{"ymdb_id":"YMDB00623","created_at":"2011-05-29T18:37:07.000Z","updated_at":"2016-09-08T18:35:42.000Z","name":"N-(24-Hydroxytetracosanoyl)phytosphingosine","cas":null,"state":null,"melting_point":null,"description":"N-(24-Hydroxytetracosanoyl)phytosphingosine is a phytoceramide. Phytoceramides can be made by hydroxylating dihydrosphingosine to form phytosphingosine which is then amide-linked to a fatty acid. High concentrations of phytoceramides have been found in mitochondria. They are also intermediates in the production of complex sphinolipids. [PMID: 18296751]\n","experimental_water_solubility":null,"experimental_logp_hydrophobicity":null,"location":"Golgi;endoplasmic reticulum","synthesis_reference":null,"chebi_id":"52373","hmdb_id":null,"kegg_id":null,"pubchem_id":null,"cs_id":"23106996","foodb_id":null,"wikipedia_link":null,"biocyc_id":null,"iupac":"24-hydroxy-N-[(2S,3S,4R)-1,3,4-trihydroxyoctadecan-2-yl]tetracosanamide","traditional_iupac":"24-hydroxy-N-[(2S,3S,4R)-1,3,4-trihydroxyoctadecan-2-yl]tetracosanamide","logp":"12.116336436666668","pka":"14.4413560488785","alogps_solubility":"8.87e-05 g/l","alogps_logp":"9.26","alogps_logs":"-6.89","acceptor_count":"5","donor_count":"5","rotatable_bond_count":"40","polar_surface_area":"110.02000000000001","refractivity":"204.91129999999998","polarizability":"92.81083986888777","formal_charge":"0","physiological_charge":"0","pka_strongest_basic":"0.03356159303818973","pka_strongest_acidic":"13.262014760738879","bioavailability":"0","number_of_rings":"0","rule_of_five":"0","ghose_filter":"0","veber_rule":"0","mddr_like_rule":"0","synonyms":["Cer(t18:0/24:0(2-OH))","cer3_24","ceramide-3 (phytosphingosine:N-C24:2OH)","N-(2-hydroxytetracosanoyl)-4S-hydroxysphinganine","N-(2-hydroxytetracosanoyl)-phytoceramide"],"pathways":[],"growth_conditions":[],"references":[{"pubmed_id":18846089,"citation":"Herrgard, M. J., Swainston, N., Dobson, P., Dunn, W. B., Arga, K. Y., Arvas, M., Bluthgen, N., Borger, S., Costenoble, R., Heinemann, M., Hucka, M., Le Novere, N., Li, P., Liebermeister, W., Mo, M. L., Oliveira, A. P., Petranovic, D., Pettifer, S., Simeonidis, E., Smallbone, K., Spasic, I., Weichart, D., Brent, R., Broomhead, D. S., Westerhoff, H. V., Kirdar, B., Penttila, M., Klipp, E., Palsson, B. O., Sauer, U., Oliver, S. G., Mendes, P., Nielsen, J., Kell, D. B. (2008). \"A consensus yeast metabolic network reconstruction obtained from a community approach to systems biology.\" Nat Biotechnol 26:1155-1160."},{"pubmed_id":12484746,"citation":"Funato, K., Vallee, B., Riezman, H. (2002). \"Biosynthesis and trafficking of sphingolipids in the yeast Saccharomyces cerevisiae.\" Biochemistry 41:15105-15114."},{"pubmed_id":9804825,"citation":"Reggiori, F., Conzelmann, A. (1998). \"Biosynthesis of inositol phosphoceramides and remodeling of glycosylphosphatidylinositol anchors in Saccharomyces cerevisiae are mediated by different enzymes.