MBOA5_HUMAN
ID MBOA5_HUMAN Reviewed; 487 AA.
AC Q6P1A2; B2RDH0; B7Z3N3; Q7KZS1; Q92980; Q9BW40;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Lysophospholipid acyltransferase 5;
DE Short=LPLAT 5;
DE EC=2.3.1.- {ECO:0000269|PubMed:18195019, ECO:0000269|PubMed:18772128, ECO:0000269|PubMed:18782225};
DE AltName: Full=1-acylglycerophosphocholine O-acyltransferase;
DE EC=2.3.1.23 {ECO:0000269|PubMed:18195019, ECO:0000269|PubMed:18772128, ECO:0000269|PubMed:18782225};
DE AltName: Full=1-acylglycerophosphoethanolamine O-acyltransferase;
DE EC=2.3.1.n7 {ECO:0000269|PubMed:18772128, ECO:0000269|PubMed:18782225};
DE AltName: Full=1-acylglycerophosphoserine O-acyltransferase;
DE EC=2.3.1.n6 {ECO:0000269|PubMed:18195019, ECO:0000269|PubMed:18772128, ECO:0000269|PubMed:18782225};
DE AltName: Full=Lysophosphatidylcholine acyltransferase;
DE Short=LPCAT;
DE Short=Lyso-PC acyltransferase;
DE AltName: Full=Lysophosphatidylcholine acyltransferase 3;
DE Short=Lyso-PC acyltransferase 3;
DE AltName: Full=Lysophosphatidylserine acyltransferase;
DE Short=LPSAT;
DE Short=Lyso-PS acyltransferase;
DE AltName: Full=Membrane-bound O-acyltransferase domain-containing protein 5;
DE Short=O-acyltransferase domain-containing protein 5;
GN Name=LPCAT3; Synonyms=MBOAT5, OACT5;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Endometrium;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4] {ECO:0000312|EMBL:AAH65194.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon {ECO:0000312|EMBL:AAH00664.2}, and
RC Pancreas {ECO:0000312|EMBL:AAH65194.1};
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 [5] {ECO:0000305, ECO:0000312|EMBL:AAC51640.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 50-487 (ISOFORM 1).
RX PubMed=9074930; DOI=10.1101/gr.7.3.268;
RA Ansari-Lari M.A., Shen Y., Muzny D.M., Lee W., Gibbs R.A.;
RT "Large-scale sequencing in human chromosome 12p13: experimental and
RT computational gene structure determination.";
RL Genome Res. 7:268-280(1997).
RN [6] {ECO:0000305, ECO:0000312|EMBL:AAP35646.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 107-487 (ISOFORM 1/2).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=18782225; DOI=10.1111/j.1365-2443.2008.01212.x;
RA Matsuda S., Inoue T., Lee H.C., Kono N., Tanaka F., Gengyo-Ando K.,
RA Mitani S., Arai H.;
RT "Member of the membrane-bound O-acyltransferase (MBOAT) family encodes a
RT lysophospholipid acyltransferase with broad substrate specificity.";
RL Genes Cells 13:879-888(2008).
RN [8]
RP IDENTIFICATION, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND TISSUE SPECIFICITY.
RX PubMed=18195019; DOI=10.1074/jbc.m710422200;
RA Zhao Y., Chen Y.Q., Bonacci T.M., Bredt D.S., Li S., Bensch W.R.,
RA Moller D.E., Kowala M., Konrad R.J., Cao G.;
RT "Identification and characterization of a major liver
RT lysophosphatidylcholine acyltransferase.";
RL J. Biol. Chem. 283:8258-8265(2008).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, TISSUE SPECIFICITY, AND
RP SUBSTRATE SPECIFICITY.
RX PubMed=18772128; DOI=10.1074/jbc.m806194200;
RA Gijon M.A., Riekhof W.R., Zarini S., Murphy R.C., Voelker D.R.;
RT "Lysophospholipid acyltransferases and arachidonate recycling in human
RT neutrophils.";
RL J. Biol. Chem. 283:30235-30245(2008).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Lysophospholipid O-acyltransferase (LPLAT) that catalyzes the
CC reacylation step of the phospholipid remodeling process also known as
CC the Lands cycle (PubMed:18782225, PubMed:18195019, PubMed:18772128).
