Serine palmitoyltransferase 2 (P40970)

Identification
NameSerine palmitoyltransferase 2
Synonyms
  • SPT 2
  • Long chain base biosynthesis protein 2
Gene NameLCB2
Enzyme Class
Biological Properties
General FunctionInvolved in transferase activity
Specific FunctionCatalytic subunit of serine palmitoyltransferase (SPT), which catalyzes the committed step in the synthesis of sphingolipids, the condensation of serine with palmitoyl CoA to form the long chain base 3-ketosphinganine
Cellular LocationCytoplasm. Endoplasmic reticulum. Membrane; Multi-pass membrane protein (Potential)
SMPDB Pathways
Sphingolipid metabolismPW002479 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Sphingolipid metabolismec00600 Map00600
SMPDB ReactionsNot Available
KEGG Reactions
Palmityl-CoA + L-Serine → 3-Dehydrosphinganine + Carbon dioxide + Coenzyme A
Metabolites
YMDB IDNameView
YMDB00045Coenzyme AShow
YMDB00112L-SerineShow
YMDB001833-DehydrosphinganineShow
YMDB00301Palmityl-CoAShow
YMDB00527palmitoyl-CoAShow
YMDB00912Carbon dioxideShow
GO Classification
Component
Not Available
Function
binding
transferase activity, transferring nitrogenous groups
cofactor binding
pyridoxal phosphate binding
catalytic activity
transferase activity
Process
biosynthetic process
metabolic process
Gene Properties
Chromosome Locationchromosome 4
LocusYDR062W
Gene Sequence>1686 bp ATGAGTACTCCTGCAAACTATACCCGTGTGCCCCTGTGCGAACCAGAGGAGCTGCCAGAC GACATACAAAAAGAAAATGAATATGGTACACTAGATTCTCCGGGGCATTTGTATCAAGTC AAGTCACGTCATGGGAAGCCACTACCTGAGCCCGTTGTCGACACCCCTCCTTATTACATT TCTTTGTTAACATATCTAAATTATTTGATTCTGATTATATTAGGTCATGTTCACGACTTC TTAGGTATGACCTTCCAAAAAAACAAACATCTGGATCTTTTAGAGCATGATGGGTTAGCA CCTTGGTTTTCAAATTTCGAGAGTTTTTATGTCAGGAGAATTAAAATGAGAATTGATGAT TGCTTTTCTAGACCAACTACTGGTGTTCCTGGTAGATTTATTCGTTGTATTGATAGAATT TCTCATAATATAAATGAGTATTTTACCTACTCAGGCGCAGTGTATCCATGCATGAACTTA TCATCATATAACTATTTAGGCTTCGCACAAAGTAAGGGTCAATGTACCGATGCCGCCTTG GAATCTGTCGATAAATATTCTATTCAATCTGGTGGTCCAAGAGCTCAAATCGGTACCACA GATTTGCACATTAAAGCAGAGAAATTAGTTGCTAGATTTATCGGTAAGGAGGATGCCCTC GTTTTTTCGATGGGTTATGGTACAAATGCAAACTTGTTCAACGCTTCCCTCGATAAAAAG TGTTTAGTTATCTCTGACGAATTGAACCACACCTCTATTAGAACAGGTGTTAGGCTTTCT GGTGCTGCTGTGCGAACTTTCAAGCATGGTGATATGGTGGGTTTAGAAAAGCTTATCAGA GAACAGATAGTACTTGGTCAACCAAAAACAAATCGTCCATGGAAGAAAATTTTAATTTGC GCAGAAGGGTTGTTTTCCATGGAAGGTACTTTGTGTAACTTGCCAAAATTGGTTGAATTG AAGAAGAAATATAAATGTTACTTGTTTATCGATGAAGCCCATTCTATAGGCGCTATGGGC CCAACTGGTCGCGGTGTTTGTGAAATATTTGGCGTTGATCCCAAGGACGTCGACATTCTA ATGGGTACTTTCACTAAGTCGTTTGGTGCTGCTGGTGGTTACATTGCTGCTGATCAATGG ATTATCGATAGACTGAGGTTGGATTTAACCACTGTGAGTTATAGTGAGTCAATGCCGGCT CCTGTTTTAGCTCAAACTATTTCCTCATTACAAACCATTAGTGGTGAAATATGTCCCGGA CAAGGTACTGAAAGATTGCAACGTATAGCCTTTAATTCCCGTTATCTACGTTTAGCTTTG CAAAGGTTAGGATTTATTGTCTACGGTGTGGCTGACTCACCAGTTATTCCCTTACTACTG TATTGTCCCTCAAAGATGCCCGCATTTTCGAGAATGATGTTACAAAGACGGATTGCTGTT GTTGTTGTTGCTTATCCTGCTACTCCGCTGATCGAATCAAGAGTAAGATTCTGTATGTCT GCATCTTTAACAAAGGAAGATATCGATTATTTACTGCGTCATGTTAGTGAAGTTGGTGAC AAATTGAATTTGAAATCAAATTCCGGCAAATCCAGTTACGACGGTAAACGTCAAAGATGG GACATCGAGGAAGTTATCAGGAGAACACCTGAAGATTGCAAGGACGACAAGTATTTTGTT AATTGA
Protein Properties
Pfam Domain Function
Protein Residues561
Protein Molecular Weight63110.19922
Protein Theoretical pI8.19
