PCAT1_MOUSE
ID PCAT1_MOUSE Reviewed; 534 AA.
AC Q3TFD2; Q3TAX4; Q6NXZ6; Q8BG23; Q8BUX7; Q99JU6;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Lysophosphatidylcholine acyltransferase 1;
DE Short=LPC acyltransferase 1;
DE Short=LPCAT-1;
DE Short=LysoPC acyltransferase 1;
DE Short=mLPCAT1;
DE EC=2.3.1.23 {ECO:0000269|PubMed:16704971, ECO:0000269|PubMed:18156367, ECO:0000269|PubMed:18285344};
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:0000269|PubMed:16704971, ECO:0000269|PubMed:18285344};
DE AltName: Full=1-alkylglycerophosphocholine O-acetyltransferase;
DE EC=2.3.1.67 {ECO:0000269|PubMed:18285344};
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND DI-LYSINE MOTIF.
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 [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Corpora quadrigemina, Head, and Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 158-534.
RC STRAIN=C57BL/6J, and Czech II; TISSUE=Egg, and Mammary tumor;
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, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, INDUCTION, AND MUTAGENESIS OF 135-HIS--ASP-140; HIS-135;
RP ASP-140; ILE-160; ILE-162; TRP-163; 164-GLY--ARG-177; GLY-164; LEU-166;
RP ILE-167; ARG-168; TYR-169; ILE-170; ARG-171; VAL-173; PHE-174; VAL-175;
RP ARG-177; 203-ILE--GLY-209; GLU-208; GLY-209; 227-PRO--PRO-233; PRO-227;
RP PRO-230 AND PRO-233.
RX PubMed=18285344; DOI=10.1074/jbc.m708909200;
RA Harayama T., Shindou H., Ogasawara R., Suwabe A., Shimizu T.;
RT "Identification of a novel noninflammatory biosynthetic pathway of
RT platelet-activating factor.";
RL J. Biol. Chem. 283:11097-11106(2008).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION,
RP AND TISSUE 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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Exhibits both acyltransferase and acetyltransferase
CC activities (PubMed:16704971, PubMed:18285344, PubMed:18156367).
CC Activity is calcium-independent (PubMed:16704971, PubMed:18285344).
CC Catalyzes the conversion of lysophosphatidylcholine (1-acyl-sn-glycero-
CC 3-phosphocholine or LPC) into phosphatidylcholine (1,2-diacyl-sn-
CC glycero-3-phosphocholine or PC) (PubMed:16704971, PubMed:18285344,
CC PubMed:18156367). 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 (By similarity). Displays a
CC clear preference for saturated fatty acyl-CoAs, and 1-myristoyl or 1-
CC palmitoyl LPC as acyl donors and acceptors, respectively
CC (PubMed:16704971, PubMed:18285344). Involved in platelet-activating
CC factor (PAF) biosynthesis by catalyzing the conversion of the PAF
CC precursor, 1-O-alkyl-sn-glycero-3-phosphocholine (lyso-PAF) into 1-O-
CC alkyl-2-acetyl-sn-glycero-3-phosphocholine (PAF) (PubMed:18285344). May
CC synthesize phosphatidylcholine in pulmonary surfactant, thereby playing
CC a pivotal role in respiratory physiology (PubMed:16704971). Involved in
CC the regulation of lipid droplet number and size (By similarity).
CC {ECO:0000250|UniProtKB:Q1HAQ0, ECO:0000250|UniProtKB:Q8NF37,
CC ECO:0000269|PubMed:16704971, ECO:0000269|PubMed:18156367,
CC ECO:0000269|PubMed:18285344}.
