LCLT1_HUMAN
ID LCLT1_HUMAN Reviewed; 414 AA.
AC Q6UWP7; A6H8Z7; Q8N1Q7;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Lysocardiolipin acyltransferase 1;
DE EC=2.3.1.- {ECO:0000250|UniProtKB:Q3UN02};
DE AltName: Full=1-acylglycerol-3-phosphate O-acyltransferase 8 {ECO:0000303|PubMed:16620771};
DE Short=1-AGP acyltransferase 8;
DE Short=1-AGPAT 8;
DE EC=2.3.1.51 {ECO:0000269|PubMed:16620771};
DE AltName: Full=Acyl-CoA:lysocardiolipin acyltransferase 1;
GN Name=LCLAT1; Synonyms=AGPAT8 {ECO:0000303|PubMed:16620771}, ALCAT1, LYCAT;
GN ORFNames=UNQ1849/PRO3579;
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).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Tongue;
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=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP ASP-206.
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 FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF ASP-206 AND LEU-207.
RX PubMed=19075029; DOI=10.1194/jlr.m800567-jlr200;
RA Zhao Y., Chen Y.-Q., Li S., Konrad R.J., Cao G.;
RT "The microsomal cardiolipin remodeling enzyme acyl-CoA lysocardiolipin
RT acyltransferase is an acyltransferase of multiple anionic
RT lysophospholipids.";
RL J. Lipid Res. 50:945-956(2009).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-221, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Exhibits acyl-CoA:lysocardiolipin acyltransferase (ALCAT)
CC activity; catalyzes the reacylation of lyso-cardiolipin to cardiolipin
CC (CL), a key step in CL remodeling (By similarity). Recognizes both
CC monolysocardiolipin and dilysocardiolipin as substrates with a
CC preference for linoleoyl-CoA and oleoyl-CoA as acyl donors (By
CC similarity). Also exhibits 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase activity (AGPAT) activity; converts 1-acyl-sn-glycerol-
CC 3- phosphate (lysophosphatidic acid or LPA) into 1,2-diacyl-sn-
CC glycerol-3- phosphate (phosphatidic acid or PA) by incorporating an
CC acyl moiety at the sn-2 position of the glycerol backbone
CC (PubMed:16620771). Possesses both lysophosphatidylinositol
CC acyltransferase (LPIAT) and lysophosphatidylglycerol acyltransferase
CC (LPGAT) activities (PubMed:19075029). Required for establishment of the
CC hematopoietic and endothelial lineages (By similarity).
CC {ECO:0000250|UniProtKB:Q3UN02, ECO:0000269|PubMed:16620771,
CC ECO:0000269|PubMed:19075029}.
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:16620771};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19710;
CC Evidence={ECO:0000305|PubMed:16620771};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phospho-(1D-myo-inositol) + an acyl-CoA
CC = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + CoA;
CC Xref=Rhea:RHEA:33195, ChEBI:CHEBI:57287, ChEBI:CHEBI:57880,
CC ChEBI:CHEBI:58342, ChEBI:CHEBI:64771;
CC Evidence={ECO:0000269|PubMed:19075029};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33196;
CC Evidence={ECO:0000305|PubMed:19075029};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-acyl-sn-glycero-3-phospho-(1'-sn-glycerol) + an acyl-CoA =
CC 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + CoA;
CC Xref=Rhea:RHEA:33203, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:64716, ChEBI:CHEBI:64840;
CC Evidence={ECO:0000269|PubMed:19075029};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33204;
CC Evidence={ECO:0000305|PubMed:19075029};
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:16620771};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33188;
CC Evidence={ECO:0000305|PubMed:16620771};