Signalling Regions
  • None
Transmembrane Regions
  • 57-77
  • 443-463
Protein Sequence>Serine palmitoyltransferase 2 MSTPANYTRVPLCEPEELPDDIQKENEYGTLDSPGHLYQVKSRHGKPLPEPVVDTPPYYI SLLTYLNYLILIILGHVHDFLGMTFQKNKHLDLLEHDGLAPWFSNFESFYVRRIKMRIDD CFSRPTTGVPGRFIRCIDRISHNINEYFTYSGAVYPCMNLSSYNYLGFAQSKGQCTDAAL ESVDKYSIQSGGPRAQIGTTDLHIKAEKLVARFIGKEDALVFSMGYGTNANLFNAFLDKK CLVISDELNHTSIRTGVRLSGAAVRTFKHGDMVGLEKLIREQIVLGQPKTNRPWKKILIC AEGLFSMEGTLCNLPKLVELKKKYKCYLFIDEAHSIGAMGPTGRGVCEIFGVDPKDVDIL MGTFTKSFGAAGGYIAADQWIIDRLRLDLTTVSYSESMPAPVLAQTISSLQTISGEICPG QGTERLQRIAFNSRYLRLALQRLGFIVYGVADSPVIPLLLYCPSKMPAFSRMMLQRRIAV VVVAYPATPLIESRVRFCMSASLTKEDIDYLLRHVSEVGDKLNLKSNSGKSSYDGKRQRW DIEEVIRRTPEDCKDDKYFVN
References
External Links
ResourceLink
Saccharomyces Genome Database LCB2
Uniprot IDP40970
Uniprot NameLCB2_YEAST
GenBank Gene IDAY723771
Genebank Protein ID51830228
General Reference
  • Zhao, C., Beeler, T., Dunn, T. (1994). "Suppressors of the Ca(2+)-sensitive yeast mutant (csg2) identify genes involved in sphingolipid biosynthesis. Cloning and characterization of SCS1, a gene required for serine palmitoyltransferase activity." J Biol Chem 269:21480-21488.8063782
  • Nagiec, M. M., Baltisberger, J. A., Wells, G. B., Lester, R. L., Dickson, R. C. (1994). "The LCB2 gene of Saccharomyces and the related LCB1 gene encode subunits of serine palmitoyltransferase, the initial enzyme in sphingolipid synthesis." Proc Natl Acad Sci U S A 91:7899-7902.8058731
  • Brandt, P., Ramlow, S., Otto, B., Bloecker, H. (1996). "Nucleotide sequence analysis of a 32,500 bp region of the right arm of Saccharomyces cerevisiae chromosome IV." Yeast 12:85-90.8789263
  • Jacq, C., Alt-Morbe, J., Andre, B., Arnold, W., Bahr, A., Ballesta, J. P., Bargues, M., Baron, L., Becker, A., Biteau, N., Blocker, H., Blugeon, C., Boskovic, J., Brandt, P., Bruckner, M., Buitrago, M. J., Coster, F., Delaveau, T., del Rey, F., Dujon, B., Eide, L. G., Garcia-Cantalejo, J. M., Goffeau, A., Gomez-Peris, A., Zaccaria, P., et, a. l. .. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." Nature 387:75-78.9169867
  • 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
  • Gable, K., Slife, H., Bacikova, D., Monaghan, E., Dunn, T. M. (2000). "Tsc3p is an 80-amino acid protein associated with serine palmitoyltransferase and required for optimal enzyme activity." J Biol Chem 275:7597-7603.10713067
  • Gable, K., Han, G., Monaghan, E., Bacikova, D., Natarajan, M., Williams, R., Dunn, T. M. (2002). "Mutations in the yeast LCB1 and LCB2 genes, including those corresponding to the hereditary sensory neuropathy type I mutations, dominantly inactivate serine palmitoyltransferase." J Biol Chem 277:10194-10200.11781309
  • 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
  • Han, G., Gable, K., Yan, L., Natarajan, M., Krishnamurthy, J., Gupta, S. D., Borovitskaya, A., Harmon, J. M., Dunn, T. M. (2004). "The topology of the Lcb1p subunit of yeast serine palmitoyltransferase." J Biol Chem 279:53707-53716.15485854
  • Breslow, D. K., Collins, S. R., Bodenmiller, B., Aebersold, R., Simons, K., Shevchenko, A., Ejsing, C. S., Weissman, J. S. (2010). "Orm family proteins mediate sphingolipid homeostasis." Nature 463:1048-1053.20182505