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SCS7/YMR272C Single Page Format

This page provides an alternative format to the SGD Locus Summary Page. Note that additional information may be available on or linked from the standard format SGD Locus Summary page.

Contents

Names and Identifiers GO Annotations Pathways Summary Paragraph Mutant Phenotypes Interactions Homologs Protein Info (physical properties, transcript info) PDB Homologs (protein structure info) Motifs Genome-wide Expression (and other large-scale analyses) Locus History (misc. notes) Sequence Retrieval and Analysis Map and Displays Localization Community Annotation Literature Guide

Sequence Coordinates   ChrXIII: 810776 to 809622 CDS: 810776 - 809622 Click on map for expanded view SGD ORF map GBrowse

SGD Locus Page

Names and Identifiers [TOP] [NEXT]
Standard Name	Systematic Name	Alias	Feature Type	SGDID
SCS7	YMR272C	FAH1	ORF, Verified	S000004885
Description
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

GO Annotations [TOP] [NEXT]
Molecular Function Annotation(s) Reference(s) Evidence Assigned By fatty acid alpha-hydroxylase activity Mitchell AG and Martin CE (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(45):28281-8        IMP : Inferred from Mutant Phenotype Assigned on 2009-09-18 SGD Dunn TM, et al. (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(4):311-21        IMP : Inferred from Mutant Phenotype Assigned on 2009-09-18 SGD heme binding DDB, et al. (2001) Gene Ontology annotation through association of InterPro records with GO terms.      IEA : Inferred from Electronic Annotation with EBI:IPR001199 , EBI:IPR018506 Assigned on 2007-05-23 UniProtKB iron ion binding DDB, et al. (2001) Gene Ontology annotation through association of InterPro records with GO terms.      IEA : Inferred from Electronic Annotation with EBI:IPR006694 , EBI:IPR014430 Assigned on 2008-10-13 UniProtKB GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0408 Assigned on 2007-05-23 UniProtKB metal ion binding GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0479 Assigned on 2007-05-23 UniProtKB oxidoreductase activity DDB, et al. (2001) Gene Ontology annotation through association of InterPro records with GO terms.      IEA : Inferred from Electronic Annotation with EBI:IPR006694 , EBI:IPR014430 Assigned on 2008-10-13 UniProtKB GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0560 Assigned on 2007-05-23 UniProtKB
Biological Process Annotation(s) Reference(s) Evidence Assigned By electron transport chain GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0249 Assigned on 2008-10-02 UniProtKB fatty acid biosynthetic process DDB, et al. (2001) Gene Ontology annotation through association of InterPro records with GO terms.      IEA : Inferred from Electronic Annotation with EBI:IPR006694 Assigned on 2008-10-13 UniProtKB GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0275 Assigned on 2007-05-23 UniProtKB inositol phosphorylceramide metabolic process Mitchell AG and Martin CE (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(45):28281-8        IMP : Inferred from Mutant Phenotype Assigned on 2009-09-18 SGD Dunn TM, et al. (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(4):311-21        IGI : Inferred from Genetic Interaction with SGD:SUR1, SGD:CSG2 IMP : Inferred from Mutant Phenotype Assigned on 2009-09-18 SGD Haak D, et al. (1997) Hydroxylation of Saccharomyces cerevisiae ceramides requires Sur2p and Scs7p. J Biol Chem 272(47):29704-10        IMP : Inferred from Mutant Phenotype Assigned on 2009-09-18 SGD Guan XL and Wenk MR (2006) Mass spectrometry-based profiling of phospholipids and sphingolipids in extracts from Saccharomyces cerevisiae. Yeast 23(6):465-77        IMP : Inferred from Mutant Phenotype Assigned on 2009-09-18 SGD lipid biosynthetic process GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0444 Assigned on 2007-05-23 UniProtKB oxidation reduction DDB, et al. (2001) Gene Ontology annotation through association of InterPro records with GO terms.      IEA : Inferred from Electronic Annotation with EBI:IPR006694 , EBI:IPR014430 Assigned on 2008-10-13 UniProtKB GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0560 Assigned on 2008-05-21 UniProtKB sphingolipid metabolic process DDB, et al. (2001) Gene Ontology annotation through association of InterPro records with GO terms.      IEA : Inferred from Electronic Annotation with EBI:IPR014430 Assigned on 2009-01-12 UniProtKB transport GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0813 Assigned on 2007-05-23 UniProtKB
Cellular Component Annotation(s) Reference(s) Evidence Assigned By endoplasmic reticulum Huh WK, et al. (2003) Global analysis of protein localization in budding yeast. Nature 425(6959):686-91          IDA : Inferred from Direct Assay Assigned on 2006-07-24 SGD DDB, et al. (2001) Gene Ontology annotation through association of InterPro records with GO terms.      IEA : Inferred from Electronic Annotation with EBI:IPR006694 , EBI:IPR014430 Assigned on 2008-10-13 UniProtKB GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0256 Assigned on 2007-05-23 UniProtKB integral to membrane GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0812 Assigned on 2007-05-23 UniProtKB GOA curators and UniProt curators (2007) Gene Ontology annotation based on Swiss-Prot Subcellular Location vocabulary mapping.      IEA : Inferred from Electronic Annotation with EBI:SL-9909 Assigned on 2009-10-01 UniProtKB membrane Mitchell AG and Martin CE (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(45):28281-8        ISS : Inferred from Sequence or structural Similarity Assigned on 2006-07-24 SGD GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0472 Assigned on 2007-05-23 UniProtKB

