PLCE_HUMAN
ID PLCE_HUMAN Reviewed; 364 AA.
AC Q9NUQ2; Q8IZ47; Q9BQG4;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2003, sequence version 3.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase epsilon;
DE EC=2.3.1.51 {ECO:0000269|PubMed:21173190};
DE AltName: Full=1-acylglycerol-3-phosphate O-acyltransferase 5;
DE Short=1-AGP acyltransferase 5;
DE Short=1-AGPAT 5;
DE AltName: Full=Lysophosphatidic acid acyltransferase epsilon;
DE Short=LPAAT-epsilon;
GN Name=AGPAT5;
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].
RA Leung D.W.;
RT "Cloning and expression of LPAAT-epsilon.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Amygdala;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Lung;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-364.
RC TISSUE=Placenta;
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 [5]
RP TISSUE SPECIFICITY.
RX PubMed=16620771; DOI=10.1016/j.abb.2006.03.014;
RA Agarwal A.K., Barnes R.I., Garg A.;
RT "Functional characterization of human 1-acylglycerol-3-phosphate
RT acyltransferase isoform 8: cloning, tissue distribution, gene structure,
RT and enzymatic activity.";
RL Arch. Biochem. Biophys. 449:64-76(2006).
RN [6]
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).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=21173190; DOI=10.1194/jlr.m007575;
RA Prasad S.S., Garg A., Agarwal A.K.;
RT "Enzymatic activities of the human AGPAT isoform 3 and isoform 5:
RT localization of AGPAT5 to mitochondria.";
RL J. Lipid Res. 52:451-462(2011).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [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: Converts 1-acyl-sn-glycerol-3-phosphate (lysophosphatidic
CC acid or LPA) into 1,2-diacyl-sn-glycerol-3-phosphate (phosphatidic acid
CC or PA) by incorporating an acyl moiety at the sn-2 position of the
CC glycerol backbone (PubMed:21173190). Acts on LPA containing saturated
CC or unsaturated fatty acids C15:0-C20:4 at the sn-1 position using
CC C18:1-CoA as the acyl donor (PubMed:21173190). Also acts on
CC lysophosphatidylethanolamine using oleoyl-CoA, but not arachidonoyl-
CC CoA, and lysophosphatidylinositol using arachidonoyl-CoA, but not
CC oleoyl-CoA (PubMed:21173190). Activity toward lysophosphatidylglycerol
CC not detectable (PubMed:21173190). {ECO:0000269|PubMed:21173190}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-
CC sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:19709,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:58608; EC=2.3.1.51;
CC Evidence={ECO:0000269|PubMed:21173190};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19710;
CC Evidence={ECO:0000305|PubMed:21173190};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + tetradecanoyl-CoA
CC = 1-(9Z)-octadecenoyl-2-tetradecanoyl-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37171, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385,
CC ChEBI:CHEBI:74544, ChEBI:CHEBI:74579;
CC Evidence={ECO:0000269|PubMed:21173190};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37172;
CC Evidence={ECO:0000305|PubMed:21173190};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + pentadecanoyl-CoA
CC = 1-(9Z)-octadecenoyl-2-pentadecanoyl-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37175, ChEBI:CHEBI:57287, ChEBI:CHEBI:74309,
CC ChEBI:CHEBI:74544, ChEBI:CHEBI:74578;
CC Evidence={ECO:0000269|PubMed:21173190};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37176;
CC Evidence={ECO:0000305|PubMed:21173190};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + octadecanoyl-CoA
CC = 1-(9Z-octadecenoyl)-2-octadecanoyl-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37147, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394,
CC ChEBI:CHEBI:74544, ChEBI:CHEBI:74552;
CC Evidence={ECO:0000269|PubMed:21173190};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37148;
CC Evidence={ECO:0000305|PubMed:21173190};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + nonadecanoyl-CoA
CC = 1-(9Z)-octadecenoyl-2-nonadecanoyl-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37595, ChEBI:CHEBI:57287, ChEBI:CHEBI:74544,
CC ChEBI:CHEBI:75104, ChEBI:CHEBI:75105;
CC Evidence={ECO:0000269|PubMed:21173190};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37596;
CC Evidence={ECO:0000305|PubMed:21173190};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine + CoA; Xref=Rhea:RHEA:37499, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:74971, ChEBI:CHEBI:74986;
CC Evidence={ECO:0000269|PubMed:21173190};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37500;
CC Evidence={ECO:0000305|PubMed:21173190};
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:21173190};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37388;
CC Evidence={ECO:0000305|PubMed:21173190};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-(9Z-octadecenoyl)-sn-
CC glycero-3-phospho-(1D-myo-inositol) = 1-(9Z-octadecenoyl)-2-
CC (5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phospho-1D-myo-inositol
CC + CoA; Xref=Rhea:RHEA:42216, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368,
CC ChEBI:CHEBI:78762, ChEBI:CHEBI:78765;
CC Evidence={ECO:0000269|PubMed:21173190};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42217;
CC Evidence={ECO:0000305|PubMed:21173190};
