LPCT4_HUMAN
ID LPCT4_HUMAN Reviewed; 524 AA.
AC Q643R3; A8K2K8; O43412; Q7Z4P4; Q8IUL7; Q8TB38;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Lysophospholipid acyltransferase LPCAT4;
DE AltName: Full=1-acylglycerol-3-phosphate O-acyltransferase 7;
DE Short=1-AGP acyltransferase 7;
DE Short=1-AGPAT 7;
DE AltName: Full=1-acylglycerophosphocholine O-acyltransferase;
DE EC=2.3.1.23 {ECO:0000269|PubMed:18458083};
DE AltName: Full=1-acylglycerophosphoserine O-acyltransferase;
DE EC=2.3.1.n6 {ECO:0000269|PubMed:18458083};
DE AltName: Full=1-alkenylglycerophosphoethanolamine O-acyltransferase;
DE EC=2.3.1.121 {ECO:0000269|PubMed:18458083};
DE AltName: Full=1-alkylglycerophosphocholine O-acetyltransferase;
DE EC=2.3.1.67 {ECO:0000269|PubMed:18458083};
DE AltName: Full=Acyltransferase-like 3;
DE AltName: Full=Lysophosphatidylcholine acyltransferase 4;
DE AltName: Full=Lysophosphatidylethanolamine acyltransferase 2;
DE EC=2.3.1.n7 {ECO:0000269|PubMed:18458083};
DE AltName: Full=Plasmalogen synthase;
GN Name=LPCAT4; Synonyms=AGPAT7, AYTL3, LPEAT2;
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], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=16243729; DOI=10.1080/10425170500213712;
RA Ye G.-M., Chen C., Huang S., Han D.-D., Guo J.-H., Wan B., Yu L.;
RT "Cloning and characterization a novel human 1-acyl-sn-glycerol-3-phosphate
RT acyltransferase gene AGPAT7.";
RL DNA Seq. 16:386-390(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RA Guo J.H., Yu L.;
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 268-414.
RC TISSUE=Brain;
RA Yu W., Sarginson J., Gibbs R.A.;
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=18458083; DOI=10.1074/jbc.m800364200;
RA Cao J., Shan D., Revett T., Li D., Wu L., Liu W., Tobin J.F., Gimeno R.E.;
RT "Molecular identification of a novel mammalian brain isoform of acyl-
RT CoA:lysophospholipid acyltransferase with prominent ethanolamine
RT lysophospholipid acylating activity, LPEAT2.";
RL J. Biol. Chem. 283:19049-19057(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Displays acyl-CoA-dependent lysophospholipid acyltransferase
CC activity with a subset of lysophospholipids as substrates; converts
CC lysophosphatidylethanolamine to phosphatidylethanolamine,
CC lysophosphatidylcholine to phosphatidycholine, 1-alkenyl-
CC lysophatidylethanolamine to 1-alkenyl-phosphatidylethanolamine,
CC lysophosphatidylglycerol and alkyl-lysophosphatidylcholine to
CC phosphatidylglycerol and alkyl-phosphatidylcholine, respectively. In
CC contrast, has no lysophosphatidylinositol, glycerol-3-phosphate,
CC diacylglycerol or lysophosphatidic acid acyltransferase activity.
CC Prefers long chain acyl-CoAs (C16, C18) as acyl donors.