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:16704971, ECO:0000269|PubMed:18156367,
CC ECO:0000269|PubMed:18285344};
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:0000269|PubMed:18285344};
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-(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:0000269|PubMed:16704971, ECO:0000269|PubMed:18285344};
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=1-hexadecanoyl-sn-glycero-3-phosphocholine + hexadecanoyl-CoA
CC = 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:35983, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:72999;
CC Evidence={ECO:0000269|PubMed:16704971, ECO:0000269|PubMed:18285344};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35984;
CC Evidence={ECO:0000305|PubMed:16704971};
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:0000269|PubMed:16704971, ECO:0000269|PubMed:18285344};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37812;
CC Evidence={ECO:0000305|PubMed:16704971};
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:0000269|PubMed:16704971, ECO:0000269|PubMed:18285344};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37820;
CC Evidence={ECO:0000305|PubMed:16704971};
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:16704971};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35852;
CC Evidence={ECO:0000305|PubMed:16704971};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-dodecanoyl-sn-glycero-3-phosphocholine + hexadecanoyl-CoA =
CC 1-dodecanoyl-2-hexadecanoyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:37511, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:74966, ChEBI:CHEBI:75017;
CC Evidence={ECO:0000269|PubMed:16704971};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37512;
CC Evidence={ECO:0000305|PubMed:16704971};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-tetradecanoyl-sn-glycero-3-phosphocholine + hexadecanoyl-CoA
CC = 1-tetradecanoyl-2-hexadecanoyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:37655, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:64489, ChEBI:CHEBI:75062;
CC Evidence={ECO:0000269|PubMed:16704971};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37656;
CC Evidence={ECO:0000305|PubMed:16704971};
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:0000269|PubMed:16704971};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37840;
CC Evidence={ECO:0000305|PubMed:16704971};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-sn-glycero-3-phosphocholine + hexadecanoyl-CoA
CC = 1-octadecanoyl-2-hexadecanoyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:37527, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:73858, ChEBI:CHEBI:75026;
CC Evidence={ECO:0000269|PubMed:18285344};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37528;
CC Evidence={ECO:0000305|PubMed:18285344};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine +
CC hexadecanoyl-CoA = 1-(9Z-octadecenoyl)-2-hexadecanoyl-sn-glycero-3-
CC phosphocholine + CoA; Xref=Rhea:RHEA:37383, ChEBI:CHEBI:28610,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:74667;
CC Evidence={ECO:0000269|PubMed:16704971};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37384;
CC Evidence={ECO:0000305|PubMed:16704971};
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:0000269|PubMed:16704971};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37844;
CC Evidence={ECO:0000305|PubMed:16704971};
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:0000269|PubMed:16704971, ECO:0000269|PubMed:18285344};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37856;
CC Evidence={ECO:0000305|PubMed:16704971};
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:0000269|PubMed:16704971, ECO:0000269|PubMed:18285344};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37860;
CC Evidence={ECO:0000305|PubMed:16704971};
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:0000269|PubMed:16704971, ECO:0000269|PubMed:18285344};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37864;
CC Evidence={ECO:0000305|PubMed:16704971};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + dodecanoyl-CoA =
CC 1-hexadecanoyl-2-dodecanoyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:37515, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:75018;
CC Evidence={ECO:0000269|PubMed:16704971, ECO:0000269|PubMed:18285344};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37516;
CC Evidence={ECO:0000305|PubMed:16704971};
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:0000269|PubMed:16704971, ECO:0000269|PubMed:18285344};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37868;