CC Catalyzes transfer of the fatty acyl chain from fatty acyl-CoA to 1-
CC acyl lysophospholipid to form various classes of phospholipids.
CC Converts 1-acyl lysophosphatidylcholine (LPC) into phosphatidylcholine
CC (PC) (LPCAT activity), 1-acyl lysophosphatidylserine (LPS) into
CC phosphatidylserine (PS) (LPSAT activity) and 1-acyl
CC lysophosphatidylethanolamine (LPE) into phosphatidylethanolamine (PE)
CC (LPEAT activity) (PubMed:18782225, PubMed:18195019, PubMed:18772128).
CC Favors polyunsaturated fatty acyl-CoAs as acyl donors compared to
CC saturated fatty acyl-CoAs (PubMed:18195019, PubMed:18772128). Has
CC higher activity for LPC acyl acceptors compared to LPEs and LPSs. Can
CC also transfer the fatty acyl chain from fatty acyl-CoA to 1-O-alkyl
CC lysophospholipid or 1-O-alkenyl lysophospholipid with lower efficiency
CC (By similarity). Acts as a major LPC O-acyltransferase in liver and
CC intestine. As a component of the liver X receptor/NR1H3 or NR1H2
CC signaling pathway, mainly catalyzes the incorporation of arachidonate
CC into PCs of endoplasmic reticulum (ER) membranes, increasing membrane
CC dynamics and enabling triacylglycerols transfer to nascent very low-
CC density lipoprotein (VLDL) particles. Promotes processing of sterol
CC regulatory protein SREBF1 in hepatocytes, likely by facilitating the
CC translocation of SREBF1-SCAP complex from ER to the Golgi apparatus (By
CC similarity). Participates in mechanisms by which the liver X
CC receptor/NR1H3 or NR1H2 signaling pathway counteracts lipid-induced ER
CC stress response and inflammation. Down-regulates hepatic inflammation
CC by limiting arachidonic acid availability for synthesis of inflammatory
CC eicosanoids, such as prostaglandins (By similarity). In enterocytes,
CC acts as a component of a gut-brain feedback loop that coordinates
CC dietary lipid absorption and food intake. Regulates the abundance of
CC PCs containing linoleate and arachidonate in enterocyte membranes,
CC enabling passive diffusion of fatty acids and cholesterol across the
CC membrane for efficient chylomicron assembly (By similarity). In the
CC intestinal crypt, acts as a component of dietary-responsive
CC phospholipid-cholesterol axis, regulating the biosynthesis of
CC cholesterol and its mitogenic effects on intestinal stem cells (By
CC similarity). {ECO:0000250|UniProtKB:Q91V01,
CC ECO:0000269|PubMed:18195019, ECO:0000269|PubMed:18772128,
CC ECO:0000269|PubMed:18782225}.
