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Protein

1-acylglycerol-3-phosphate O-acyltransferase

Gene

At4g24160

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Lysophosphatidic acid acyltransferase which functions in phosphatidic acid biosynthesis. Is highly specific for lysophosphatidic acid and able to use different acyl-CoA donors. May regulate neutral lipid accumulation and participate in the regulation of lipid turnover in vegetative cells. Possesses additional triacylglycerol lipase and phospholipase A2 activities in vitro. Is not active as esterase or lysophospholipase.2 Publications

Catalytic activityi

Acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate.1 Publication

GO - Molecular functioni

  • 1-acylglycerol-3-phosphate O-acyltransferase activity Source: UniProtKB-EC
  • lipase activity Source: TAIR
  • lysophosphatidic acid acyltransferase activity Source: TAIR
  • phospholipase A2 activity Source: TAIR

GO - Biological processi

  • fatty acid homeostasis Source: TAIR
  • lipid homeostasis Source: TAIR
  • phospholipid biosynthetic process Source: UniProtKB-KW
  • phospholipid homeostasis Source: TAIR
  • triglyceride homeostasis Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Enzyme and pathway databases

BioCyciARA:AT4G24160-MONOMER.
BRENDAi2.3.1.51. 399.
ReactomeiR-ATH-1483152. Hydrolysis of LPE.

Protein family/group databases

ESTHERiarath-LPAAT. CGI-58_ABHD5_ABHD4.
MEROPSiS33.009.

Names & Taxonomyi

Protein namesi
Recommended name:
1-acylglycerol-3-phosphate O-acyltransferase (EC:2.3.1.51)
Alternative name(s):
Lipid droplet-binding protein CGI-58 homolog
Gene namesi
Ordered Locus Names:At4g24160
ORF Names:T19F6.4
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G24160.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Accumulation of neutral lipid droplets with marked increase in absolute triacylglycerol levels in leaf mesophyll cells.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4184181-acylglycerol-3-phosphate O-acyltransferasePRO_0000430169Add
BLAST

Proteomic databases

PaxDbiO22975.
PRIDEiO22975.

PTM databases

iPTMnetiO22975.

Expressioni

Gene expression databases

ExpressionAtlasiO22975. baseline and differential.
GenevisibleiO22975. AT.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT4G24160.1.

Structurei

3D structure databases

ProteinModelPortaliO22975.
SMRiO22975. Positions 105-253.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi197 – 2015GXSXG
Motifi379 – 3846HXXXXD motif

Domaini

The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG4409. Eukaryota.
COG0596. LUCA.
HOGENOMiHOG000243247.
InParanoidiO22975.
OMAiPMIHRIK.
PhylomeDBiO22975.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
[Graphical view]
PfamiPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
PRINTSiPR00111. ABHYDROLASE.
SUPFAMiSSF53474. SSF53474. 1 hit.

Sequencei

Sequence statusi: Complete.

This entry describes 1 isoform i produced by alternative splicing. AlignAdd to basket

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: O22975-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MNLSRFASRL RMAEEISKTK VGSSSTASVA DSSAAASAAT NAAKSRWKIL
60 70 80 90 100
WPNSLRWIPT STDYIIAAEK RLLSILKTPY VQEQVSIGSG PPGSKIRWFR
110 120 130 140 150
STSNESRYIN TVTFDAKEGA PTLVMVHGYG ASQGFFFRNF DALASRFRVI
160 170 180 190 200
AIDQLGWGGS SRPDFTCRST EETEAWFIDS FEEWRKAQNL SNFILLGHSF
210 220 230 240 250
GGYVAAKYAL KHPEHVQHLI LVGSAGFSAE ADAKSEWLTK FRATWKGAVL
260 270 280 290 300
NHLWESNFTP QKLVRGLGPW GPGLVNRYTT ARFGAHSEGT GLTEEEAKLL
310 320 330 340 350
TDYVYHTLAA KASGELCLKY IFSFGAFARK PLLQSASEWK VPTTFIYGMN
360 370 380 390 400
DWMNYQGAVE ARKSMKVPCE IIRVPQGGHF VFIDNPIGFH SAVLYACRKF
410
ISQDSSHDQQ LLDGLRLV
Length:418
Mass (Da):46,526
Last modified:January 1, 1998 - v1
Checksum:i8CC1A5D46F1A5611
GO

