PCAT1_HUMAN
ID PCAT1_HUMAN Reviewed; 534 AA.
AC Q8NF37; Q1HAQ1; Q7Z4G6; Q8N3U7; Q8WUL8; Q9GZW6;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Lysophosphatidylcholine acyltransferase 1;
DE Short=LPC acyltransferase 1;
DE Short=LPCAT-1;
DE Short=LysoPC acyltransferase 1;
DE EC=2.3.1.23 {ECO:0000269|PubMed:18156367, ECO:0000269|PubMed:21498505};
DE AltName: Full=1-acylglycerol-3-phosphate O-acyltransferase;
DE EC=2.3.1.51 {ECO:0000250|UniProtKB:Q1HAQ0};
DE AltName: Full=1-acylglycerophosphocholine O-acyltransferase;
DE AltName: Full=1-alkenylglycerophosphocholine O-acyltransferase;
DE EC=2.3.1.25 {ECO:0000250|UniProtKB:Q3TFD2};
DE AltName: Full=1-alkylglycerophosphocholine O-acetyltransferase;
DE EC=2.3.1.67 {ECO:0000250|UniProtKB:Q3TFD2};
DE AltName: Full=Acetyl-CoA:lyso-platelet-activating factor acetyltransferase;
DE Short=Acetyl-CoA:lyso-PAF acetyltransferase;
DE Short=Lyso-PAF acetyltransferase;
DE Short=LysoPAFAT;
DE AltName: Full=Acyltransferase-like 2;
DE AltName: Full=Phosphonoformate immuno-associated protein 3;
GN Name=LPCAT1; Synonyms=AYTL2, PFAAP3;
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].
RX PubMed=16704971; DOI=10.1074/jbc.m600225200;
RA Nakanishi H., Shindou H., Hishikawa D., Harayama T., Ogasawara R.,
RA Suwabe A., Taguchi R., Shimizu T.;
RT "Cloning and characterization of mouse lung-type acyl-
RT CoA:lysophosphatidylcholine acyltransferase 1 (LPCAT1): expression in
RT alveolar type II cells and possible involvement in surfactant production.";
RL J. Biol. Chem. 281:20140-20147(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 136-534.
RC TISSUE=Spleen;
RX PubMed=12693554; DOI=10.1093/dnares/10.1.49;
RA Jikuya H., Takano J., Kikuno R., Hirosawa M., Nagase T., Nomura N.,
RA Ohara O.;
RT "Characterization of long cDNA clones from human adult spleen. II. The
RT complete sequences of 81 cDNA clones.";
RL DNA Res. 10:49-57(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 140-534.
RC TISSUE=Eye;
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 236-534.
RC TISSUE=Teratocarcinoma;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 298-534.
RA Liu Y., Cheng J., Lu Y.;
RT "Screening and cloning of a new immuno-associated gene regulated by
RT phosphonoformate.";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 448-534.
RC TISSUE=Amygdala;
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 [7]
RP IDENTIFICATION.
RX PubMed=16864775; DOI=10.1073/pnas.0604946103;
RA Chen X., Hyatt B.A., Mucenski M.L., Mason R.J., Shannon J.M.;
RT "Identification and characterization of a lysophosphatidylcholine
RT acyltransferase in alveolar type II cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11724-11729(2006).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE
RP SPECIFICITY.
RX PubMed=18156367; DOI=10.1073/pnas.0709737104;
RA Soupene E., Fyrst H., Kuypers F.A.;
RT "Mammalian acyl-CoA:lysophosphatidylcholine acyltransferase enzymes.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:88-93(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, TOPOLOGY, AND
RP DI-LYSINE MOTIF.
RX PubMed=21498505; DOI=10.1074/jbc.m110.202424;
RA Moessinger C., Kuerschner L., Spandl J., Shevchenko A., Thiele C.;
RT "Human lysophosphatidylcholine acyltransferases 1 and 2 are located in
RT lipid droplets where they catalyze the formation of phosphatidylcholine.";
RL J. Biol. Chem. 286:21330-21339(2011).
