LGAT1_HUMAN
ID LGAT1_HUMAN Reviewed; 370 AA.
AC Q92604; Q53YL2;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Acyl-CoA:lysophosphatidylglycerol acyltransferase 1 {ECO:0000305};
DE AltName: Full=Acyl-CoA:monoacylglycerol acyltransferase LPGAT1 {ECO:0000250|UniProtKB:Q91YX5};
DE EC=2.3.1.22 {ECO:0000250|UniProtKB:Q91YX5};
DE AltName: Full=Lysophospholipid acyltransferase 7 {ECO:0000303|PubMed:34890643};
DE Short=LPLAT7 {ECO:0000303|PubMed:34890643};
DE EC=2.3.1.- {ECO:0000269|PubMed:15485873};
DE AltName: Full=Stearoyl-CoA:1-lyso-2-acyl-PE acyltransferase {ECO:0000250|UniProtKB:Q91YX5};
GN Name=LPGAT1 {ECO:0000312|HGNC:HGNC:28985};
GN Synonyms=FAM34A, KIAA0205 {ECO:0000303|PubMed:9039502};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND CATALYTIC ACTIVITY.
RC TISSUE=Liver;
RX PubMed=15485873; DOI=10.1074/jbc.m406710200;
RA Yang Y., Cao J., Shi Y.;
RT "Identification and characterization of a gene encoding human LPGAT1, an
RT endoplasmic reticulum-associated lysophosphatidylglycerol
RT acyltransferase.";
RL J. Biol. Chem. 279:55866-55874(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Ji D., Cheng J., Dong J., Liu Y., Wang J.-J., Guo J.;
RT "Screening and identification of genes trans-regulated by hepatitis B virus
RT pre-S2 protein by microarray assay.";
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow;
RX PubMed=9039502; DOI=10.1093/dnares/3.5.321;
RA Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O.,
RA Tanaka A., Kotani H., Miyajima N., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. VI. The
RT coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of
RT cDNA clones from cell line KG-1 and brain.";
RL DNA Res. 3:321-329(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [8]
RP NOMENCLATURE.
RX PubMed=34890643; DOI=10.1016/j.jbc.2021.101470;
RA Valentine W.J., Yanagida K., Kawana H., Kono N., Noda N.N., Aoki J.,
RA Shindou H.;
RT "Update and nomenclature proposal for mammalian lysophospholipid
RT acyltransferases, which create membrane phospholipid diversity.";
RL J. Biol. Chem. 298:101470-101470(2022).
CC -!- FUNCTION: Lysophospholipid acyltransferase involved in fatty acyl chain
CC remodeling of glycerophospholipids in the endoplasmic reticulum
CC membrane (By similarity). Selectively catalyzes the transfer and
CC esterification of saturated long-chain fatty acids from acyl-CoA to the
CC sn-1 position of 1-lyso-2-acyl phosphatidylethanolamines (1-lyso-PE,
CC LPE), with a preference for stearoyl CoA over palmitoyl CoA as acyl
CC donor. Acts in concert with an unknown phospholipase A1 to convert
CC palmitate phosphatidylethanolamine (PE) species into stearate ones.
CC Provides substrates to the PE methylation pathway, controlling
CC stearate/palmitate composition of PE and phosphatidylcholine (PC)
CC species with an overall impact on de novo hepatic lipid synthesis, body
CC fat content and life span (By similarity). Can acylate
CC lysophosphatidylglycerols (LPG) using various saturated fatty acyl-CoAs
CC as acyl donors (PubMed:15485873). Can also acylate monoacylglycerols
CC with a preference for 2-monoacylglycerols over 1-monoacylglycerols (By
CC similarity). Has no activity toward lysophosphatidic acids (LPA) and
CC lysophosphatidylcholines (LPC) (By similarity).