Pathways [TOP] [NEXT]
sphingolipid metabolism

Summary Paragraph [TOP] [NEXT]

SUMMARY PARAGRAPH for SCS7/YMR272C for SCS7 About sphingolipid metabolism Sphingolipids are essential components of the plasma membrane in all eukaryotic cells. S. cerevisiae cells make three complex sphingolipids: inositol-phosphoceramide (IPC), mannose-inositol-phosphoceramide (MIPC), and mannose-(inositol phosphate)2-ceramide (M(IP)2C)(1). In the yeast plasma membrane sphingolipids concentrate with ergosterol to form lipid rafts, specialized membrane microdomains implicated in a variety of cellular processes, including sorting of membrane proteins and lipids, as well as organizing and regulating signaling cascades (2). Intermediates in sphingolipid biosynthesis have been shown to play important roles as signaling molecules and growth regulators. Sphingolipid long chain bases (LCBs), dihydrosphingosine (DHS) and phytosphingosine (PHS), have been implicated as secondary messengers in signaling pathways that regulate heat stress response (3, 4). Other intermediates, phytoceramide and long-chain base phosphates (LCBPs), have been shown to be components of the tightly-controlled ceramide/LCBP rheostat, which regulates cell growth (5). Since phosphoinositol-containing sphingolipids are unique to fungi, the sphingolipid biosynthesis pathway is considered a target for antifungal drugs (6, 7). Last Updated: 2007-10-05

Basic References [TOP]

BASIC INFORMATION REFERENCES forSCS7/YMR272C for SCS7 1) Dickson RC and Lester RL (2002) Sphingolipid functions in Saccharomyces cerevisiae. Biochim Biophys Acta 1583(1):13-25            2) Bagnat M and Simons K (2002) Lipid rafts in protein sorting and cell polarity in budding yeast Saccharomyces cerevisiae. Biol Chem 383(10):1475-80        3) Jenkins GM, et al. (1997) Involvement of yeast sphingolipids in the heat stress response of Saccharomyces cerevisiae. J Biol Chem 272(51):32566-72        4) Ferguson-Yankey SR, et al. (2002) Mutant analysis reveals complex regulation of sphingolipid long chain base phosphates and long chain bases during heat stress in yeast. Yeast 19(7):573-86      5) Kobayashi SD and Nagiec MM (2003) Ceramide/long-chain base phosphate rheostat in Saccharomyces cerevisiae: regulation of ceramide synthesis by Elo3p and Cka2p. Eukaryot Cell 2(2):284-94        6) Nagiec MM, et al. (1997) Sphingolipid synthesis as a target for antifungal drugs. Complementation of the inositol phosphorylceramide synthase defect in a mutant strain of Saccharomyces cerevisiae by the AUR1 gene. J Biol Chem 272(15):9809-17        7) Sugimoto Y, et al. (2004) IPC synthase as a useful target for antifungal drugs. Curr Drug Targets Infect Disord 4(4):311-22        8) Mitchell AG and Martin CE (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(45):28281-8        9) Hama H, et al. (2000) Requirement of sphingolipid alpha-hydroxylation for fungicidal action of syringomycin E. FEBS Lett 478(1-2):26-8        10) Haak D, et al. (1997) Hydroxylation of Saccharomyces cerevisiae ceramides requires Sur2p and Scs7p. J Biol Chem 272(47):29704-10        11) Zhao C, et al. (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(34):21480-8

Mutant Phenotypes [TOP] [NEXT]
Phenotype page for SCS7/YMR272C

Interactions: genetic, physical, and other gene-gene links. [TOP] [NEXT]
Interaction page for SCS7/YMR272C

Homologs [TOP] [NEXT]
Comparison Resources PSI-BLAST Results Ashbya Homologs (AGD) BLASTN vs. fungi BLASTP at NCBI BLASTP vs. fungi Candida Homologs (CGD) Candida Homologs (CandidaDB) Fungal Alignment Fungal Orthogroups Repository Ortholog Search (P-POD) PhylomeDB Synteny Viewer Yeast Gene Order Browser (YGOB) eukarYotic OrtholoGY (YOGY)

