Reviewed,
UniProtKB/Swiss-Prot P10614 (CP51_YEAST)
Last modified
January 19, 2010.
Version 100.
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Lanosterol 14-alpha demethylase EC=1.14.13.70 Alternative name(s): Cytochrome P450 51 CYPLI Cytochrome P450-LIA1 Sterol 14-alpha demethylase Cytochrome P450-14DM | ||||||
| Gene names |
| ||||||
| Organism | Saccharomyces cerevisiae (Baker's yeast) [Complete proteome] | ||||||
| Taxonomic identifier | 4932 [NCBI] | ||||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces |
Protein attributes
| Sequence length | 530 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Catalyzes C14-demethylation of lanosterol which is critical for ergosterol biosynthesis. It transforms lanosterol into 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol. |
| Catalytic activity | Obtusifoliol + 3 O2 + 3 NADPH = 4-alpha-methyl-5-alpha-ergosta-8,14,24(28)-trien-3-beta-ol + formate + 3 NADP+ + 4 H2O. |
| Cofactor | Heme group By similarity. |
| Pathway | Steroid biosynthesis; zymosterol biosynthesis; zymosterol from lanosterol: step 1/6. |
| Subunit structure | Interacts with ERG28. Ref.6 |
| Subcellular location | |
| Miscellaneous | It is the main target for antifungal compounds of the triazole family like ketoconazole which inhibits by coordinating the iron atom at the sixth ligand position. Present with 73200 molecules/cell in log phase SD medium. Ref.5 |
| Sequence similarities | Belongs to the cytochrome P450 family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Lipid synthesis Steroid biosynthesis Sterol biosynthesis |
| Cellular component | Membrane |
| Domain | Transmembrane |
| Ligand | Heme Iron Metal-binding NADP |
| Molecular function | Monooxygenase Oxidoreductase |
| PTM | Phosphoprotein |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW sterol biosynthetic processInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | endoplasmic reticulum Inferred from direct assay. Source: SGD integral to membraneInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | electron carrier activity Inferred from electronic annotation. Source: InterPro heme bindingInferred from electronic annotation. Source: InterPro identical protein bindingInferred from physical interaction. Source: IntAct sterol 14-demethylase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Binary interactions
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 530 | 530 | Lanosterol 14-alpha demethylase | PRO_0000052012 | |||||
Regions | |||||||||
| Topological domain | 1 – 20 | 20 | Extracellular Potential | ||||||
| Transmembrane | 21 – 41 | 21 | Potential | ||||||
| Topological domain | 42 – 530 | 489 | Cytoplasmic Potential | ||||||
Sites | |||||||||
| Metal binding | 470 | 1 | Iron (heme axial ligand) By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 458 | 1 | Phosphoserine Ref.8 Ref.9 | ||||||
Experimental info | |||||||||
| Sequence conflict | 433 | 1 | K → N in AAA34546. Ref.2 | ||||||
| Sequence conflict | 433 | 1 | K → N in AAA34547. Ref.2 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Primary structure of the P450 lanosterol demethylase gene from Saccharomyces cerevisiae." Kalb V.F., Woods C.W., Turi T.G., Dey C.R., Sutter T.R., Loper J.C. DNA 6:529-537(1987) [PubMed: 3322742] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "A single amino acid substitution converts cytochrome P450(14DM) to an inactive form, cytochrome P450SG1: complete primary structures deduced from cloned DNAS." Ishida N., Aoyama Y., Hatanaka R., Oyama Y., Imajo S., Ishiguro M., Oshima T., Nakazato H., Noguchi T., Maitra U.S., Mohan V.P., Sprinson D.B., Yoshida Y. Biochem. Biophys. Res. Commun. 155:317-323(1988) [PubMed: 3046615] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [3] | "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII." Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P.  Vaudin M.Science 265:2077-2082(1994) [PubMed: 8091229] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972. |
| [4] | "Isolation of a cytochrome P-450 structural gene from Saccharomyces cerevisiae." Kalb V.F., Loper J.C., Dey C.R., Woods C.W., Sutter T.R. Gene 45:237-245(1986) [PubMed: 3542713] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 444-530. |
| [5] | "Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. |
| [6] | "Erg28p is a key protein in the yeast sterol biosynthetic enzyme complex." Mo C., Bard M. J. Lipid Res. 46:1991-1998(2005) [PubMed: 15995173] [Abstract] Cited for: INTERACTION WITH ERG28. |
| [7] | "A global topology map of the Saccharomyces cerevisiae membrane proteome." Kim H., Melen K., Oesterberg M., von Heijne G. Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed: 16847258] [Abstract] Cited for: TOPOLOGY [LARGE SCALE ANALYSIS]. |
| [8] | "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-458, MASS SPECTROMETRY. |
| [9] | "A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-458, MASS SPECTROMETRY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | M18109 Genomic DNA. Translation: AAA34379.1. M15663 Genomic DNA. Translation: AAA34837.1. M21483 Genomic DNA. Translation: AAA34546.1. M21484 Genomic DNA. Translation: AAA34547.1. U10555 Genomic DNA. Translation: AAB68433.1. |
| PIR | A27491. |
| RefSeq | NP_011871.1. |
3D structure databases | |
| SMR | P10614. Positions 57-525. |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP-7886N. |
| IntAct | P10614. 118 interactions. |
| STRING | P10614. |
Proteomic databases | |
| PeptideAtlas | P10614. |
Genome annotation databases | |
| Ensembl | YHR007C; YHR007C; YHR007C; Saccharomyces cerevisiae. [Genome view] |
| GeneID | 856398. |
| KEGG | sce:YHR007C. |
| NMPDR | fig|4932.3.peg.3015. |
Organism-specific databases | |
| CYGD | YHR007c. |
| SGD | S000001049. ERG11. |
Phylogenomic databases | |
| eggNOG | fuNOG06039. |
| HOGENOM | HBG566517. |
| OMA | VLMGGQH. |
| OrthoDB | EOG99W3XX. |
| PhylomeDB | P10614. |
Enzyme and pathway databases | |
| BioCyc | MetaCyc:YHR007C-MONOMER. |
| BRENDA | 1.14.13.70. 250. |
Gene expression databases | |
| ArrayExpress | P10614. |
| Genevestigator | P10614. |
| GermOnline | YHR007C. Saccharomyces cerevisiae. |
Family and domain databases | |
| InterPro | IPR001128. Cyt_P450. IPR017973. Cyt_P450_C. IPR017972. Cyt_P450_CS. IPR002403. Cyt_P450_E_grp-IV. [Graphical view] |
| Gene3D | G3DSA:1.10.630.10. Cyt_P450. 1 hit. |
| PANTHER | PTHR19383. Cyt_P450. 1 hit. |
| Pfam | PF00067. p450. 1 hit. [Graphical view] |
| PRINTS | PR00465. EP450IV. PR00385. P450. |
| PROSITE | PS00086. CYTOCHROME_P450. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| DrugBank | DB00257. Clotrimazole. DB01127. Econazole. DB00196. Fluconazole. DB01026. Ketoconazole. DB01263. Posaconazole. DB01153. Sertaconazole. DB00251. Terconazole. DB01007. Tioconazole. DB00582. Voriconazole. |
| NextBio | 981925. |
Entry information
| Entry name | CP51_YEAST | ||||||||
| Accession | Primary (citable) accession number: P10614 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |
| Yeast Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD |
| Yeast chromosome VIII Yeast (Saccharomyces cerevisiae) chromosome VIII: entries and gene names |