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:18195019, ECO:0000269|PubMed:18772128,
CC ECO:0000269|PubMed:18782225};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12938;
CC Evidence={ECO:0000305|PubMed:18195019, ECO:0000305|PubMed:18772128,
CC ECO:0000305|PubMed:18782225};
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:18772128, ECO:0000269|PubMed:18782225};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32996;
CC Evidence={ECO:0000305|PubMed:18772128, ECO:0000305|PubMed:18782225};
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:18195019, ECO:0000269|PubMed:18772128,
CC ECO:0000269|PubMed:18782225};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33192;
CC Evidence={ECO:0000305|PubMed:18195019, ECO:0000305|PubMed:18772128,
CC ECO:0000305|PubMed:18782225};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + a 1-acyl-sn-glycero-3-
CC phosphocholine = 1-acyl-2-(9Z,12Z)-octadecadienoyl-sn-glycero-3-
CC phosphocholine + CoA; Xref=Rhea:RHEA:37563, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57383, ChEBI:CHEBI:58168, ChEBI:CHEBI:60000;
CC Evidence={ECO:0000269|PubMed:18782225};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37564;
CC Evidence={ECO:0000305|PubMed:18782225};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + a 1-acyl-sn-glycero-3-
CC phosphocholine = 1-acyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-
CC glycero-3-phosphocholine + CoA; Xref=Rhea:RHEA:37559,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57368, ChEBI:CHEBI:58168,
CC ChEBI:CHEBI:75063; Evidence={ECO:0000269|PubMed:18782225};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37560;
CC Evidence={ECO:0000305|PubMed:18782225};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + dodecanoyl-CoA =
CC 1-hexadecanoyl-2-dodecanoyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:37515, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:75018;
CC Evidence={ECO:0000269|PubMed:18195019};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37516;
CC Evidence={ECO:0000305|PubMed:18195019};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + octadecanoyl-CoA
CC = 1-hexadecanoyl-2-octadecanoyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:35987, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:73000;
CC Evidence={ECO:0000269|PubMed:18195019};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35988;
CC Evidence={ECO:0000305|PubMed:18195019};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-dodecanoyl-sn-glycero-3-phosphocholine + hexadecanoyl-CoA =
CC 1-dodecanoyl-2-hexadecanoyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:37511, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:74966, ChEBI:CHEBI:75017;
CC Evidence={ECO:0000269|PubMed:18195019};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37512;
CC Evidence={ECO:0000305|PubMed:18195019};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-tetradecanoyl-sn-glycero-3-phosphocholine + hexadecanoyl-CoA
CC = 1-tetradecanoyl-2-hexadecanoyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:37655, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:64489, ChEBI:CHEBI:75062;
CC Evidence={ECO:0000269|PubMed:18195019};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37656;
CC Evidence={ECO:0000305|PubMed:18195019};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + hexadecanoyl-CoA
CC = 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:35983, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:72999;
CC Evidence={ECO:0000269|PubMed:18195019};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35984;
CC Evidence={ECO:0000305|PubMed:18195019};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-sn-glycero-3-phosphocholine + hexadecanoyl-CoA
CC = 1-octadecanoyl-2-hexadecanoyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:37527, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:73858, ChEBI:CHEBI:75026;
CC Evidence={ECO:0000269|PubMed:18195019};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37528;
CC Evidence={ECO:0000305|PubMed:18195019};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine +
CC hexadecanoyl-CoA = 1-(9Z-octadecenoyl)-2-hexadecanoyl-sn-glycero-3-
CC phosphocholine + CoA; Xref=Rhea:RHEA:37383, ChEBI:CHEBI:28610,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:74667;
CC Evidence={ECO:0000269|PubMed:18195019, ECO:0000269|PubMed:18772128};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37384;