Physical Properties and Transcript Information: predicted from sequence [TOP] [NEXT]

Protein Sequence Calculations from Predicted Full length Translation N-term MSTNTSK C-term LSKMKYE Length(aa) 384 MW(Da) 44,881 pI 6.54 Amino Acid Composition (full length) GCG tools: PepPlot, Helical Wheel, PepStruct Transcript Translation Calculations Codon Bias 0.270   Codon Adaptation Index 0.244   Frequency of Optimal Codons 0.566   Hydropathicity of Protein -0.188   Aromaticity Score 0.161

10 20 30 40 50 | | | | | MSTNTSKTLELFSKKTVQEHNTANDCWVTYQNRKIYDVTRFLSEHPGGDE SILDYAGKDITEIMKDSDVHEHSDSAYEILEDEYLIGYLATDEEAARLLT NKNHKVEVQLSADGTEFDSTTFVKELPAEEKLSIATDYSNDYKKHKFLDL NRPLLMQILRSDFKKDFYVDQIHRPRHYGKGSAPLFGNFLEPLTKTAWWV VPVAWLPVVVYHMGVALKNMNQLFACFLFCVGVFVWTLIEYGLHRFLFHF DDWLPESNIAFATHFLLHGCHHYLPMDKYRLVMPPTLFVILCAPFYKLVF ALLPLYWAYAGFAGGLFGYVCYDECHFFLHHSKLPPFMRKLKKYHLEHHY KNYQLGFGVTSWFWDEVFGTYLGPDAPLSKMKYE*

Protein Structures from PDB: proteins of known structure with sequence similarity to SCS7/YMR272C, based on Smith-Waterman analysis. [TOP] [NEXT]