RN [11]
RP FUNCTION.
RX PubMed=25491198; DOI=10.1186/s12860-014-0043-3;
RA Moessinger C., Klizaite K., Steinhagen A., Philippou-Massier J.,
RA Shevchenko A., Hoch M., Ejsing C.S., Thiele C.;
RT "Two different pathways of phosphatidylcholine synthesis, the Kennedy
RT Pathway and the Lands Cycle, differentially regulate cellular
RT triacylglycerol storage.";
RL BMC Cell Biol. 15:43-43(2014).
RN [12]
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: Exhibits acyltransferase activity (PubMed:21498505,
CC PubMed:18156367). Exhibits acetyltransferase activity (By similarity).
CC Activity is calcium-independent (By similarity). Catalyzes the
CC conversion of lysophosphatidylcholine (1-acyl-sn-glycero-3-
CC phosphocholine or LPC) into phosphatidylcholine (1,2-diacyl-sn-glycero-
CC 3-phosphocholine or PC) (PubMed:21498505, PubMed:18156367). Catalyzes
CC the conversion 1-acyl-sn-glycerol-3-phosphate (lysophosphatidic acid or
CC LPA) into 1,2-diacyl-sn-glycerol-3-phosphate (phosphatidic acid or PA)
CC by incorporating an acyl moiety at the sn-2 position of the glycerol
CC backbone (By similarity). Displays a clear preference for saturated
CC fatty acyl-CoAs, and 1-myristoyl or 1-palmitoyl LPC as acyl donors and
CC acceptors, respectively (By similarity). Involved in platelet-
CC activating factor (PAF) biosynthesis by catalyzing the conversion of
CC the PAF precursor, 1-O-alkyl-sn-glycero-3-phosphocholine (lyso-PAF)
CC into 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine (PAF) (By
CC similarity). May synthesize phosphatidylcholine in pulmonary
CC surfactant, thereby playing a pivotal role in respiratory physiology
CC (By similarity). Involved in the regulation of lipid droplet number and
CC size (PubMed:25491198). {ECO:0000250|UniProtKB:Q3TFD2,
CC ECO:0000269|PubMed:18156367, ECO:0000269|PubMed:21498505,
CC ECO:0000269|PubMed:25491198}.
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:18156367, ECO:0000269|PubMed:21498505};
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:0000250|UniProtKB:Q1HAQ0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-alkyl-sn-glycero-3-phosphocholine + acetyl-CoA = a 1-O-
CC alkyl-2-acetyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:18461, ChEBI:CHEBI:30909, ChEBI:CHEBI:36707,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.67;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-(1Z-alkenyl)-sn-glycero-3-phosphocholine + an acyl-CoA =
CC 1-O-(1Z-alkenyl)-2-acyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:10344, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:77286, ChEBI:CHEBI:77287; EC=2.3.1.25;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
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:0000250|UniProtKB:Q1HAQ0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33204;
CC Evidence={ECO:0000250|UniProtKB:Q1HAQ0};
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:21498505};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35992;
CC Evidence={ECO:0000305|PubMed:21498505};
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:0000250|UniProtKB:Q3TFD2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35984;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-hexadecyl-sn-glycero-3-phosphocholine + hexadecanoyl-CoA =
CC 1-O-hexadecyl-2-hexadecanoyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:37811, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:64496, ChEBI:CHEBI:72744;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37812;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-(1Z-alkenyl)-sn-glycero-3-phosphocholine + hexadecanoyl-
CC CoA = 1-O-(1Z)-alkenyl-2-hexadecanoyl-sn-glycero-3-phosphocholine +
CC CoA; Xref=Rhea:RHEA:37819, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:77287, ChEBI:CHEBI:77304;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37820;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
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:0000250|UniProtKB:Q3TFD2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35852;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
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:0000250|UniProtKB:Q3TFD2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37512;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