CC Evidence={ECO:0000305|PubMed:18195019, ECO:0000305|PubMed:18772128};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-hexadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-
CC phosphocholine = 1-hexadecanoyl-2-(9Z-hexadecenoyl)-sn-glycero-3-
CC phosphocholine + CoA; Xref=Rhea:RHEA:37207, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:61540, ChEBI:CHEBI:72998, ChEBI:CHEBI:74000;
CC Evidence={ECO:0000269|PubMed:18772128};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37208;
CC Evidence={ECO:0000305|PubMed:18772128};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-
CC phosphocholine = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphocholine + CoA; Xref=Rhea:RHEA:35991, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:72998, ChEBI:CHEBI:73001;
CC Evidence={ECO:0000269|PubMed:18195019, ECO:0000269|PubMed:18772128};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35992;
CC Evidence={ECO:0000305|PubMed:18195019, ECO:0000305|PubMed:18772128};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + 1-hexadecanoyl-sn-glycero-3-
CC phosphocholine = 1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-
CC glycero-3-phosphocholine + CoA; Xref=Rhea:RHEA:35995,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57383, ChEBI:CHEBI:72998,
CC ChEBI:CHEBI:73002; Evidence={ECO:0000269|PubMed:18195019,
CC ECO:0000269|PubMed:18772128};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35996;
CC Evidence={ECO:0000305|PubMed:18195019, ECO:0000305|PubMed:18772128};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-dodecanoyl-sn-
CC glycero-3-phosphocholine = 1-dodecanoyl-2-(5Z,8Z,11Z,14Z)-
CC eicosatetraenoyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:37483, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368,
CC ChEBI:CHEBI:74966, ChEBI:CHEBI:74967;
CC Evidence={ECO:0000250|UniProtKB:Q91V01};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37484;
CC Evidence={ECO:0000250|UniProtKB:Q91V01};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-hexadecanoyl-sn-
CC glycero-3-phosphocholine = 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-
CC eicosatetraenoyl)-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:35999, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:73003;
CC Evidence={ECO:0000269|PubMed:18195019, ECO:0000269|PubMed:18772128};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36000;
CC Evidence={ECO:0000305|PubMed:18195019, ECO:0000305|PubMed:18772128};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-octadecanoyl-sn-
CC glycero-3-phosphocholine = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-
CC eicosatetraenoyl)-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:37479, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368,
CC ChEBI:CHEBI:73858, ChEBI:CHEBI:74965;
CC Evidence={ECO:0000250|UniProtKB:Q91V01};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37480;
CC Evidence={ECO:0000250|UniProtKB:Q91V01};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-eicosanoyl-sn-
CC glycero-3-phosphocholine = 1-eicosanoyl-2-(5Z,8Z,11Z,14Z)-
CC eicosatetraenoyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:37487, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368,
CC ChEBI:CHEBI:74968, ChEBI:CHEBI:74970;
CC Evidence={ECO:0000250|UniProtKB:Q91V01};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37488;
CC Evidence={ECO:0000250|UniProtKB:Q91V01};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphocholine = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine
CC + CoA; Xref=Rhea:RHEA:37387, ChEBI:CHEBI:28610, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:74669;
CC Evidence={ECO:0000269|PubMed:18772128};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37388;
CC Evidence={ECO:0000305|PubMed:18772128};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-
CC 3-phosphocholine = 1-(9Z)-octadecenoyl-2-(9Z,12Z)-octadecadienoyl-sn-
CC glycero-3-phosphocholine + CoA; Xref=Rhea:RHEA:37391,
CC ChEBI:CHEBI:28610, ChEBI:CHEBI:57287, ChEBI:CHEBI:57383,
CC ChEBI:CHEBI:74670; Evidence={ECO:0000269|PubMed:18772128};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37392;
CC Evidence={ECO:0000305|PubMed:18772128};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-(9Z-octadecenoyl)-sn-
CC glycero-3-phosphocholine = 1-(9Z)-octadecenoyl-2-(5Z,8Z,11Z,14Z)-
CC icosatetraenoyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:37395, ChEBI:CHEBI:28610, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57368, ChEBI:CHEBI:74671;