PDB protein structure(s) homologous to SCS7 Homolog Source (per PDB) Protein Alignment: SCS7 vs. Homolog External Links P-Value %Identical %Similar Alignment 2ibj ( Chain: A) Structure of house fly cytochrome b5 PDB_Info PDB_Structure Musca domestica 1.3e-08 37 34 View alignment SCOP MMDB CATH 1bfx ( Chain: A) The solution nmr structure of the b form of oxidized rat microsomal cytochrome b5, minimized average structure PDB_Info PDB_Structure Rattus norvegicus 3.5e-08 36 31 View alignment SCOP MMDB CATH 1b5m ( Chain: A) Rat outer mitochondrial membrane cytochrome b5 PDB_Info PDB_Structure Rattus norvegicus 4.9e-08 48 27 View alignment SCOP MMDB CATH 1hko ( Chain: A) Nmr structure of bovine cytochrome b5 PDB_Info PDB_Structure Bos taurus 6.4e-08 36 32 View alignment SCOP MMDB CATH 1eue ( Chain: B, A) Rat outer mitochondrial membrane cytochrome b5 PDB_Info PDB_Structure Rattus norvegicus Chain B = 7.0e-08 48 27 View alignment SCOP MMDB CATH Chain A = 7.0e-08 48 27 View alignment 1awp ( Chain: A, B) Rat outer mitochondrial membrane cytochrome b5 PDB_Info PDB_Structure Rattus norvegicus Chain A = 7.7e-08 48 27 View alignment SCOP MMDB CATH Chain B = 7.7e-08 48 27 View alignment 1cyo ( Chain: A) Bovine cytochrome b(5) PDB_Info PDB_Structure Bos taurus 7.8e-08 37 31 View alignment SCOP MMDB CATH 1j0q ( Chain: A) Solution structure of oxidized bovine microsomal cytochrome b5 mutant v61h PDB_Info PDB_Structure Bos taurus 9.3e-08 38 29 View alignment SCOP MMDB CATH 1es1 ( Chain: A) Crystal structure of val61his mutant of trypsin-solubilized fragment of cytochrome b5 PDB_Info PDB_Structure Bos taurus 9.3e-08 38 29 View alignment SCOP MMDB CATH 1i8c ( Chain: A) Solution structure of the water-soluble fragment of rat hepatic apocytochrome b5 PDB_Info PDB_Structure Rattus norvegicus 1.1e-07 36 31 View alignment SCOP MMDB CATH 1ieu ( Chain: A) Apocytochrome b5, ph 6.2, 298 k, nmr, 10 structures PDB_Info PDB_Structure Rattus norvegicus 1.1e-07 36 31 View alignment SCOP MMDB CATH 1i87 ( Chain: A) Solution structure of the water-soluble fragment of rat hepatic apocytochrome b5 PDB_Info PDB_Structure Rattus norvegicus 1.1e-07 36 31 View alignment SCOP MMDB CATH 1iet ( Chain: A) Apocytochrome b5, ph 6.2, 298 k, nmr, minimized average structure PDB_Info PDB_Structure Rattus norvegicus 1.1e-07 36 31 View alignment SCOP MMDB CATH 1b5b ( Chain: A) Rat ferrocytochrome b5 b conformation, nmr, 1 structure PDB_Info PDB_Structure Rattus norvegicus 1.6e-07 37 29 View alignment SCOP MMDB CATH 2axx ( Chain: A) The solution structure of oxidized rat microsomal cytochrome b5, nmr, 21 structures PDB_Info PDB_Structure Rattus norvegicus 1.6e-07 37 29 View alignment SCOP MMDB CATH 1b5a ( Chain: A) Rat ferrocytochrome b5 a conformation, nmr, 1 structure PDB_Info PDB_Structure Rattus norvegicus 1.6e-07 37 29 View alignment SCOP MMDB CATH 1aqa ( Chain: A) Solution structure of reduced microsomal rat cytochrome b5, nmr, minimized average structure PDB_Info PDB_Structure Rattus norvegicus 1.6e-07 37 29 View alignment SCOP MMDB CATH 1mny ( Chain: A) Dimethyl propionate ester heme-containing cytochrome b5 PDB_Info PDB_Structure Rattus norvegicus 1.6e-07 37 29 View alignment SCOP MMDB CATH 1aw3 ( Chain: A) The solution nmr structure of oxidized rat microsomal cytochrome b5, minimized average structure PDB_Info PDB_Structure Rattus norvegicus 1.6e-07 37 29 View alignment SCOP MMDB CATH 1axx ( Chain: A) The solution structure of oxidized rat microsomal cytochrome b5, nmr, 19 structures PDB_Info PDB_Structure Rattus norvegicus 1.6e-07 37 29 View alignment SCOP MMDB CATH 1blv ( Chain: A) Solution structure of oxidized rat microsomal cytochrome b5 in the presence of 2 m guanidinium chloride: monitoring the early steps in protein unfolding PDB_Info PDB_Structure Rattus norvegicus 1.6e-07 37 29 View alignment SCOP MMDB CATH 2i96 ( Chain: A) Solution structure of the oxidized microsomal human cytochrome b5 PDB_Info PDB_Structure Homo sapiens 1.9e-07 33 35 View alignment SCOP MMDB CATH 1ib7 ( Chain: A) Solution structure of f35y mutant of rat ferro cytochrome b5, a conformation, ensemble of 20 structures PDB_Info PDB_Structure Rattus rattus 3.0e-07 36 30 View alignment SCOP MMDB CATH 1jex ( Chain: A) Solution structure of a67v mutant of rat ferro cytochrome b5 PDB_Info PDB_Structure Rattus norvegicus 3.6e-07 36 30 View alignment SCOP MMDB CATH 1lqx ( Chain: A) Crystal structure of v45e mutant of cytochrome b5 PDB_Info PDB_Structure Bos taurus 4.4e-07 37 29 View alignment SCOP MMDB CATH 1sh4 ( Chain: A) Solution structure of oxidized bovine microsomal cytochrome b5 mutant v45h PDB_Info PDB_Structure Bos taurus 4.4e-07 37 29 View alignment SCOP MMDB CATH 1do9 ( Chain: A) Solution structure of oxidized microsomal rabbit cytochrome b5. factors determining the heterogeneous binding of the heme. PDB_Info PDB_Structure Oryctolagus cuniculus 5.2e-07 35 31 View alignment SCOP MMDB CATH 1ehb ( Chain: A) Crystal structure of recombinant trypsin-solubilized fragment of cytochrome b5 PDB_Info PDB_Structure Bos taurus 5.2e-07 37 29 View alignment SCOP MMDB CATH 1lr6 ( Chain: A) Crystal structure of v45y mutant of cytochrome b5 PDB_Info PDB_Structure Bos taurus 5.2e-07 37 29 View alignment SCOP MMDB CATH 1u9u ( Chain: A) Crystal structure of f58y mutant of cytochrome b5 PDB_Info PDB_Structure Bos taurus 5.2e-07 37 29 View alignment SCOP MMDB CATH 1nx7 ( Chain: A) Solution structure of oxidized bovine microsomal