CC {ECO:0000269|PubMed:18458083}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphoethanolamine + an acyl-CoA = a
CC 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CoA;
CC Xref=Rhea:RHEA:32995, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:64381, ChEBI:CHEBI:64612; EC=2.3.1.n7;
CC Evidence={ECO:0000269|PubMed:18458083};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-(1Z-alkenyl)-sn-glycero-3-phosphoethanolamine + an acyl-
CC CoA = 1-O-(1Z-alkenyl)-2-acyl-sn-glycero-3-phosphoethanolamine + CoA;
CC Xref=Rhea:RHEA:16245, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:77288, ChEBI:CHEBI:77290; EC=2.3.1.121;
CC Evidence={ECO:0000269|PubMed:18458083};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphocholine + an acyl-CoA = a 1,2-
CC diacyl-sn-glycero-3-phosphocholine + CoA; Xref=Rhea:RHEA:12937,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168,
CC ChEBI:CHEBI:58342; EC=2.3.1.23;
CC Evidence={ECO:0000269|PubMed:18458083};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-alkyl-sn-glycero-3-phosphocholine + acetyl-CoA = a 1-O-
CC alkyl-2-acetyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:18461, ChEBI:CHEBI:30909, ChEBI:CHEBI:36707,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.67;
CC Evidence={ECO:0000269|PubMed:18458083};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phospho-L-serine + an acyl-CoA = a 1,2-
CC diacyl-sn-glycero-3-phospho-L-serine + CoA; Xref=Rhea:RHEA:33191,
CC ChEBI:CHEBI:57262, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:64379; EC=2.3.1.n6;
CC Evidence={ECO:0000269|PubMed:18458083};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphoethanolamine + octanoyl-CoA = 1-
CC acyl-2-octanoyl-sn-glycero-3-phosphoethanolamine + CoA;
CC Xref=Rhea:RHEA:37775, ChEBI:CHEBI:57287, ChEBI:CHEBI:57386,
CC ChEBI:CHEBI:64381, ChEBI:CHEBI:75263;
CC Evidence={ECO:0000269|PubMed:18458083};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37776;
CC Evidence={ECO:0000305|PubMed:18458083};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphoethanolamine + hexadecanoyl-CoA =
CC 1-acyl-2-hexadecanoyl-sn-glycero-3-phosphoethanolamine + CoA;
CC Xref=Rhea:RHEA:37767, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:64381, ChEBI:CHEBI:75265;
CC Evidence={ECO:0000269|PubMed:18458083};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37768;
CC Evidence={ECO:0000305|PubMed:18458083};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphoethanolamine + octadecanoyl-CoA =
CC 1-acyl-2-octadecanoyl-sn-glycero-3-phosphoethanolamine + CoA;
CC Xref=Rhea:RHEA:37771, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394,
CC ChEBI:CHEBI:64381, ChEBI:CHEBI:75264;
CC Evidence={ECO:0000269|PubMed:18458083};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37772;
CC Evidence={ECO:0000305|PubMed:18458083};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + a 1-acyl-sn-glycero-3-
CC phosphoethanolamine = 1-acyl-2-(9Z)-octadecenoyl-sn-glycero-3-
CC phosphoethanolamine + CoA; Xref=Rhea:RHEA:37731, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:64381, ChEBI:CHEBI:75238;
CC Evidence={ECO:0000269|PubMed:18458083};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37732;
CC Evidence={ECO:0000305|PubMed:18458083};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + a 1-acyl-sn-glycero-3-
CC phosphoethanolamine = 1-acyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-
CC glycero-3-phosphoethanolamine + CoA; Xref=Rhea:RHEA:37575,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57368, ChEBI:CHEBI:64381,
CC ChEBI:CHEBI:75067; Evidence={ECO:0000269|PubMed:18458083};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37576;
CC Evidence={ECO:0000305|PubMed:18458083};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-(1Z-alkenyl)-sn-glycero-3-phosphoethanolamine + octanoyl-
CC CoA = 1-O-(1Z)-alkenyl-2-octanoyl-sn-glycero-3-phosphoethanolamine +
CC CoA; Xref=Rhea:RHEA:37763, ChEBI:CHEBI:57287, ChEBI:CHEBI:57386,
CC ChEBI:CHEBI:77288, ChEBI:CHEBI:77301;
CC Evidence={ECO:0000269|PubMed:18458083};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37764;
CC Evidence={ECO:0000305|PubMed:18458083};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-(1Z-alkenyl)-sn-glycero-3-phosphoethanolamine +
CC hexadecanoyl-CoA = 1-O-(1Z)-alkenyl-2-hexadecanoyl-sn-glycero-3-
CC phosphoethanolamine + CoA; Xref=Rhea:RHEA:37755, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57379, ChEBI:CHEBI:77288, ChEBI:CHEBI:77303;
CC Evidence={ECO:0000269|PubMed:18458083};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37756;
CC Evidence={ECO:0000305|PubMed:18458083};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-(1Z-alkenyl)-sn-glycero-3-phosphoethanolamine +
CC octadecanoyl-CoA = 1-O-(1Z)-alkenyl-2-octadecanoyl-sn-glycero-3-