CC Evidence={ECO:0000269|PubMed:18772128};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37396;
CC Evidence={ECO:0000305|PubMed:18772128};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + a 1-acyl-sn-glycero-3-
CC phosphoethanolamine = 1-acyl-2-(9Z,12Z)-octadecadienoyl-sn-glycero-3-
CC phosphoethanolamine + CoA; Xref=Rhea:RHEA:37579, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57383, ChEBI:CHEBI:64381, ChEBI:CHEBI:75069;
CC Evidence={ECO:0000269|PubMed:18782225};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37580;
CC Evidence={ECO:0000305|PubMed:18782225};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-
CC 3-phosphoethanolamine = 1-(9Z)-octadecenoyl-2-(9Z,12Z)-
CC octadecadienoyl-sn-glycero-3-phosphoethanolamine + CoA;
CC Xref=Rhea:RHEA:37503, ChEBI:CHEBI:57287, ChEBI:CHEBI:57383,
CC ChEBI:CHEBI:74971, ChEBI:CHEBI:74977;
CC Evidence={ECO:0000250|UniProtKB:Q91V01};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37504;
CC Evidence={ECO:0000250|UniProtKB:Q91V01};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + 1-(10Z-heptadecenoyl)-sn-
CC glycero-3-phosphoethanolamine = 1-(10Z-heptadecenoyl)-2-(9Z,12Z-
CC octadecadienoyl)-sn-glycero-3-phosphoethanolamine + CoA;
CC Xref=Rhea:RHEA:64228, ChEBI:CHEBI:57287, ChEBI:CHEBI:57383,
CC ChEBI:CHEBI:149768, ChEBI:CHEBI:149770;
CC Evidence={ECO:0000250|UniProtKB:Q91V01};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64229;
CC Evidence={ECO:0000250|UniProtKB:Q91V01};
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:18782225};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37576;
CC Evidence={ECO:0000305|PubMed:18782225};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-hexadecanoyl-sn-
CC glycero-3-phosphoethanolamine = 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-
CC eicosatetraenoyl)-sn-glycero-3-phosphoethanolamine + CoA;
CC Xref=Rhea:RHEA:36023, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368,
CC ChEBI:CHEBI:73004, ChEBI:CHEBI:73009;
CC Evidence={ECO:0000269|PubMed:18772128};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36024;
CC Evidence={ECO:0000305|PubMed:18772128};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-(9Z-octadecenoyl)-sn-
CC glycero-3-phosphoethanolamine = 1-(9Z)-octadecenoyl-2-
CC (5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphoethanolamine +
CC CoA; Xref=Rhea:RHEA:37495, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368,
CC ChEBI:CHEBI:74971, ChEBI:CHEBI:74975;
CC Evidence={ECO:0000250|UniProtKB:Q91V01};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37496;
CC Evidence={ECO:0000250|UniProtKB:Q91V01};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-(10Z-heptadecenoyl)-
CC sn-glycero-3-phosphoethanolamine = 1-(10Z-heptadecenoyl)-2-
CC (5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphoethanolamine +
CC CoA; Xref=Rhea:RHEA:64204, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368,
CC ChEBI:CHEBI:149768, ChEBI:CHEBI:149769;
CC Evidence={ECO:0000250|UniProtKB:Q91V01};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64205;
CC Evidence={ECO:0000250|UniProtKB:Q91V01};
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:0000250|UniProtKB:Q91V01};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37636;
CC Evidence={ECO:0000250|UniProtKB:Q91V01};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + a 1-acyl-sn-glycero-3-phospho-
CC L-serine = 1-acyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phospho-L-
CC serine + CoA; Xref=Rhea:RHEA:37567, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57383, ChEBI:CHEBI:64379, ChEBI:CHEBI:75066;
CC Evidence={ECO:0000269|PubMed:18782225};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37568;
CC Evidence={ECO:0000305|PubMed:18782225};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + a 1-acyl-sn-glycero-3-
CC phospho-L-serine = 1-acyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-
CC glycero-3-phospho-L-serine + CoA; Xref=Rhea:RHEA:37571,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57368, ChEBI:CHEBI:64379,
CC ChEBI:CHEBI:75065; Evidence={ECO:0000269|PubMed:18782225};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37572;
CC Evidence={ECO:0000305|PubMed:18782225};
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:18195019};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37532;