cytochrome b5 PDB_Info PDB_Structure Bos taurus 5.2e-07 37 29 View alignment SCOP MMDB CATH 2i89 ( Chain: B, D, C, A) Structure of septuple mutant of rat outer mitochondrial membrane cytochrome b5 PDB_Info PDB_Structure Rattus norvegicus Chain B = 6.0e-07 45 25 View alignment SCOP MMDB CATH Chain D = 6.0e-07 45 25 View alignment Chain C = 6.0e-07 45 25 View alignment Chain A = 6.0e-07 45 25 View alignment 1u9m ( Chain: C, E, B, A, D, F) Crystal structure of f58w mutant of cytochrome b5 PDB_Info PDB_Structure Bos taurus Chain C = 6.0e-07 37 28 View alignment SCOP MMDB CATH Chain E = 6.0e-07 37 28 View alignment Chain B = 6.0e-07 37 28 View alignment Chain A = 6.0e-07 37 28 View alignment Chain D = 6.0e-07 37 28 View alignment Chain F = 6.0e-07 37 28 View alignment 1icc ( Chain: C, B, A, D) Rat outer mitochondrial membrane cytochrome b5 PDB_Info PDB_Structure Rattus norvegicus Chain C = 6.6e-07 45 28 View alignment SCOP MMDB CATH Chain B = 6.6e-07 45 28 View alignment Chain A = 6.6e-07 45 28 View alignment Chain D = 6.6e-07 45 28 View alignment 1m20 ( Chain: A) Crystal structure of f35y mutant of trypsin-solubilized fragment of cytochrome b5 PDB_Info PDB_Structure Bos taurus 9.9e-07 35 31 View alignment SCOP MMDB CATH 1lj0 ( Chain: A, D, C, B) Structure of quintuple mutant of the rat outer mitocondrial cytochrome b5. PDB_Info PDB_Structure Rattus norvegicus Chain A = 2.4e-06 44 26 View alignment SCOP MMDB CATH Chain D = 2.4e-06 44 26 View alignment Chain C = 2.4e-06 44 26 View alignment Chain B = 2.4e-06 44 26 View alignment 1m59 ( Chain: A) Crystal structure of p40v mutant of trypsin-solubilized fragment of cytochrome b5 PDB_Info PDB_Structure Bos taurus 4.7e-06 35 30 View alignment SCOP MMDB CATH 1m2i ( Chain: A) Crystal structure of e44a/e56a mutant of cytochrome b5 PDB_Info PDB_Structure Bos taurus 5.5e-06 34 30 View alignment SCOP MMDB CATH 1cxy ( Chain: A) Structure and characterization of ectothiorhodospira vacuolata cytochrome b558, a prokaryotic homologue of cytochrome b5 PDB_Info PDB_Structure Ectothiorhodospira shaposhnikovii 6.4e-06 36 31 View alignment SCOP MMDB CATH 1x3x ( Chain: B, A) Crystal structure of cytochrome b5 from ascaris suum PDB_Info PDB_Structure Ascaris suum Chain B = 1.0e-05 42 29 View alignment SCOP MMDB CATH Chain A = 1.0e-05 42 29 View alignment 1i5u ( Chain: A) Solution structure of cytochrome b5 triple mutant (e48a/e56a/d60a) PDB_Info PDB_Structure Bos taurus 1.5e-05 34 30 View alignment SCOP MMDB CATH 1f03 ( Chain: A) Solution structure of oxidized bovine microsomal cytochrome b5 mutant (e44a, e48a, e56a, d60a) and its interaction with cytochrome c PDB_Info PDB_Structure Bos taurus 5.2e-05 33 29 View alignment SCOP MMDB CATH 1f04 ( Chain: A) Solution structure of oxidized bovine microsomal cytochrome b5 mutant (e44a, e48a, e56a, d60a) and its interaction with cytochrome c PDB_Info PDB_Structure Bos taurus 5.2e-05 33 29 View alignment SCOP MMDB CATH 1m2m ( Chain: A) Crystal structure of e44a/e48a/e56a/d60a mutant of cytochrome b5 PDB_Info PDB_Structure Bos taurus 5.2e-05 33 29 View alignment SCOP MMDB CATH 1ltd ( Chain: A, B) The 2.6 angstroms refined structure of the escherichia coli recombinant saccharomyces cerevisiae flavocytochrome b2- sulphite complex PDB_Info PDB_Structure Saccharomyces cerevisiae Chain A = 0.000110 49 21 View alignment SCOP MMDB CATH Chain B = 0.000110 49 21 View alignment 2oz0 ( Chain: A, B) Mechanistic and structural studies of h373q flavocytochrome b2: effects of mutating the active site base PDB_Info PDB_Structure Saccharomyces cerevisiae Chain A = 0.000120 49 21 View alignment SCOP MMDB CATH Chain B = 0.000120 49 21 View alignment 1szf ( Chain: B, A) A198g:l230a mutant flavocytochrome b2 with pyruvate bound PDB_Info PDB_Structure Saccharomyces cerevisiae Chain B = 0.000120 49 21 View alignment SCOP MMDB CATH Chain A = 0.000120 49 21 View alignment 1szg ( Chain: A, B) A198g:l230a flavocytochrome b2 with sulfite bound PDB_Info PDB_Structure Saccharomyces cerevisiae Chain A = 0.000120 49 21 View alignment SCOP MMDB CATH Chain B = 0.000120 49 21 View alignment 1sze ( Chain: A, B) L230a mutant flavocytochrome b2 with benzoylformate PDB_Info PDB_Structure Saccharomyces cerevisiae Chain A = 0.000120 49 21 View alignment SCOP MMDB CATH Chain B = 0.000120 49 21 View alignment 1lco ( Chain: B, A) X-ray structure of two complexes of the y143f flavocytochrome b2 mutant crystallized in the presence of lactate or phenyl-lactate PDB_Info PDB_Structure Saccharomyces cerevisiae Chain B = 0.000120 49 21 View alignment SCOP MMDB CATH Chain A = 0.000120 49 21 View alignment 1ldc ( Chain: A, B) X-ray structure of two complexes of the y143f flavocytochrome b2 mutant crystallized in the presence of lactate or phenyl-lactate PDB_Info PDB_Structure Saccharomyces cerevisiae Chain A = 0.000120 49 21 View alignment SCOP MMDB CATH Chain B = 0.000120 49 21 View alignment 1fcb ( Chain: A, B) Molecular structure of flavocytochrome b2 at 2.4 angstroms resolution PDB_Info PDB_Structure Saccharomyces cerevisiae Chain A = 0.000120 49 21 View alignment SCOP MMDB CATH Chain B = 0.000120 49 21 View alignment 1kbi ( Chain: A, B) Crystallographic study of the recombinant flavin-binding domain of baker's yeast flavocytochrome b2: comparison with the intact wild-type enzyme PDB_Info PDB_Structure Saccharomyces cerevisiae Chain A = 0.000120 49 21 View alignment SCOP MMDB CATH Chain B = 0.000120 49 21 View alignment

