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Protein

Lysophospholipid acyltransferase

Gene

ALE1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Membrane-bound O-acyltransferase that mediates the incorporation of unsaturated acyl chains into the sn-2 position of phospholipids. Preferentially acylates lysophosphocholine, but also lysophosphoethanolamine and lysophosphatidylglycerol.4 Publications

Catalytic activityi

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.

Kineticsi

  1. KM=10 µM for oleoyl-CoA (with lysophosphoethanolamine as cosubstrate)
  2. KM=17 µM for palmitoleoyl-CoA (with lysophosphoethanolamine as cosubstrate)
  3. KM=0.9 µM for palmitoyl-CoA (with lysophosphoethanolamine as cosubstrate)
  4. KM=0.4 µM for myristoyl-CoA (with lysophosphoethanolamine as cosubstrate)
  5. KM=49 µM for oleoyl-CoA (with lysophosphocholine as cosubstrate)
  6. KM=21 µM for palmitoleoyl-CoA (with lysophosphocholine as cosubstrate)
  7. KM=1.8 µM for palmitoyl-CoA (with lysophosphocholine as cosubstrate)
  8. KM=5.9 µM for stearoyl-CoA (with lysophosphocholine as cosubstrate)
  9. KM=11 µM for arachidonyl-CoA (with lysophosphocholine as cosubstrate)
  1. Vmax=38 nmol/min/mg enzyme with oleoyl-CoA as substrate (with lysophosphoethanolamine as cosubstrate)
  2. Vmax=44 nmol/min/mg enzyme with palmitoleoyl-CoA as substrate (with lysophosphoethanolamine as substrate)
  3. Vmax=3.7 nmol/min/mg enzyme with palmitoyl-CoA as substrate (with lysophosphoethanolamine as substrate)
  4. Vmax=1.2 nmol/min/mg enzyme with myristoyl-CoA as substrate (with lysophosphoethanolamine as substrate)
  5. Vmax=125 nmol/min/mg enzyme with oleoyl-CoA as substrate (with lysophosphocholine as substrate)
  6. Vmax=142 nmol/min/mg enzyme with palmitoleoyl-CoA as substrate (with lysophosphocholine as substrate)
  7. Vmax=7.8 nmol/min/mg enzyme with palmitoyl-CoA as substrate (with lysophosphocholine as substrate)
  8. Vmax=12 nmol/min/mg enzyme with stearoyl-CoA as substrate (with lysophosphocholine as substrate)
  9. Vmax=58 nmol/min/mg enzyme with arachidonyl-CoA as substrate (with lysophosphocholine as substrate)

pH dependencei

Optimum pH is 6.5-7.5.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei382 – 3821Sequence analysis

GO - Molecular functioni

  • 1-acylglycerol-3-phosphate O-acyltransferase activity Source: SGD
  • 1-acylglycerophosphocholine O-acyltransferase activity Source: SGD
  • O-acyltransferase activity Source: SGD

GO - Biological processi

  • glycerophospholipid biosynthetic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Enzyme and pathway databases

BioCyciMetaCyc:G3O-33688-MONOMER.
YEAST:G3O-33688-MONOMER.
BRENDAi2.3.1.51. 984.
ReactomeiR-SCE-1482788. Acyl chain remodelling of PC.
R-SCE-1482801. Acyl chain remodelling of PS.
R-SCE-1482839. Acyl chain remodelling of PE.
R-SCE-1482922. Acyl chain remodelling of PI.
SABIO-RKQ08548.

Chemistry

SwissLipidsiSLP:000000083.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysophospholipid acyltransferase (EC:2.3.1.23, EC:2.3.1.51)
Short name:
LPLAT
Alternative name(s):
1-acyl-sn-glycerol-3-phosphate acyltransferase
Short name:
AGPAT
Lysophosphatidic acid acyltransferase
Short name:
LPAAT
Lysophosphatidylcholine acyltransferase
Short name:
LPCAT
Lysophosphatidylethanolamine acyltransferase
Short name:
LPEAT
Gene namesi
Name:ALE1
Synonyms:LCA1, LPT1, SLC4
Ordered Locus Names:YOR175C
ORF Names:O3635
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOR175C.
SGDiS000005701. ALE1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1919LumenalSequence analysisAdd
BLAST
Transmembranei20 – 3920HelicalSequence analysisAdd
BLAST
Topological domaini40 – 5112CytoplasmicSequence analysisAdd
BLAST
Transmembranei52 – 7221HelicalSequence analysisAdd
BLAST
Topological domaini73 – 9220LumenalSequence analysisAdd
BLAST
Transmembranei93 – 11321HelicalSequence analysisAdd
BLAST
Topological domaini114 – 231118CytoplasmicSequence analysisAdd
BLAST
Transmembranei232 – 25221HelicalSequence analysisAdd
BLAST
Topological domaini253 – 27422LumenalSequence analysisAdd
BLAST
Transmembranei275 – 29521HelicalSequence analysisAdd
BLAST
Topological domaini296 – 429134CytoplasmicSequence analysisAdd
BLAST
Transmembranei430 – 45021HelicalSequence analysisAdd
BLAST
Topological domaini451 – 4566LumenalSequence analysis
Transmembranei457 – 47721HelicalSequence analysisAdd
BLAST
Topological domaini478 – 619142CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 619619Lysophospholipid acyltransferasePRO_0000245257Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei513 – 5131PhosphoserineCombined sources
Modified residuei605 – 6051PhosphoserineCombined sources
Modified residuei610 – 6101PhosphoserineCombined sources
Modified residuei615 – 6151PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ08548.