CC Evidence={ECO:0000305|PubMed:18195019};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-
CC phospho-L-serine = 1,2-di-(9Z)-octadecenoyl-sn-glycero-3-phospho-L-
CC serine + CoA; Xref=Rhea:RHEA:37407, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:74617, ChEBI:CHEBI:74905;
CC Evidence={ECO:0000250|UniProtKB:Q91V01};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37408;
CC Evidence={ECO:0000250|UniProtKB:Q91V01};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + 1-hexadecanoyl-sn-glycero-3-
CC phospho-L-serine = 1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-
CC glycero-3-phospho-L-serine + CoA; Xref=Rhea:RHEA:37535,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57383, ChEBI:CHEBI:75020,
CC ChEBI:CHEBI:75031; Evidence={ECO:0000269|PubMed:18195019};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37536;
CC Evidence={ECO:0000305|PubMed:18195019};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-
CC 3-phospho-L-serine = 1-(9Z-octadecenoyl)-2-(9Z,12Z-octadienoyl)-sn-
CC glycero-3-phospho-L-serine + CoA; Xref=Rhea:RHEA:37375,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57383, ChEBI:CHEBI:74617,
CC ChEBI:CHEBI:74892; Evidence={ECO:0000269|PubMed:18772128};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37376;
CC Evidence={ECO:0000305|PubMed:18772128};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-hexadecanoyl-sn-
CC glycero-3-phospho-L-serine = 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-
CC eicosatetraenoyl)-sn-glycero-3-phospho-L-serine + CoA;
CC Xref=Rhea:RHEA:37539, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368,
CC ChEBI:CHEBI:75020, ChEBI:CHEBI:75032;
CC Evidence={ECO:0000269|PubMed:18195019};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37540;
CC Evidence={ECO:0000305|PubMed:18195019};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-(9Z-octadecenoyl)-sn-
CC glycero-3-phospho-L-serine = 1-(9Z-octadecenoyl)-2-(5Z,8Z,11Z,14Z-
CC eicosatetraenoyl)-sn-glycero-3-phospho-L-serine + CoA;
CC Xref=Rhea:RHEA:37379, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368,
CC ChEBI:CHEBI:74617, ChEBI:CHEBI:74897;
CC Evidence={ECO:0000269|PubMed:18772128};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37380;
CC Evidence={ECO:0000305|PubMed:18772128};
CC -!- ACTIVITY REGULATION: Activity is inhibited by thimerosal.
CC {ECO:0000269|PubMed:18772128}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=41.29 uM for palmitoyl-CoA {ECO:0000269|PubMed:18195019};
CC KM=36.65 uM for stearoyl-CoA {ECO:0000269|PubMed:18195019};
CC KM=72.68 uM for oleoyl-CoA {ECO:0000269|PubMed:18195019};
CC KM=201.4 uM for linoleoyl-CoA {ECO:0000269|PubMed:18195019};
CC KM=71.56 uM for arachidonoyl-CoA {ECO:0000269|PubMed:18195019};
CC KM=72.19 uM for 1-palmitoyl-lysophosphatidylcholine
CC {ECO:0000269|PubMed:18195019};
CC Vmax=1782 nmol/min/mg enzyme with palmitoyl-CoA and 1-palmitoyl-
CC lysophosphatidylcholine as substrates {ECO:0000269|PubMed:18195019};
CC Vmax=996 nmol/min/mg enzyme with stearoyl-CoA and 1-palmitoyl-
CC lysophosphatidylcholine as substrates {ECO:0000269|PubMed:18195019};
CC Vmax=4698 nmol/min/mg enzyme with oleoyl-CoA and 1-palmitoyl-
CC lysophosphatidylcholine as substrates {ECO:0000269|PubMed:18195019};
CC Vmax=18148 nmol/min/mg enzyme with linoleoyl-CoA and 1-palmitoyl-
CC lysophosphatidylcholine as substrates {ECO:0000269|PubMed:18195019};
CC Vmax=6247 nmol/min/mg enzyme with arachidonoyl-CoA and 1-palmitoyl-
CC lysophosphatidylcholine as substrates {ECO:0000269|PubMed:18195019};
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC {ECO:0000269|PubMed:18195019}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:18195019}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6P1A2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6P1A2-2; Sequence=VSP_053680;
CC -!- TISSUE SPECIFICITY: Highly expressed in liver, pancreas and adipose
CC tissue. Very low expression in skeletal muscle and heart. Detected in
CC neutrophils. {ECO:0000269|PubMed:18195019,
CC ECO:0000269|PubMed:18772128}.
CC -!- DOMAIN: The di-lysine motif confers endoplasmic reticulum localization.
CC -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB51326.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAC51640.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAG37917.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BX648009; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK296145; BAH12269.1; -; mRNA.
