P40030 (ERG28_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ergosterol biosynthetic protein 28

Gene names

Name:	ERG28
Synonyms:	BUD18
Ordered Locus Names:	YER044C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	148 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (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. Ref.4
Subunit structure	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. Ref.5 Ref.7 Ref.8
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein Probable Ref.5.
Miscellaneous	Present with 377 molecules/cell in log phase SD medium. Ref.6
Sequence similarities	Belongs to the ERG28 family.

Ontologies

Keywords
Biological process	Lipid synthesis Steroid biosynthesis Sterol biosynthesis
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane Transmembrane helix
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	ergosterol biosynthetic process Inferred from direct assay Ref.4. Source: SGD
Cellular component	endoplasmic reticulum membrane Inferred from direct assay Ref.5. Source: SGD integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	protein binding, bridging Inferred from physical interaction Ref.5Ref.7. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ERG25	P53045	3	EBI-22518,EBI-6506
ERG26	P53199	3	EBI-22518,EBI-6514
ERG27	Q12452	6	EBI-22518,EBI-38132

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 148	148	Ergosterol biosynthetic protein 28		PRO_0000193908
Regions
	Topological domain	1 – 25	25	Cytoplasmic Potential
	Transmembrane	26 – 46	21	Helical; Potential
	Topological domain	47 – 92	46	Lumenal Potential
	Transmembrane	93 – 113	21	Helical; Potential
	Topological domain	114 – 120	7	Cytoplasmic Potential
	Transmembrane	121 – 136	16	Helical; Potential
	Topological domain	137 – 148	12	Lumenal Potential

Sequences

	Sequence		Length	Mass (Da)
	P40030 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: F1BD39AFA180E367	FASTA	148	17,135
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome V." 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. Nature 387:78-81(1997) [PubMed: 9169868] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[3]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." 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. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	"A novel gene conserved from yeast to humans is involved in sterol biosynthesis." Gachotte D., Eckstein J., Barbuch R., Hughes T., Roberts C., Bard M. J. Lipid Res. 42:150-154(2001) [PubMed: 11160377] [Abstract] Cited for: FUNCTION.
[5]	"Protein-protein interactions among C-4 demethylation enzymes involved in yeast sterol biosynthesis." Mo C., Valachovic M., Randall S.K., Nickels J.T., Bard M. Proc. Natl. Acad. Sci. U.S.A. 99:9739-9744(2002) [PubMed: 12119386] [Abstract] Cited for: SUBUNIT, INTERACTION WITH ERG25 AND ERG27, SUBCELLULAR LOCATION.
[6]	"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].
[7]	"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)." Mo C., Valachovic M., Bard M. Biochim. Biophys. Acta 1686:30-36(2004) [PubMed: 15522820] [Abstract] Cited for: INTERACTION WITH ERG6.
[8]	"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 ERG1; ERG3; ERG5; ERG6; ERG11; ERG25; ERG26 AND ERG27.
[9]	"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]. Strain: ATCC 208353 / W303-1A.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U18796 Genomic DNA. Translation: AAB64579.1. AY558453 Genomic DNA. Translation: AAS56779.1. BK006939 Genomic DNA. Translation: DAA07698.1.
PIR	S50547.
RefSeq	NP_010962.1. NM_001178935.1.
3D structure databases
ProteinModelPortal	P40030.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-2672N.
IntAct	P40030. 18 interactions.
MINT	MINT-510893.
STRING	P40030.
Proteomic databases
PeptideAtlas	P40030.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YER044C; YER044C; YER044C.
GeneID	856767.
KEGG	sce:YER044C.
NMPDR	fig|4932.3.peg.2024.
Organism-specific databases
CYGD	YER044c.
SGD	S000000846. ERG28.
Phylogenomic databases
eggNOG	fuNOG12242.
GeneTree	EFGT00050000004124.
HOGENOM	HBG444695.
OMA	TVQSFRD.
OrthoDB	EOG46X2JT.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-14347.
Gene expression databases
ArrayExpress	P40030.
Genevestigator	P40030.
GermOnline	YER044C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR005352. Erg28. [Graphical view]
Pfam	PF03694. Erg28. 1 hit. [Graphical view]
ProtoNet	Search...
Other
DrugBank	DB00681. Amphotericin B. DB04794. Bifonazole. DB01152. Candicidin. DB00826. Natamycin. DB00239. Oxiconazole.
NextBio	982950.

Entry information

Entry name

ERG28_YEAST

Accession

Primary (citable) accession number: P40030
Secondary accession number(s): D3DLU4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	December 14, 2011
This is version 94 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program