CC Evidence={ECO:0000305|PubMed:16704971};
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:16704971};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35992;
CC Evidence={ECO:0000305|PubMed:16704971};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + 1-hexadecanoyl-sn-glycero-3-
CC phosphocholine = 1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-
CC glycero-3-phosphocholine + CoA; Xref=Rhea:RHEA:35995,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57383, ChEBI:CHEBI:72998,
CC ChEBI:CHEBI:73002; Evidence={ECO:0000269|PubMed:16704971};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35996;
CC Evidence={ECO:0000305|PubMed:16704971};
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:0000269|PubMed:16704971};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37476;
CC Evidence={ECO:0000305|PubMed:16704971};
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:0000269|PubMed:18285344};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37704;
CC Evidence={ECO:0000305|PubMed:18285344};
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:0000269|PubMed:18285344};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43265;
CC Evidence={ECO:0000305|PubMed:18285344};
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:0000269|PubMed:18285344};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37720;
CC Evidence={ECO:0000305|PubMed:18285344};
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 -!- ACTIVITY REGULATION: Not activated by inflammatory stimulation
CC (PubMed:18285344). Inhibited by Cu(2+), Fe(2+), Ca(2+) and Mg(2+)
CC (PubMed:18285344, PubMed:18156367). Activity is not affected by Co(2+)
CC or Mn(2+) (PubMed:18285344). {ECO:0000269|PubMed:18156367,
CC ECO:0000269|PubMed:18285344}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.3 uM for 1-palmitoyl-LPC {ECO:0000269|PubMed:16704971,
CC ECO:0000269|PubMed:18285344};
CC KM=3 uM for palmitoyl-CoA {ECO:0000269|PubMed:16704971,
CC ECO:0000269|PubMed:18285344};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:16704971,
CC ECO:0000269|PubMed:18285344};
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16704971}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q8NF37}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:16704971}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q8NF37}. Cell membrane
CC {ECO:0000305|PubMed:18156367}; 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q3TFD2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3TFD2-2; Sequence=VSP_019914;
CC Name=3;
CC IsoId=Q3TFD2-3; Sequence=VSP_019913;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in lung where it is
CC enriched in alveolar type II cells. Expressed at lower levels in spleen
CC and brain. Also detected in erythroleukemic cells and reticulocytes.
CC Weakly or not expressed in other tissues. {ECO:0000269|PubMed:16704971,
CC ECO:0000269|PubMed:16864775, ECO:0000269|PubMed:18156367}.
CC -!- DEVELOPMENTAL STAGE: Expression increases steadily throughout
CC embryogenesis and decreases slightly in the adult.
CC {ECO:0000269|PubMed:16864775}.
CC -!- INDUCTION: Constitutively expressed. Not induced by inflammatory
CC stimulation. {ECO:0000269|PubMed:18285344}.
CC -!- DOMAIN: The di-lysine motif may confer endoplasmic reticulum
CC localization. {ECO:0000305|PubMed:16704971}.
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:0000269|PubMed:18285344}.
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH05662.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC32594.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC32760.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB244717; BAE94687.2; -; mRNA.
DR EMBL; AK046079; BAC32594.1; ALT_INIT; mRNA.
DR EMBL; AK046507; BAC32760.1; ALT_INIT; mRNA.
DR EMBL; AK081865; BAC38353.1; -; mRNA.
DR EMBL; AK155286; BAE33166.1; -; mRNA.
DR EMBL; AK169190; BAE40966.1; -; mRNA.
DR EMBL; AK170723; BAE41980.1; -; mRNA.
DR EMBL; AK171582; BAE42540.1; -; mRNA.
DR EMBL; BC005662; AAH05662.1; ALT_INIT; mRNA.
DR EMBL; BC066809; AAH66809.1; -; mRNA.
DR CCDS; CCDS36726.1; -. [Q3TFD2-1]
DR RefSeq; NP_663351.3; NM_145376.5. [Q3TFD2-1]
DR AlphaFoldDB; Q3TFD2; -.
DR SMR; Q3TFD2; -.
DR BioGRID; 229195; 6.
DR STRING; 10090.ENSMUSP00000022099; -.
DR SwissLipids; SLP:000000297; -.
DR iPTMnet; Q3TFD2; -.
DR PhosphoSitePlus; Q3TFD2; -.
DR SwissPalm; Q3TFD2; -.
DR EPD; Q3TFD2; -.
DR MaxQB; Q3TFD2; -.
DR PaxDb; Q3TFD2; -.
DR PeptideAtlas; Q3TFD2; -.
DR PRIDE; Q3TFD2; -.
DR ProteomicsDB; 294337; -. [Q3TFD2-1]
DR ProteomicsDB; 294338; -. [Q3TFD2-2]
DR ProteomicsDB; 294339; -. [Q3TFD2-3]
DR Antibodypedia; 1587; 229 antibodies from 28 providers.