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:0000250|UniProtKB:Q3TFD2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37656;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-octadecyl-sn-glycero-3-phosphocholine + hexadecanoyl-CoA =
CC 1-O-octadecyl-2-hexadecanoyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:37839, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:75216, ChEBI:CHEBI:75290;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37840;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
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:0000250|UniProtKB:Q3TFD2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37528;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
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:0000250|UniProtKB:Q3TFD2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37384;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-eicosanoyl-sn-glycero-3-phosphocholine + hexadecanoyl-CoA =
CC 1-eicosanoyl-2-hexadecanoyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:37843, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:74968, ChEBI:CHEBI:75294;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37844;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + hexanoyl-CoA = 1-
CC hexadecanoyl-2-hexanoyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:37855, ChEBI:CHEBI:57287, ChEBI:CHEBI:62620,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:75301;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37856;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + octanoyl-CoA = 1-
CC hexadecanoyl-2-octanoyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:37859, ChEBI:CHEBI:57287, ChEBI:CHEBI:57386,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:75302;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37860;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + decanoyl-CoA = 1-
CC hexadecanoyl-2-decanoyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:37863, ChEBI:CHEBI:57287, ChEBI:CHEBI:61430,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:75300;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37864;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
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:0000250|UniProtKB:Q3TFD2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37516;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + tetradecanoyl-CoA
CC = 1-hexadecanoyl-2-tetradecanoyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:37867, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:75304;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37868;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
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:0000250|UniProtKB:Q3TFD2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35996;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoyl-CoA + 1-hexadecanoyl-
CC sn-glycero-3-phosphocholine = 1-hexadecanoyl-2-
CC (4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-phosphocholine +
CC CoA; Xref=Rhea:RHEA:37475, ChEBI:CHEBI:57287, ChEBI:CHEBI:72998,
CC ChEBI:CHEBI:74298, ChEBI:CHEBI:74963;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37476;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + acetyl-CoA = 1-
CC hexadecanoyl-2-acetyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:37703, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:75219;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37704;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + eicosanoyl-CoA =
CC 1-hexadecanoyl-2-eicosanoyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:43264, ChEBI:CHEBI:57287, ChEBI:CHEBI:57380,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:82943;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43265;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-hexadecyl-sn-glycero-3-phosphocholine + acetyl-CoA = 1-O-
CC hexadecyl-2-acetyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:37719, ChEBI:CHEBI:44811, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:64496;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37720;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphocholine + hexadecanoyl-CoA = 1-
CC acyl-2-hexadecanoyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:37803, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:58168, ChEBI:CHEBI:75279;