Sequence cautioni

The sequence CAB51659.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAB79326.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC002343 Genomic DNA. Translation: AAB63608.1.
AL109619 Genomic DNA. Translation: CAB51659.1. Different initiation.
AL161561 Genomic DNA. Translation: CAB79326.1. Different initiation.
CP002687 Genomic DNA. Translation: AEE84857.1.
AK117965 mRNA. Translation: BAC42602.1.
BT029749 mRNA. Translation: ABM06019.1.
PIRiT13464.
RefSeqiNP_194147.2. NM_118548.2. [O22975-1]
UniGeneiAt.20387.

Genome annotation databases

EnsemblPlantsiAT4G24160.1; AT4G24160.1; AT4G24160. [O22975-1]
GeneIDi828516.
KEGGiath:AT4G24160.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC002343 Genomic DNA. Translation: AAB63608.1.
AL109619 Genomic DNA. Translation: CAB51659.1. Different initiation.
AL161561 Genomic DNA. Translation: CAB79326.1. Different initiation.
CP002687 Genomic DNA. Translation: AEE84857.1.
AK117965 mRNA. Translation: BAC42602.1.
BT029749 mRNA. Translation: ABM06019.1.
PIRiT13464.
RefSeqiNP_194147.2. NM_118548.2. [O22975-1]
UniGeneiAt.20387.

3D structure databases

ProteinModelPortaliO22975.
SMRiO22975. Positions 105-253.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT4G24160.1.

Protein family/group databases

ESTHERiarath-LPAAT. CGI-58_ABHD5_ABHD4.
MEROPSiS33.009.

PTM databases

iPTMnetiO22975.

Proteomic databases

PaxDbiO22975.
PRIDEiO22975.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G24160.1; AT4G24160.1; AT4G24160. [O22975-1]
GeneIDi828516.
KEGGiath:AT4G24160.

Organism-specific databases

TAIRiAT4G24160.

Phylogenomic databases

eggNOGiKOG4409. Eukaryota.
COG0596. LUCA.
HOGENOMiHOG000243247.
InParanoidiO22975.
OMAiPMIHRIK.
PhylomeDBiO22975.

Enzyme and pathway databases

BioCyciARA:AT4G24160-MONOMER.
BRENDAi2.3.1.51. 399.
ReactomeiR-ATH-1483152. Hydrolysis of LPE.

Miscellaneous databases

PROiO22975.

Gene expression databases

ExpressionAtlasiO22975. baseline and differential.
GenevisibleiO22975. AT.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
[Graphical view]
PfamiPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
PRINTSiPR00111. ABHYDROLASE.
SUPFAMiSSF53474. SSF53474. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  4. "Arabidopsis ORF clones."
    Bautista V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C., Ecker J.R.
    Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "At4g24160, a soluble acyl-coenzyme A-dependent lysophosphatidic acid acyltransferase."
    Ghosh A.K., Chauhan N., Rajakumari S., Daum G., Rajasekharan R.
    Plant Physiol. 151:869-881(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY.
  6. "Disruption of the Arabidopsis CGI-58 homologue produces Chanarin-Dorfman-like lipid droplet accumulation in plants."
    James C.N., Horn P.J., Case C.R., Gidda S.K., Zhang D., Mullen R.T., Dyer J.M., Anderson R.G., Chapman K.D.
    Proc. Natl. Acad. Sci. U.S.A. 107:17833-17838(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiLPAAT_ARATH
AccessioniPrimary (citable) accession number: O22975
Secondary accession number(s): Q9SU43
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 3, 2014
Last sequence update: January 1, 1998
Last modified: January 20, 2016
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

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.