ID LPAT5_ARATH Reviewed; 375 AA.
AC Q9LHN4; Q2V3U6;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 129.
DE RecName: Full=Probable 1-acyl-sn-glycerol-3-phosphate acyltransferase 5;
DE EC=2.3.1.51;
DE AltName: Full=Lysophosphatidyl acyltransferase 5;
GN Name=LPAT5; Synonyms=LPAAT5; OrderedLocusNames=At3g18850; ORFNames=MCB22.2;
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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 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: May convert lysophosphatidic acid (LPA) into phosphatidic
CC acid by incorporating acyl moiety at the 2 position (By similarity).
CC Has no activity when expressed in bacteria or yeast. {ECO:0000250}.
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 -!- 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 -!- 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=Q9LHN4-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Widely expressed at low level.
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}.
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DR EMBL; AP002039; BAB03094.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76155.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76156.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76157.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76158.1; -; Genomic_DNA.
DR EMBL; AY099849; AAM20700.1; -; mRNA.
DR EMBL; BT008462; AAP37821.1; -; mRNA.
DR RefSeq; NP_001030724.2; NM_001035647.3. [Q9LHN4-1]
DR RefSeq; NP_001078183.1; NM_001084714.1. [Q9LHN4-1]
DR RefSeq; NP_188515.1; NM_112771.5. [Q9LHN4-1]
DR RefSeq; NP_974335.1; NM_202606.2. [Q9LHN4-1]
DR AlphaFoldDB; Q9LHN4; -.
DR STRING; 3702.Q9LHN4; -.
DR PaxDb; 3702-AT3G18850-2; -.
DR ProteomicsDB; 238520; -. [Q9LHN4-1]
DR EnsemblPlants; AT3G18850.1; AT3G18850.1; AT3G18850. [Q9LHN4-1]
DR EnsemblPlants; AT3G18850.2; AT3G18850.2; AT3G18850. [Q9LHN4-1]
DR EnsemblPlants; AT3G18850.3; AT3G18850.3; AT3G18850. [Q9LHN4-1]
DR EnsemblPlants; AT3G18850.4; AT3G18850.4; AT3G18850. [Q9LHN4-1]
DR GeneID; 821418; -.
DR Gramene; AT3G18850.1; AT3G18850.1; AT3G18850. [Q9LHN4-1]
DR Gramene; AT3G18850.2; AT3G18850.2; AT3G18850. [Q9LHN4-1]
DR Gramene; AT3G18850.3; AT3G18850.3; AT3G18850. [Q9LHN4-1]
DR Gramene; AT3G18850.4; AT3G18850.4; AT3G18850. [Q9LHN4-1]
DR KEGG; ath:AT3G18850; -.
DR Araport; AT3G18850; -.
DR TAIR; AT3G18850; LPAT5.
DR eggNOG; KOG1505; Eukaryota.
DR InParanoid; Q9LHN4; -.
DR OMA; CPRIHIH; -.
DR OrthoDB; 2906776at2759; -.
DR PhylomeDB; Q9LHN4; -.
DR BioCyc; ARA:AT3G18850-MONOMER; -.
DR BRENDA; 2.3.1.51; 399.
DR UniPathway; UPA00557; UER00613.
DR PRO; PR:Q9LHN4; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LHN4; baseline and differential.
DR Genevisible; Q9LHN4; AT.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd07990; LPLAT_LCLAT1-like; 1.
DR InterPro; IPR032098; Acyltransf_C.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR PANTHER; PTHR10983:SF76; 1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE EPSILON; 1.
DR PANTHER; PTHR10983; 1-ACYLGLYCEROL-3-PHOSPHATE ACYLTRANSFERASE-RELATED; 1.
DR Pfam; PF16076; Acyltransf_C; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Alternative splicing; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..375
FT /note="Probable 1-acyl-sn-glycerol-3-phosphate
FT acyltransferase 5"
FT /id="PRO_0000208184"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 312..332
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 337..357
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 100..105
FT /note="HXXXXD motif"
SQ SEQUENCE 375 AA; 43490 MW; 8F6F5DC313A3D704 CRC64;
MEKKSVPNSD KLSLIRVLRG IICLMVLVST AFMMLIFWGF LSAVVLRLFS IRYSRKCVSF
FFGSWLALWP FLFEKINKTK VIFSGDKVPC EDRVLLIANH RTEVDWMYFW DLALRKGQIG
NIKYVLKSSL MKLPLFGWAF HLFEFIPVER RWEVDEANLR QIVSSFKDPR DALWLALFPE
GTDYTEAKCQ RSKKFAAENG LPILNNVLLP RTKGFVSCLQ ELSCSLDAVY DVTIGYKTRC
PSFLDNVYGI EPSEVHIHIR RINLTQIPNQ EKDINAWLMN TFQLKDQLLN DFYSNGHFPN
EGTEKEFNTK KYLINCLAVI AFTTICTHLT FFSSMIWFRI YVSLACVYLT SATHFNLRSV
PLVETAKNSL KLVNK
//
