PCAT1_RAT
ID PCAT1_RAT Reviewed; 534 AA.
AC Q1HAQ0;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 113.
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:16864775};
DE AltName: Full=1-acylglycerol-3-phosphate O-acyltransferase;
DE EC=2.3.1.51 {ECO:0000269|PubMed:16864775};
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;
GN Name=Lpcat1; Synonyms=Aytl2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, INDUCTION, AND ACTIVITY REGULATION.
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 46-534, AND TISSUE SPECIFICITY.
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).
CC -!- FUNCTION: Exhibits acyltransferase activity (PubMed:16864775). Exhibits
CC acetyltransferase activity (By similarity). Activity is calcium-
CC independent (By similarity). Catalyzes the conversion of
CC lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine or LPC)
CC into phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine or PC)
CC (PubMed:16864775). Catalyzes the conversion 1-acyl-sn-glycerol-3-
CC phosphate (lysophosphatidic acid or LPA) into 1,2-diacyl-sn-glycerol-3-
CC phosphate (phosphatidic acid or PA) by incorporating an acyl moiety at
CC the sn-2 position of the glycerol backbone (PubMed:16864775). Displays
CC a clear preference for saturated fatty acyl-CoAs, and 1-myristoyl or 1-
CC palmitoyl LPC as acyl donors and acceptors, respectively (By
CC similarity). Involved in platelet-activating factor (PAF) biosynthesis
CC by catalyzing the conversion of the PAF precursor, 1-O-alkyl-sn-
CC glycero-3-phosphocholine (lyso-PAF) into 1-O-alkyl-2-acetyl-sn-glycero-
CC 3-phosphocholine (PAF) (By similarity). May synthesize
CC phosphatidylcholine in pulmonary surfactant, thereby playing a pivotal
CC role in respiratory physiology (PubMed:16864775). Involved in the
CC regulation of lipid droplet number and size (By similarity).
CC {ECO:0000250|UniProtKB:Q3TFD2, ECO:0000250|UniProtKB:Q8NF37,
CC ECO:0000269|PubMed:16864775}.
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:16864775};
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=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:16864775};
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:0000269|PubMed:16864775};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33204;
CC Evidence={ECO:0000305|PubMed:16864775};
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:0000269|PubMed:16864775};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37804;
CC Evidence={ECO:0000305|PubMed:16864775};
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:0000269|PubMed:16864775};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33316;
CC Evidence={ECO:0000305|PubMed:16864775};
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:0000269|PubMed:16864775};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37808;
CC Evidence={ECO:0000305|PubMed:16864775};
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)-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:0000250|UniProtKB:Q3TFD2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35992;
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 -!- ACTIVITY REGULATION: Activity is stimulated by Mg(2+) or Mn(2+).
CC {ECO:0000269|PubMed:16864775}.
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q8NF37}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q8NF37}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q3TFD2}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q8NF37}. Cell membrane
CC {ECO:0000250|UniProtKB:Q8NF37}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q8NF37}. Lipid droplet
CC {ECO:0000250|UniProtKB:Q8NF37}. Note=May adopt a monotopic topology
CC when embedded in the lipid monolayer of the lipid droplet, with both
CC termini exposed to the cytoplasm. {ECO:0000250|UniProtKB:Q8NF37}.
CC -!- TISSUE SPECIFICITY: Enriched in alveolar type II cells of lung. Also
CC highly expressed in stomach. {ECO:0000269|PubMed:16704971,
CC ECO:0000269|PubMed:16864775}.
CC -!- INDUCTION: By FGF7. {ECO:0000269|PubMed:16864775}.
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}.
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DR EMBL; AABR03001349; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03001854; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB244983; BAE94689.2; -; mRNA.
DR RefSeq; NP_001094205.1; NM_001100735.1.
DR AlphaFoldDB; Q1HAQ0; -.
DR SMR; Q1HAQ0; -.
DR STRING; 10116.ENSRNOP00000024111; -.
DR SwissLipids; SLP:000000296; -.
DR SwissPalm; Q1HAQ0; -.
DR jPOST; Q1HAQ0; -.
DR PaxDb; Q1HAQ0; -.
DR PRIDE; Q1HAQ0; -.
DR Ensembl; ENSRNOT00000024111; ENSRNOP00000024111; ENSRNOG00000017930.
DR GeneID; 361467; -.
DR KEGG; rno:361467; -.
DR UCSC; RGD:1311599; rat.
DR CTD; 79888; -.
DR RGD; 1311599; Lpcat1.
DR eggNOG; KOG4666; Eukaryota.
DR GeneTree; ENSGT01030000234574; -.
DR HOGENOM; CLU_025017_0_1_1; -.
DR InParanoid; Q1HAQ0; -.
DR OMA; EIEFLPI; -.
DR OrthoDB; 1266853at2759; -.
DR PhylomeDB; Q1HAQ0; -.
DR TreeFam; TF323244; -.
DR BRENDA; 2.3.1.23; 5301.
DR Reactome; R-RNO-1482788; Acyl chain remodelling of PC.
DR Reactome; R-RNO-1482925; Acyl chain remodelling of PG.
DR Reactome; R-RNO-1483166; Synthesis of PA.
DR Reactome; R-RNO-1483191; Synthesis of PC.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR UniPathway; UPA00085; -.
DR PRO; PR:Q1HAQ0; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000017930; Expressed in lung and 20 other tissues.
DR Genevisible; Q1HAQ0; RN.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IDA: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; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0036151; P:phosphatidylcholine acyl-chain remodeling; ISO:RGD.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IEA:Ensembl.
DR GO; GO:0008654; P:phospholipid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; ISO:RGD.
DR GO; GO:0030163; P:protein catabolic process; IEA:Ensembl.
DR GO; GO:0060041; P:retina development in camera-type eye; ISO:RGD.
DR GO; GO:0043129; P:surfactant homeostasis; ISO:RGD.
DR CDD; cd07991; LPLAT_LPCAT1-like; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
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; 3.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 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_0000247066"
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..25
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:0000250|UniProtKB:Q3TFD2"
FT BINDING 392
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 394
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 398
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 403
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ SEQUENCE 534 AA; 59762 MW; 952C0478DC66738A CRC64;
MRLRGRGPRA APSSSSGAGD ARRLAPPGRN PFVHELRLSA LQKAQVAFMT LTLFPIRLLF
AAFMMLLAWP FALVASLGPP DKEPEQPLAL WRKVVDFLLK AIMRTMWFAG GFHRVAVKGR
QALPTEAAIL TLAPHSSYFD AIPVTMTMSS IVMKAESRDI PIWGTLIRYI RPVFVSRSDQ
DSRRKTVEEI KRRAQSNGKW PQIMIFPEGT CTNRTCLITF KPGAFIPGVP VQPVVLRYPN
KLDTITWTWQ GPGALKILWL TLCQFQNQVE IEFLPVYCPS EEEKRNPALY ASNVRRVMAK
ALGVSVTDYT FEDCQLALAE GQLRLPADTC LLEFARLVRG LGLKPENLEK DLDKYSESAR
MKRGEKIRLP EFAAYLEVPV SDALEDMFSL FDESGGGEID LREYVVALSV VCRPSQTLAT
IQLAFKMYGS PEDGSIDEAD LSCILKTALG ISELTVTDLF QAIDQEERGR ITFDDFCGFA
EMYPDFAEDY LYPDQTHSDS CAQTPPAPTP NGFCIDFSPE HSDFGRKNSC KKVD
