GPAT9_ARATH
ID GPAT9_ARATH Reviewed; 376 AA.
AC Q8GWG0; Q9FF57;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Glycerol-3-phosphate acyltransferase 9 {ECO:0000303|PubMed:19539490};
DE Short=AtGPAT9 {ECO:0000303|PubMed:19539490};
DE EC=2.3.1.15 {ECO:0000269|PubMed:26586834, ECO:0000269|PubMed:27325892};
GN Name=GPAT9 {ECO:0000303|PubMed:19539490};
GN OrderedLocusNames=At5g60620 {ECO:0000312|Araport:AT5G60620};
GN ORFNames=MUP24.4 {ECO:0000312|EMBL:BAB09835.1};
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 [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP MUTAGENESIS OF 369-ILE--LEU-373.
RX PubMed=19539490; DOI=10.1016/j.plaphy.2009.05.008;
RA Gidda S.K., Shockey J.M., Rothstein S.J., Dyer J.M., Mullen R.T.;
RT "Arabidopsis thaliana GPAT8 and GPAT9 are localized to the ER and possess
RT distinct ER retrieval signals: functional divergence of the dilysine ER
RT retrieval motif in plant cells.";
RL Plant Physiol. Biochem. 47:867-879(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP REVIEW, AND GENE FAMILY.
RX PubMed=16449762; DOI=10.1194/jlr.m500556-jlr200;
RA Beigneux A.P., Vergnes L., Qiao X., Quatela S., Davis R., Watkins S.M.,
RA Coleman R.A., Walzem R.L., Philips M., Reue K., Young S.G.;
RT "Agpat6--a novel lipid biosynthetic gene required for triacylglycerol
RT production in mammary epithelium.";
RL J. Lipid Res. 47:734-744(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=27325892; DOI=10.1093/jxb/erw242;
RA Singer S.D., Chen G., Mietkiewska E., Tomasi P., Jayawardhane K.,
RA Dyer J.M., Weselake R.J.;
RT "Arabidopsis GPAT9 contributes to synthesis of intracellular glycerolipids
RT but not surface lipids.";
RL J. Exp. Bot. 67:4627-4638(2016).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, PATHWAY, SUBUNIT, AND
RP INTERACTION WITH LPAT2 AND LPCAT2.
RC STRAIN=cv. Columbia;
RX PubMed=26586834; DOI=10.1104/pp.15.01563;
RA Shockey J., Regmi A., Cotton K., Adhikari N., Browse J., Bates P.D.;
RT "Identification of Arabidopsis GPAT9 (At5g60620) as an essential gene
RT involved in triacylglycerol biosynthesis.";
RL Plant Physiol. 170:163-179(2016).
CC -!- FUNCTION: Essential protein. Required for male and female gametophytes
CC development (PubMed:26586834). Exhibits sn-1 acyltransferase activity
CC with high specificity for acyl-coenzyme A, thus triggering storage
CC lipid biosynthesis and playing an important role in the Kennedy pathway
CC of glycerolipid biosynthesis (PubMed:27325892). Catalyzes
CC triacylglycerol (TAG) accumulation involved in membrane lipid and oil
CC biosynthesis, especially in seeds (PubMed:26586834, PubMed:27325892).
CC Contributes also to the biosynthesis of both polar lipids and TAG in
CC developing leaves, as well as lipid droplet production in developing
CC pollen grains. Seems to not contribute to surface lipid biosynthesis
CC (e.g. waxes and cutin) (PubMed:27325892). {ECO:0000269|PubMed:26586834,
CC ECO:0000269|PubMed:27325892}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acyl-CoA + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-
CC phosphate + CoA; Xref=Rhea:RHEA:15325, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57597, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342; EC=2.3.1.15;
CC Evidence={ECO:0000269|PubMed:26586834, ECO:0000269|PubMed:27325892};
CC -!- PATHWAY: Glycerolipid metabolism; triacylglycerol biosynthesis.
CC {ECO:0000269|PubMed:26586834, ECO:0000269|PubMed:27325892}.
CC -!- SUBUNIT: Self-interacts. Interacts with LPAT2 and LPCAT2.
CC {ECO:0000269|PubMed:26586834}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:19539490}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:19539490}.
CC -!- TISSUE SPECIFICITY: Up-regulated during embryogenesis (PubMed:19539490,
CC PubMed:27325892). Expressed in seedlings, leaves, stems, roots, floral
CC buds, flowers, pollen, and siliques at various developmental stages
CC (PubMed:27325892). {ECO:0000269|PubMed:19539490,
CC ECO:0000269|PubMed:27325892}.
CC -!- DEVELOPMENTAL STAGE: Within siliques, accumulates strongly in
CC developing embryos in the mid-stages of embryo development, during the
CC time of abundant glycerolipid biosynthesis. In stems, confined to
CC phloem and xylem. In flowers, mostly restricted to anthers (and more
CC specifically pollen), and barely in sepals and petals.
CC {ECO:0000269|PubMed:27325892}.
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|UniProtKB:Q9D517}.
CC -!- DISRUPTION PHENOTYPE: Homozygous lethal. Male (pollen) and female
CC gametophytic lethality. Reduces oil content and altered fatty acids
CC (FA) composition. {ECO:0000269|PubMed:26586834}.