DR EMBL; AK315538; BAG37917.1; ALT_INIT; mRNA.
DR EMBL; AC006512; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000664; AAH00664.2; -; mRNA.
DR EMBL; BC065194; AAH65194.1; -; mRNA.
DR EMBL; U47924; AAB51326.1; ALT_INIT; Genomic_DNA.
DR EMBL; U72515; AAC51640.1; ALT_INIT; mRNA.
DR EMBL; BT007000; AAP35646.1; -; mRNA.
DR CCDS; CCDS8572.1; -. [Q6P1A2-1]
DR RefSeq; NP_005759.4; NM_005768.5. [Q6P1A2-1]
DR AlphaFoldDB; Q6P1A2; -.
DR SMR; Q6P1A2; -.
DR BioGRID; 115464; 81.
DR IntAct; Q6P1A2; 24.
DR MINT; Q6P1A2; -.
DR STRING; 9606.ENSP00000261407; -.
DR SwissLipids; SLP:000000127; -.
DR iPTMnet; Q6P1A2; -.
DR PhosphoSitePlus; Q6P1A2; -.
DR SwissPalm; Q6P1A2; -.
DR BioMuta; LPCAT3; -.
DR DMDM; 74737127; -.
DR EPD; Q6P1A2; -.
DR jPOST; Q6P1A2; -.
DR MassIVE; Q6P1A2; -.
DR MaxQB; Q6P1A2; -.
DR PaxDb; Q6P1A2; -.
DR PeptideAtlas; Q6P1A2; -.
DR PRIDE; Q6P1A2; -.
DR ProteomicsDB; 6534; -.
DR ProteomicsDB; 66828; -. [Q6P1A2-1]
DR Antibodypedia; 67641; 75 antibodies from 11 providers.
DR DNASU; 10162; -.
DR Ensembl; ENST00000261407.9; ENSP00000261407.4; ENSG00000111684.11. [Q6P1A2-1]
DR GeneID; 10162; -.
DR KEGG; hsa:10162; -.
DR MANE-Select; ENST00000261407.9; ENSP00000261407.4; NM_005768.6; NP_005759.4.
DR UCSC; uc001qsi.4; human. [Q6P1A2-1]
DR CTD; 10162; -.
DR DisGeNET; 10162; -.
DR GeneCards; LPCAT3; -.
DR HGNC; HGNC:30244; LPCAT3.
DR HPA; ENSG00000111684; Low tissue specificity.
DR MIM; 611950; gene.
DR neXtProt; NX_Q6P1A2; -.
DR OpenTargets; ENSG00000111684; -.
DR PharmGKB; PA162394266; -.
DR VEuPathDB; HostDB:ENSG00000111684; -.
DR eggNOG; KOG2705; Eukaryota.
DR GeneTree; ENSGT01030000234564; -.
DR HOGENOM; CLU_011340_6_1_1; -.
DR InParanoid; Q6P1A2; -.
DR OMA; CILVLRM; -.
DR OrthoDB; 881262at2759; -.
DR PhylomeDB; Q6P1A2; -.
DR TreeFam; TF106143; -.
DR BRENDA; 2.3.1.23; 2681.
DR PathwayCommons; Q6P1A2; -.
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 SABIO-RK; Q6P1A2; -.
DR SignaLink; Q6P1A2; -.
DR UniPathway; UPA00085; -.
DR BioGRID-ORCS; 10162; 53 hits in 1086 CRISPR screens.
DR ChiTaRS; LPCAT3; human.
DR GeneWiki; MBOAT5; -.
DR GenomeRNAi; 10162; -.
DR Pharos; Q6P1A2; Tbio.
DR PRO; PR:Q6P1A2; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q6P1A2; protein.
DR Bgee; ENSG00000111684; Expressed in right lobe of liver and 170 other tissues.
DR ExpressionAtlas; Q6P1A2; baseline and differential.
DR Genevisible; Q6P1A2; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA: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: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:0047144; F:2-acylglycerol-3-phosphate O-acyltransferase activity; TAS:Reactome.