CC Evidence={ECO:0000250|UniProtKB:Q1HAQ0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37804;
CC Evidence={ECO:0000250|UniProtKB:Q1HAQ0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphate + hexadecanoyl-CoA = 1-acyl-2-
CC hexadecanoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:33315,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:57970,
CC ChEBI:CHEBI:64862; Evidence={ECO:0000250|UniProtKB:Q1HAQ0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33316;
CC Evidence={ECO:0000250|UniProtKB:Q1HAQ0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-acyl-sn-glycero-3-phospho-(1'-sn-glycerol) + hexadecanoyl-
CC CoA = 1-acyl-2-hexadecanoyl-sn-glycero-3-phospho-(1'-sn-glycerol) +
CC CoA; Xref=Rhea:RHEA:37807, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:64840, ChEBI:CHEBI:75280;
CC Evidence={ECO:0000250|UniProtKB:Q1HAQ0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37808;
CC Evidence={ECO:0000250|UniProtKB:Q1HAQ0};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.6 uM for palmitoyl-CoA (in the presence of 1-palmitoyl-LPC as
CC cosubstrate) {ECO:0000269|PubMed:18156367};
CC KM=4 uM for oleoyl-CoA (in the presence of 1-palmitoyl-LPC as
CC cosubstrate) {ECO:0000269|PubMed:18156367};
CC KM=7.8 uM for linoleoyl-CoA (in the presence of 1-palmitoyl-LPC as
CC cosubstrate) {ECO:0000269|PubMed:18156367};
CC KM=4.3 uM for arachidonyl-CoA (in the presence of 1-palmitoyl-LPC as
CC cosubstrate) {ECO:0000269|PubMed:18156367};
CC KM=6.8 uM for 1-palmitoyl-LPC (in the presence of palmitoyl-CoA as
CC cosubstrate) {ECO:0000269|PubMed:18156367};
CC KM=27 uM for 1-palmitoyl-LPC (in the presence of oleoyl-CoA as
CC cosubstrate) {ECO:0000269|PubMed:18156367};
CC KM=44.5 uM for 1-palmitoyl-LPC (in the presence of linoleoyl-CoA as
CC cosubstrate) {ECO:0000269|PubMed:18156367};
CC KM=9.2 uM for 1-palmitoyl-LPC (in the presence of arachidonyl-CoA as
CC cosubstrate) {ECO:0000269|PubMed:18156367};
CC Vmax=2.8 nmol/min/mg enzyme towards palmitoyl-CoA using 1-palmitoyl-
CC LPC as cosubstrate {ECO:0000269|PubMed:18156367};
CC Vmax=5.6 nmol/min/mg enzyme towards oleoyl-CoA using 1-palmitoyl-LPC
CC as cosubstrate {ECO:0000269|PubMed:18156367};
CC Vmax=11.3 nmol/min/mg enzyme towards linoleoyl-CoA using 1-palmitoyl-
CC LPC as cosubstrate {ECO:0000269|PubMed:18156367};
CC Vmax=4.6 nmol/min/mg enzyme towards arachidonyl-CoA using 1-
CC palmitoyl-LPC as cosubstrate {ECO:0000269|PubMed:18156367};
CC Vmax=1.4 nmol/min/mg enzyme towards 1-palmitoyl-LPC using palmitoyl-
CC CoA as cosubstrate {ECO:0000269|PubMed:18156367};
CC Vmax=6.8 nmol/min/mg enzyme towards 1-palmitoyl-LPC using oleoyl-CoA
CC as cosubstrate {ECO:0000269|PubMed:18156367};
CC Vmax=11.8 nmol/min/mg enzyme towards 1-palmitoyl-LPC using linoleoyl-
CC CoA as cosubstrate {ECO:0000269|PubMed:18156367};
CC Vmax=3.6 nmol/min/mg enzyme with towards 1-palmitoyl-LPC using
CC arachidonyl-CoA as cosubstrate {ECO:0000269|PubMed:18156367};
CC pH dependence:
CC Optimum pH is 5.5 and 7.5. {ECO:0000269|PubMed:18156367};
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC {ECO:0000269|PubMed:21498505}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:21498505}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:21498505}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q3TFD2}; Single-pass type II membrane protein
CC {ECO:0000305|PubMed:21498505}. Cell membrane
CC {ECO:0000305|PubMed:18156367}; Single-pass type II membrane protein
CC {ECO:0000305|PubMed:21498505}. Lipid droplet
CC {ECO:0000269|PubMed:21498505}. Note=May adopt a monotopic topology when
CC embedded in the lipid monolayer of the lipid droplet, with both termini
CC exposed to the cytoplasm. {ECO:0000269|PubMed:21498505}.
CC -!- TISSUE SPECIFICITY: Erythrocytes. {ECO:0000269|PubMed:18156367}.
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-phosphocholine. {ECO:0000250|UniProtKB:Q3TFD2}.
CC -!- DOMAIN: The di-lysine motif may confer endoplasmic reticulum
CC localization. {ECO:0000250|UniProtKB:Q3TFD2}.
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14061.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB14065.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB244719; BAE94688.1; -; mRNA.
DR EMBL; AK090444; BAC03425.1; -; mRNA.
DR EMBL; BC020166; AAH20166.3; -; mRNA.
DR EMBL; AK022505; BAB14065.1; ALT_INIT; mRNA.