CC phosphoethanolamine + CoA; Xref=Rhea:RHEA:37759, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57394, ChEBI:CHEBI:77288, ChEBI:CHEBI:77302;
CC Evidence={ECO:0000269|PubMed:18458083};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37760;
CC Evidence={ECO:0000305|PubMed:18458083};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-O-(1Z-alkenyl)-sn-glycero-3-
CC phosphoethanolamine = 1-O-(1Z)-alkenyl-2-(9Z)-octadecenoyl-sn-
CC glycero-3-phosphoethanolamine + CoA; Xref=Rhea:RHEA:37631,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:77288,
CC ChEBI:CHEBI:77291; Evidence={ECO:0000269|PubMed:18458083};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37632;
CC Evidence={ECO:0000305|PubMed:18458083};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-O-(1Z-alkenyl)-sn-
CC glycero-3-phosphoethanolamine = 1-O-(1Z)-alkenyl-2-(5Z,8Z,11Z,14Z)-
CC eicosatetraenoyl-sn-glycero-3-phosphoethanolamine + CoA;
CC Xref=Rhea:RHEA:37635, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368,
CC ChEBI:CHEBI:77288, ChEBI:CHEBI:77295;
CC Evidence={ECO:0000269|PubMed:18458083};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37636;
CC Evidence={ECO:0000305|PubMed:18458083};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphocholine + hexadecanoyl-CoA = 1-
CC acyl-2-hexadecanoyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:37803, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:58168, ChEBI:CHEBI:75279;
CC Evidence={ECO:0000250|UniProtKB:Q6NVG1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37804;
CC Evidence={ECO:0000250|UniProtKB:Q6NVG1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + a 1-acyl-sn-glycero-3-phosphocholine =
CC 1-acyl-2-(9Z)-octadecenoyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:33359, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:58168, ChEBI:CHEBI:58293;
CC Evidence={ECO:0000269|PubMed:18458083};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33360;
CC Evidence={ECO:0000305|PubMed:18458083};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-O-hexadecyl-sn-glycero-3-
CC phosphocholine = 1-O-hexadecyl-2-(9Z)-octadecenoyl-sn-glycero-3-
CC phosphocholine + CoA; Xref=Rhea:RHEA:37783, ChEBI:CHEBI:34112,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:64496;
CC Evidence={ECO:0000269|PubMed:18458083};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37784;
CC Evidence={ECO:0000305|PubMed:18458083};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-O-hexadecyl-sn-
CC glycero-3-phosphocholine = 1-O-hexadecyl-2-(5Z,8Z,11Z,14Z)-
CC eicosatetraenoyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:37787, ChEBI:CHEBI:55430, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57368, ChEBI:CHEBI:64496;
CC Evidence={ECO:0000269|PubMed:18458083};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37788;
CC Evidence={ECO:0000305|PubMed:18458083};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-phospho-L-
CC serine = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-
CC serine + CoA; Xref=Rhea:RHEA:37531, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:75020, ChEBI:CHEBI:75029;
CC Evidence={ECO:0000269|PubMed:18458083};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37532;
CC Evidence={ECO:0000305|PubMed:18458083};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-octadecanoyl-sn-glycero-3-phospho-
CC (1'-sn-glycerol) = 1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-
CC phospho-(1'-sn-glycerol) + CoA; Xref=Rhea:RHEA:37647,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:72827,
CC ChEBI:CHEBI:72845; Evidence={ECO:0000269|PubMed:18458083};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37648;
CC Evidence={ECO:0000305|PubMed:18458083};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-octadecanoyl-sn-
CC glycero-3-phospho-(1'-sn-glycerol) = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-
CC eicosatetraenoyl)-sn-glycero-3-phospho-(1'-sn-glycerol) + CoA;
CC Xref=Rhea:RHEA:37779, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368,
CC ChEBI:CHEBI:72827, ChEBI:CHEBI:75266;
CC Evidence={ECO:0000269|PubMed:18458083};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37780;
CC Evidence={ECO:0000305|PubMed:18458083};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=80 uM for lysophosphatidylethanolamine
CC {ECO:0000269|PubMed:18458083};
CC KM=20 uM for oleoyl-CoA {ECO:0000269|PubMed:18458083};
CC Vmax=270 pmol/min/mg enzyme with lysophosphatidylethanolamine and
CC oleoyl-CoA as substrates {ECO:0000269|PubMed:18458083};
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16243729, ECO:0000269|PubMed:18458083}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:16243729,
CC ECO:0000269|PubMed:18458083}.