Genome-wide Expression and Other Large-Scale Analyses [TOP] [NEXT]
Functional Analysis Expression Connection Summary Cell cycle and metabolic oscillation Cell cycle transcript profile Cyclebase Genevestigator GermOnline SPELL Microarray Search YGAC Triples Yeast Microarray Global Viewer YeastFunc	You can also search multiple datasets simultaneously using Expression Connection for expression studies or Function Junction for other large scale analyses.

Locus History (misc. notes) [TOP] [NEXT]

Nomenclature History

Standard Name	Reference
SCS7	SGD (2007) Information without a citation in SGD

Alias Name(s)	Reference
FAH1	Mitchell AG and Martin CE (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(45):28281-8

Sequence Retrieval [TOP] [NEXT]
Sequence Type	Output Format
Genomic DNA	GCG | FASTA | NoHeader
Genomic DNA with 1 kb up and downstream	GCG | FASTA | NoHeader
DNA coding sequence (without introns, without flanking regions)	GCG | FASTA | NoHeader
Protein Translation of ORF	GCG | FASTA | NoHeader
6-Frame Translation(with Restriction Map)	GCG
Restriction Fragment Sizes	GCG
Sequence Analysis Tools BLASTP BLASTN Design Primers FASTA aa FASTA nt Restriction Fragment Map Restriction Fragment Sizes Six-Frame Translation

Sequence from other databases
Sequence ID	Source
YMR272C	SGD Systematic Sequence
855315	NCBI: Gene ID
NP_013999.1	NCBI: RefSeq protein version ID
NP_013999.1	NCBI: RefSeq protein version ID
6323928	NCBI: NCBI protein GI

Map and Displays [TOP] [NEXT]
Physical, Genetic Maps:	Chromosomal Feature Map	GBrowse	Combined Physical and Genetic Map	Genetic Distance vs. Physical Distance Ratios
Similarity Viewers:	Synteny Viewer	Genomic Stripe View	SAGE Results Map

Localization [TOP] [NEXT]
Localization Resources YeastRC Localization (Seattle) Organelle DB (UMich) YGAC Triples YPL.db at Uni Graz YeastGFP DB (UCSF) at SGD

Community Annotation [TOP] [NEXT]
No community annotation available.