DR EMBL; AK022499; BAB14061.1; ALT_INIT; mRNA.
DR EMBL; AF530061; AAQ09945.1; -; mRNA.
DR EMBL; AL831864; CAD38556.1; -; mRNA.
DR CCDS; CCDS3864.1; -.
DR RefSeq; NP_079106.3; NM_024830.4.
DR AlphaFoldDB; Q8NF37; -.
DR SMR; Q8NF37; -.
DR BioGRID; 122973; 105.
DR IntAct; Q8NF37; 34.
DR MINT; Q8NF37; -.
DR STRING; 9606.ENSP00000283415; -.
DR ChEMBL; CHEMBL4295903; -.
DR SwissLipids; SLP:000000295; -.
DR GlyGen; Q8NF37; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q8NF37; -.
DR PhosphoSitePlus; Q8NF37; -.
DR SwissPalm; Q8NF37; -.
DR BioMuta; LPCAT1; -.
DR DMDM; 110815902; -.
DR EPD; Q8NF37; -.
DR jPOST; Q8NF37; -.
DR MassIVE; Q8NF37; -.
DR MaxQB; Q8NF37; -.
DR PaxDb; Q8NF37; -.
DR PeptideAtlas; Q8NF37; -.
DR PRIDE; Q8NF37; -.
DR ProteomicsDB; 73259; -.
DR TopDownProteomics; Q8NF37; -.
DR Antibodypedia; 1587; 229 antibodies from 28 providers.
DR DNASU; 79888; -.
DR Ensembl; ENST00000283415.4; ENSP00000283415.3; ENSG00000153395.10.
DR Ensembl; ENST00000475622.5; ENSP00000423472.1; ENSG00000153395.10.
DR GeneID; 79888; -.
DR KEGG; hsa:79888; -.
DR MANE-Select; ENST00000283415.4; ENSP00000283415.3; NM_024830.5; NP_079106.3.
DR UCSC; uc003jcm.4; human.
DR CTD; 79888; -.
DR DisGeNET; 79888; -.
DR GeneCards; LPCAT1; -.
DR HGNC; HGNC:25718; LPCAT1.
DR HPA; ENSG00000153395; Tissue enhanced (lung, lymphoid tissue).
DR MIM; 610472; gene.
DR neXtProt; NX_Q8NF37; -.
DR OpenTargets; ENSG00000153395; -.
DR PharmGKB; PA162394232; -.
DR VEuPathDB; HostDB:ENSG00000153395; -.
DR eggNOG; KOG2898; Eukaryota.
DR eggNOG; KOG4666; Eukaryota.
DR GeneTree; ENSGT01030000234574; -.
DR HOGENOM; CLU_025017_0_1_1; -.
DR InParanoid; Q8NF37; -.
DR OMA; EIEFLPI; -.
DR OrthoDB; 1266853at2759; -.
DR PhylomeDB; Q8NF37; -.
DR TreeFam; TF323244; -.
DR BRENDA; 2.3.1.23; 2681.
DR BRENDA; 2.3.1.51; 2681.
DR BRENDA; 2.3.1.62; 2681.
DR PathwayCommons; Q8NF37; -.
DR Reactome; R-HSA-1482788; Acyl chain remodelling of PC.
DR Reactome; R-HSA-1482925; Acyl chain remodelling of PG.
DR Reactome; R-HSA-1483166; Synthesis of PA.
DR Reactome; R-HSA-1483191; Synthesis of PC.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; Q8NF37; -.
DR UniPathway; UPA00085; -.
DR BioGRID-ORCS; 79888; 18 hits in 1085 CRISPR screens.
DR ChiTaRS; LPCAT1; human.
DR GenomeRNAi; 79888; -.
DR Pharos; Q8NF37; Tbio.
DR PRO; PR:Q8NF37; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q8NF37; protein.
DR Bgee; ENSG00000153395; Expressed in upper lobe of left lung and 91 other tissues.
DR Genevisible; Q8NF37; HS.