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB09835.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; FJ479752; ACT32031.1; -; mRNA.
DR EMBL; AB005246; BAB09835.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED97358.1; -; Genomic_DNA.
DR EMBL; AK118869; BAC43455.1; -; mRNA.
DR EMBL; BT006033; AAP04020.1; -; mRNA.
DR RefSeq; NP_568925.1; NM_125455.4.
DR AlphaFoldDB; Q8GWG0; -.
DR STRING; 3702.AT5G60620.1; -.
DR iPTMnet; Q8GWG0; -.
DR PaxDb; Q8GWG0; -.
DR PRIDE; Q8GWG0; -.
DR ProteomicsDB; 248505; -.
DR EnsemblPlants; AT5G60620.1; AT5G60620.1; AT5G60620.
DR GeneID; 836183; -.
DR Gramene; AT5G60620.1; AT5G60620.1; AT5G60620.
DR KEGG; ath:AT5G60620; -.
DR Araport; AT5G60620; -.
DR TAIR; locus:2175791; AT5G60620.
DR eggNOG; KOG2898; Eukaryota.
DR HOGENOM; CLU_031080_1_0_1; -.
DR InParanoid; Q8GWG0; -.
DR OMA; CVMFKKG; -.
DR OrthoDB; 526132at2759; -.
DR PhylomeDB; Q8GWG0; -.
DR BioCyc; ARA:AT5G60620-MON; -.
DR BioCyc; MetaCyc:AT5G60620-MON; -.
DR BRENDA; 2.3.1.15; 399.
DR UniPathway; UPA00282; -.
DR PRO; PR:Q8GWG0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8GWG0; baseline and differential.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004366; F:glycerol-3-phosphate O-acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0043621; F:protein self-association; IDA:UniProtKB.
DR GO; GO:0102420; F:sn-1-glycerol-3-phosphate C16:0-DCA-CoA acyl transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006651; P:diacylglycerol biosynthetic process; ISS:TAIR.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IMP:UniProtKB.
DR GO; GO:0048229; P:gametophyte development; IMP:UniProtKB.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IMP:UniProtKB.
DR GO; GO:0019915; P:lipid storage; IMP:UniProtKB.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0010152; P:pollen maturation; IMP:UniProtKB.
DR GO; GO:0010344; P:seed oilbody biogenesis; IMP:UniProtKB.
DR GO; GO:0019432; P:triglyceride biosynthetic process; IDA:UniProtKB.
DR CDD; cd07991; LPLAT_LPCAT1-like; 1.
DR InterPro; IPR045252; LPCAT1-like.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR Pfam; PF01553; Acyltransferase; 1.
DR SMART; SM00563; PlsC; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Endoplasmic reticulum; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Phospholipid biosynthesis;
KW Phospholipid metabolism; Phosphoprotein; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..376
FT /note="Glycerol-3-phosphate acyltransferase 9"
FT /id="PRO_0000441887"
FT TOPO_DOM 1..78
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:19539490"
FT TRANSMEM 79..99
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 135..155
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 156..376
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:19539490"
FT REGION 168..180
FT /note="Catalytic"
FT /evidence="ECO:0000305|PubMed:16449762"
FT REGION 242..262
FT /note="Glycerol-3-phosphate binding"
FT /evidence="ECO:0000305|PubMed:16449762"
FT REGION 266..275
FT /note="Catalytic"
FT /evidence="ECO:0000305|PubMed:16449762"
FT REGION 369..373
FT /note="Endoplasmic reticulum targeting"
FT /evidence="ECO:0000269|PubMed:19539490"
FT MOTIF 171..176
FT /note="HXXXXD motif"
FT /evidence="ECO:0000250|UniProtKB:Q4V8J4"
FT BINDING 209..218
FT /ligand="sn-glycerol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:57597"
FT /evidence="ECO:0000305|PubMed:16449762"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MUTAGEN 369..373
FT /note="ILARL->AAAAA: Abnormal subcellular localization at
FT the plasma membrane."
FT /evidence="ECO:0000269|PubMed:19539490"
SQ SEQUENCE 376 AA; 43020 MW; E3BB28AC6EBDED65 CRC64;
MSSTAGRLVT SKSELDLDHP NIEDYLPSGS SINEPRGKLS LRDLLDISPT LTEAAGAIVD
DSFTRCFKSN PPEPWNWNIY LFPLYCFGVV VRYCILFPLR CFTLAFGWII FLSLFIPVNA
LLKGQDRLRK KIERVLVEMI CSFFVASWTG VVKYHGPRPS IRPKQVYVAN HTSMIDFIVL
EQMTAFAVIM QKHPGWVGLL QSTILESVGC IWFNRSEAKD REIVAKKLRD HVQGADSNPL
LIFPEGTCVN NNYTVMFKKG AFELDCTVCP IAIKYNKIFV DAFWNSRKQS FTMHLLQLMT
SWAVVCEVWY LEPQTIRPGE TGIEFAERVR DMISLRAGLK KVPWDGYLKY SRPSPKHSER
KQQSFAESIL ARLEEK