DR GO; GO:0016746; F:acyltransferase activity; IBA:GO_Central.
DR GO; GO:0071617; F:lysophospholipid acyltransferase activity; IBA:GO_Central.
DR GO; GO:0034378; P:chylomicron assembly; ISS:UniProtKB.
DR GO; GO:0090158; P:endoplasmic reticulum membrane organization; ISS:UniProtKB.
DR GO; GO:0036335; P:intestinal stem cell homeostasis; ISS:UniProtKB.
DR GO; GO:0030258; P:lipid modification; IBA:GO_Central.
DR GO; GO:0050728; P:negative regulation of inflammatory response; ISS:UniProtKB.
DR GO; GO:1903573; P:negative regulation of response to endoplasmic reticulum stress; ISS:UniProtKB.
DR GO; GO:0036151; P:phosphatidylcholine acyl-chain remodeling; IDA:UniProtKB.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IBA:GO_Central.
DR GO; GO:0036152; P:phosphatidylethanolamine acyl-chain remodeling; IDA:UniProtKB.
DR GO; GO:0036150; P:phosphatidylserine acyl-chain remodeling; IDA:UniProtKB.
DR GO; GO:0045797; P:positive regulation of intestinal cholesterol absorption; ISS:UniProtKB.
DR GO; GO:1901310; P:positive regulation of sterol regulatory element binding protein cleavage; ISS:UniProtKB.
DR GO; GO:1905885; P:positive regulation of triglyceride transport; ISS:UniProtKB.
DR GO; GO:0045540; P:regulation of cholesterol biosynthetic process; ISS:UniProtKB.
DR GO; GO:0034379; P:very-low-density lipoprotein particle assembly; ISS:UniProtKB.
DR InterPro; IPR004299; MBOAT_fam.
DR Pfam; PF03062; MBOAT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Acyltransferase; Alternative splicing; Endoplasmic reticulum;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:25944712"
FT CHAIN 2..487
FT /note="Lysophospholipid acyltransferase 5"
FT /id="PRO_0000233382"
FT TRANSMEM 44..64
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 285..305
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 364..384
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 422..442
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 453..473
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 484..487
FT /note="Di-lysine motif"
FT ACT_SITE 338
FT /evidence="ECO:0000250"
FT ACT_SITE 374
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:25944712"
FT VAR_SEQ 21..100
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_053680"
FT VARIANT 63
FT /note="F -> L (in dbSNP:rs34196984)"
FT /id="VAR_050027"
FT VARIANT 217
FT /note="I -> T (in dbSNP:rs1984564)"
FT /id="VAR_050028"
FT CONFLICT 387
FT /note="E -> K (in Ref. 4; AAH00664 and 6; AAP35646)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 487 AA; 56035 MW; 429258B54585B4A7 CRC64;
MASSAEGDEG TVVALAGVLQ SGFQELSLNK LATSLGASEQ ALRLIISIFL GYPFALFYRH
YLFYKETYLI HLFHTFTGLS IAYFNFGNQL YHSLLCIVLQ FLILRLMGRT ITAVLTTFCF
QMAYLLAGYY YTATGNYDIK WTMPHCVLTL KLIGLAVDYF DGGKDQNSLS SEQQKYAIRG
VPSLLEVAGF SYFYGAFLVG PQFSMNHYMK LVQGELIDIP GKIPNSIIPA LKRLSLGLFY
LVGYTLLSPH ITEDYLLTED YDNHPFWFRC MYMLIWGKFV LYKYVTCWLV TEGVCILTGL
GFNGFEEKGK AKWDACANMK VWLFETNPRF TGTIASFNIN TNAWVARYIF KRLKFLGNKE
LSQGLSLLFL ALWHGLHSGY LVCFQMEFLI VIVERQAARL IQESPTLSKL AAITVLQPFY
YLVQQTIHWL FMGYSMTAFC LFTWDKWLKV YKSIYFLGHI FFLSLLFILP YIHKAMVPRK
EKLKKME