DR DNASU; 210992; -.
DR Ensembl; ENSMUST00000022099; ENSMUSP00000022099; ENSMUSG00000021608. [Q3TFD2-1]
DR Ensembl; ENSMUST00000223060; ENSMUSP00000152190; ENSMUSG00000021608. [Q3TFD2-2]
DR GeneID; 210992; -.
DR KEGG; mmu:210992; -.
DR UCSC; uc007rdk.1; mouse. [Q3TFD2-1]
DR CTD; 79888; -.
DR MGI; MGI:2384812; Lpcat1.
DR VEuPathDB; HostDB:ENSMUSG00000021608; -.
DR eggNOG; KOG4666; Eukaryota.
DR GeneTree; ENSGT01030000234574; -.
DR HOGENOM; CLU_025017_0_1_1; -.
DR InParanoid; Q3TFD2; -.
DR OMA; EIEFLPI; -.
DR OrthoDB; 1266853at2759; -.
DR PhylomeDB; Q3TFD2; -.
DR TreeFam; TF323244; -.
DR BRENDA; 2.3.1.23; 3474.
DR BRENDA; 2.3.1.51; 3474.
DR BRENDA; 2.3.1.62; 3474.
DR BRENDA; 2.3.1.67; 3474.
DR Reactome; R-MMU-1482788; Acyl chain remodelling of PC.
DR Reactome; R-MMU-1482925; Acyl chain remodelling of PG.
DR Reactome; R-MMU-1483166; Synthesis of PA.
DR Reactome; R-MMU-1483191; Synthesis of PC.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR UniPathway; UPA00085; -.
DR BioGRID-ORCS; 210992; 5 hits in 77 CRISPR screens.
DR ChiTaRS; Lpcat1; mouse.
DR PRO; PR:Q3TFD2; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q3TFD2; protein.
DR Bgee; ENSMUSG00000021608; Expressed in left lung and 259 other tissues.
DR ExpressionAtlas; Q3TFD2; baseline and differential.
DR Genevisible; Q3TFD2; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA: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; ISO:MGI.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; IDA:UniProtKB.
DR GO; GO:0047192; F:1-alkylglycerophosphocholine O-acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0047191; F:1-alkylglycerophosphocholine O-acyltransferase activity; IDA:UniProtKB.
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; IDA:MGI.
DR GO; GO:0036151; P:phosphatidylcholine acyl-chain remodeling; ISO:MGI.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IDA:MGI.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IDA:MGI.
DR GO; GO:0030163; P:protein catabolic process; IDA:MGI.
DR GO; GO:0060041; P:retina development in camera-type eye; IMP:MGI.
DR GO; GO:0043129; P:surfactant homeostasis; IDA:MGI.
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; Alternative splicing; Calcium; Cell membrane;
KW Endoplasmic reticulum; Golgi apparatus; Lipid biosynthesis; Lipid droplet;
KW Lipid metabolism; 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_0000247065"
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:0000269|PubMed:18285344"
FT MOTIF 531..534
FT /note="Di-lysine motif"
FT /evidence="ECO:0000305|PubMed:16704971"
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"
FT VAR_SEQ 1..203
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019913"
FT VAR_SEQ 1..48
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019914"
FT MUTAGEN 135..140
FT /note="Missing: Abolishes activity."
FT /evidence="ECO:0000269|PubMed:18285344"
FT MUTAGEN 135
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:18285344"
FT MUTAGEN 140
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:18285344"
FT MUTAGEN 160
FT /note="I->A: No effect on activity for acetyl-CoA. Reduced
FT activity for palmitoyl-CoA."
FT /evidence="ECO:0000269|PubMed:18285344"
FT MUTAGEN 162
FT /note="I->A: Greatly reduced activity."
FT /evidence="ECO:0000269|PubMed:18285344"
FT MUTAGEN 163
FT /note="W->A: Greatly reduced activity."
FT /evidence="ECO:0000269|PubMed:18285344"
FT MUTAGEN 164..177
FT /note="Missing: Abolishes activity."