CC -!- TISSUE SPECIFICITY: Widely expressed with predominant level in brain.
CC {ECO:0000269|PubMed:16243729, ECO:0000269|PubMed:18458083}.
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC19156.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAC19156.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC Sequence=AAN33178.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAP97722.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY734233; AAU34184.1; -; mRNA.
DR EMBL; AF529233; AAP97722.1; ALT_FRAME; mRNA.
DR EMBL; AF542964; AAN33178.1; ALT_FRAME; mRNA.
DR EMBL; AK290273; BAF82962.1; -; mRNA.
DR EMBL; CH471125; EAW92306.1; -; Genomic_DNA.
DR EMBL; BC024892; AAH24892.2; -; mRNA.
DR EMBL; BC092463; AAH92463.1; -; mRNA.
DR EMBL; AF007155; AAC19156.1; ALT_SEQ; mRNA.
DR CCDS; CCDS32191.1; -.
DR RefSeq; NP_705841.2; NM_153613.2.
DR AlphaFoldDB; Q643R3; -.
DR SMR; Q643R3; -.
DR BioGRID; 129039; 67.
DR IntAct; Q643R3; 11.
DR STRING; 9606.ENSP00000317300; -.
DR SwissLipids; SLP:000000294; -.
DR GlyGen; Q643R3; 1 site.
DR iPTMnet; Q643R3; -.
DR MetOSite; Q643R3; -.
DR PhosphoSitePlus; Q643R3; -.
DR SwissPalm; Q643R3; -.
DR BioMuta; LPCAT4; -.
DR DMDM; 74736281; -.
DR EPD; Q643R3; -.
DR jPOST; Q643R3; -.
DR MassIVE; Q643R3; -.
DR MaxQB; Q643R3; -.
DR PaxDb; Q643R3; -.
DR PeptideAtlas; Q643R3; -.
DR PRIDE; Q643R3; -.
DR ProteomicsDB; 65914; -.
DR Antibodypedia; 22726; 65 antibodies from 22 providers.
DR DNASU; 254531; -.
DR Ensembl; ENST00000314891.11; ENSP00000317300.6; ENSG00000176454.15.
DR GeneID; 254531; -.
DR KEGG; hsa:254531; -.
DR MANE-Select; ENST00000314891.11; ENSP00000317300.6; NM_153613.3; NP_705841.2.
DR UCSC; uc001zig.4; human.
DR CTD; 254531; -.
DR DisGeNET; 254531; -.
DR GeneCards; LPCAT4; -.
DR HGNC; HGNC:30059; LPCAT4.
DR HPA; ENSG00000176454; Low tissue specificity.
DR MIM; 612039; gene.
DR neXtProt; NX_Q643R3; -.
DR OpenTargets; ENSG00000176454; -.
DR PharmGKB; PA162394297; -.
DR VEuPathDB; HostDB:ENSG00000176454; -.
DR eggNOG; KOG4666; Eukaryota.
DR GeneTree; ENSGT01030000234574; -.
DR HOGENOM; CLU_025017_1_0_1; -.
DR InParanoid; Q643R3; -.
DR OMA; PGRLLYQ; -.
DR OrthoDB; 1266853at2759; -.
DR PhylomeDB; Q643R3; -.
DR TreeFam; TF323244; -.
DR BioCyc; MetaCyc:HS16664-MON; -.
DR BRENDA; 2.3.1.23; 2681.
DR BRENDA; 2.3.1.51; 2681.