Literature Guide: papers categorized by topic. [TOP]
Topics	Reference	Other Genes Addressed
29 curated references; 0 references not yet curated
Mutants/Phenotypes Strains/Constructs Substrates/Ligands/Cofactors Techniques and Reagents	Bosson R, et al. (2009) Incorporation of ceramides into Saccharomyces cerevisiae glycosylphosphatidylinositol-anchored proteins can be monitored in vitro. Eukaryot Cell 8(3):306-14	|CWH43 |GUP1 |MCD4 |SUR2
Disease Gene Related Reviews	Ozbayraktar FB and Ulgen KO (2009) Molecular facets of sphingolipids: mediators of diseases. Biotechnol J 4(7):1028-41	|AUR1 |CSG2 |CSH1 |IPT1 |ISC1 |LAC1 |LAG1 |LCB1 |LCB2 |LCB4 |LCB5 |SUR1 |SUR2 |TSC10 |MORE
RNA Levels and Processing Regulation of	Guo N, et al. (2008) Global gene expression profile of Saccharomyces cerevisiae induced by dictamnine. Yeast 25(9):631-41	|ADE1 |ADE12 |ADE13 |ADE16 |ADE17 |ADE2 |ADE4 |ADE5,7 |ADE6 |ADE8 |ADY2 |APT1 |CBF1 |CIS3 |MORE
Mutants/Phenotypes	Herrero AB, et al. (2008) Levels of SCS7/FA2H-Mediated Fatty Acid 2-Hydroxylation Determine the Sensitivity of Cells to Antitumor PM02734. Cancer Res 68(23):9779-87	|AIM44 |ALD6 |ALG6 |API2 |APL1 |APL5 |APM3 |ATP15 |ATP4 |ATP5 |ATP7 |BRE5 |BST1 |CAT5 |MORE
Non-Fungal Related Genes/Proteins	Nagano M, et al. (2008) Functional association of cell death suppressor, Arabidopsis Bax Inhibitor-1, with fatty acid 2-hydroxylation through cytochrome b. Plant J
Non-Fungal Related Genes/Proteins	Uchida Y, et al. (2007) Fatty acid 2-hydroxylase, encoded by FA2H, accounts for differentiation-associated increase in 2-OH ceramides during keratinocyte differentiation. J Biol Chem 282(18):13211-9
Reviews	Dickson RC, et al. (2006) Functions and metabolism of sphingolipids in Saccharomyces cerevisiae. Prog Lipid Res 45(6):447-65	|ARV1 |AUR1 |CSH1 |DPL1 |FEN1 |IPT1 |LCB1 |LCB2 |LCB3 |LCB4 |LCB5 |NCR1 |PKH1 |PKH2 |MORE
Function/Process Mutants/Phenotypes	Guan XL and Wenk MR (2006) Mass spectrometry-based profiling of phospholipids and sphingolipids in extracts from Saccharomyces cerevisiae. Yeast 23(6):465-77	|SLC1
Fungal Related Genes/Proteins	Insenser M, et al. (2006) Proteomic analysis of detergent-resistant membranes from Candida albicans. Proteomics 6 Suppl 1:S74-81	|ATP2 |ECM33 |EFT1 |EFT2 |ERG11 |HSC82 |HXT6 |KRE2 |KTR1 |PET2 |PMA1 |PMT2 |POR1 |RPL16A |MORE
RNA Levels and Processing Regulation of	Tanaka F, et al. (2006) Functional genomic analysis of commercial baker's yeast during initial stages of model dough-fermentation. Food Microbiol 23(8):717-28	|ACE2 |ACO1 |ACS1 |ACS2 |ACT1 |ADH1 |ADH2 |ADH5 |ADK1 |AIM38 |ALD2 |ALG8 |ARG1 |ARG3 |MORE
Genetic Interactions Mutants/Phenotypes Strains/Constructs	Gaigg B, et al. (2005) Synthesis of sphingolipids with very long chain fatty acids but not ergosterol is required for routing of newly synthesized plasma membrane ATPase to the cell surface of yeast. J Biol Chem 280(23):22515-22	|ACB1 |ACC1 |ARE1 |ARE2 |AYR1 |CSG2 |DPL1 |ELO1 |ERG24 |ERG3 |ERG4 |ERG5 |FEN1 |HEM1 |MORE
RNA Levels and Processing Regulation of Transcription	Puig S, et al. (2005) Coordinated remodeling of cellular metabolism during iron deficiency through targeted mRNA degradation. Cell 120(1):99-110	|ACO1 |AFT1 |AFT2 |CCC1 |CCP1 |CIR2 |CIT1 |CIT3 |COQ6 |COR1 |COX4 |COX6 |COX8 |COX9 |MORE
Function/Process Mutants/Phenotypes Strains/Constructs	Zaremberg V, et al. (2005) Cytotoxicity of an anti-cancer lysophospholipid through selective modification of lipid raft composition. J Biol Chem 280(45):38047-58	|ERG3 |FEN1 |LCB1 |PCT1 |PMA1 |SUR4
Non-Fungal Related Genes/Proteins	Alderson NL, et al. (2004) The human FA2H gene encodes a fatty acid 2-hydroxylase. J Biol Chem 279(47):48562-8