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:16620771};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37132;
CC Evidence={ECO:0000305|PubMed:16620771};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z,12Z)-octadecadienoyl-sn-glycero-
CC 3-phosphate = 1-(9Z,12Z)-octadecadienoyl-2-(9Z)-octadecenoyl-sn-
CC glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37135, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:74547, ChEBI:CHEBI:74548;
CC Evidence={ECO:0000269|PubMed:16620771};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37136;
CC Evidence={ECO:0000305|PubMed:16620771};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z,12Z,15Z)-octadecatrienoyl-sn-
CC glycero-3-phosphate = 1-(9Z,12Z,15Z)-octadecatrienoyl-2-(9Z)-
CC octadecenoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37139,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:74549,
CC ChEBI:CHEBI:74550; Evidence={ECO:0000269|PubMed:16620771};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37140;
CC Evidence={ECO:0000305|PubMed:16620771};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + hexadecanoyl-CoA
CC = 1-(9Z)-octadecenoyl-2-hexadecanoyl-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37143, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:74544, ChEBI:CHEBI:74551;
CC Evidence={ECO:0000269|PubMed:16620771};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37144;
CC Evidence={ECO:0000305|PubMed:16620771};
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:16620771};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37148;
CC Evidence={ECO:0000305|PubMed:16620771};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-acyl-sn-glycero-3-phospho-(1'-sn-
CC glycerol) = 1-acyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-sn-
CC glycerol) + CoA; Xref=Rhea:RHEA:37619, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:64840, ChEBI:CHEBI:75173;
CC Evidence={ECO:0000269|PubMed:19075029};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37620;
CC Evidence={ECO:0000305|PubMed:19075029};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + a 1-acyl-sn-glycero-3-phospho-(1D-myo-
CC inositol) = a 1-acyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1D-
CC myo-inositol) + CoA; Xref=Rhea:RHEA:37623, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:64771, ChEBI:CHEBI:75116;
CC Evidence={ECO:0000269|PubMed:19075029};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37624;
CC Evidence={ECO:0000305|PubMed:19075029};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol) +
CC hexadecanoyl-CoA = 1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-
CC inositol) + CoA; Xref=Rhea:RHEA:35871, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57379, ChEBI:CHEBI:72833, ChEBI:CHEBI:72835;
CC Evidence={ECO:0000269|PubMed:19075029};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35872;
CC Evidence={ECO:0000305|PubMed:19075029};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol) +
CC octadecanoyl-CoA = 1-hexadecanoyl-2-octadecanoyl-sn-glycero-3-
CC phospho-(1D-myo-inositol) + CoA; Xref=Rhea:RHEA:35875,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57394, ChEBI:CHEBI:72833,
CC ChEBI:CHEBI:72836; Evidence={ECO:0000269|PubMed:19075029};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35876;
CC Evidence={ECO:0000305|PubMed:19075029};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-phospho-
CC (1D-myo-inositol) = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-
CC phospho-(1D-myo-inositol) + CoA; Xref=Rhea:RHEA:35879,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:72833,
