Reviewed, UniProtKB/Swiss-Prot Q08548 (ALE1_YEAST)

Names and origin

Protein names

Recommended name:
    Lysophospholipid acyltransferase
      Short name=LPLAT
    EC=2.3.1.51
    EC=2.3.1.23
Alternative name(s):
    1-acyl-sn-glycerol-3-phosphate acyltransferase
      Short name=AGPAT
    Lysophosphatidic acid acyltransferase
      Short name=LPAAT
    Lysophosphatidylethanolamine acyltransferase
      Short name=LPEAT
    Lysophosphatidylcholine acyltransferase
      Short name=LPCAT

Gene names

Name:	ALE1
Synonyms:	LCA1, LPT1, SLC4
Ordered Locus Names:	YOR175C
ORF Names:	O3635

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

General annotation (Comments)

Function	Membrane-bound O-acyltransferase that mediates the incorporation of unsaturated acyl chains into the sn-2 position of phopholipids. Preferentially acylates lysophosphocholine, but also lysophosphoethanolamine and lysophosphatidylglycerol. Ref.8 Ref.9 Ref.10 Ref.11
Catalytic activity	Acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate. Acyl-CoA + 1-acyl-sn-glycero-3-phosphocholine = CoA + 1,2-diacyl-sn-glycero-3-phosphocholine. Acyl-CoA + 1-acyl-sn-glycero-3-phosphoethanolamine = CoA + 1,2-diacyl-sn-glycero-3-phosphoethanolamine.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein. Microsome membrane; Multi-pass membrane protein. Ref.9 Ref.10 Ref.5
Sequence similarities	Belongs to the membrane-bound acyltransferase family.
Biophysicochemical properties	Kinetic parameters: KM=10 µM for oleoyl-CoA (with lysophosphoethanolamine as cosubstrate) KM=17 µM for palmitoleoyl-CoA (with lysophosphoethanolamine as cosubstrate) KM=0.9 µM for palmitoyl-CoA (with lysophosphoethanolamine as cosubstrate) KM=0.4 µM for myristoyl-CoA (with lysophosphoethanolamine as cosubstrate) KM=49 µM for oleoyl-CoA (with lysophosphocholine as cosubstrate) KM=21 µM for palmitoleoyl-CoA (with lysophosphocholine as cosubstrate) KM=1.8 µM for palmitoyl-CoA (with lysophosphocholine as cosubstrate) KM=5.9 µM for stearoyl-CoA (with lysophosphocholine as cosubstrate) KM=11 µM for arachidonyl-CoA (with lysophosphocholine as cosubstrate) Vmax=38 nmol/min/mg enzyme with oleoyl-CoA as substrate (with lysophosphoethanolamine as cosubstrate) Vmax=44 nmol/min/mg enzyme with palmitoleoyl-CoA as substrate (with lysophosphoethanolamine as substrate) Vmax=3.7 nmol/min/mg enzyme with palmitoyl-CoA as substrate (with lysophosphoethanolamine as substrate) Vmax=1.2 nmol/min/mg enzyme with myristoyl-CoA as substrate (with lysophosphoethanolamine as substrate) Vmax=125 nmol/min/mg enzyme with oleoyl-CoA as substrate (with lysophosphocholine as substrate) Vmax=142 nmol/min/mg enzyme with palmitoleoyl-CoA as substrate (with lysophosphocholine as substrate) Vmax=7.8 nmol/min/mg enzyme with palmitoyl-CoA as substrate (with lysophosphocholine as substrate) Vmax=12 nmol/min/mg enzyme with stearoyl-CoA as substrate (with lysophosphocholine as substrate) Vmax=58 nmol/min/mg enzyme with arachidonyl-CoA as substrate (with lysophosphocholine as substrate) pH dependence: Optimum pH is 6.5-7.5.

