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UniProtKB/Swiss-Prot entry P40030


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ERG28_YEAST
Primary accession number P40030
Secondary accession numbers None
Integrated into Swiss-Prot on February 1, 1995
Sequence was last modified on February 1, 1995 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 70)
Name and origin of the protein
Protein name Ergosterol biosynthetic protein 28
Synonyms None
Gene name
Name: ERG28
Synonyms: BUD18
OrderedLocusNames: YER044C
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204511 / S288c / AB972;
PubMed=9169868 [NCBI, ExPASy, EBI, Israel, Japan]
Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y., Botstein D., Davis R.W.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
Nature 387:78-81(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
DOI=10.1101/gr.6037607; PubMed=17322287 [NCBI, ExPASy, EBI, Israel, Japan]
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., 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.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[3]
FUNCTION.
PubMed=11160377 [NCBI, ExPASy, EBI, Israel, Japan]
Gachotte D., Eckstein J., Barbuch R., Hughes T., Roberts C., Bard M.;
"A novel gene conserved from yeast to humans is involved in sterol biosynthesis.";
J. Lipid Res. 42:150-154(2001).
[4]
SUBUNIT, INTERACTION WITH ERG25 AND ERG27, AND SUBCELLULAR LOCATION.
DOI=10.1073/pnas.112202799; PubMed=12119386 [NCBI, ExPASy, EBI, Israel, Japan]
Mo C., Valachovic M., Randall S.K., Nickels J.T., Bard M.;
"Protein-protein interactions among C-4 demethylation enzymes involved in yeast sterol biosynthesis.";
Proc. Natl. Acad. Sci. U.S.A. 99:9739-9744(2002).
[5]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[6]
INTERACTION WITH ERG6.
DOI=10.1016/j.bbalip.2004.08.001; PubMed=15522820 [NCBI, ExPASy, EBI, Israel, Japan]
Mo C., Valachovic M., Bard M.;
"The ERG28-encoded protein, Erg28p, interacts with both the sterol C-4 demethylation enzyme complex as well as the late biosynthetic protein, the C-24 sterol methyltransferase (Erg6p).";
Biochim. Biophys. Acta 1686:30-36(2004).
[7]
INTERACTION WITH ERG1; ERG3; ERG5; ERG6; ERG11; ERG25; ERG26 AND ERG27.
DOI=10.1194/jlr.M500153-JLR200; PubMed=15995173 [NCBI, ExPASy, EBI, Israel, Japan]
Mo C., Bard M.;
"Erg28p is a key protein in the yeast sterol biosynthetic enzyme complex.";
J. Lipid Res. 46:1991-1998(2005).
[8]
TOPOLOGY [LARGE SCALE ANALYSIS].
DOI=10.1073/pnas.0604075103; PubMed=16847258 [NCBI, ExPASy, EBI, Israel, Japan]
Kim H., Melen K., Oesterberg M., von Heijne G.;
"A global topology map of the Saccharomyces cerevisiae membrane proteome.";
Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
Comments
  • FUNCTION: Has a role as a scaffold to help anchor ERG25, ERG26 and ERG27 to the endoplasmic reticulum. May also be responsible for facilitating their interaction.
  • SUBUNIT: Heterotetramer of ERG25, ERG26, ERG27 and ERG28. ERG28 acts as a scaffold to tether ERG27 and other 4,4-demethylation-related enzymes, forming a demethylation enzyme complex, in the endoplasmic reticulum. Interacts with ERG25, ERG26 and ERG27. Also interacts with ERG1, ERG3, ERG5, ERG6 and ERG11.
  • INTERACTION:
    P53045:ERG25; NbExp=1; IntAct=EBI-22518, EBI-6506;
    P53199:ERG26; NbExp=1; IntAct=EBI-22518, EBI-6514;
    Q12452:ERG27; NbExp=2; IntAct=EBI-22518, EBI-38132;
  • SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein (Probable).
  • MISCELLANEOUS: Present with 377 molecules/cell in log phase SD medium.
  • SIMILARITY: Belongs to the ERG28 family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U18796; AAB64579.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY558453; AAS56779.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S50547; S50547.
RefSeq NP_010962.1; -.
3D structure databases
ModBase P40030.
Protein-protein interaction databases
DIP DIP:2672N; -.
IntAct P40030; -.
Organism-specific databases
CYGD YER044c; -.
SGD S000000846; ERG28.
Yeast-GFP YER044C.
Gene expression databases
GermOnline YER044C; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005789; Cellular component: endoplasmic reticulum membrane (inferred from direct assay from SGD).
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from InterPro).
GO:0030674; Molecular function: protein binding, bridging (inferred from physical interaction from SGD).
GO:0006696; Biological process: ergosterol biosynthetic process (inferred from direct assay from SGD).
QuickGo view.
Family and domain databases
InterPro IPR005352; Erg28.
Graphical view of domain structure.
Pfam PF03694; Erg28; 1.
Pfam graphical view of domain structure.
ProDom PD089646; UPF0143; 1.
[Domain structure / List of seq. sharing at least 1 domain]
ProtoNet P40030.
Proteomic databases
PeptideAtlas P40030; -.
Genome annotation databases
Ensembl YER044C; Saccharomyces cerevisiae. [Contig view]
GeneID 856767; -.
GenomeReviews U00092_GR; YER044C.
KEGG sce:YER044C; -.
NMPDR fig|4932.3.peg.2024; -.
Phylogenomic databases
HOGENOM P40030; -.
Other
DrugBank DB00681; Amphotericin B.
DB04794; Bifonazole.
DB01152; Candicidin.
DB00826; Natamycin.
DB00239; Oxiconazole.
LinkHub P40030; -.
NextBio 982950; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Endoplasmic reticulum; Lipid synthesis; Membrane; Steroid biosynthesis; Sterol biosynthesis; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   148  148     Ergosterol biosynthetic protein 28. PRO_0000193908
TOPO_DOM   1    25  25     Cytoplasmic (Potential). 
TRANSMEM   26    46  21     Potential. 
TOPO_DOM   47    92  46     Lumenal (Potential). 
TRANSMEM   93   113  21     Potential. 
TOPO_DOM   114   120  7     Cytoplasmic (Potential). 
TRANSMEM   121   136  16     Potential. 
TOPO_DOM   137   148  12     Lumenal (Potential). 
Sequence information
Length: 148 AA [This is the length of the unprocessed precursor] Molecular weight: 17135 Da [This is the MW of the unprocessed precursor] CRC64: F1BD39AFA180E367 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MFSLQDVITT TKTTLAAMPK GYLPKWLLFI SIVSVFNSIQ TYVSGLELTR KVYERKPTET 

        70         80         90        100        110        120 
THLSARTFGT WTFISCVIRF YGAMYLNEPH IFELVFMSYM VALFHFGSEL LIFRTCKLGK 

       130        140 
GFMGPLVVST TSLVWMYKQR EYYTGVAW 

P40030 in FASTA format

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