\" J Biol Chem 273:30550-30559."},{"pubmed_id":18296751,"citation":"Dickson, R. C. (2008). \"Thematic review series: sphingolipids. New insights into sphingolipid metabolism and function in budding yeast.\" J Lipid Res 49:909-921."}],"proteins":[{"created_at":"2011-05-27T07:58:49.000Z","updated_at":"2011-07-22T17:54:25.000Z","name":"Ceramide very long chain fatty acid hydroxylase SCS7","uniprot_id":"Q03529","uniprot_name":"SCS7_YEAST","enzyme":true,"transporter":false,"gene_name":"SCS7","num_residues":384,"molecular_weight":"44881.10156","theoretical_pi":"6.55","general_function":"Involved in heme binding","specific_function":"Ceramide 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","reactions":[{"id":1371,"direction":"\u003e","locations":"endoplasmic reticulum","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1373,"direction":"\u003e","locations":"endoplasmic reticulum","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1378,"direction":"\u003e","locations":"endoplasmic reticulum","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1379,"direction":"\u003e","locations":"endoplasmic reticulum","altext":null,"export":true,"pw_reaction_id":null,"source":null}],"signal_regions":"None","transmembrane_regions":"197-217;223-243;298-318;353-373","pdb_id":null,"cellular_location":"Endoplasmic reticulum membrane; Multi-pass membrane protein","genbank_gene_id":"AY693150","genbank_protein_id":"51013751","gene_card_id":"SCS7","chromosome_location":"chromosome 13","locus":"YMR272C","synonyms":["Ceramide VLCFA hydroxylase SCS7","Suppressor of calcium sensitivity 7"],"enzyme_classes":["1.-.-.-"],"go_classes":[{"category":"Component","description":" endoplasmic reticulum"},{"category":"Component","description":" organelle"},{"category":"Component","description":" membrane-bounded organelle"},{"category":"Component","description":" intracellular membrane-bounded organelle"},{"category":"Function","description":" ion binding"},{"category":"Function","description":" cation binding"},{"category":"Function","description":" metal ion binding"},{"category":"Function","description":" transition metal ion binding"},{"category":"Function","description":" iron ion binding"},{"category":"Function","description":" oxidoreductase activity"},{"category":"Function","description":" heme binding"},{"category":"Function","description":" catalytic activity"},{"category":"Function","description":" binding"},{"category":"Process","description":" membrane lipid metabolic process"},{"category":"Process","description":" sphingolipid metabolic process"},{"category":"Process","description":" monocarboxylic acid metabolic process"},{"category":"Process","description":" fatty acid metabolic process"},{"category":"Process","description":" fatty acid biosynthetic