FT /evidence="ECO:0000269|PubMed:18285344"
FT MUTAGEN 164
FT /note="G->A: Slightly increased activity."
FT /evidence="ECO:0000269|PubMed:18285344"
FT MUTAGEN 166
FT /note="L->A: Greatly reduced activity."
FT /evidence="ECO:0000269|PubMed:18285344"
FT MUTAGEN 167
FT /note="I->A: Slightly reduced activity."
FT /evidence="ECO:0000269|PubMed:18285344"
FT MUTAGEN 168
FT /note="R->A: Reduced activity."
FT /evidence="ECO:0000269|PubMed:18285344"
FT MUTAGEN 169
FT /note="Y->A: Slightly reduced activity."
FT /evidence="ECO:0000269|PubMed:18285344"
FT MUTAGEN 170
FT /note="I->A: Slightly reduced activity."
FT /evidence="ECO:0000269|PubMed:18285344"
FT MUTAGEN 171
FT /note="R->A: Reduced activity."
FT /evidence="ECO:0000269|PubMed:18285344"
FT MUTAGEN 173
FT /note="V->A: Greatly reduced activity."
FT /evidence="ECO:0000269|PubMed:18285344"
FT MUTAGEN 174
FT /note="F->A: Loss of lyso-PAFAT activity. LPCAT activity is
FT partially reduced."
FT /evidence="ECO:0000269|PubMed:18285344"
FT MUTAGEN 175
FT /note="V->A: No activity for acetyl-CoA. Activity for
FT palmitoyl-CoA decreased."
FT /evidence="ECO:0000269|PubMed:18285344"
FT MUTAGEN 177
FT /note="R->A: Loss of lyso-PAFAT activity. LPCAT activity is
FT partially reduced."
FT /evidence="ECO:0000269|PubMed:18285344"
FT MUTAGEN 203..209
FT /note="Missing: Abolishes activity."
FT /evidence="ECO:0000269|PubMed:18285344"
FT MUTAGEN 208
FT /note="E->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:18285344"
FT MUTAGEN 209
FT /note="G->A: Reduced activity."
FT /evidence="ECO:0000269|PubMed:18285344"
FT MUTAGEN 227..233
FT /note="Missing: Abolishes activity."
FT /evidence="ECO:0000269|PubMed:18285344"
FT MUTAGEN 227
FT /note="P->A: Reduced activity."
FT /evidence="ECO:0000269|PubMed:18285344"
FT MUTAGEN 230
FT /note="P->A: Reduced activity."
FT /evidence="ECO:0000269|PubMed:18285344"
FT MUTAGEN 233
FT /note="P->A: Reduced activity."
FT /evidence="ECO:0000269|PubMed:18285344"
FT CONFLICT 25
FT /note="A -> T (in Ref. 3; BAC38353)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="A -> T (in Ref. 4; AAH66809)"
FT /evidence="ECO:0000305"
FT CONFLICT 232
FT /note="Q -> R (in Ref. 3; BAE42540)"
FT /evidence="ECO:0000305"
FT CONFLICT 272
FT /note="E -> G (in Ref. 4; AAH66809)"
FT /evidence="ECO:0000305"
FT CONFLICT 338
FT /note="V -> M (in Ref. 3; BAC32594/BAC32760)"
FT /evidence="ECO:0000305"
FT CONFLICT 442
FT /note="S -> P (in Ref. 4; AAH66809)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 534 AA; 59744 MW; 50C1EF4A5D494DF2 CRC64;
MRLRGRGPRA APSSSSGAGD ARRLAPPGRN PFVHELRLSA LQKAQVAFMT LTLFPIRLLF
AAFMMLLAWP FALLASLGPP 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 PEDGSIDEAN LSCILKTALG VSELTVTDLF QAIDQEDKGR ITFDDFCGFA
EMYPDYAEDY LYPDQTHFDS CAQTPPAPTP NGFCIDFSPE NSDFGRKNSC KKAD
