LPAT2_ARATH
ID LPAT2_ARATH Reviewed; 389 AA.
AC Q8LG50; Q9SVX9;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase 2;
DE EC=2.3.1.51;
DE AltName: Full=Lysophosphatidyl acyltransferase 2;
GN Name=LPAT2; Synonyms=LPAAT2; OrderedLocusNames=At3g57650;
GN ORFNames=F15B8.160;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=14976237; DOI=10.1104/pp.103.035832;
RA Kim H.U., Huang A.H.C.;
RT "Plastid lysophosphatidyl acyltransferase is essential for embryo
RT development in Arabidopsis.";
RL Plant Physiol. 134:1206-1216(2004).
RN [5]
RP FUNCTION, ENZYME ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15772283; DOI=10.1105/tpc.104.030403;
RA Kim H.U., Li Y., Huang A.H.C.;
RT "Ubiquitous and endoplasmic reticulum-located lysophosphatidyl
RT acyltransferase, LPAT2, is essential for female but not male gametophyte
RT development in Arabidopsis.";
RL Plant Cell 17:1073-1089(2005).
RN [6]
RP INTERACTION WITH GPAT9 AND DGAT1.
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: Converts lysophosphatidic acid (LPA) into phosphatidic acid
CC by incorporating acyl moiety at the 2 position. Has preference for C-
CC 18-CoA substrates compared to C-16-CoA substrates. Required for female
CC but not male gametophyte development. {ECO:0000269|PubMed:15772283}.
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:15772283};
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
CC -!- SUBUNIT: Interacts with GPAT9 and DGAT1. {ECO:0000269|PubMed:26586834}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:15772283}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15772283}.
CC -!- TISSUE SPECIFICITY: Present in roots, leaves, stems, floral buds and
CC siliques (at protein level). Widely expressed. In contrast to LPAT1, it
CC is not expressed at higher level in leaves.
CC {ECO:0000269|PubMed:14976237, ECO:0000269|PubMed:15772283}.
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 -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB41190.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL049660; CAB41190.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE79683.1; -; Genomic_DNA.
DR EMBL; AY084461; AAM61033.1; -; mRNA.
DR PIR; T06755; T06755.
DR RefSeq; NP_567052.1; NM_115625.4.
DR AlphaFoldDB; Q8LG50; -.
DR BioGRID; 10249; 17.
DR IntAct; Q8LG50; 17.
DR STRING; 3702.AT3G57650.1; -.
DR PaxDb; Q8LG50; -.
DR PRIDE; Q8LG50; -.
DR ProteomicsDB; 238793; -.
DR EnsemblPlants; AT3G57650.1; AT3G57650.1; AT3G57650.
DR GeneID; 824934; -.
DR Gramene; AT3G57650.1; AT3G57650.1; AT3G57650.
DR KEGG; ath:AT3G57650; -.
DR Araport; AT3G57650; -.
DR TAIR; locus:2076676; AT3G57650.
DR eggNOG; KOG1505; Eukaryota.
DR HOGENOM; CLU_041844_5_0_1; -.
DR InParanoid; Q8LG50; -.
DR OMA; WPTWLIS; -.
DR OrthoDB; 959325at2759; -.
DR BioCyc; ARA:AT3G57650-MON; -.
DR BRENDA; 2.3.1.51; 399.
DR UniPathway; UPA00557; UER00613.
DR PRO; PR:Q8LG50; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8LG50; baseline and differential.
DR Genevisible; Q8LG50; AT.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
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:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IDA:TAIR.
DR GO; GO:0016746; F:acyltransferase activity; IBA:GO_Central.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR032098; Acyltransf_C.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR Pfam; PF16076; Acyltransf_C; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR SMART; SM00563; PlsC; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Developmental protein; Endoplasmic reticulum;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..389
FT /note="1-acyl-sn-glycerol-3-phosphate acyltransferase 2"
FT /id="PRO_0000208179"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 333..353
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 357..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 91..96
FT /note="HXXXXD motif"
FT COMPBIAS 369..389
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 205
FT /note="G -> S (in Ref. 3; AAM61033)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 389 AA; 43676 MW; FA9B7A6F2B786823 CRC64;
MVIAAAVIVP LGLLFFISGL AVNLFQAVCY VLIRPLSKNT YRKINRVVAE TLWLELVWIV
DWWAGVKIQV FADNETFNRM GKEHALVVCN HRSDIDWLVG WILAQRSGCL GSALAVMKKS
SKFLPVIGWS MWFSEYLFLE RNWAKDESTL KSGLQRLSDF PRPFWLALFV EGTRFTEAKL
KAAQEYAASS ELPIPRNVLI PRTKGFVSAV SNMRSFVPAI YDMTVTIPKT SPPPTMLRLF
KGQPSVVHVH IKCHSMKDLP ESDDAIAQWC RDQFVAKDAL LDKHIAADTF PGQQEQNIGR
PIKSLAVVLS WACVLTLGAI KFLHWAQLFS SWKGITISAL GLGIITLCMQ ILIRSSQSER
STPAKVVPAK PKDNHHPESS SQTETEKEK