process"},{"category":"Process","description":" oxidation reduction"},{"category":"Process","description":" organic acid metabolic process"},{"category":"Process","description":" oxoacid metabolic process"},{"category":"Process","description":" carboxylic acid metabolic process"},{"category":"Process","description":" metabolic process"},{"category":"Process","description":" cellular metabolic process"},{"category":"Process","description":" lipid metabolic process"},{"category":"Process","description":" cellular lipid metabolic process"},{"category":"Process","description":" primary metabolic process"}],"pfams":[{"name":"Cyt-b5","identifier":"PF00173"},{"name":"FA_hydroxylase","identifier":"PF04116"}],"pathways":[],"gene_sequence":"ATGTCGACTAATACTTCCAAGACTTTGGAACTGTTTTCAAAAAAGACGGTACAAGAACACAATACTGCCAATGACTGCTGGGTCACTTATCAAAACAGAAAGATTTATGACGTGACCAGGTTTTTGAGCGAACACCCTGGTGGTGACGAGTCCATCTTGGACTATGCTGGTAAGGACATTACTGAGATCATGAAAGACTCAGATGTGCATGAACACAGCGACTCCGCGTATGAAATCCTTGAGGACGAATATTTGATTGGTTACTTGGCAACTGACGAAGAGGCAGCGAGATTGTTGACTAACAAGAACCATAAGGTTGAAGTGCAGTTGTCAGCTGACGGTACTGAGTTTGACTCCACTACTTTTGTAAAGGAGTTGCCCGCCGAGGAGAAACTAAGTATTGCTACGGACTACAGTAACGACTACAAAAAGCATAAATTTTTGGATCTGAACCGTCCTTTGCTGATGCAGATTCTGCGTAGTGATTTCAAGAAAGATTTTTACGTTGACCAAATCCATAGACCAAGACATTACGGTAAGGGGTCTGCCCCGCTATTTGGTAATTTCTTGGAACCATTAACTAAAACAGCTTGGTGGGTTGTTCCAGTTGCTTGGTTGCCTGTAGTTGTGTACCACATGGGTGTTGCTTTGAAGAACATGAACCAGCTATTTGCATGTTTCTTGTTCTGTGTCGGTGTCTTTGTTTGGACTTTGATTGAATACGGTCTTCACCGTTTCCTATTTCATTTCGATGATTGGTTACCTGAAAGTAACATCGCATTCGCCACACATTTTCTACTACATGGTTGCCATCATTACTTGCCCATGGACAAGTACCGTTTAGTTATGCCACCTACTCTGTTCGTCATCCTTTGTGCTCCATTTTACAAGTTGGTATTTGCTCTGCTGCCACTTTATTGGGCTTACGCTGGTTTTGCTGGCGGTCTTTTCGGTTATGTCTGTTATGACGAATGTCATTTCTTCTTGCACCACTCTAAATTGCCTCCCTTCATGCGTAAGTTGAAAAAATATCACCTGGAACATCATTATAAAAACTACCAACTGGGATTTGGCGTCACATCCTGGTTTTGGGACGAAGTTTTTGGCACCTACTTAGGCCCCGATGCCCCATTGTCCAAAATGAAATATGAATAA","protein_sequence":"MSTNTSKTLELFSKKTVQEHNTANDCWVTYQNRKIYDVTRFLSEHPGGDESILDYAGKDITEIMKDSDVHEHSDSAYEILEDEYLIGYLATDEEAARLLTNKNHKVEVQLSADGTEFDSTTFVKELPAEEKLSIATDYSNDYKKHKFLDLNRPLLMQILRSDFKKDFYVDQIHRPRHYGKGSAPLFGNFLEPLTKTAWWVVPVAWLPVVVYHMGVALKNMNQLFACFLFCVGVFVWTLIEYGLHRFLFHFDDWLPESNIAFATHFLLHGCHHYLPMDKYRLVMPPTLFVILCAPFYKLVFALLPLYWAYAGFAGGLFGYVCYDECHFFLHHSKLPPFMRKLKKYHLEHHYKNYQLGFGVTSWFWDEVFGTYLGPDAPLSKMKYE"},{"created_at":"2011-05-27T09:13:37.000Z","updated_at":"2011-05-27T15:01:30.000Z","name":"Inositol phosphorylceramide synthase","uniprot_id":"P36107","uniprot_name":"AUR1_YEAST","enzyme":true,"transporter":false,"gene_name":"AUR1","num_residues":401,"molecular_weight":"45192.80078","theoretical_pi":"6.02","general_function":"Involved in catalytic activity","specific_function":"Catalyzes the addition of a phosphorylinositol group onto ceramide to form inositol phosphorylceramide, an essential step in sphingolipid