LPAT3_ARATH
ID LPAT3_ARATH Reviewed; 376 AA.
AC Q9SYC8;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase 3;
DE EC=2.3.1.51;
DE AltName: Full=Lysophosphatidyl acyltransferase 3;
GN Name=LPAT3; Synonyms=LPAAT3; OrderedLocusNames=At1g51260;
GN ORFNames=F11M15.12;
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=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [4]
RP ENZYME ACTIVITY, 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).
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.
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in pollen.
CC {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=BX813937; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC006085; AAD30638.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32642.1; -; Genomic_DNA.
DR EMBL; BX813937; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; D96550; D96550.
DR RefSeq; NP_175537.1; NM_104004.3.
DR AlphaFoldDB; Q9SYC8; -.
DR STRING; 3702.AT1G51260.1; -.
DR iPTMnet; Q9SYC8; -.
DR PaxDb; Q9SYC8; -.
DR PRIDE; Q9SYC8; -.
DR ProteomicsDB; 238667; -.
DR EnsemblPlants; AT1G51260.1; AT1G51260.1; AT1G51260.
DR GeneID; 841549; -.
DR Gramene; AT1G51260.1; AT1G51260.1; AT1G51260.
DR KEGG; ath:AT1G51260; -.
DR Araport; AT1G51260; -.
DR TAIR; locus:2008226; AT1G51260.
DR eggNOG; KOG1505; Eukaryota.
DR HOGENOM; CLU_041844_5_0_1; -.
DR InParanoid; Q9SYC8; -.
DR OMA; HLMQELP; -.
DR OrthoDB; 959325at2759; -.
DR PhylomeDB; Q9SYC8; -.
DR BioCyc; ARA:AT1G51260-MON; -.
DR BRENDA; 2.3.1.51; 399.
DR UniPathway; UPA00557; UER00613.
DR PRO; PR:Q9SYC8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SYC8; baseline and differential.
DR Genevisible; Q9SYC8; AT.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Acyltransferase; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..376
FT /note="1-acyl-sn-glycerol-3-phosphate acyltransferase 3"
FT /id="PRO_0000208182"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 335..355
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 92..97
FT /note="HXXXXD motif"
FT CONFLICT 354
FT /note="I -> S (in Ref. 3; BX813937)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 376 AA; 43435 MW; 0B9AE143B09ED4D0 CRC64;
MKIPAALVFI PVGVLFLISG LIVNIIQLVF FIIVRPFSRS LYRRINKNVA ELLWLQLIWL
FDWWACIKIN LYVDAETLEL IGKEHALVLS NHRSDIDWLI GWVMAQRVGC LGSSLAIMKK
EAKYLPIIGW SMWFSDYIFL ERSWAKDENT LKAGFKRLED FPMTFWLALF VEGTRFTQEK
LEAAQEYASI RSLPSPRNVL IPRTKGFVSA VSEIRSFVPA IYDCTLTVHN NQPTPTLLRM
FSGQSSEINL QMRRHKMSEL PETDDGIAQW CQDLFITKDA QLEKYFTKDV FSDLEVHQIN
RPIKPLIVVI IWLGFLVFGG FKLLQWLSIV ASWKIILLFV FFLVIATITM QILIQSSESQ
RSTPAKRPLQ EQLISA