CC ChEBI:CHEBI:72837; Evidence={ECO:0000269|PubMed:19075029};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35880;
CC Evidence={ECO:0000305|PubMed:19075029};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + 1-hexadecanoyl-sn-glycero-3-
CC phospho-(1D-myo-inositol) = 1-hexadecanoyl-2-(9Z,12Z-
CC octadecadienoyl)-sn-glycero-3-phospho-(1D-myo-inositol) + CoA;
CC Xref=Rhea:RHEA:35883, ChEBI:CHEBI:57287, ChEBI:CHEBI:57383,
CC ChEBI:CHEBI:72833, ChEBI:CHEBI:72838;
CC Evidence={ECO:0000269|PubMed:19075029};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35884;
CC Evidence={ECO:0000305|PubMed:19075029};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-hexadecanoyl-sn-
CC glycero-3-phospho-(1D-myo-inositol) = 1-hexadecanoyl-2-
CC (5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phospho-D-myo-inositol
CC + CoA; Xref=Rhea:RHEA:35867, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368,
CC ChEBI:CHEBI:72833, ChEBI:CHEBI:72834;
CC Evidence={ECO:0000269|PubMed:19075029};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35868;
CC Evidence={ECO:0000305|PubMed:19075029};
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:19075029};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35852;
CC Evidence={ECO:0000305|PubMed:19075029};
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:19075029};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35888;
CC Evidence={ECO:0000305|PubMed:19075029};
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:19075029};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35892;
CC Evidence={ECO:0000305|PubMed:19075029};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + 1-hexadecanoyl-sn-glycero-3-
CC phospho-(1'-sn-glycerol) = 1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-
CC sn-glycero-3-phospho-(1'-sn-glycerol) + CoA; Xref=Rhea:RHEA:35895,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57383, ChEBI:CHEBI:72840,
CC ChEBI:CHEBI:75158; Evidence={ECO:0000269|PubMed:19075029};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35896;
CC Evidence={ECO:0000305|PubMed:19075029};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-tetradecanoyl-sn-glycero-3-phospho-
CC (1'-sn-glycerol) = 1-tetradecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-
CC phospho-(1'-sn-glycerol) + CoA; Xref=Rhea:RHEA:37643,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:72826,
CC ChEBI:CHEBI:75161; Evidence={ECO:0000269|PubMed:19075029};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37644;
CC Evidence={ECO:0000305|PubMed:19075029};
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:19075029};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37648;
CC Evidence={ECO:0000305|PubMed:19075029};
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:19075029};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37652;
CC Evidence={ECO:0000305|PubMed:19075029};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol) +
CC dodecanoyl-CoA = 1-hexadecanoyl-2-dodecanoyl-sn-glycero-3-phospho-
CC (1D-myo-inositol) + CoA; Xref=Rhea:RHEA:37639, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57375, ChEBI:CHEBI:72833, ChEBI:CHEBI:75160;
CC Evidence={ECO:0000269|PubMed:19075029};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37640;
CC Evidence={ECO:0000305|PubMed:19075029};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1',3'-bis-[1-acyl-sn-glycero-3-
CC phospho]-glycerol = 1'-[1-acyl-2-(9Z)-octadecenoyl-sn-glycero-3-
CC phospho],3'-[1-acyl,2-hydroxy-sn-glycero-3-phospho]-glycerol + CoA;