DR PathwayCommons; Q643R3; -.
DR Reactome; R-HSA-1482788; Acyl chain remodelling of PC.
DR Reactome; R-HSA-1482801; Acyl chain remodelling of PS.
DR Reactome; R-HSA-1482839; Acyl chain remodelling of PE.
DR Reactome; R-HSA-1482925; Acyl chain remodelling of PG.
DR Reactome; R-HSA-1483166; Synthesis of PA.
DR SABIO-RK; Q643R3; -.
DR SignaLink; Q643R3; -.
DR UniPathway; UPA00085; -.
DR BioGRID-ORCS; 254531; 13 hits in 1075 CRISPR screens.
DR ChiTaRS; LPCAT4; human.
DR GenomeRNAi; 254531; -.
DR Pharos; Q643R3; Tdark.
DR PRO; PR:Q643R3; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q643R3; protein.
DR Bgee; ENSG00000176454; Expressed in right hemisphere of cerebellum and 194 other tissues.
DR ExpressionAtlas; Q643R3; baseline and differential.
DR Genevisible; Q643R3; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
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:0047184; F:1-acylglycerophosphocholine O-acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0106262; F:1-acylglycerophosphoethanolamine O-acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0106263; F:1-acylglycerophosphoserine O-acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0047166; F:1-alkenylglycerophosphoethanolamine O-acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0047192; F:1-alkylglycerophosphocholine O-acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0047144; F:2-acylglycerol-3-phosphate O-acyltransferase activity; TAS:Reactome.
DR GO; GO:0071617; F:lysophospholipid acyltransferase activity; IDA:MGI.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; TAS:Reactome.
DR GO; GO:0036151; P:phosphatidylcholine acyl-chain remodeling; IDA:UniProtKB.
DR GO; GO:0036152; P:phosphatidylethanolamine acyl-chain remodeling; IDA:UniProtKB.
DR GO; GO:0036148; P:phosphatidylglycerol acyl-chain remodeling; TAS:Reactome.
DR GO; GO:0036150; P:phosphatidylserine acyl-chain remodeling; IDA:UniProtKB.
DR GO; GO:0006644; P:phospholipid metabolic process; IDA:MGI.
DR CDD; cd07991; LPLAT_LPCAT1-like; 1.
DR InterPro; IPR045252; LPCAT1-like.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR Pfam; PF01553; Acyltransferase; 1.
DR SMART; SM00563; PlsC; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Endoplasmic reticulum; Glycoprotein; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..524
FT /note="Lysophospholipid acyltransferase LPCAT4"
FT /id="PRO_0000247054"
FT TRANSMEM 40..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 489..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 129..134
FT /note="HXXXXD motif"
FT COMPBIAS 489..516
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 524 AA; 57219 MW; 3A2A12656E1241BC CRC64;
MSQGSPGDWA PLDPTPGPPA SPNPFVHELH LSRLQRVKFC LLGALLAPIR VLLAFIVLFL
LWPFAWLQVA GLSEEQLQEP ITGWRKTVCH NGVLGLSRLL FFLLGFLRIR VRGQRASRLQ
APVLVAAPHS TFFDPIVLLP CDLPKVVSRA ENLSVPVIGA LLRFNQAILV SRHDPASRRR
VVEEVRRRAT SGGKWPQVLF FPEGTCSNKK ALLKFKPGAF IAGVPVQPVL IRYPNSLDTT
SWAWRGPGVL KVLWLTASQP CSIVDVEFLP VYHPSPEESR DPTLYANNVQ RVMAQALGIP
ATECEFVGSL PVIVVGRLKV ALEPQLWELG KVLRKAGLSA GYVDAGAEPG RSRMISQEEF
ARQLQLSDPQ TVAGAFGYFQ QDTKGLVDFR DVALALAALD GGRSLEELTR LAFELFAEEQ
AEGPNRLLYK DGFSTILHLL LGSPHPAATA LHAELCQAGS SQGLSLCQFQ NFSLHDPLYG
KLFSTYLRPP HTSRGTSQTP NASSPGNPTA LANGTVQAPK QKGD