PTM databases

iPTMnetiQ08548.

Interactioni

Protein-protein interaction databases

BioGridi34569. 30 interactions.
DIPiDIP-5617N.
MINTiMINT-570086.

Structurei

3D structure databases

ProteinModelPortaliQ08548.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili545 – 59349Sequence analysisAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00550000074565.
HOGENOMiHOG000200782.
InParanoidiQ08548.
KOiK13519.
OMAiECLEAWN.
OrthoDBiEOG7P2Z21.

Family and domain databases

InterProiIPR004299. MBOAT_fam.
[Graphical view]
PfamiPF03062. MBOAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q08548-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYNPVDAVLT KIITNYGIDS FTLRYAICLL GSFPLNAILK RIPEKRIGLK
60 70 80 90 100
CCFIISMSMF YLFGVLNLVS GFRTLFISTM FTYLISRFYR SKFMPHLNFM
110 120 130 140 150
FVMGHLAINH IHAQFLNEQT QTTVDITSSQ MVLAMKLTSF AWSYYDGSCT
160 170 180 190 200
SESDFKDLTE HQKSRAVRGH PPLLKFLAYA FFYSTLLTGP SFDYADFDSW
210 220 230 240 250
LNCEMFRDLP ESKKPMRRHH PGERRQIPKN GKLALWKVVQ GLAWMILSTL
260 270 280 290 300
GMKHFPVKYV LDKDGFPTRS FIFRIHYLFL LGFIHRFKYY AAWTISEGSC
310 320 330 340 350
ILCGLGYNGY DSKTQKIRWD RVRNIDIWTV ETAQNTREML EAWNMNTNKW
360 370 380 390 400
LKYSVYLRVT KKGKKPGFRS TLFTFLTSAF WHGTRPGYYL TFATGALYQT
410 420 430 440 450
CGKIYRRNFR PIFLREDGVT PLPSKKIYDL VGIYAIKLAF GYMVQPFIIL
460 470 480 490 500
DLKPSLMVWG SVYFYVHIIV AFSFFLFRGP YAKQVTEFFK SKQPKEIFIR
510 520 530 540 550
KQKKLEKDIS ASSPNLGGIL KAKIEHEKGK TAEEEEMNLG IPPIELEKWD
560 570 580 590 600
NAKEDWEDFC KDYKEWRNKN GLEIEEENLS KAFERFKQEF SNAASGSGER
610
VRKMSFSGYS PKPISKKEE
Length:619
Mass (Da):72,228
Last modified:November 1, 1996 - v1
Checksum:i87C74C9194BE0BC5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z75083 Genomic DNA. Translation: CAA99384.1.
U55021 Genomic DNA. Translation: AAB47420.1.
BK006948 Genomic DNA. Translation: DAA10947.1.
PIRiS67067.
RefSeqiNP_014818.1. NM_001183594.1.

Genome annotation databases

EnsemblFungiiYOR175C; YOR175C; YOR175C.
GeneIDi854346.
KEGGisce:YOR175C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z75083 Genomic DNA. Translation: CAA99384.1.
U55021 Genomic DNA. Translation: AAB47420.1.
BK006948 Genomic DNA. Translation: DAA10947.1.
PIRiS67067.
RefSeqiNP_014818.1. NM_001183594.1.

3D structure databases

ProteinModelPortaliQ08548.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34569. 30 interactions.
DIPiDIP-5617N.
MINTiMINT-570086.

Chemistry

SwissLipidsiSLP:000000083.

PTM databases

iPTMnetiQ08548.

Proteomic databases

MaxQBiQ08548.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR175C; YOR175C; YOR175C.
GeneIDi854346.
KEGGisce:YOR175C.

Organism-specific databases

EuPathDBiFungiDB:YOR175C.
SGDiS000005701. ALE1.

Phylogenomic databases

GeneTreeiENSGT00550000074565.
HOGENOMiHOG000200782.
InParanoidiQ08548.
KOiK13519.
OMAiECLEAWN.
OrthoDBiEOG7P2Z21.

Enzyme and pathway databases

BioCyciMetaCyc:G3O-33688-MONOMER.
YEAST:G3O-33688-MONOMER.
BRENDAi2.3.1.51. 984.
ReactomeiR-SCE-1482788. Acyl chain remodelling of PC.
R-SCE-1482801. Acyl chain remodelling of PS.
R-SCE-1482839. Acyl chain remodelling of PE.
R-SCE-1482922. Acyl chain remodelling of PI.
SABIO-RKQ08548.

Miscellaneous databases

PROiQ08548.

Family and domain databases

InterProiIPR004299. MBOAT_fam.
[Graphical view]
PfamiPF03062. MBOAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 270-619.
    Strain: S288c / FY1678.
  4. "A superfamily of membrane-bound O-acyltransferases with implications for wnt signaling."
    Hofmann K.
    Trends Biochem. Sci. 25:111-112(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SIMILARITY.
  5. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  6. "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] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: ATCC 208353 / W303-1A.
  7. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  9. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  10. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-513 AND SER-605, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  12. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-605, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-513; SER-605; SER-610 AND SER-615, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiALE1_YEAST
AccessioniPrimary (citable) accession number: Q08548
Secondary accession number(s): D6W2N1, Q03130
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.