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:0000269|PubMed:21173190};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37408;
CC Evidence={ECO:0000305|PubMed:21173190};
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:21173190};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37380;
CC Evidence={ECO:0000305|PubMed:21173190};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-phosphate
CC = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:33187, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:57518, ChEBI:CHEBI:64839;
CC Evidence={ECO:0000269|PubMed:21173190};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33188;
CC Evidence={ECO:0000305|PubMed:21173190};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-heptadecanoyl-sn-glycero-3-phosphate
CC = 1-heptadecanoyl-2-(9Z)-octadecenoyl-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37151, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:74554, ChEBI:CHEBI:74556;
CC Evidence={ECO:0000269|PubMed:21173190};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37152;
CC Evidence={ECO:0000305|PubMed:21173190};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-
CC glycero-3-phosphate = 1-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-2-(9Z)-
CC octadecenoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37455,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:74938,
CC ChEBI:CHEBI:74941; Evidence={ECO:0000269|PubMed:21173190};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37456;
CC Evidence={ECO:0000305|PubMed:21173190};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-octadecanoyl-sn-glycero-3-phosphate
CC = 1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37163, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:74560, ChEBI:CHEBI:74565;
CC Evidence={ECO:0000269|PubMed:21173190};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37164;
CC Evidence={ECO:0000305|PubMed:21173190};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-(9Z-octadecenoyl)-sn-
CC glycero-3-phosphate = 1-(9Z)-octadecenoyl-2-(5Z,8Z,11Z,14Z)-
CC eicosatetraenoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37443,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57368, ChEBI:CHEBI:74544,
CC ChEBI:CHEBI:74928; Evidence={ECO:0000269|PubMed:21173190};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37444;
CC Evidence={ECO:0000305|PubMed:21173190};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + heptadecanoyl-CoA
CC = 1-(9Z)-octadecenoyl-2-heptadecanoyl-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37155, ChEBI:CHEBI:57287, ChEBI:CHEBI:74307,
CC ChEBI:CHEBI:74544, ChEBI:CHEBI:74558;
CC Evidence={ECO:0000269|PubMed:21173190};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37156;
CC Evidence={ECO:0000305|PubMed:21173190};
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:21173190};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37396;
CC Evidence={ECO:0000305|PubMed:21173190};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphate = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37131, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:74544, ChEBI:CHEBI:74546;
CC Evidence={ECO:0000269|PubMed:21173190};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37132;
CC Evidence={ECO:0000305|PubMed:21173190};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + hexadecanoyl-CoA
CC = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:42592, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:64839, ChEBI:CHEBI:74544;
CC Evidence={ECO:0000269|PubMed:21173190};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42593;
CC Evidence={ECO:0000305|PubMed:21173190};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.52 uM for LPA sn-1 C18:1 {ECO:0000269|PubMed:21173190};
CC KM=16.30 uM for C18:1-CoA {ECO:0000269|PubMed:21173190};
CC Vmax=2.42 nmol/min/mg enzyme toward LPA sn-1 C18:1
CC {ECO:0000269|PubMed:21173190};
CC Vmax=1.22 nmol/min/mg enzyme toward C18:1-CoA
CC {ECO:0000269|PubMed:21173190};
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
CC -!- INTERACTION:
CC Q9NUQ2; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-6916385, EBI-6942903;
CC Q9NUQ2; Q8NBI2: CYB561A3; NbExp=3; IntAct=EBI-6916385, EBI-10269179;
CC Q9NUQ2; Q9NY72: SCN3B; NbExp=3; IntAct=EBI-6916385, EBI-17247926;
CC Q9NUQ2; Q9Y320: TMX2; NbExp=3; IntAct=EBI-6916385, EBI-6447886;
CC Q9NUQ2; Q9UMX0: UBQLN1; NbExp=6; IntAct=EBI-6916385, EBI-741480;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:21173190}; Multi-pass membrane protein
CC {ECO:0000255}. Nucleus envelope {ECO:0000269|PubMed:21173190}.
CC Mitochondrion {ECO:0000269|PubMed:21173190}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:16620771,
CC ECO:0000269|PubMed:21173190}.
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|UniProtKB:Q9D517}.
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-12 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA92069.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF375789; AAK54809.1; -; mRNA.
DR EMBL; AL136587; CAB66522.1; -; mRNA.
DR EMBL; BC023550; AAH23550.1; -; mRNA.
DR EMBL; BC080537; AAH80537.1; -; mRNA.
DR EMBL; AK002072; BAA92069.1; ALT_INIT; mRNA.
DR CCDS; CCDS34796.1; -.
DR RefSeq; NP_060831.2; NM_018361.3.
DR AlphaFoldDB; Q9NUQ2; -.
DR BioGRID; 120607; 95.
DR IntAct; Q9NUQ2; 13.
DR MINT; Q9NUQ2; -.
DR STRING; 9606.ENSP00000285518; -.