RNA Levels and Processing Regulation of Substrates/Ligands/Cofactors	Bro C, et al. (2004) Genome-wide transcriptional response of a Saccharomyces cerevisiae strain with an altered redox metabolism. Biotechnol Bioeng 85(3):269-76	|ADE3 |AIM5 |ALD6 |ARP3 |ATP15 |BRR6 |EAF5 |GDH1 |GND1 |HOM6 |IMD2 |KGD1 |LYS9 |MET13 |MORE
Genetic Interactions Strains/Constructs	Parsons AB, et al. (2004) Integration of chemical-genetic and genetic interaction data links bioactive compounds to cellular target pathways. Nat Biotechnol 22(1):62-9	|ARV1 |BEM1 |BEM2 |BRE1 |BRE2 |BTS1 |BUD25 |CAX4 |CHO2 |CIK1 |CIN1 |CIN2 |CIN4 |CLB3 |MORE
Large-scale phenotype analysis Mutants/Phenotypes	Riles L, et al. (2004) Large-scale screening of yeast mutants for sensitivity to the IMP dehydrogenase inhibitor 6-azauracil. Yeast 21(3):241-8	|ADE12 |BUL1 |CGI121 |COG1 |DLT1 |DST1 |DUN1 |EAF7 |FYV10 |GAL11 |GET1 |GIS4 |HUR1 |ILV6 |MORE
Genetic Interactions Strains/Constructs	Tong AH, et al. (2004) Global mapping of the yeast genetic interaction network. Science 303(5659):808-13	|AAD4 |AAH1 |ABF2 |ACE2 |ADH6 |AEP2 |AFG1 |AGP1 |AHC1 |AHC2 |AIM21 |AIM22 |AIM26 |AIM29 |MORE
Regulation of Transcription	Lucau-Danila A, et al. (2003) Competitive promoter occupancy by two yeast paralogous transcription factors controlling the multidrug resistance phenomenon. J Biol Chem 278(52):52641-50	|ADH7 |AZR1 |CSH1 |FLR1 |LPX1 |PDR17 |PLB1 |SNG1 |SNQ2 |TPO4 |YDR061W |YGR035C |YJL216C |YLL056C |MORE
Genetic Interactions Mutants/Phenotypes Strains/Constructs	Uemura S, et al. (2003) Csg1p and newly identified Csh1p function in mannosylinositol phosphorylceramide synthesis by interacting with Csg2p. J Biol Chem 278(46):45049-55	|CSG2 |CSH1 |IPT1 |SUR1 |SUR2
Reviews	Funato K, et al. (2002) Biosynthesis and trafficking of sphingolipids in the yeast Saccharomyces cerevisiae. Biochemistry 41(51):15105-14	|ACB1 |AUR1 |CCC2 |CSG2 |DPL1 |ELO1 |FEN1 |FMP45 |IFA38 |IPT1 |ISC1 |LAC1 |LAG1 |LCB1 |MORE
Function/Process	Swain E, et al. (2002) Sterol-dependent regulation of sphingolipid metabolism in Saccharomyces cerevisiae. J Biol Chem 277(29):26177-84	|CCC2 |ERG26 |LCB3 |SUR2
Alias Function/Process Mutants/Phenotypes Strains/Constructs	Hama H, et al. (2000) Requirement of sphingolipid alpha-hydroxylation for fungicidal action of syringomycin E. FEBS Lett 478(1-2):26-8
Function/Process Reviews	Dickson RC and Lester RL (1999) Metabolism and selected functions of sphingolipids in the yeast Saccharomyces cerevisiae. Biochim Biophys Acta 1438(3):305-21	|AUR1 |CSG2 |DPL1 |ERG2 |FAS2 |FEN1 |IPT1 |LCB1 |LCB2 |LCB3 |LCB4 |LCB5 |MSN2 |MSN4 |MORE
Reviews	Daum G, et al. (1998) Biochemistry, cell biology and molecular biology of lipids of Saccharomyces cerevisiae. Yeast 14(16):1471-510	|ACC1 |ACP1 |AUR1 |CDS1 |CEM1 |CHO1 |CHO2 |CKI1 |CPT1 |CRD1 |CSG2 |DPL1 |DPP1 |EPT1 |MORE
Function/Process Genetic Interactions Mutants/Phenotypes Protein Sequence Features Strains/Constructs	Dunn TM, et al. (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(4):311-21	|CSG2 |SUR1
Function/Process Genetic Interactions Mutants/Phenotypes Strains/Constructs	Haak D, et al. (1997) Hydroxylation of Saccharomyces cerevisiae ceramides requires Sur2p and Scs7p. J Biol Chem 272(47):29704-10	|CSG2 |SUR1 |SUR2
Alias Cross-species Expression DNA/RNA Sequence Features Function/Process Mapping Mutants/Phenotypes Non-Fungal Related Genes/Proteins Protein Sequence Features Strains/Constructs Techniques and Reagents Transcription	Mitchell AG and Martin CE (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(45):28281-8	|OLE1
Fungal Related Genes/Proteins Mutants/Phenotypes Strains/Constructs	Zhao C, et al. (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(34):21480-8	|CSG2 |LCB1 |LCB2

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