CC Xref=Rhea:RHEA:37615, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:75137, ChEBI:CHEBI:75139;
CC Evidence={ECO:0000250|UniProtKB:Q3UN02};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37616;
CC Evidence={ECO:0000250|UniProtKB:Q3UN02};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1'-[1,2-diacyl-sn-glycero-3-
CC phospho],3'-[1-acyl-sn-glycero-3-phospho]-glycerol = 1'-[1,2-diacyl-
CC sn-glycero-3-phospho],3'-[1-acyl,2-(9Z)-octadecenoyl-sn-glycero-3-
CC phospho]-glycerol + CoA; Xref=Rhea:RHEA:37611, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:64743, ChEBI:CHEBI:75140;
CC Evidence={ECO:0000250|UniProtKB:Q3UN02};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37612;
CC Evidence={ECO:0000250|UniProtKB:Q3UN02};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + 1'-[1,2-diacyl-sn-glycero-3-
CC phospho],3'-[1-acyl-sn-glycero-3-phospho]-glycerol = 1'-[1,2-diacyl-
CC sn-glycero-3-phospho],3'-[1-acyl,2-(9Z,12Z)-octadecadienoyl-sn-
CC glycero-3-phospho]-glycerol + CoA; Xref=Rhea:RHEA:37675,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57383, ChEBI:CHEBI:64743,
CC ChEBI:CHEBI:75205; Evidence={ECO:0000250|UniProtKB:Q3UN02};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37676;
CC Evidence={ECO:0000250|UniProtKB:Q3UN02};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1'-[1,2-diacyl-sn-glycero-3-phospho],3'-[1-acyl-sn-glycero-3-
CC phospho]-glycerol + dodecanoyl-CoA = 1'-[1,2-diacyl-sn-glycero-3-
CC phospho],3'-[1-acyl,2-dodecanoyl-sn-glycero-3-phospho]-glycerol +
CC CoA; Xref=Rhea:RHEA:37679, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375,
CC ChEBI:CHEBI:64743, ChEBI:CHEBI:75203;
CC Evidence={ECO:0000250|UniProtKB:Q3UN02};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37680;
CC Evidence={ECO:0000250|UniProtKB:Q3UN02};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1',3'-bis-[1-acyl-sn-glycero-3-phospho]-glycerol + dodecanoyl-
CC CoA = 1'-[1-acyl-2-dodecanoyl-sn-glycero-3-phospho],3'-[1-acyl,2-
CC hydroxy-sn-glycero-3-phospho]-glycerol + CoA; Xref=Rhea:RHEA:37683,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57375, ChEBI:CHEBI:75137,
CC ChEBI:CHEBI:75201; Evidence={ECO:0000250|UniProtKB:Q3UN02};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37684;
CC Evidence={ECO:0000250|UniProtKB:Q3UN02};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + a 1-acyl-sn-glycero-3-phosphate = a 1-
CC acyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37427, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:57970, ChEBI:CHEBI:74917;
CC Evidence={ECO:0000250|UniProtKB:Q3UN02};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37428;
CC Evidence={ECO:0000250|UniProtKB:Q3UN02};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + 1',3'-bis-[1-acyl-sn-glycero-3-
CC phospho]-glycerol = 1'-[1-acyl-2-(9Z,12Z)-octadecadienoyl-sn-glycero-
CC 3-phospho],3'-[1-acyl,2-hydroxy-sn-glycero-3-phospho]-glycerol + CoA;
CC Xref=Rhea:RHEA:37687, ChEBI:CHEBI:57287, ChEBI:CHEBI:57383,
CC ChEBI:CHEBI:75137, ChEBI:CHEBI:75209;
CC Evidence={ECO:0000250|UniProtKB:Q3UN02};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37688;
CC Evidence={ECO:0000250|UniProtKB:Q3UN02};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1',3'-bis-[1-acyl-sn-glycero-3-phospho]-glycerol +
CC hexadecanoyl-CoA = 1'-[1-acyl-2-hexadecanoyl-sn-glycero-3-
CC phospho],3'-[1-acyl,2-hydroxy-sn-glycero-3-phospho]-glycerol + CoA;
CC Xref=Rhea:RHEA:37691, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:75137, ChEBI:CHEBI:75207;
CC Evidence={ECO:0000250|UniProtKB:Q3UN02};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37692;