DR GO; GO:0035577; C:azurophil granule membrane; TAS:Reactome.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005811; C:lipid droplet; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; ISS:UniProtKB.
DR GO; GO:0047184; F:1-acylglycerophosphocholine O-acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0047159; F:1-alkenylglycerophosphocholine O-acyltransferase activity; ISS:UniProtKB.
DR GO; GO:0047192; F:1-alkylglycerophosphocholine O-acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0047191; F:1-alkylglycerophosphocholine O-acyltransferase activity; IEA:Ensembl.
DR GO; GO:0047144; F:2-acylglycerol-3-phosphate O-acyltransferase activity; TAS:Reactome.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0050200; F:plasmalogen synthase activity; IEA:UniProtKB-EC.
DR GO; GO:2001246; P:negative regulation of phosphatidylcholine biosynthetic process; IEA:Ensembl.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; TAS:Reactome.
DR GO; GO:0036151; P:phosphatidylcholine acyl-chain remodeling; IDA:UniProtKB.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IEA:Ensembl.
DR GO; GO:0036148; P:phosphatidylglycerol acyl-chain remodeling; TAS:Reactome.
DR GO; GO:0008654; P:phospholipid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IEA:Ensembl.
DR GO; GO:0030163; P:protein catabolic process; IEA:Ensembl.
DR GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
DR GO; GO:0043129; P:surfactant homeostasis; IEA:Ensembl.
DR CDD; cd07991; LPLAT_LPCAT1-like; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR045252; LPCAT1-like.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR Pfam; PF01553; Acyltransferase; 1.
DR Pfam; PF13833; EF-hand_8; 1.
DR SMART; SM00054; EFh; 2.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
PE 1: Evidence at protein level;
KW Acyltransferase; Calcium; Cell membrane; Endoplasmic reticulum;
KW Golgi apparatus; Lipid biosynthesis; Lipid droplet; Lipid metabolism;
KW Membrane; Metal-binding; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Repeat; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..534
FT /note="Lysophosphatidylcholine acyltransferase 1"
FT /id="PRO_0000247064"
FT TOPO_DOM 1..57
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..78
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 79..534
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 379..414
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 451..486
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 135..140
FT /note="HXXXXD motif"
FT /evidence="ECO:0000250|UniProtKB:Q3TFD2"
FT MOTIF 531..534
FT /note="Di-lysine motif"
FT /evidence="ECO:0000305|PubMed:21498505"
FT BINDING 392
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT BINDING 394
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT BINDING 396
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT BINDING 398
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT BINDING 403
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
SQ SEQUENCE 534 AA; 59151 MW; 69A9C3AEC698F6BD CRC64;
MRLRGCGPRA APASSAGASD ARLLAPPGRN PFVHELRLSA LQKAQVALMT LTLFPVRLLV
AAAMMLLAWP LALVASLGSA EKEPEQPPAL WRKVVDFLLK AIMRTMWFAG GFHRVAVKGR
QALPTEAAIL TLAPHSSYFD AIPVTMTMSS IVMKAESRDI PIWGTLIQYI RPVFVSRSDQ
DSRRKTVEEI KRRAQSNGKW PQIMIFPEGT CTNRTCLITF KPGAFIPGAP VQPVVLRYPN
KLDTITWTWQ GPGALEILWL TLCQFHNQVE IEFLPVYSPS EEEKRNPALY ASNVRRVMAE
ALGVSVTDYT FEDCQLALAE GQLRLPADTC LLEFARLVRG LGLKPEKLEK DLDRYSERAR
MKGGEKIGIA EFAASLEVPV SDLLEDMFSL FDESGSGEVD LRECVVALSV VCRPARTLDT
IQLAFKMYGA QEDGSVGEGD LSCILKTALG VAELTVTDLF RAIDQEEKGK ITFADFHRFA
EMYPAFAEEY LYPDQTHFES CAETSPAPIP NGFCADFSPE NSDAGRKPVR KKLD