CC {ECO:0000250|UniProtKB:Q91YX5}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2-acyl-sn-glycero-3-phosphoethanolamine + octadecanoyl-CoA =
CC 1-octadecanoyl-2-acyl-sn-glycero-3-phosphoethanolamine + CoA;
CC Xref=Rhea:RHEA:70583, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394,
CC ChEBI:CHEBI:65213, ChEBI:CHEBI:189703;
CC Evidence={ECO:0000250|UniProtKB:Q91YX5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70584;
CC Evidence={ECO:0000250|UniProtKB:Q91YX5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine +
CC octadecanoyl-CoA = 1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine + CoA; Xref=Rhea:RHEA:70579, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57394, ChEBI:CHEBI:75038, ChEBI:CHEBI:76088;
CC Evidence={ECO:0000250|UniProtKB:Q91YX5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70580;
CC Evidence={ECO:0000250|UniProtKB:Q91YX5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2-acyl-sn-glycero-3-phosphoethanolamine + hexadecanoyl-CoA =
CC 1-hexadecanoyl-2-acyl-sn-glycero-3-phosphoethanolamine + CoA;
CC Xref=Rhea:RHEA:70595, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:65213, ChEBI:CHEBI:77370;
CC Evidence={ECO:0000250|UniProtKB:Q91YX5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70596;
CC Evidence={ECO:0000250|UniProtKB:Q91YX5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine +
CC hexadecanoyl-CoA = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine + CoA; Xref=Rhea:RHEA:70591, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57379, ChEBI:CHEBI:73007, ChEBI:CHEBI:76088;
CC Evidence={ECO:0000250|UniProtKB:Q91YX5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70592;
CC Evidence={ECO:0000250|UniProtKB:Q91YX5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-tetradecanoyl-sn-glycero-3-phospho-(1'-sn-glycerol) +
CC hexadecanoyl-CoA = 1-tetradecanoyl-2-hexadecanoyl-sn-glycero-3-
CC phospho-(1'-sn-glycerol) + CoA; Xref=Rhea:RHEA:35855,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:72826,
CC ChEBI:CHEBI:72830; Evidence={ECO:0000269|PubMed:15485873};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35856;
CC Evidence={ECO:0000269|PubMed:15485873};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phospho-(1'-sn-glycerol) +
CC dodecanoyl-CoA = 1-hexadecanoyl-2-dodecanoyl-sn-glycero-3-phospho-
CC (1'-sn-glycerol) + CoA; Xref=Rhea:RHEA:40107, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57375, ChEBI:CHEBI:75158, ChEBI:CHEBI:77001;
CC Evidence={ECO:0000269|PubMed:15485873};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40108;
CC Evidence={ECO:0000269|PubMed:15485873};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phospho-(1'-sn-glycerol) +
CC hexadecanoyl-CoA = 1,2-dihexadecanoyl-sn-glycero-3-phospho-(1'-sn-
CC glycerol) + CoA; Xref=Rhea:RHEA:35851, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57379, ChEBI:CHEBI:72829, ChEBI:CHEBI:75158;
CC Evidence={ECO:0000269|PubMed:15485873};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35852;
CC Evidence={ECO:0000269|PubMed:15485873};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phospho-(1'-sn-glycerol) +
CC octadecanoyl-CoA = 1-hexadecanoyl-2-octadecanoyl-sn-glycero-3-
CC phospho-(1'-sn-glycerol) + CoA; Xref=Rhea:RHEA:35887,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57394, ChEBI:CHEBI:72839,
CC ChEBI:CHEBI:75158; Evidence={ECO:0000269|PubMed:15485873};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35888;
CC Evidence={ECO:0000269|PubMed:15485873};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-sn-glycero-3-phospho-(1'-sn-glycerol) +
CC hexadecanoyl-CoA = 1-octadecanoyl-2-hexadecanoyl-sn-glycero-3-
CC phospho-(1'-sn-glycerol) + CoA; Xref=Rhea:RHEA:35859,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:72827,
CC ChEBI:CHEBI:72831; Evidence={ECO:0000269|PubMed:15485873};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35860;
CC Evidence={ECO:0000269|PubMed:15485873};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-sn-glycerol) +
CC dodecanoyl-CoA = 1-(9Z-octadecenoyl)-2-dodecanoyl-sn-glycero-3-
CC phospho-(1'-sn-glycerol) + CoA; Xref=Rhea:RHEA:40099,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57375, ChEBI:CHEBI:72828,
CC ChEBI:CHEBI:77000; Evidence={ECO:0000269|PubMed:15485873};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40100;
