MBOA1_ARATH
ID MBOA1_ARATH Reviewed; 462 AA.
AC F4IDU4; Q8RWH4; Q9LN83;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Lysophospholipid acyltransferase 1 {ECO:0000303|PubMed:18154737};
DE Short=AtLPLAT1 {ECO:0000303|PubMed:18154737};
DE EC=2.3.1.- {ECO:0000269|PubMed:18154737};
DE AltName: Full=1-acylglycerophosphocholine O-acyltransferase {ECO:0000305};
DE EC=2.3.1.23 {ECO:0000269|PubMed:18154737};
DE AltName: Full=1-acylglycerophosphoethanolamine O-acyltransferase {ECO:0000305};
DE EC=2.3.1.n7 {ECO:0000269|PubMed:18154737};
DE AltName: Full=1-acylglycerophosphoserine O-acyltransferase {ECO:0000305};
DE EC=2.3.1.n6 {ECO:0000269|PubMed:18154737};
DE AltName: Full=Lysophosphatidylcholine acyltransferase 1 {ECO:0000303|PubMed:23150634};
DE Short=LPCAT1 {ECO:0000303|PubMed:23150634};
DE AltName: Full=Lysophosphatidylethanolamine acyltransferase {ECO:0000303|PubMed:18154737};
DE Short=LPEAT {ECO:0000303|PubMed:18154737};
DE AltName: Full=Lysophosphatidylglycerol acyltransferase {ECO:0000303|PubMed:18154737};
DE Short=LPGAT {ECO:0000303|PubMed:18154737};
DE AltName: Full=Lysophosphatidylserine acyltransferase {ECO:0000303|PubMed:18154737};
DE Short=LPSAT {ECO:0000303|PubMed:18154737};
GN Name=LPCAT1 {ECO:0000303|PubMed:23150634};
GN Synonyms=LPLAT1 {ECO:0000303|PubMed:18154737};
GN OrderedLocusNames=At1g12640 {ECO:0000312|Araport:AT1G12640};
GN ORFNames=T12C24.17 {ECO:0000312|EMBL:AAF88094.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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].
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 [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=18154737; DOI=10.1016/j.febslet.2007.12.020;
RA Stahl U., Stalberg K., Stymne S., Ronne H.;
RT "A family of eukaryotic lysophospholipid acyltransferases with broad
RT specificity.";
RL FEBS Lett. 582:305-309(2008).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=22233193; DOI=10.1186/1471-2229-12-4;
RA Xu J., Carlsson A.S., Francis T., Zhang M., Hoffman T., Giblin M.E.,
RA Taylor D.C.;
RT "Triacylglycerol synthesis by PDAT1 in the absence of DGAT1 activity is
RT dependent on re-acylation of LPC by LPCAT2.";
RL BMC Plant Biol. 12:4-4(2012).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=23150634; DOI=10.1105/tpc.112.104604;
RA Wang L., Shen W., Kazachkov M., Chen G., Chen Q., Carlsson A.S., Stymne S.,
RA Weselake R.J., Zou J.;
RT "Metabolic interactions between the Lands cycle and the Kennedy pathway of
RT glycerolipid synthesis in Arabidopsis developing seeds.";
RL Plant Cell 24:4652-4669(2012).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=22923678; DOI=10.1104/pp.112.204263;
RA Nikolovski N., Rubtsov D., Segura M.P., Miles G.P., Stevens T.J.,
RA Dunkley T.P., Munro S., Lilley K.S., Dupree P.;
RT "Putative glycosyltransferases and other plant Golgi apparatus proteins are
RT revealed by LOPIT proteomics.";
RL Plant Physiol. 160:1037-1051(2012).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22932756; DOI=10.1104/pp.112.204438;
RA Bates P.D., Fatihi A., Snapp A.R., Carlsson A.S., Browse J., Lu C.;
RT "Acyl editing and headgroup exchange are the major mechanisms that direct
RT polyunsaturated fatty acid flux into triacylglycerols.";
RL Plant Physiol. 160:1530-1539(2012).
RN [9]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=24189065; DOI=10.1074/jbc.m113.521815;
RA Lager I., Yilmaz J.L., Zhou X.R., Jasieniecka K., Kazachkov M., Wang P.,
RA Zou J., Weselake R., Smith M.A., Bayon S., Dyer J.M., Shockey J.M.,
RA Heinz E., Green A., Banas A., Stymne S.;
RT "Plant acyl-CoA:lysophosphatidylcholine acyltransferases (LPCATs) have
RT different specificities in their forward and reverse reactions.";
RL J. Biol. Chem. 288:36902-36914(2013).
RN [10]
RP FUNCTION.
RX PubMed=25268378; DOI=10.1111/tpj.12683;
RA Wang L., Kazachkov M., Shen W., Bai M., Wu H., Zou J.;
RT "Deciphering the roles of Arabidopsis LPCAT and PAH in phosphatidylcholine
RT homeostasis and pathway coordination for chloroplast lipid synthesis.";
RL Plant J. 80:965-976(2014).
