LPIAT_CAEEL
ID LPIAT_CAEEL Reviewed; 391 AA.
AC Q20800;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Lysophosphatidylinositol acyltransferase 10;
DE Short=ACL-10 {ECO:0000303|PubMed:20668164};
DE Short=sn-2 acyl LPIAT;
DE EC=2.3.1.- {ECO:0000269|PubMed:20668164};
DE AltName: Full=2-acylglycerol 3-phosphate O-acyltransferase 10;
DE Short=AGPAT 10;
DE AltName: Full=PlsC domain-containing protein {ECO:0000312|EMBL:CAA96659.2};
GN Name=bus-18 {ECO:0000312|EMBL:CAA96659.2, ECO:0000312|WormBase:F55A11.5};
GN ORFNames=F55A11.5 {ECO:0000312|WormBase:F55A11.5};
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:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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 [2]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP PATHWAY, AND DISRUPTION PHENOTYPE.
RX PubMed=20668164; DOI=10.1091/mbc.e10-03-0195;
RA Imae R., Inoue T., Kimura M., Kanamori T., Tomioka N.H., Kage-Nakadai E.,
RA Mitani S., Arai H.;
RT "Intracellular phospholipase A1 and acyltransferase, which are involved in
RT Caenorhabditis elegans stem cell divisions, determine the sn-1 fatty acyl
RT chain of phosphatidylinositol.";
RL Mol. Biol. Cell 21:3114-3124(2010).
CC -!- FUNCTION: Acyltransferase required for the fatty acid remodeling of
CC phosphatidylinositol (1,2-diacyl-sn-glycero-3-phosphoinositol or PI).
CC Mediates the conversion of lysophosphatidylinositol (2-
CC acylglycerophosphatidylinositol or LPI) into PI (LPIAT activity). Has
CC preference for saturated and mono-unsaturated fatty acids as acyl
CC donors and sn-2-acyl lysoPI (2-acyl-sn-glycero-3-phospho-D-myo-
CC inositol) as acyl acceptor. Contributes to the asymmetric cell division
CC of epithelial cells. Asymmetric cell division is the fundamental
CC mechanism by which multicellular organisms generate cell diversity.
CC {ECO:0000269|PubMed:20668164}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2-acyl-sn-glycero-3-phospho-D-myo-inositol + an acyl-CoA = a
CC 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + CoA;
CC Xref=Rhea:RHEA:35271, ChEBI:CHEBI:57287, ChEBI:CHEBI:57880,
CC ChEBI:CHEBI:58342, ChEBI:CHEBI:64872;
CC Evidence={ECO:0000269|PubMed:20668164};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35272;
CC Evidence={ECO:0000269|PubMed:20668164};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2-acyl-sn-glycero-3-phospho-D-myo-inositol + octadecanoyl-
CC CoA = 1-octadecanoyl-2-acyl-sn-glycero-3-phospho-(1D-myo-inositol) +
CC CoA; Xref=Rhea:RHEA:43964, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394,
CC ChEBI:CHEBI:64872, ChEBI:CHEBI:83940;
CC Evidence={ECO:0000269|PubMed:20668164};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43965;
CC Evidence={ECO:0000269|PubMed:20668164};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylinositol metabolism.
CC {ECO:0000269|PubMed:20668164}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:20668164}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in seam cells, vulval epithelial cells
CC and the major epithelial syncytium hyp7, and in several head neurons
CC including AIY interneurons. {ECO:0000269|PubMed:20668164}.
CC -!- DISRUPTION PHENOTYPE: Mutants showed defects in vulval morphology and
CC in the asymmetric division of stem cell-like epithelial cells.
CC {ECO:0000269|PubMed:20668164}.
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000305}.
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DR EMBL; BX284605; CAA96659.2; -; Genomic_DNA.
DR PIR; T22689; T22689.
DR RefSeq; NP_505971.2; NM_073570.3.
DR AlphaFoldDB; Q20800; -.
DR STRING; 6239.F55A11.5; -.
DR SwissLipids; SLP:000001013; -.
DR EPD; Q20800; -.
DR PaxDb; Q20800; -.
DR PeptideAtlas; Q20800; -.
DR EnsemblMetazoa; F55A11.5.1; F55A11.5.1; WBGene00044631.
DR GeneID; 186277; -.
DR KEGG; cel:CELE_F55A11.5; -.
DR UCSC; F55A11.5; c. elegans.
DR CTD; 186277; -.
DR WormBase; F55A11.5; CE39507; WBGene00044631; bus-18.
DR eggNOG; KOG1505; Eukaryota.
DR GeneTree; ENSGT00950000182836; -.
DR HOGENOM; CLU_041844_4_0_1; -.
DR InParanoid; Q20800; -.
DR OMA; MDRAISY; -.
DR OrthoDB; 959325at2759; -.
DR PhylomeDB; Q20800; -.
DR UniPathway; UPA00949; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00044631; Expressed in embryo and 3 other tissues.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:WormBase.
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:0016746; F:acyltransferase activity; IMP:WormBase.
DR GO; GO:0002009; P:morphogenesis of an epithelium; IMP:WormBase.
DR GO; GO:0036149; P:phosphatidylinositol acyl-chain remodeling; IBA:GO_Central.
DR GO; GO:0046488; P:phosphatidylinositol metabolic process; IMP:WormBase.
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; Endoplasmic reticulum; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..391
FT /note="Lysophosphatidylinositol acyltransferase 10"
FT /id="PRO_0000453137"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 323..343
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 347..367
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 391 AA; 46520 MW; CE7D5188006C567D CRC64;
MRIPCLLRPL LGWFFGLCIL FSALFGNYII TLFLGLPILG RHKQWRNLMD RAISYWMTIP
MGLLEFLMGV RIRVSGDEIE FGSPAMIVMN HRTRLDWMYM WCALYQINPW LITSNKISLK
AQLKKLPGAG FGMAAAQFVF LERNAEVDKR SFDDAIDYFK NIDKKYQILL FPEGTDKSEW
TTLKSREFAK KNGLRHLDYV LYPRTTGFLH LLNKMREQEY VEYIYDITIA YPYNIVQSEI
DLVLKGASPR EVHFHIRKIP ISQVPLNEQD ASRWLTDRWT IKEQLLHDFY SEEQPINRQF
PVERGDGVWR SWKEPRRHFY VKLTSLMFWT LVISFCSYHI FFVRTLQLGF LYFFVISFYL
SWRYGGIDKY IIFKWQESRK SLQKSPSSSS I