CC Evidence={ECO:0000250|UniProtKB:Q3UN02};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1',3'-bis-[1-acyl-sn-glycero-3-phospho]-glycerol +
CC octadecanoyl-CoA = 1'-[1-acyl-2-octadecanoyl-sn-glycero-3-
CC phospho],3'-[1-acyl,2-hydroxy-sn-glycero-3-phospho]-glycerol + CoA;
CC Xref=Rhea:RHEA:37695, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394,
CC ChEBI:CHEBI:75137, ChEBI:CHEBI:75208;
CC Evidence={ECO:0000250|UniProtKB:Q3UN02};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37696;
CC Evidence={ECO:0000250|UniProtKB:Q3UN02};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1'-[1,2-diacyl-sn-glycero-3-phospho],3'-[1-acyl-sn-glycero-3-
CC phospho]-glycerol + octanoyl-CoA = 1'-[1,2-diacyl-sn-glycero-3-
CC phospho],3'-[1-acyl,2-octanoyl-sn-glycero-3-phospho]-glycerol + CoA;
CC Xref=Rhea:RHEA:38623, ChEBI:CHEBI:57287, ChEBI:CHEBI:57386,
CC ChEBI:CHEBI:64743, ChEBI:CHEBI:75990;
CC Evidence={ECO:0000250|UniProtKB:Q3UN02};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38624;
CC Evidence={ECO:0000250|UniProtKB:Q3UN02};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1',3'-bis-[1-acyl-sn-glycero-3-phospho]-glycerol + octanoyl-
CC CoA = 1'-[1-acyl-2-octanoyl-sn-glycero-3-phospho],3'-[1-acyl,2-
CC hydroxy-sn-glycero-3-phospho]-glycerol + CoA; Xref=Rhea:RHEA:38627,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57386, ChEBI:CHEBI:75137,
CC ChEBI:CHEBI:75993; Evidence={ECO:0000250|UniProtKB:Q3UN02};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38628;
CC Evidence={ECO:0000250|UniProtKB:Q3UN02};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1'-[1,2-diacyl-sn-glycero-3-phospho],3'-[1-acyl-sn-glycero-3-
CC phospho]-glycerol + hexadecanoyl-CoA = 1'-[1,2-diacyl-sn-glycero-3-
CC phospho],3'-[1-acyl,2-hexadecanoyl-sn-glycero-3-phospho]-glycerol +
CC CoA; Xref=Rhea:RHEA:38631, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:64743, ChEBI:CHEBI:75994;
CC Evidence={ECO:0000250|UniProtKB:Q3UN02};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38632;
CC Evidence={ECO:0000250|UniProtKB:Q3UN02};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1'-[1,2-diacyl-sn-
CC glycero-3-phospho],3'-[1-acyl-sn-glycero-3-phospho]-glycerol = 1'-
CC [1,2-diacyl-sn-glycero-3-phospho],3'-[1-acyl,2-(5Z,8Z,11Z,14Z)-
CC eicosatetraenoyl-sn-glycero-3-phospho]-glycerol + CoA;
CC Xref=Rhea:RHEA:38635, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368,
CC ChEBI:CHEBI:64743, ChEBI:CHEBI:75995;
CC Evidence={ECO:0000250|UniProtKB:Q3UN02};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38636;
CC Evidence={ECO:0000250|UniProtKB:Q3UN02};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1',3'-bis-[1-acyl-sn-
CC glycero-3-phospho]-glycerol = 1'-[1-acyl-2-(5Z,8Z,11Z,14Z)-
CC eicosatetraenoyl-sn-glycero-3-phospho],3'-[1-acyl,2-hydroxy-sn-
CC glycero-3-phospho]-glycerol + CoA; Xref=Rhea:RHEA:38639,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57368, ChEBI:CHEBI:75137,
CC ChEBI:CHEBI:75996; Evidence={ECO:0000250|UniProtKB:Q3UN02};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38640;
CC Evidence={ECO:0000250|UniProtKB:Q3UN02};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phospho-(1D-myo-inositol) +
CC octadecanoyl-CoA = a 1-acyl-2-octadecanoyl-sn-glycero-3-phospho-(1D-
CC myo-inositol) + CoA; Xref=Rhea:RHEA:43960, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57394, ChEBI:CHEBI:64771, ChEBI:CHEBI:83939;
CC Evidence={ECO:0000250|UniProtKB:Q3UN02};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43961;
