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 08-NOV-2023, entry version 175. DE RecName: Full=Acyl-CoA:lysophosphatidylglycerol acyltransferase 1 {ECO:0000305}; DE AltName: Full=2-acylglycerophosphocholine O-acyltransferase; DE EC=2.3.1.62 {ECO:0000269|PubMed:36049524}; 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). RN [9] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=36049524; DOI=10.1016/j.jlr.2022.100271; RA Kawana H., Ozawa M., Shibata T., Onishi H., Sato Y., Kano K., Shindou H., RA Shimizu T., Kono N., Aoki J.; RT "Identification and characterization of LPLAT7 as an sn-1-specific RT lysophospholipid acyltransferase."; RL J. Lipid Res. 63:100271-100271(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 (PubMed:36049524). Acts in concert with an unknown phospholipase CC A1 to convert palmitate phosphatidylethanolamine (PE) species into CC stearate ones. Provides substrates to the PE methylation pathway, CC controlling stearate/palmitate composition of PE and CC phosphatidylcholine (PC) species with an overall impact on de novo CC hepatic lipid synthesis, body fat content and life span (By CC similarity). Can acylate lysophosphatidylglycerols (LPG) using various CC saturated fatty acyl-CoAs as acyl donors (PubMed:15485873). Can also CC acylate monoacylglycerols with a preference for 2-monoacylglycerols CC over 1-monoacylglycerols (By similarity). Has no activity toward CC lysophosphatidic acids (LPA) (By similarity). CC {ECO:0000250|UniProtKB:Q91YX5, ECO:0000269|PubMed:15485873, CC ECO:0000269|PubMed:36049524}. 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:0000269|PubMed:36049524}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70580; CC Evidence={ECO:0000305|PubMed:36049524}; 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:0000269|PubMed:36049524}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70592; CC Evidence={ECO:0000305|PubMed:36049524}; 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-diacylglycerol + CoA; CC Xref=Rhea:RHEA:16741, ChEBI:CHEBI:17389, ChEBI:CHEBI:49172, 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:16742; 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 -!- CATALYTIC ACTIVITY: CC Reaction=a 2-acyl-sn-glycero-3-phosphocholine + an acyl-CoA = a 1,2- CC diacyl-sn-glycero-3-phosphocholine + CoA; Xref=Rhea:RHEA:10332, CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57643, ChEBI:CHEBI:57875, CC ChEBI:CHEBI:58342; EC=2.3.1.62; CC Evidence={ECO:0000269|PubMed:36049524}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + CC octadecanoyl-CoA = 1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3- CC phosphocholine + CoA; Xref=Rhea:RHEA:74799, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:57394, ChEBI:CHEBI:75034, ChEBI:CHEBI:76071; CC Evidence={ECO:0000269|PubMed:36049524}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine + CC octadecanoyl-CoA = 1-octadecanoyl-2-(9Z,12Z)-octadecadienoyl-sn- CC glycero-3-phosphocholine + CoA; Xref=Rhea:RHEA:74803, CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57394, ChEBI:CHEBI:76084, CC ChEBI:CHEBI:84822; Evidence={ECO:0000269|PubMed:36049524}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphocholine CC + octadecanoyl-CoA = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z- CC eicosatetraenoyl)-sn-glycero-3-phosphocholine + CoA; CC Xref=Rhea:RHEA:74807, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394, CC ChEBI:CHEBI:74965, ChEBI:CHEBI:76079; CC Evidence={ECO:0000269|PubMed:36049524}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + CC hexadecanoyl-CoA = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3- CC phosphocholine + CoA; Xref=Rhea:RHEA:74811, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:57379, ChEBI:CHEBI:73001, ChEBI:CHEBI:76071; CC Evidence={ECO:0000269|PubMed:36049524}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + CC hexadecanoyl-CoA = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3- CC phospho-L-serine + CoA; Xref=Rhea:RHEA:74815, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:57379, ChEBI:CHEBI:75029, ChEBI:CHEBI:77342; CC Evidence={ECO:0000269|PubMed:36049524}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3- CC phosphocholine + octadecanoyl-CoA = 1-octadecanoyl-2- CC (4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-phosphocholine + CC CoA; Xref=Rhea:RHEA:74823, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394, CC ChEBI:CHEBI:76085, ChEBI:CHEBI:84829; CC Evidence={ECO:0000269|PubMed:36049524}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + CC octadecanoyl-CoA = 1-(9Z-octadecenoyl)-2-octadecanoyl-sn-glycero-3- CC phospho-L-serine + CoA; Xref=Rhea:RHEA:37403, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:57394, ChEBI:CHEBI:74617, ChEBI:CHEBI:74902; CC Evidence={ECO:0000269|PubMed:36049524}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 2-acyl-sn-glycero-3-phosphoethanolamine + a fatty acyl-CoA = CC a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CoA; CC Xref=Rhea:RHEA:70599, ChEBI:CHEBI:57287, ChEBI:CHEBI:64612, CC ChEBI:CHEBI:65213, ChEBI:CHEBI:77636; CC Evidence={ECO:0000269|PubMed:36049524}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70600; CC Evidence={ECO:0000305|PubMed:36049524}; 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 106. 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; 9606-ENSP00000355964; -. DR PeptideAtlas; Q92604; -. DR ProteomicsDB; 75351; -. DR Pumba; Q92604; -. DR Antibodypedia; 1888; 100 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 AGR; HGNC:28985; -. 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; PLDIQTW; -. DR OrthoDB; 3012482at2759; -. 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; 30 hits in 1153 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: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:0047190; F:2-acylglycerophosphocholine O-acyltransferase activity; IDA:UniProtKB. 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; IDA: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 CDD; cd07990; LPLAT_LCLAT1-like; 1. DR InterPro; IPR032098; Acyltransf_C. DR InterPro; IPR002123; Plipid/glycerol_acylTrfase. DR PANTHER; PTHR10983; 1-ACYLGLYCEROL-3-PHOSPHATE ACYLTRANSFERASE-RELATED; 1. DR PANTHER; PTHR10983:SF2; ACYL-COA:LYSOPHOSPHATIDYLGLYCEROL ACYLTRANSFERASE 1; 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 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 //