DR SwissLipids; SLP:000000822; -.
DR iPTMnet; Q9NUQ2; -.
DR PhosphoSitePlus; Q9NUQ2; -.
DR SwissPalm; Q9NUQ2; -.
DR BioMuta; AGPAT5; -.
DR DMDM; 30923427; -.
DR EPD; Q9NUQ2; -.
DR jPOST; Q9NUQ2; -.
DR MassIVE; Q9NUQ2; -.
DR MaxQB; Q9NUQ2; -.
DR PaxDb; Q9NUQ2; -.
DR PeptideAtlas; Q9NUQ2; -.
DR PRIDE; Q9NUQ2; -.
DR ProteomicsDB; 82706; -.
DR Antibodypedia; 2138; 320 antibodies from 27 providers.
DR DNASU; 55326; -.
DR Ensembl; ENST00000285518.11; ENSP00000285518.6; ENSG00000155189.12.
DR Ensembl; ENST00000646327.2; ENSP00000495562.1; ENSG00000284980.2.
DR GeneID; 55326; -.
DR KEGG; hsa:55326; -.
DR MANE-Select; ENST00000285518.11; ENSP00000285518.6; NM_018361.5; NP_060831.2.
DR UCSC; uc003wqo.4; human.
DR CTD; 55326; -.
DR DisGeNET; 55326; -.
DR GeneCards; AGPAT5; -.
DR HGNC; HGNC:20886; AGPAT5.
DR HPA; ENSG00000155189; Low tissue specificity.
DR MIM; 614796; gene.
DR neXtProt; NX_Q9NUQ2; -.
DR OpenTargets; ENSG00000155189; -.
DR PharmGKB; PA134952751; -.
DR VEuPathDB; HostDB:ENSG00000155189; -.
DR eggNOG; KOG1505; Eukaryota.
DR GeneTree; ENSGT00950000182836; -.
DR HOGENOM; CLU_041844_2_0_1; -.
DR InParanoid; Q9NUQ2; -.
DR OMA; KAETPMY; -.
DR OrthoDB; 959325at2759; -.
DR PhylomeDB; Q9NUQ2; -.
DR TreeFam; TF314346; -.
DR BioCyc; MetaCyc:HS08034-MON; -.
DR BRENDA; 2.3.1.51; 2681.
DR PathwayCommons; Q9NUQ2; -.
DR Reactome; R-HSA-1483166; Synthesis of PA.
DR SABIO-RK; Q9NUQ2; -.
DR SignaLink; Q9NUQ2; -.
DR SIGNOR; Q9NUQ2; -.
DR UniPathway; UPA00557; UER00613.
DR BioGRID-ORCS; 55326; 18 hits in 1079 CRISPR screens.
DR ChiTaRS; AGPAT5; human.
DR GeneWiki; AGPAT5; -.
DR GenomeRNAi; 55326; -.
DR Pharos; Q9NUQ2; Tbio.
DR PRO; PR:Q9NUQ2; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q9NUQ2; protein.
DR Bgee; ENSG00000155189; Expressed in corpus callosum and 110 other tissues.
DR ExpressionAtlas; Q9NUQ2; baseline and differential.
DR Genevisible; Q9NUQ2; HS.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
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:0005741; C:mitochondrial outer membrane; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0016746; F:acyltransferase activity; IBA:GO_Central.
DR GO; GO:0006639; P:acylglycerol metabolic process; IEA:Ensembl.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; TAS:Reactome.
DR GO; GO:0008654; P:phospholipid biosynthetic process; NAS: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; Mitochondrion; Nucleus;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..364
FT /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
FT epsilon"
FT /id="PRO_0000208200"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 93..98
FT /note="HXXXXD motif"
FT /evidence="ECO:0000250|UniProtKB:Q9D517"
FT VARIANT 77
FT /note="Y -> C (in dbSNP:rs17077958)"
FT /id="VAR_022696"
FT CONFLICT 156
FT /note="L -> V (in Ref. 2; BAA92069)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 364 AA; 42072 MW; 90A0F87FC7C78081 CRC64;
MLLSLVLHTY SMRYLLPSVV LLGTAPTYVL AWGVWRLLSA FLPARFYQAL DDRLYCVYQS
MVLFFFENYT GVQILLYGDL PKNKENIIYL ANHQSTVDWI VADILAIRQN ALGHVRYVLK
EGLKWLPLYG CYFAQHGGIY VKRSAKFNEK EMRNKLQSYV DAGTPMYLVI FPEGTRYNPE
QTKVLSASQA FAAQRGLAVL KHVLTPRIKA THVAFDCMKN YLDAIYDVTV VYEGKDDGGQ
RRESPTMTEF LCKECPKIHI HIDRIDKKDV PEEQEHMRRW LHERFEIKDK MLIEFYESPD
PERRKRFPGK SVNSKLSIKK TLPSMLILSG LTAGMLMTDA GRKLYVNTWI YGTLLGCLWV
TIKA