CC Evidence={ECO:0000250|UniProtKB:Q3UN02};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2-acyl-sn-glycero-3-phospho-D-myo-inositol + octadecanoyl-
CC CoA = 1-octadecanoyl-2-acyl-sn-glycero-3-phospho-(1D-myo-inositol) +
CC CoA; Xref=Rhea:RHEA:43964, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394,
CC ChEBI:CHEBI:64872, ChEBI:CHEBI:83940;
CC Evidence={ECO:0000250|UniProtKB:Q3UN02};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43965;
CC Evidence={ECO:0000250|UniProtKB:Q3UN02};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=39 uM for arachidonoyl-CoA (20:4) for LPIAT activity
CC {ECO:0000269|PubMed:19075029};
CC KM=289 uM for oleoyl-CoA (18:1) for LPIAT activity
CC {ECO:0000269|PubMed:19075029};
CC KM=134 uM for linoleoyl-CoA (18:2) for LPIAT activity
CC {ECO:0000269|PubMed:19075029};
CC KM=34 uM for stearoyl-CoA (18:0) for LPIAT activity
CC {ECO:0000269|PubMed:19075029};
CC KM=53 uM for palmitoyl-CoA (16:0) for LPIAT activity
CC {ECO:0000269|PubMed:19075029};
CC KM=54 uM for oleoyl-CoA (18:1) for LPGAT activity
CC {ECO:0000269|PubMed:19075029};
CC KM=36 uM for linoleoyl-CoA (18:2) for LPGAT activity
CC {ECO:0000269|PubMed:19075029};
CC KM=70 uM for stearoyl-CoA (18:0) for LPGAT activity
CC {ECO:0000269|PubMed:19075029};
CC KM=34 uM for palmitoyl-CoA (16:0) for LPGAT activity
CC {ECO:0000269|PubMed:19075029};
CC Vmax=3230 nmol/min/mg enzyme toward arachidonoyl-CoA (20:4) for LPIAT
CC activity {ECO:0000269|PubMed:19075029};
CC Vmax=7489 nmol/min/mg enzyme toward oleoyl-CoA (18:1) for LPIAT
CC activity {ECO:0000269|PubMed:19075029};
CC Vmax=4696 nmol/min/mg enzyme toward linoleoyl-CoA (18:2) for LPIAT
CC activity {ECO:0000269|PubMed:19075029};
CC Vmax=1078 nmol/min/mg enzyme toward stearoyl-CoA (18:0) for LPIAT
CC activity {ECO:0000269|PubMed:19075029};
CC Vmax=11203 nmol/min/mg enzyme toward palmitoyl-CoA (16:0) for LPIAT
CC activity {ECO:0000269|PubMed:19075029};
CC Vmax=5514 nmol/min/mg enzyme toward oleoyl-CoA (18:1) for LPGAT
CC activity {ECO:0000269|PubMed:19075029};
CC Vmax=1358 nmol/min/mg enzyme toward linoleoyl-CoA (18:2) for LPGAT
CC activity {ECO:0000269|PubMed:19075029};
CC Vmax=3530 nmol/min/mg enzyme toward stearoyl-CoA (18:0) for LPGAT
CC activity {ECO:0000269|PubMed:19075029};
CC Vmax=1673 nmol/min/mg enzyme toward palmitoyl-CoA (16:0) for LPGAT
CC activity {ECO:0000269|PubMed:19075029};
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
CC -!- INTERACTION:
CC Q6UWP7; Q9HD26: GOPC; NbExp=3; IntAct=EBI-10254507, EBI-349832;
CC Q6UWP7; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-10254507, EBI-739832;
CC Q6UWP7; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-10254507, EBI-79165;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:19075029}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6UWP7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6UWP7-2; Sequence=VSP_026181, VSP_026182;
CC Name=3;
CC IsoId=Q6UWP7-3; Sequence=VSP_044307;
CC -!- TISSUE SPECIFICITY: Expressed at higher level in heart, kidney and
CC pancreas than in brain, spleen, liver, lung, small intestine and
CC placenta. {ECO:0000269|PubMed:16620771, ECO:0000269|PubMed:19075029}.
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: PubMed:16620771 does not detect acyl-CoA:lysocardiolipin
CC acyltransferase activity. {ECO:0000305}.
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DR EMBL; AY358702; AAQ89065.1; -; mRNA.
DR EMBL; AK095284; BAC04522.1; -; mRNA.
DR EMBL; AC073255; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC132154; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC146817; AAI46818.1; -; mRNA.