biosynthesis","reactions":[{"id":1668,"direction":"\u003c\u003e","locations":"Golgi","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1669,"direction":"\u003c\u003e","locations":"Golgi","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1670,"direction":"\u003c\u003e","locations":"Golgi","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1671,"direction":"\u003c\u003e","locations":"Golgi","altext":null,"export":true,"pw_reaction_id":null,"source":null}],"signal_regions":"None","transmembrane_regions":"42-62;65-85;88-108;156-176;179-199;246-266;269-289;292-312","pdb_id":null,"cellular_location":"Golgi apparatus, Golgi stack membrane; Multi-pass membrane protein","genbank_gene_id":"U49090","genbank_protein_id":"1515352","gene_card_id":"AUR1","chromosome_location":"chromosome 11","locus":"YKL004W","synonyms":["IPC synthase","Aureobasidin A resistance protein","Phosphatidylinositol:ceramide phosphoinositol transferase"],"enzyme_classes":["2.-.-.-"],"go_classes":[{"category":"Component","description":" cell part"},{"category":"Component","description":" membrane"},{"category":"Function","description":" catalytic activity"},{"category":"Process","description":" Not Available"}],"pfams":[{"name":"PAP2","identifier":"PF01569"}],"pathways":[],"gene_sequence":"ATGGCAAACCCTTTTTCGAGATGGTTTCTATCAGAGAGACCTCCAAACTGCCATGTAGCCGATTTAGAAACAAGTTTAGATCCCCATCAAACGTTGTTGAAGGTGCAAAAATACAAACCCGCTTTAAGCGACTGGGTGCATTACATCTTCTTGGGATCCATCATGCTGTTTGTGTTCATTACTAATCCCGCACCTTGGATCTTCAAGATCCTTTTTTATTGTTTCTTGGGCACTTTATTCATCATTCCAGCTACGTCACAGTTTTTCTTCAATGCCTTGCCCATCCTAACATGGGTGGCGCTGTATTTCACTTCATCGTACTTTCCAGATGACCGCAGGCCTCCTATTACTGTCAAAGTGTTACCAGCGGTGGAAACAATTTTATACGGCGACAATTTAAGTGATATTCTTGCAACATCGACGAATTCCTTTTTGGACATTTTAGCATGGTTACCGTACGGACTATTTCATTATGGGGCCCCATTTGTCGTTGCTGCCATCTTATTCGTATTTGGTCCACCAACTGTTTTGCAAGGTTATGCTTTTGCATTTGGTTATATGAACCTGTTTGGTGTTATCATGCAAAATGTCTTTCCAGCCGCTCCCCCATGGTATAAAATTCTCTATGGATTGCAATCAGCCAACTATGATATGCATGGCTCGCCTGGTGGATTAGCTAGAATTGATAAGCTACTCGGTATTAATATGTATACTACAGCTTTTTCAAATTCCTCCGTCATTTTCGGTGCTTTTCCTTCACTGCATTCCGGGTGTGCTACTATGGAAGCCCTGTTTTTCTGTTATTGTTTTCCAAAATTGAAGCCCTTGTTTATTGCTTATGTTTGCTGGTTATGGTGGTCAACTATGTATCTGACACACCATTATTTTGTAGACCTTATGGCAGGTTCTGTGCTGTCATACGTTATTTTCCAGTACACAAAGTACACACATTTACCAATTGTAGATACATCTCTTTTTTGCAGATGGTCATACACTTCAATTGAGAAATACGATATATCAAAGAGTGATCCATTGGCTGCAGATTCAAACGATATCGAAAGTGTCCCTTTGTCCAACTTGGAACTTGACTTTGATCTTAATATGACTGATGAACCCAGTGTAAGCCCTTCGTTATTTGATGGATCTACTTCTGTTTCTCGTTCGTCCGCCACGTCTATAACGTCACTAGGTGTAAAGAGGGCTTAA","protein_sequence":"MANPFSRWFLSERPPNCHVADLETSLDPHQTLLKVQKYKPALSDWVHYIFLGSIMLFVFITNPAPWIFKILFYCFLGTLFIIPATSQFFFNALPILTWVALYFTSSYFPDDRRPPITVKVLPAVETILYGDNLSDILATSTNSFLDILAWLPYGLFHFGAPFVVAAILFVFGPPTVLQGYAFAFGYMNLFGVIMQNVFPAAPPWYKILYGLQSANYDMHGSPGGLARIDKLLGINMYTTAFSNSSVIFGAFPSLHSGCATMEALFFCYCFPKLKPLFIAYVCWLWWSTMYLTHHYFVDLMAGSVLSYVIFQYTKYTHLPIVDTSLFCRWSYTSIEKYDISKSDPLAADSNDIESVPLSNLELDFDLNMTDEPSVSPSLFDGSTSVSRSSATSITSLGVKRA"}]}