Ontologies

Keywords
Biological process	Phospholipid biosynthesis
Cellular component	Endoplasmic reticulum Membrane Microsome
Domain	Coiled coil Transmembrane
Molecular function	Acyltransferase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	glycerophospholipid biosynthetic process Ref.10 Ref.11 Inferred from mutant phenotype. Source: SGD
Cellular component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW microsome Ref.11 Inferred from direct assay. Source: SGD
Molecular function	1-acylglycerol-3-phosphate O-acyltransferase activity Ref.10 Ref.11 Inferred from mutant phenotype. Source: SGD 1-acylglycerophosphocholine O-acyltransferase activity Ref.10 Inferred from mutant phenotype. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 619	619	Lysophospholipid acyltransferase		PRO_0000245257
Regions
	Topological domain	1 – 19	19	Lumenal Potential
	Transmembrane	20 – 39	20	Potential
	Topological domain	40 – 51	12	Cytoplasmic Potential
	Transmembrane	52 – 72	21	Potential
	Topological domain	73 – 92	20	Lumenal Potential
	Transmembrane	93 – 113	21	Potential
	Topological domain	114 – 231	118	Cytoplasmic Potential
	Transmembrane	232 – 252	21	Potential
	Topological domain	253 – 274	22	Lumenal Potential
	Transmembrane	275 – 295	21	Potential
	Topological domain	296 – 429	134	Cytoplasmic Potential
	Transmembrane	430 – 450	21	Potential
	Topological domain	451 – 456	6	Lumenal Potential
	Transmembrane	457 – 477	21	Potential
	Topological domain	478 – 619	142	Cytoplasmic Potential
	Coiled coil	545 – 593	49	Potential
Sites
	Active site	382	1	Potential
Amino acid modifications
	Modified residue	512	1	Phosphoserine Ref.15
	Modified residue	513	1	Phosphoserine Ref.15 Ref.6 Ref.12
	Modified residue	605	1	Phosphoserine Ref.15 Ref.12 Ref.13 Ref.14
	Modified residue	607	1	Phosphoserine Ref.15 Ref.4
	Modified residue	610	1	Phosphoserine Ref.15 Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q08548-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 87C74C9194BE0BC5	FASTA	619	72,228
	10 20 30 40 50 60 MYNPVDAVLT KIITNYGIDS FTLRYAICLL GSFPLNAILK RIPEKRIGLK CCFIISMSMF 70 80 90 100 110 120 YLFGVLNLVS GFRTLFISTM FTYLISRFYR SKFMPHLNFM FVMGHLAINH IHAQFLNEQT 130 140 150 160 170 180 QTTVDITSSQ MVLAMKLTSF AWSYYDGSCT SESDFKDLTE HQKSRAVRGH PPLLKFLAYA 190 200 210 220 230 240 FFYSTLLTGP SFDYADFDSW LNCEMFRDLP ESKKPMRRHH PGERRQIPKN GKLALWKVVQ 250 260 270 280 290 300 GLAWMILSTL GMKHFPVKYV LDKDGFPTRS FIFRIHYLFL LGFIHRFKYY AAWTISEGSC 310 320 330 340 350 360 ILCGLGYNGY DSKTQKIRWD RVRNIDIWTV ETAQNTREML EAWNMNTNKW LKYSVYLRVT 370 380 390 400 410 420 KKGKKPGFRS TLFTFLTSAF WHGTRPGYYL TFATGALYQT CGKIYRRNFR PIFLREDGVT 430 440 450 460 470 480 PLPSKKIYDL VGIYAIKLAF GYMVQPFIIL DLKPSLMVWG SVYFYVHIIV AFSFFLFRGP 490 500 510 520 530 540 YAKQVTEFFK SKQPKEIFIR KQKKLEKDIS ASSPNLGGIL KAKIEHEKGK TAEEEEMNLG 550 560 570 580 590 600 IPPIELEKWD NAKEDWEDFC KDYKEWRNKN GLEIEEENLS KAFERFKQEF SNAASGSGER 610 VRKMSFSGYS PKPISKKEE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV." Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D. , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K. Nature 387:98-102(1997) [PubMed: 9169874] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[2]	"Analysis of a 22,956 bp region on the right arm of Saccharomyces cerevisiae chromosome XV." Madania A., Poch O., Tarassov I.A., Winsor B., Martin R.P. Yeast 12:1563-1573(1996) [PubMed: 8972579] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 270-619. Strain: S288c / FY1678.
[3]	"A superfamily of membrane-bound O-acyltransferases with implications for wnt signaling." Hofmann K. Trends Biochem. Sci. 25:111-112(2000) [PubMed: 10694878] [Abstract] Cited for: SIMILARITY.
[4]	"Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae." Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M., Shabanowitz J., Hunt D.F., White F.M. Nat. Biotechnol. 20:301-305(2002) [PubMed: 11875433] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-607 AND SER-610, MASS SPECTROMETRY.
[5]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[6]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed: 15665377] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-513, MASS SPECTROMETRY.
[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]	"The yeast acylglycerol acyltransferase LCA1 is a key component of Lands cycle for phosphatidylcholine turnover." Chen Q., Kazachkov M., Zheng Z., Zou J. FEBS Lett. 581:5511-5516(2007) [PubMed: 17996202] [Abstract] Cited for: FUNCTION.
[9]	"Identification and characterization of the major lysophosphatidylethanolamine acyltransferase in Saccharomyces cerevisiae." Riekhof W.R., Wu J., Jones J.L., Voelker D.R. J. Biol. Chem. 282:28344-28352(2007) [PubMed: 17652094] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[10]	"Identification of a novel lysophospholipid acyltransferase in Saccharomyces cerevisiae." Jain S., Stanford N., Bhagwat N., Seiler B., Costanzo M., Boone C., Oelkers P. J. Biol. Chem. 282:30562-30569(2007) [PubMed: 17726007] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[11]	"SLC1 and SLC4 encode partially redundant acyl-coenzyme A 1-acylglycerol-3-phosphate O-acyltransferases of budding yeast." Benghezal M., Roubaty C., Veepuri V., Knudsen J., Conzelmann A. J. Biol. Chem. 282:30845-30855(2007) [PubMed: 17675291] [Abstract] Cited for: FUNCTION.
[12]	"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-513 AND SER-605, MASS SPECTROMETRY.
[13]	"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-605, MASS SPECTROMETRY.
[14]	"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-605, MASS SPECTROMETRY.
[15]	"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-512; SER-513; SER-605; SER-607 AND SER-610, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z75083 Genomic DNA. Translation: CAA99384.1. U55021 Genomic DNA. Translation: AAB47420.1.
PIR	S67067.
RefSeq	NP_014818.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:5617N.
IntAct	Q08548. 1 interaction.
Proteomic databases
PeptideAtlas	Q08548.
Genome annotation databases
Ensembl	YOR175C. Saccharomyces cerevisiae. [Contig view]
GeneID	854346.
NMPDR	fig|4932.3.peg.5926.
Organism-specific databases
CYGD	YOR175c.
SGD	S000005701. ALE1.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	Q08548.
OMA	Q08548. MNTNKWL.
Enzyme and pathway databases
BRENDA	2.3.1.23. 250. 2.3.1.51. 250.
Gene expression databases
ArrayExpress	Q08548.
GermOnline	YOR175C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR004299. MBOAT_fam. [Graphical view]
Pfam	PF03062. MBOAT. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	976426.

Entry information

Entry name

ALE1_YEAST

Accession

Primary (citable) accession number: Q08548
Secondary accession number(s): Q03130

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 11, 2006
Last sequence update:	November 1, 1996
Last modified:	June 16, 2009
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)