DR CCDS; CCDS1772.1; -. [Q6UWP7-1]
DR CCDS; CCDS42670.1; -. [Q6UWP7-3]
DR RefSeq; NP_001002257.1; NM_001002257.2. [Q6UWP7-3]
DR RefSeq; NP_001291374.1; NM_001304445.1. [Q6UWP7-3]
DR RefSeq; NP_872357.2; NM_182551.4. [Q6UWP7-1]
DR RefSeq; XP_005264301.1; XM_005264244.1. [Q6UWP7-1]
DR RefSeq; XP_005264302.1; XM_005264245.3. [Q6UWP7-3]
DR RefSeq; XP_011531043.1; XM_011532741.2. [Q6UWP7-1]
DR RefSeq; XP_011531044.1; XM_011532742.2. [Q6UWP7-3]
DR RefSeq; XP_011531045.1; XM_011532743.2.
DR RefSeq; XP_016859235.1; XM_017003746.1. [Q6UWP7-3]
DR AlphaFoldDB; Q6UWP7; -.
DR BioGRID; 128972; 81.
DR IntAct; Q6UWP7; 26.
DR MINT; Q6UWP7; -.
DR STRING; 9606.ENSP00000310551; -.
DR SwissLipids; SLP:000000126; -.
DR GlyGen; Q6UWP7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q6UWP7; -.
DR PhosphoSitePlus; Q6UWP7; -.
DR SwissPalm; Q6UWP7; -.
DR BioMuta; LCLAT1; -.
DR DMDM; 74749398; -.
DR EPD; Q6UWP7; -.
DR jPOST; Q6UWP7; -.
DR MassIVE; Q6UWP7; -.
DR MaxQB; Q6UWP7; -.
DR PaxDb; Q6UWP7; -.
DR PeptideAtlas; Q6UWP7; -.
DR PRIDE; Q6UWP7; -.
DR ProteomicsDB; 67509; -. [Q6UWP7-1]
DR ProteomicsDB; 67510; -. [Q6UWP7-2]
DR ProteomicsDB; 790; -.
DR TopDownProteomics; Q6UWP7-1; -. [Q6UWP7-1]
DR Antibodypedia; 28989; 98 antibodies from 20 providers.
DR DNASU; 253558; -.
DR Ensembl; ENST00000309052.8; ENSP00000310551.4; ENSG00000172954.14. [Q6UWP7-1]
DR Ensembl; ENST00000319406.8; ENSP00000368826.1; ENSG00000172954.14. [Q6UWP7-2]
DR Ensembl; ENST00000379509.8; ENSP00000368823.3; ENSG00000172954.14. [Q6UWP7-3]
DR GeneID; 253558; -.
DR KEGG; hsa:253558; -.
DR MANE-Select; ENST00000379509.8; ENSP00000368823.3; NM_001002257.3; NP_001002257.1. [Q6UWP7-3]
DR UCSC; uc002rnj.3; human. [Q6UWP7-1]
DR CTD; 253558; -.
DR DisGeNET; 253558; -.
DR GeneCards; LCLAT1; -.
DR HGNC; HGNC:26756; LCLAT1.
DR HPA; ENSG00000172954; Low tissue specificity.
DR neXtProt; NX_Q6UWP7; -.
DR OpenTargets; ENSG00000172954; -.
DR PharmGKB; PA164722072; -.
DR VEuPathDB; HostDB:ENSG00000172954; -.
DR eggNOG; KOG1505; Eukaryota.
DR GeneTree; ENSGT00950000182836; -.
DR HOGENOM; CLU_041844_4_0_1; -.
DR InParanoid; Q6UWP7; -.
DR OrthoDB; 959325at2759; -.
DR PhylomeDB; Q6UWP7; -.
DR TreeFam; TF314346; -.
DR PathwayCommons; Q6UWP7; -.
