MBOA7_CAEEL
ID MBOA7_CAEEL Reviewed; 453 AA.
AC Q19468;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Lysophospholipid acyltransferase 7;
DE Short=LPLAT 7;
DE EC=2.3.1.- {ECO:0000269|PubMed:18094042, ECO:0000269|PubMed:22862955};
DE AltName: Full=1-acylglycerophosphatidylinositol O-acyltransferase {ECO:0000303|PubMed:18094042};
DE AltName: Full=Lysophosphatidylinositol acyltransferase {ECO:0000312|EMBL:ABV66274.1};
DE Short=LPIAT {ECO:0000303|PubMed:18094042};
DE Short=Lyso-PI acyltransferase {ECO:0000303|PubMed:18094042};
DE AltName: Full=Membrane-bound O-acyltransferase domain-containing protein 7 {ECO:0000303|PubMed:18094042};
DE Short=MBOA-7 {ECO:0000303|PubMed:18094042, ECO:0000303|PubMed:22862955};
GN Name=mboa-7 {ECO:0000312|WormBase:F14F3.3};
GN Synonyms=lpiat {ECO:0000312|EMBL:ABV66274.1},
GN tag-289 {ECO:0000312|WormBase:F14F3.3}; ORFNames=F14F3.3;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ABV66274.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, TISSUE
RP SPECIFICITY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF HIS-350.
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:ABV66274.1};
RX PubMed=18094042; DOI=10.1091/mbc.e07-09-0893;
RA Lee H.C., Inoue T., Imae R., Kono N., Shirae S., Matsuda S.,
RA Gengyo-Ando K., Mitani S., Arai H.;
RT "Caenorhabditis elegans mboa-7, a member of the MBOAT family, is required
RT for selective incorporation of polyunsaturated fatty acids into
RT phosphatidylinositol.";
RL Mol. Biol. Cell 19:1174-1184(2008).
RN [2] {ECO:0000312|EMBL:CAA90185.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:CAA90185.2};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=22862955; DOI=10.1111/j.1365-2443.2012.01624.x;
RA Lee H.C., Kubo T., Kono N., Kage-Nakadai E., Gengyo-Ando K., Mitani S.,
RA Inoue T., Arai H.;
RT "Depletion of mboa-7, an enzyme that incorporates polyunsaturated fatty
RT acids into phosphatidylinositol (PI), impairs PI 3-phosphate signaling in
RT Caenorhabditis elegans.";
RL Genes Cells 17:748-757(2012).
CC -!- FUNCTION: Acyltransferase which mediates the conversion of
CC lysophosphatidylinositol (1-acyl-sn-glycero-3-phosphatidylinositol or
CC LPI) into phosphatidylinositol (1,2-diacyl-sn-glycero-3-phosphoinositol
CC or PI) (LPIAT activity). Prefers sn-2-LPI rather than sn-1-LPI as the
CC acyl acceptor. Lysophospholipid acyltransferases (LPLATs) catalyze the
CC reacylation step of the phospholipid remodeling pathway also known as
CC the Lands cycle. Involved in the selective incorporation of
CC arachidonoyl-CoA ((5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA) and
CC (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoyl-CoA (EPA-CoA) into PI
CC (PubMed:18094042). Besides its role in biomembranes, PI is a precursor
CC of PI 3-phosphate (PIP3) and its fatty acid composition has an
CC important role in PI3P signaling (PubMed:22862955).
CC {ECO:0000269|PubMed:18094042, ECO:0000269|PubMed:22862955}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoyl-CoA + 1-octadecanoyl-sn-
CC glycero-3-phospho-(1D-myo-inositol) = 1-octadecanoyl-2-
CC (5Z,8Z,11Z,14Z,17Z-eicosapentaenoyl)-sn-glycero-3-phospho-(1D-myo-
CC inositol) + CoA; Xref=Rhea:RHEA:36839, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:73862, ChEBI:CHEBI:74243, ChEBI:CHEBI:74245;
CC Evidence={ECO:0000269|PubMed:18094042};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36840;
CC Evidence={ECO:0000269|PubMed:18094042};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoyl-CoA + a 1-acyl-sn-
CC glycero-3-phospho-(1D-myo-inositol) = a 1-acyl-2-(5Z,8Z,11Z,14Z,17Z-
CC eicosapentaenoyl)-sn-glycero-3-phospho-(1D-myo-inositol) + CoA;
CC Xref=Rhea:RHEA:37011, ChEBI:CHEBI:57287, ChEBI:CHEBI:64771,
CC ChEBI:CHEBI:73862, ChEBI:CHEBI:74335;
CC Evidence={ECO:0000269|PubMed:18094042};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37012;
CC Evidence={ECO:0000269|PubMed:18094042};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + a 1-acyl-sn-glycero-3-
CC phospho-(1D-myo-inositol) = a 1-acyl-2-(5Z,8Z,11Z,14Z-
CC eicosatetraenoyl)-sn-glycero-3-phospho-(1D-myo-inositol) + CoA;
CC Xref=Rhea:RHEA:37015, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368,
CC ChEBI:CHEBI:64771, ChEBI:CHEBI:75243;
CC Evidence={ECO:0000269|PubMed:18094042, ECO:0000269|PubMed:22862955};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37016;
CC Evidence={ECO:0000269|PubMed:18094042, ECO:0000269|PubMed:22862955};
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC {ECO:0000269|PubMed:18094042, ECO:0000269|PubMed:22862955}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously throughout development from
CC early embryo to larval and adult stages. In adults, strongly expressed
CC in pharyngeal muscle, body wall muscle, vulval cells, distal tip cells,
CC intestinal cells and spermatheca. {ECO:0000269|PubMed:18094042}.
