Reviewed, UniProtKB/Swiss-Prot P53629 (ARE2_YEAST)

Names and origin

Protein names

Recommended name:
    Sterol O-acyltransferase 2
    EC=2.3.1.26
Alternative name(s):
    Sterol-ester synthase 2

Gene names

Name:	ARE2
Synonyms:	SAT1
Ordered Locus Names:	YNR019W
ORF Names:	N3206

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	642 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Ensures probably most of the acyltransferase activity. Suppression of ARE2 reduces sterol ester levels to 25% of the normal value.
Catalytic activity	Acyl-CoA + cholesterol = CoA + cholesterol ester.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein.
Miscellaneous	Present with 279 molecules/cell in log phase SD medium. Ref.4
Sequence similarities	Belongs to the membrane-bound acyltransferase family. Sterol o-acyltransferase subfamily.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane
Molecular function	Acyltransferase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	ergosterol metabolic process Inferred from genetic interaction. Source: SGD
Cellular component	endoplasmic reticulum Inferred from direct assay. Source: SGD integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	cholesterol O-acyltransferase activity Inferred from electronic annotation. Source: EC ergosterol O-acyltransferase activity Inferred from genetic interaction. Source: SGD lanosterol O-acyltransferase activity Inferred from electronic annotation. Source: EC protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PTC1	P35182	1	EBI-2808,EBI-12784

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 642	642	Sterol O-acyltransferase 2		PRO_0000207651
Regions
	Transmembrane	215 – 235	21	Potential
	Transmembrane	292 – 312	21	Potential
	Transmembrane	404 – 424	21	Potential
	Transmembrane	442 – 462	21	Potential
	Transmembrane	485 – 505	21	Potential
	Transmembrane	567 – 587	21	Potential
	Transmembrane	622 – 642	21	Potential
Sites
	Active site	579	1	Potential
Amino acid modifications
	Modified residue	29	1	Phosphoserine Ref.8
	Modified residue	47	1	Phosphoserine Ref.8
	Modified residue	175	1	Phosphoserine Ref.8 Ref.5 Ref.6 Ref.7
	Modified residue	176	1	Phosphoserine Ref.8 Ref.7
Experimental info
	Sequence conflict	80	1	G → D in AAC49441. Ref.2
	Sequence conflict	184	1	G → E in AAC49441. Ref.2
	Sequence conflict	211	1	I → L in AAC49441. Ref.2
	Sequence conflict	612	1	F → S in AAC49441. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P53629-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 035FC4ED9C7CD830	FASTA	642	74,023
	10 20 30 40 50 60 MDKKKDLLEN EQFLRIQKLN AADAGKRQSI TVDDEGELYG LDTSGNSPAN EHTATTITQN 70 80 90 100 110 120 HSVVASNGDV AFIPGTATEG NTEIVTEEVI ETDDNMFKTH VKTLSSKEKA RYRQGSSNFI 130 140 150 160 170 180 SYFDDMSFEH RPSILDGSVN EPFKTKFVGP TLEKEIRRRE KELMAMRKNL HHRKSSPDAV 190 200 210 220 230 240 DSVGKNDGAA PTTVPTAATS ETVVTVETTI ISSNFSGLYV AFWMAIAFGA VKALIDYYYQ 250 260 270 280 290 300 HNGSFKDSEI LKFMTTNLFT VASVDLLMYL STYFVVGIQY LCKWGVLKWG TTGWIFTSIY 310 320 330 340 350 360 EFLFVIFYMY LTENILKLHW LSKIFLFLHS LVLLMKMHSF AFYNGYLWGI KEELQFSKSA 370 380 390 400 410 420 LAKYKDSIND PKVIGALEKS CEFCSFELSS QSLSDQTQKF PNNISAKSFF WFTMFPTLIY 430 440 450 460 470 480 QIEYPRTKEI RWSYVLEKIC AIFGTIFLMM IDAQILMYPV AMRALAVRNS EWTGILDRLL 490 500 510 520 530 540 KWVGLLVDIV PGFIVMYILD FYLIWDAILN CVAELTRFGD RYFYGDWWNC VSWADFSRIW 550 560 570 580 590 600 NIPVHKFLLR HVYHSSMSSF KLNKSQATLM TFFLSSVVHE LAMYVIFKKL RFYLFFFQML 610 620 630 640 QMPLVALTNT KFMRNRTIIG NVIFWLGICM GPSVMCTLYL TF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sterol esterification in yeast: a two-gene process." Yang H., Bard M., Bruner D.A., Gleeson A., Deckelbaum R.J., Aljinovic G., Pohl T.M., Rothstein R., Sturley S.L. Science 272:1353-1356(1996) [PubMed: 8650549] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
[2]	"Molecular cloning and characterization of two isoforms of Saccharomyces cerevisiae acyl-CoA:sterol acyltransferase." Yu C., Kennedy N.J., Chang C.C.Y., Rothblatt J.A. J. Biol. Chem. 271:24157-24163(1996) [PubMed: 8798656] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: S288c / SNY243.
[3]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications." Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J. , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J. Nature 387:93-98(1997) [PubMed: 9169873] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	"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].
[5]	"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-175, MASS SPECTROMETRY.
[6]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175, MASS SPECTROMETRY.
[7]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175 AND SER-176, MASS SPECTROMETRY.
[8]	"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-29; SER-47; SER-175 AND SER-176, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U51790 Genomic DNA. Translation: AAB02203.1. U55383 Genomic DNA. Translation: AAC49441.1. Z71634 Genomic DNA. Translation: CAA96298.1.
PIR	S63350.
RefSeq	NP_014416.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:4050N.
IntAct	P53629. 14 interactions.
STRING	P53629.
Proteomic databases
PeptideAtlas	P53629.
PRIDE	P53629.
Genome annotation databases
Ensembl	YNR019W; YNR019W; YNR019W; Saccharomyces cerevisiae. [Genome view]
GeneID	855753.
GenomeReviews	Gene locus YNR019W in contig Y13139_GR.
KEGG	sce:YNR019W.
NMPDR	fig|4932.3.peg.5496.
Organism-specific databases
CYGD	YNR019w.
SGD	S000005302. ARE2.
Phylogenomic databases
HOGENOM	P53629.
OMA	WDAILNC.
Enzyme and pathway databases
BRENDA	2.3.1.26. 250.
Gene expression databases
ArrayExpress	P53629.
Genevestigator	P53629.
GermOnline	YNR019W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR004299. MBOAT_fam. [Graphical view]
Pfam	PF03062. MBOAT. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	980172.

Entry information

Entry name

ARE2_YEAST

Accession

Primary (citable) accession number: P53629
Secondary accession number(s): Q12673

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	November 3, 2009
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)