CC Evidence={ECO:0000269|PubMed:15485873};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-phospho-
CC (1'-sn-glycerol) = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-
CC phospho-(1'-sn-glycerol) + CoA; Xref=Rhea:RHEA:35891,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:72841,
CC ChEBI:CHEBI:75158; Evidence={ECO:0000269|PubMed:15485873};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35892;
CC Evidence={ECO:0000269|PubMed:15485873};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-sn-glycerol) +
CC hexadecanoyl-CoA = 1-(9Z-octadecenoyl)-2-hexadecanoyl-sn-glycero-3-
CC phospho-(1'-sn-glycerol) + CoA; Xref=Rhea:RHEA:35863,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:72828,
CC ChEBI:CHEBI:72832; Evidence={ECO:0000269|PubMed:15485873};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35864;
CC Evidence={ECO:0000269|PubMed:15485873};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-
CC phospho-(1'-sn-glycerol) = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-
CC phospho-(1'-sn-glycerol) + CoA; Xref=Rhea:RHEA:37651,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:72828,
CC ChEBI:CHEBI:75163; Evidence={ECO:0000269|PubMed:15485873};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37652;
CC Evidence={ECO:0000269|PubMed:15485873};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2-acylglycerol + an acyl-CoA = a 1,2-diacyl-sn-glycerol +
CC CoA; Xref=Rhea:RHEA:32947, ChEBI:CHEBI:17389, ChEBI:CHEBI:17815,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:58342; EC=2.3.1.22;
CC Evidence={ECO:0000250|UniProtKB:Q91YX5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32948;
CC Evidence={ECO:0000250|UniProtKB:Q91YX5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2-acylglycerol + hexadecanoyl-CoA = a 1-hexadecanoyl-2-
CC acylglycerol + CoA; Xref=Rhea:RHEA:65096, ChEBI:CHEBI:17389,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:156324;
CC Evidence={ECO:0000250|UniProtKB:Q91YX5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65097;
CC Evidence={ECO:0000250|UniProtKB:Q91YX5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acylglycerol + hexadecanoyl-CoA = an hexadecanoyl-
CC acylglycerol + CoA; Xref=Rhea:RHEA:65100, ChEBI:CHEBI:35759,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:156325;
CC Evidence={ECO:0000250|UniProtKB:Q91YX5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65101;
CC Evidence={ECO:0000250|UniProtKB:Q91YX5};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:15485873}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15485873}.
CC -!- TISSUE SPECIFICITY: Highly expressed in liver and placenta. Also
CC expressed in peripheral blood, lung, kidney and brain. Detected at
CC lower levels in colon. High expression is detected in brain and testis.
CC {ECO:0000269|PubMed:15485873}.
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 -!- CAUTION: The role in phosphatidylglycerols remodeling and cardiolipin
CC synthesis is questioned as both processes occur in mitochondria. The
CC monoacylglycerol acyltransferase activity is also weak and a direct
CC role in triacylglycerol synthesis appears unlikely.
CC {ECO:0000250|UniProtKB:Q91YX5}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA13196.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D86960; BAA13196.2; ALT_INIT; mRNA.
DR EMBL; AY561706; AAS66979.1; -; mRNA.
DR EMBL; AC096637; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL445488; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471100; EAW93407.1; -; Genomic_DNA.
DR EMBL; CH471100; EAW93408.1; -; Genomic_DNA.
DR EMBL; BC034621; AAH34621.1; -; mRNA.
DR CCDS; CCDS31018.1; -.
DR RefSeq; NP_001307737.1; NM_001320808.1.
DR RefSeq; NP_055688.1; NM_014873.2.
DR RefSeq; XP_011508530.1; XM_011510228.2.
DR RefSeq; XP_011508531.1; XM_011510229.2.
DR AlphaFoldDB; Q92604; -.
DR BioGRID; 115254; 98.
DR IntAct; Q92604; 21.
DR MINT; Q92604; -.
DR STRING; 9606.ENSP00000355964; -.
DR SwissLipids; SLP:000000128; -.
DR iPTMnet; Q92604; -.
DR PhosphoSitePlus; Q92604; -.
DR BioMuta; LPGAT1; -.
DR DMDM; 6136501; -.
DR EPD; Q92604; -.
DR jPOST; Q92604; -.
DR MassIVE; Q92604; -.
DR MaxQB; Q92604; -.
DR PaxDb; Q92604; -.
DR PeptideAtlas; Q92604; -.
DR PRIDE; Q92604; -.
DR ProteomicsDB; 75351; -.
DR Antibodypedia; 1888; 97 antibodies from 22 providers.