DR Reactome; R-HSA-1482798; Acyl chain remodeling of CL.
DR Reactome; R-HSA-1483166; Synthesis of PA.
DR SABIO-RK; Q6UWP7; -.
DR SignaLink; Q6UWP7; -.
DR UniPathway; UPA00557; UER00613.
DR BioGRID-ORCS; 253558; 11 hits in 1078 CRISPR screens.
DR ChiTaRS; LCLAT1; human.
DR GenomeRNAi; 253558; -.
DR Pharos; Q6UWP7; Tbio.
DR PRO; PR:Q6UWP7; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q6UWP7; protein.
DR Bgee; ENSG00000172954; Expressed in left ventricle myocardium and 191 other tissues.
DR ExpressionAtlas; Q6UWP7; baseline and differential.
DR Genevisible; Q6UWP7; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0016746; F:acyltransferase activity; IBA:GO_Central.
DR GO; GO:0008374; F:O-acyltransferase activity; TAS:Reactome.
DR GO; GO:0035965; P:cardiolipin acyl-chain remodeling; TAS:UniProtKB.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; TAS:Reactome.
DR GO; GO:0036149; P:phosphatidylinositol acyl-chain remodeling; IBA:GO_Central.
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 Acetylation; Acyltransferase; Alternative splicing; Developmental protein;
KW Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..414
FT /note="Lysocardiolipin acyltransferase 1"
FT /id="PRO_0000291577"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 340..360
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 362..382
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 123..128
FT /note="HXXXXD motif"
FT /evidence="ECO:0000250|UniProtKB:Q9D517"
FT MOD_RES 221
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 1..38
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_044307"
FT VAR_SEQ 249..308
FT /note="KNLDAVHDITVAYPHNIPQSEKHLLQGDFPREIHFHVHRYPIDTLPTSKEDL
FT QLWCHKRW -> RRQSEGSKGPLQGELQITAQGNQRGHKQMEKHSMLMDWKNQYREIGH
FT TAQSNLQIQCYSH (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_026181"
FT VAR_SEQ 309..414
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_026182"
FT VARIANT 290
FT /note="I -> V (in dbSNP:rs12471868)"
FT /id="VAR_032830"
FT MUTAGEN 206
FT /note="D->C: Abolishes LPIAT and LPGAT activities."
FT /evidence="ECO:0000269|PubMed:16620771,
FT ECO:0000269|PubMed:19075029"
FT MUTAGEN 206
FT /note="D->R: Does not increase enzyme activity."
FT /evidence="ECO:0000269|PubMed:16620771,
FT ECO:0000269|PubMed:19075029"
FT MUTAGEN 207
FT /note="L->T: Abolishes LPIAT activity. No effect on LPGAT
FT activity."
FT /evidence="ECO:0000269|PubMed:19075029"
SQ SEQUENCE 414 AA; 48920 MW; F83A1911CC19F959 CRC64;
MHSRGREIVV LLNPWSINEA VSSYCTYFIK QDSKSFGIMV SWKGIYFILT LFWGSFFGSI
FMLSPFLPLM FVNPSWYRWI NNRLVATWLT LPVALLETMF GVKVIITGDA FVPGERSVII
MNHRTRMDWM FLWNCLMRYS YLRLEKICLK ASLKGVPGFG WAMQAAAYIF IHRKWKDDKS
HFEDMIDYFC DIHEPLQLLI FPEGTDLTEN SKSRSNAFAE KNGLQKYEYV LHPRTTGFTF
VVDRLREGKN LDAVHDITVA YPHNIPQSEK HLLQGDFPRE IHFHVHRYPI DTLPTSKEDL
QLWCHKRWEE KEERLRSFYQ GEKNFYFTGQ SVIPPCKSEL RVLVVKLLSI LYWTLFSPAM
CLLIYLYSLV KWYFIITIVI FVLQERIFGG LEIIELACYR LLHKQPHLNS KKNE