CC -!- DISRUPTION PHENOTYPE: Mutants show larval arrest at an early
CC developmental stage and egg-laying defects; 14% of mutants accumulate
CC unlaid eggs that hatched internally. {ECO:0000269|PubMed:18094042}.
CC -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC {ECO:0000255}.
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DR EMBL; EU016382; ABV66274.1; -; mRNA.
DR EMBL; Z49937; CAA90185.2; -; Genomic_DNA.
DR PIR; T20899; T20899.
DR RefSeq; NP_509760.2; NM_077359.5.
DR AlphaFoldDB; Q19468; -.
DR SMR; Q19468; -.
DR STRING; 6239.F14F3.3; -.
DR SwissLipids; SLP:000000135; -.
DR EPD; Q19468; -.
DR PaxDb; Q19468; -.
DR PeptideAtlas; Q19468; -.
DR EnsemblMetazoa; F14F3.3.1; F14F3.3.1; WBGene00008806.
DR GeneID; 181252; -.
DR KEGG; cel:CELE_F14F3.3; -.
DR UCSC; F14F3.3; c. elegans.
DR CTD; 181252; -.
DR WormBase; F14F3.3; CE40384; WBGene00008806; mboa-7.
DR eggNOG; KOG2706; Eukaryota.
DR GeneTree; ENSGT01030000234564; -.
DR HOGENOM; CLU_011340_1_1_1; -.
DR InParanoid; Q19468; -.
DR OMA; EVERCWT; -.
DR OrthoDB; 881262at2759; -.
DR PhylomeDB; Q19468; -.
DR BRENDA; 2.3.1.B46; 1045.
DR Reactome; R-CEL-1482922; Acyl chain remodelling of PI.
DR UniPathway; UPA00085; -.
DR PRO; PR:Q19468; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00008806; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:WormBase.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0044233; C:mitochondria-associated endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016746; F:acyltransferase activity; IBA:GO_Central.
DR GO; GO:0071617; F:lysophospholipid acyltransferase activity; IBA:GO_Central.
DR GO; GO:0008374; F:O-acyltransferase activity; IDA:WormBase.
DR GO; GO:0030258; P:lipid modification; IBA:GO_Central.
DR GO; GO:0035264; P:multicellular organism growth; IGI:WormBase.
DR GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR GO; GO:0018991; P:oviposition; IMP:WormBase.
DR GO; GO:0006661; P:phosphatidylinositol biosynthetic process; IDA:WormBase.
DR InterPro; IPR004299; MBOAT_fam.
DR Pfam; PF03062; MBOAT; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Glycoprotein; Lipid biosynthesis; Lipid metabolism;
KW Membrane; Phospholipid biosynthesis; Phospholipid metabolism;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..453
FT /note="Lysophospholipid acyltransferase 7"
FT /id="PRO_0000393937"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 79..99
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 354..374
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 421..441
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 350
FT /evidence="ECO:0000269|PubMed:18094042"
FT CARBOHYD 319
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 350
FT /note="H->A: Disrupts LPIAT activity."
FT /evidence="ECO:0000269|PubMed:18094042"
SQ SEQUENCE 453 AA; 51975 MW; BD33F33AE8076297 CRC64;
MENILGLMSK DDWIYTGLLL FSFGASCYVR KIGNNILASG ALGFAMSLFI IGPKIVYSLG
ICSIAISIQL LANKKSTPLY VFLTTFTYLM FVRFAHYILP VNEVASHTNV IQLIITLRII
GITFEENDAW VHKSDENPTK RYLTELPTIL EKFAYFYHFC GLFTGPYYTY QMLIDSQNPI
LKSWDPTLEV KSRFVRLLWS VPVFVITNHY FPLDILRSDA IWEVSFFTRL VYAALIFVVF
KTRVYSAWAI AESICVILGI GIYPAASNPK IIMGPTDLNA FDKLKTRENI EMSSDAIVNL
DIPKVEFSDG FRDGMKAWNR SVQTWLALYV HSRVKVMRVE TTMLVSAVWH GTYAGYFMSF
GVVAMCAILE DVIFKLVPVD TETGVRPKWF RILYTHTIRC RGFEMLATGF LLKNAYDVHH
FWSSIYYWLP LLCIPFYIYS AKISKPKKAQ KSE