RN [11]
RP FUNCTION.
RX PubMed=31511316; DOI=10.1105/tpc.19.00121;
RA Karki N., Johnson B.S., Bates P.D.;
RT "Metabolically distinct pools of phosphatidylcholine are involved in
RT trafficking of fatty acids out of and into the chloroplast for membrane
RT production.";
RL Plant Cell 31:2768-2788(2019).
CC -!- FUNCTION: Lysophospholipid acyltransferase with broad specificity
CC (PubMed:18154737). Mediates the conversion of
CC lysophosphatidylethanolamine (1-acyl-sn-glycero-3-phosphoethanolamine
CC or LPE) into phosphatidylethanolamine (1,2-diacyl-sn-glycero-3-
CC phosphoethanolamine or PE) (LPEAT activity) (PubMed:18154737).
CC Catalyzes the acylation of lysophosphatidylserine (1-acyl-2-hydroxy-sn-
CC glycero-3-phospho-L-serine or LPS) into phosphatidylserine (1,2-diacyl-
CC sn-glycero-3-phospho-L-serine or PS) (LPSAT activity)
CC (PubMed:18154737). Can convert lysophosphatidylcholine (1-acyl-sn-
CC glycero-3-phosphocholine or LPC) into phosphatidylcholine (1,2-diacyl-
CC sn-glycero-3-phosphocholine or PC) (LPCAT activity) (PubMed:18154737,
CC PubMed:24189065, PubMed:25268378). Exhibits preference for C18-
CC unsaturated acyl-CoA when transferring an acyl group to
CC lysophosphatidylcholine (PubMed:24189065, PubMed:25268378). Can also
CC utilize lysophosphatidylglycerol (LPG) as substrate in vitro
CC (PubMed:18154737). Has neither activity towards lysophosphatidic acid
CC (LPA) nor lysophosphatidylinositol (LPI) (PubMed:18154737).
CC Lysophospholipid acyltransferases catalyze the reacylation step of the
CC phospholipid remodeling pathway also known as the Lands cycle
CC (Probable). The primary function of the Lands cycle is to provide a
CC route for acyl remodeling to modify fatty acid (FA) composition of
CC phospholipids derived from the Kennedy pathway (PubMed:23150634,
CC PubMed:22932756). Is involved in PC acyl editing and phosphocholine
CC headgroup exchange between PC and diacylglycerols. This processes
CC control the majority of acyl fluxes through PC to provide
CC polyunsaturated fatty acids for triacylglycerols synthesis in seeds
CC (PubMed:22932756, PubMed:24189065). Involved with LPCAT2 in the direct
CC incorporation of newly synthesized fatty acids exported form the
CC chloroplast into PC through acyl editing (PubMed:31511316).
CC {ECO:0000269|PubMed:18154737, ECO:0000269|PubMed:22932756,
CC ECO:0000269|PubMed:23150634, ECO:0000269|PubMed:24189065,
CC ECO:0000269|PubMed:25268378, ECO:0000269|PubMed:31511316,
CC ECO:0000305|PubMed:18154737}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphocholine + an acyl-CoA = a 1,2-
CC diacyl-sn-glycero-3-phosphocholine + CoA; Xref=Rhea:RHEA:12937,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168,
CC ChEBI:CHEBI:58342; EC=2.3.1.23;
CC Evidence={ECO:0000269|PubMed:18154737, ECO:0000269|PubMed:24189065};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12938;
CC Evidence={ECO:0000269|PubMed:18154737, ECO:0000269|PubMed:24189065};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphocholine = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine
CC + CoA; Xref=Rhea:RHEA:37387, ChEBI:CHEBI:28610, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:74669;
CC Evidence={ECO:0000269|PubMed:24189065};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37388;
CC Evidence={ECO:0000269|PubMed:24189065};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-
CC 3-phosphocholine = 1-(9Z)-octadecenoyl-2-(9Z,12Z)-octadecadienoyl-sn-
CC glycero-3-phosphocholine + CoA; Xref=Rhea:RHEA:37391,
CC ChEBI:CHEBI:28610, ChEBI:CHEBI:57287, ChEBI:CHEBI:57383,
CC ChEBI:CHEBI:74670; Evidence={ECO:0000269|PubMed:24189065};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37392;
CC Evidence={ECO:0000269|PubMed:24189065};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z,15Z)-octadecatrienoyl-CoA + 1-(9Z-octadecenoyl)-sn-
CC glycero-3-phosphocholine = 1-(9Z-octadecaenoyl)-2-(9Z,12Z,15Z-
CC octadecatrienoyl)-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:56408, ChEBI:CHEBI:28610, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:74034, ChEBI:CHEBI:86133;
CC Evidence={ECO:0000269|PubMed:24189065};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56409;
CC Evidence={ECO:0000269|PubMed:24189065};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphoethanolamine + an acyl-CoA = a
CC 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CoA;
CC Xref=Rhea:RHEA:32995, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:64381, ChEBI:CHEBI:64612; EC=2.3.1.n7;
CC Evidence={ECO:0000269|PubMed:18154737};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32996;
CC Evidence={ECO:0000269|PubMed:18154737};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phospho-L-serine + an acyl-CoA = a 1,2-
CC diacyl-sn-glycero-3-phospho-L-serine + CoA; Xref=Rhea:RHEA:33191,
CC ChEBI:CHEBI:57262, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:64379; EC=2.3.1.n6;
CC Evidence={ECO:0000269|PubMed:18154737};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33192;
CC Evidence={ECO:0000269|PubMed:18154737};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000305|PubMed:22923678}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:22923678}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, rosette leaves, petals, stigma,
CC chalazal endosperm of developing seeds and vascular bundles of
CC siliques. {ECO:0000269|PubMed:23150634}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but the double mutants lpcat1 and lpcat2-2 show increased
CC contents of very-long-chain fatty acids and decreased polyunsaturated
CC fatty acids in seed triacylglycerols. {ECO:0000269|PubMed:22233193,
CC ECO:0000269|PubMed:22932756, ECO:0000269|PubMed:23150634}.
