA
Protein Properties
Pfam Domain Function
Protein Residues384
Protein Molecular Weight44881.10156
Protein Theoretical pI6.55
Signalling Regions
  • None
Transmembrane Regions
  • 197-217
  • 223-243
  • 298-318
  • 353-373
Protein Sequence>Ceramide very long chain fatty acid hydroxylase SCS7 MSTNTSKTLELFSKKTVQEHNTANDCWVTYQNRKIYDVTRFLSEHPGGDESILDYAGKDI TEIMKDSDVHEHSDSAYEILEDEYLIGYLATDEEAARLLTNKNHKVEVQLSADGTEFDST TFVKELPAEEKLSIATDYSNDYKKHKFLDLNRPLLMQILRSDFKKDFYVDQIHRPRHYGK GSAPLFGNFLEPLTKTAWWVVPVAWLPVVVYHMGVALKNMNQLFACFLFCVGVFVWTLIE YGLHRFLFHFDDWLPESNIAFATHFLLHGCHHYLPMDKYRLVMPPTLFVILCAPFYKLVF ALLPLYWAYAGFAGGLFGYVCYDECHFFLHHSKLPPFMRKLKKYHLEHHYKNYQLGFGVT SWFWDEVFGTYLGPDAPLSKMKYE
References
External Links
ResourceLink
Saccharomyces Genome Database SCS7
Uniprot IDQ03529
Uniprot NameSCS7_YEAST
GenBank Gene IDAY693150
Genebank Protein ID51013751
General Reference
  • Bowman, S., Churcher, C., Badcock, K., Brown, D., Chillingworth, T., Connor, R., Dedman, K., Devlin, K., Gentles, S., Hamlin, N., Hunt, S., Jagels, K., Lye, G., Moule, S., Odell, C., Pearson, D., Rajandream, M., Rice, P., Skelton, J., Walsh, S., Whitehead, S., Barrell, B. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII." Nature 387:90-93.9169872
  • Hu, Y., Rolfs, A., Bhullar, B., Murthy, T. V., Zhu, C., Berger, M. F., Camargo, A. A., Kelley, F., McCarron, S., Jepson, D., Richardson, A., Raphael, J., Moreira, D., Taycher, E., Zuo, D., Mohr, S., Kane, M. F., Williamson, J., Simpson, A., Bulyk, M. L., Harlow, E., Marsischky, G., Kolodner, R. D., LaBaer, J. (2007). "Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Genome Res 17:536-543.17322287
  • Mitchell, A. G., Martin, C. E. (1997). "Fah1p, a Saccharomyces cerevisiae cytochrome b5 fusion protein, and its Arabidopsis thaliana homolog that lacks the cytochrome b5 domain both function in the alpha-hydroxylation of sphingolipid-associated very long chain fatty acids." J Biol Chem 272:28281-28288.9353282
  • Haak, D., Gable, K., Beeler, T., Dunn, T. (1997). "Hydroxylation of Saccharomyces cerevisiae ceramides requires Sur2p and Scs7p." J Biol Chem 272:29704-29710.9368039
  • Dunn, T. M., Haak, D., Monaghan, E., Beeler, T. J. (1998). "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." Yeast 14:311-321.9559540
  • Swain, E., Baudry, K., Stukey, J., McDonough, V., Germann, M., Nickels, J. T. Jr (2002). "Sterol-dependent regulation of sphingolipid metabolism in Saccharomyces cerevisiae." J Biol Chem 277:26177-26184.12006573
  • Huh, W. K., Falvo, J. V., Gerke, L. C., Carroll, A. S., Howson, R. W., Weissman, J. S., O'Shea, E. K. (2003). "Global analysis of protein localization in budding yeast." Nature 425:686-691.14562095
  • Ghaemmaghami, S., Huh, W. K., Bower, K., Howson, R. W., Belle, A., Dephoure, N., O'Shea, E. K., Weissman, J. S. (2003). "Global analysis of protein expression in yeast." Nature 425:737-741.14562106
  • Kim, H., Melen, K., Osterberg, M., von Heijne, G. (2006). "A global topology map of the Saccharomyces cerevisiae membrane proteome." Proc Natl Acad Sci U S A 103:11142-11147.16847258
  • Guan, X. L., Wenk, M. R. (2006). "Mass spectrometry-based profiling of phospholipids and sphingolipids in extracts from Saccharomyces cerevisiae." Yeast 23:465-477.16652392
  • Bosson, R., Guillas, I., Vionnet, C., Roubaty, C., Conzelmann, A. (2009). "Incorporation of ceramides into Saccharomyces cerevisiae glycosylphosphatidylinositol-anchored proteins can be monitored in vitro." Eukaryot Cell 8:306-314.19074599