LPAAT_ARATH
ID LPAAT_ARATH Reviewed; 418 AA.
AC O22975; Q9SU43;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=1-acylglycerol-3-phosphate O-acyltransferase;
DE EC=2.3.1.51;
DE AltName: Full=Lipid droplet-binding protein CGI-58 homolog;
GN OrderedLocusNames=At4g24160; ORFNames=T19F6.4;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Bautista V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=19700561; DOI=10.1104/pp.109.144261;
RA Ghosh A.K., Chauhan N., Rajakumari S., Daum G., Rajasekharan R.;
RT "At4g24160, a soluble acyl-coenzyme A-dependent lysophosphatidic acid
RT acyltransferase.";
RL Plant Physiol. 151:869-881(2009).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=20876112; DOI=10.1073/pnas.0911359107;
RA James C.N., Horn P.J., Case C.R., Gidda S.K., Zhang D., Mullen R.T.,
RA Dyer J.M., Anderson R.G., Chapman K.D.;
RT "Disruption of the Arabidopsis CGI-58 homologue produces Chanarin-Dorfman-
RT like lipid droplet accumulation in plants.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:17833-17838(2010).
CC -!- FUNCTION: Lysophosphatidic acid acyltransferase which functions in
CC phosphatidic acid biosynthesis. Is highly specific for lysophosphatidic
CC acid and able to use different acyl-CoA donors. May regulate neutral
CC lipid accumulation and participate in the regulation of lipid turnover
CC in vegetative cells. Possesses additional triacylglycerol lipase and
CC phospholipase A2 activities in vitro. Is not active as esterase or
CC lysophospholipase. {ECO:0000269|PubMed:19700561,
CC ECO:0000269|PubMed:20876112}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-
CC sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:19709,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:58608; EC=2.3.1.51;
CC Evidence={ECO:0000269|PubMed:19700561};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20876112}.
CC Note=Does not associate with endogenous lipid droplets.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=O22975-1; Sequence=Displayed;
CC -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity and
CC may constitute the binding site for the phosphate moiety of the
CC glycerol-3-phosphate. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Accumulation of neutral lipid droplets with
CC marked increase in absolute triacylglycerol levels in leaf mesophyll
CC cells. {ECO:0000269|PubMed:20876112}.
CC -!- SIMILARITY: Belongs to the peptidase S33 family. ABHD4/ABHD5 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB51659.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB79326.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC002343; AAB63608.1; -; Genomic_DNA.
DR EMBL; AL109619; CAB51659.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL161561; CAB79326.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002687; AEE84857.1; -; Genomic_DNA.
DR EMBL; AK117965; BAC42602.1; -; mRNA.
DR EMBL; BT029749; ABM06019.1; -; mRNA.
DR PIR; T13464; T13464.
DR RefSeq; NP_194147.2; NM_118548.3. [O22975-1]
DR AlphaFoldDB; O22975; -.
DR STRING; 3702.AT4G24160.1; -.
DR ESTHER; arath-LPAAT; CGI-58_ABHD5_ABHD4.
DR MEROPS; S33.009; -.
DR PaxDb; O22975; -.
DR PRIDE; O22975; -.
DR ProteomicsDB; 238720; -. [O22975-1]
DR EnsemblPlants; AT4G24160.1; AT4G24160.1; AT4G24160. [O22975-1]
DR GeneID; 828516; -.
DR Gramene; AT4G24160.1; AT4G24160.1; AT4G24160. [O22975-1]
DR KEGG; ath:AT4G24160; -.
DR Araport; AT4G24160; -.
DR TAIR; locus:2134996; AT4G24160.
DR eggNOG; KOG4409; Eukaryota.
DR InParanoid; O22975; -.
DR OMA; DWMDPEG; -.
DR PhylomeDB; O22975; -.
DR BioCyc; ARA:AT4G24160-MON; -.
DR BRENDA; 2.3.1.51; 399.
DR PRO; PR:O22975; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O22975; baseline and differential.
DR Genevisible; O22975; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IBA:GO_Central.
DR GO; GO:0016298; F:lipase activity; IDA:TAIR.
DR GO; GO:0042171; F:lysophosphatidic acid acyltransferase activity; IDA:TAIR.
DR GO; GO:0004623; F:phospholipase A2 activity; IDA:TAIR.
DR GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR GO; GO:0055089; P:fatty acid homeostasis; IMP:TAIR.
DR GO; GO:0055088; P:lipid homeostasis; IMP:TAIR.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0055091; P:phospholipid homeostasis; IMP:TAIR.
DR GO; GO:0070328; P:triglyceride homeostasis; IMP:TAIR.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PRINTS; PR00111; ABHYDROLASE.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Alternative splicing; Cytoplasm; Lipid biosynthesis;
KW Lipid metabolism; Phospholipid biosynthesis; Phospholipid metabolism;
KW Reference proteome; Transferase.
FT CHAIN 1..418
FT /note="1-acylglycerol-3-phosphate O-acyltransferase"
FT /id="PRO_0000430169"
FT DOMAIN 121..251
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT MOTIF 197..201
FT /note="GXSXG"
FT MOTIF 379..384
FT /note="HXXXXD motif"
SQ SEQUENCE 418 AA; 46526 MW; 8CC1A5D46F1A5611 CRC64;
MNLSRFASRL RMAEEISKTK VGSSSTASVA DSSAAASAAT NAAKSRWKIL WPNSLRWIPT
STDYIIAAEK RLLSILKTPY VQEQVSIGSG PPGSKIRWFR STSNESRYIN TVTFDAKEGA
PTLVMVHGYG ASQGFFFRNF DALASRFRVI AIDQLGWGGS SRPDFTCRST EETEAWFIDS
FEEWRKAQNL SNFILLGHSF GGYVAAKYAL KHPEHVQHLI LVGSAGFSAE ADAKSEWLTK
FRATWKGAVL NHLWESNFTP QKLVRGLGPW GPGLVNRYTT ARFGAHSEGT GLTEEEAKLL
TDYVYHTLAA KASGELCLKY IFSFGAFARK PLLQSASEWK VPTTFIYGMN DWMNYQGAVE
ARKSMKVPCE IIRVPQGGHF VFIDNPIGFH SAVLYACRKF ISQDSSHDQQ LLDGLRLV