CC -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF88094.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC025417; AAF88094.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002684; AEE28904.1; -; Genomic_DNA.
DR EMBL; AY093087; AAM13086.1; -; mRNA.
DR EMBL; AY128762; AAM91162.1; -; mRNA.
DR RefSeq; NP_172724.2; NM_101134.5.
DR AlphaFoldDB; F4IDU4; -.
DR SMR; F4IDU4; -.
DR STRING; 3702.AT1G12640.1; -.
DR SwissLipids; SLP:000001897; -.
DR PaxDb; F4IDU4; -.
DR PRIDE; F4IDU4; -.
DR ProteomicsDB; 238237; -.
DR EnsemblPlants; AT1G12640.1; AT1G12640.1; AT1G12640.
DR GeneID; 837820; -.
DR Gramene; AT1G12640.1; AT1G12640.1; AT1G12640.
DR KEGG; ath:AT1G12640; -.
DR Araport; AT1G12640; -.
DR TAIR; locus:2195072; AT1G12640.
DR eggNOG; KOG2704; Eukaryota.
DR HOGENOM; CLU_011340_2_0_1; -.
DR InParanoid; F4IDU4; -.
DR OMA; CILVLRM; -.
DR OrthoDB; 881262at2759; -.
DR BioCyc; ARA:AT1G12640-MON; -.
DR BioCyc; MetaCyc:MON-19024; -.
DR PRO; PR:F4IDU4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4IDU4; baseline and differential.
DR Genevisible; F4IDU4; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0047184; F:1-acylglycerophosphocholine O-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0106262; F:1-acylglycerophosphoethanolamine O-acyltransferase activity; IEA:RHEA.
DR GO; GO:0106263; F:1-acylglycerophosphoserine O-acyltransferase activity; IEA:RHEA.
DR GO; GO:0016746; F:acyltransferase activity; IDA:TAIR.
DR GO; GO:0071617; F:lysophospholipid acyltransferase activity; IGI:TAIR.
DR GO; GO:0019375; P:galactolipid biosynthetic process; IGI:TAIR.
DR GO; GO:0045017; P:glycerolipid biosynthetic process; IMP:TAIR.
DR GO; GO:0030258; P:lipid modification; IBA:GO_Central.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IGI:TAIR.
DR GO; GO:0019432; P:triglyceride biosynthetic process; IGI:TAIR.
DR InterPro; IPR004299; MBOAT_fam.
DR Pfam; PF03062; MBOAT; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Endoplasmic reticulum; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..462
FT /note="Lysophospholipid acyltransferase 1"
FT /id="PRO_0000425532"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 211..231
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 353..373
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 396..416
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 431..451
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 356
FT /evidence="ECO:0000250"
FT CONFLICT 161
FT /note="E -> K (in Ref. 3; AAM13086/AAM91162)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 462 AA; 52152 MW; 999B288E08115613 CRC64;
MDMSSMAGSI GVSVAVLRFL LCFVATIPVS FACRIVPSRL GKHLYAAASG AFLSYLSFGF
SSNLHFLVPM TIGYASMAIY RPKCGIITFF LGFAYLIGCH VFYMSGDAWK EGGIDSTGAL
MVLTLKVISC SMNYNDGMLK EEGLREAQKK NRLIQMPSLI EYFGYCLCCG SHFAGPVYEM
KDYLEWTEGK GIWDTTEKRK KPSPYGATIR AILQAAICMA LYLYLVPQYP LTRFTEPVYQ
EWGFLRKFSY QYMAGFTARW KYYFIWSISE ASIIISGLGF SGWTDDASPK PKWDRAKNVD
ILGVELAKSA VQIPLVWNIQ VSTWLRHYVY ERLVQNGKKA GFFQLLATQT VSAVWHGLYP
GYMMFFVQSA LMIAGSRVIY RWQQAISPKM AMLRNIMVFI NFLYTVLVLN YSAVGFMVLS
LHETLTAYGS VYYIGTIIPV GLILLSYVVP AKPSRPKPRK EE