DR DNASU; 9926; -.
DR Ensembl; ENST00000366996.1; ENSP00000355963.1; ENSG00000123684.13.
DR Ensembl; ENST00000366997.9; ENSP00000355964.4; ENSG00000123684.13.
DR GeneID; 9926; -.
DR KEGG; hsa:9926; -.
DR MANE-Select; ENST00000366997.9; ENSP00000355964.4; NM_014873.3; NP_055688.1.
DR UCSC; uc001hiu.4; human.
DR CTD; 9926; -.
DR DisGeNET; 9926; -.
DR GeneCards; LPGAT1; -.
DR HGNC; HGNC:28985; LPGAT1.
DR HPA; ENSG00000123684; Low tissue specificity.
DR MIM; 610473; gene.
DR neXtProt; NX_Q92604; -.
DR OpenTargets; ENSG00000123684; -.
DR PharmGKB; PA134869091; -.
DR VEuPathDB; HostDB:ENSG00000123684; -.
DR eggNOG; KOG1505; Eukaryota.
DR GeneTree; ENSGT00950000182836; -.
DR HOGENOM; CLU_046804_2_0_1; -.
DR InParanoid; Q92604; -.
DR OMA; MEWGEDV; -.
DR OrthoDB; 836124at2759; -.
DR PhylomeDB; Q92604; -.
DR TreeFam; TF314346; -.
DR PathwayCommons; Q92604; -.
DR Reactome; R-HSA-1482925; Acyl chain remodelling of PG.
DR SignaLink; Q92604; -.
DR BioGRID-ORCS; 9926; 29 hits in 1074 CRISPR screens.
DR ChiTaRS; LPGAT1; human.
DR GenomeRNAi; 9926; -.
DR Pharos; Q92604; Tbio.
DR PRO; PR:Q92604; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q92604; protein.
DR Bgee; ENSG00000123684; Expressed in middle temporal gyrus and 185 other tissues.
DR Genevisible; Q92604; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IMP:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; TAS:Reactome.
DR GO; GO:0003846; F:2-acylglycerol O-acyltransferase activity; ISS:UniProtKB.
DR GO; GO:0047144; F:2-acylglycerol-3-phosphate O-acyltransferase activity; TAS:Reactome.
DR GO; GO:0016746; F:acyltransferase activity; IBA:GO_Central.
DR GO; GO:0071618; F:lysophosphatidylethanolamine acyltransferase activity; ISS:UniProtKB.
DR GO; GO:0071617; F:lysophospholipid acyltransferase activity; IMP:UniProtKB.
DR GO; GO:0036152; P:phosphatidylethanolamine acyl-chain remodeling; ISS:UniProtKB.
DR GO; GO:0036148; P:phosphatidylglycerol acyl-chain remodeling; TAS:Reactome.
DR GO; GO:0036149; P:phosphatidylinositol acyl-chain remodeling; IBA:GO_Central.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0045723; P:positive regulation of fatty acid biosynthetic process; IMP:BHF-UCL.
DR GO; GO:0019432; P:triglyceride biosynthetic process; ISS:UniProtKB.
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; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..370
FT /note="Acyl-CoA:lysophosphatidylglycerol acyltransferase 1"
FT /id="PRO_0000208204"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 342..362
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 101..106
FT /note="HXXXXD motif"
SQ SEQUENCE 370 AA; 43089 MW; 93498544EA651541 CRC64;
MAITLEEAPW LGWLLVKALM RFAFMVVNNL VAIPSYICYV IILQPLRVLD SKRFWYIEGI
MYKWLLGMVA SWGWYAGYTV MEWGEDIKAV SKDEAVMLVN HQATGDVCTL MMCLQDKGLV
VAQMMWLMDH IFKYTNFGIV SLVHGDFFIR QGRSYRDQQL LLLKKHLENN YRSRDRKWIV
LFPEGGFLRK RRETSQAFAK KNNLPFLTNV TLPRSGATKI ILNALVAQQK NGSPAGGDAK
ELDSKSKGLQ WIIDTTIAYP KAEPIDIQTW ILGYRKPTVT HVHYRIFPIK DVPLETDDLT
TWLYQRFVEK EDLLSHFYET GAFPPSKGHK EAVSREMTLS NLWIFLIQSF AFLSGYMWYN
IIQYFYHCLF
