MBOA1_MOUSE
ID MBOA1_MOUSE Reviewed; 492 AA.
AC Q8BH98; A9EDS0; Q8R3T2;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Lysophospholipid acyltransferase 1 {ECO:0000305};
DE Short=LPLAT 1;
DE EC=2.3.1.-;
DE AltName: Full=1-acylglycerophosphocholine O-acyltransferase;
DE EC=2.3.1.23 {ECO:0000250|UniProtKB:Q6ZNC8};
DE AltName: Full=1-acylglycerophosphoethanolamine O-acyltransferase MBOAT1 {ECO:0000305};
DE EC=2.3.1.n7 {ECO:0000269|PubMed:18287005};
DE AltName: Full=1-acylglycerophosphoserine O-acyltransferase MBOAT1 {ECO:0000305};
DE EC=2.3.1.n6 {ECO:0000269|PubMed:18287005};
DE AltName: Full=Lysophosphatidylethanolamine acyltransferase 1 {ECO:0000305};
DE Short=LPE acyltransferase 1 {ECO:0000303|PubMed:18287005};
DE Short=LPEAT1 {ECO:0000303|PubMed:18287005};
DE Short=Lyso-PE acyltransferase;
DE AltName: Full=Lysophosphatidylserine acyltransferase;
DE Short=LPSAT;
DE Short=Lyso-PS acyltransferase;
DE AltName: Full=Membrane-bound O-acyltransferase domain-containing protein 1;
DE Short=O-acyltransferase domain-containing protein 1;
GN Name=Mboat1 {ECO:0000312|MGI:MGI:2387184};
GN Synonyms=Lpeat1 {ECO:0000303|PubMed:18287005}, Oact1;
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].
RX PubMed=17890783; DOI=10.1074/jbc.m704509200;
RA Tamaki H., Shimada A., Itoh Y., Ohya M., Takase J., Miyashita M.,
RA Miyagawa H., Nozaki H., Nakayama R., Kumagai H.;
RT "LPT1 encodes a membrane-bound O-acyltransferase involved in the acylation
RT of lysophospholipids in the yeast Saccharomyces cerevisiae.";
RL J. Biol. Chem. 282:34288-34298(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND CATALYTIC ACTIVITY.
RX PubMed=18287005; DOI=10.1073/pnas.0712245105;
RA Hishikawa D., Shindou H., Kobayashi S., Nakanishi H., Taguchi R.,
RA Shimizu T.;
RT "Discovery of a lysophospholipid acyltransferase family essential for
RT membrane asymmetry and diversity.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:2830-2835(2008).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Amnion, and Lung;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II, and FVB/N; TISSUE=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 [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=27048541; DOI=10.1096/fj.201500097r;
RA Tabe S., Hikiji H., Ariyoshi W., Hashidate-Yoshida T., Shindou H.,
RA Okinaga T., Shimizu T., Tominaga K., Nishihara T.;
RT "Lysophosphatidylethanolamine acyltransferase 1/membrane-bound O-
RT acyltransferase 1 regulates morphology and function of P19C6 cell-derived
RT neurons.";
RL FASEB J. 30:2591-2601(2016).
CC -!- FUNCTION: Acyltransferase which catalyzes the transfert of an acyl
CC group from an acyl-CoA towards a lysophospholipid producing a
CC phospholipid and participates in the reacylation step of the
CC phospholipid remodeling pathway also known as the Lands cycle
CC (PubMed:18287005). Acts on lysophosphatidylserine (1-acyl-2-hydroxy-sn-
CC glycero-3-phospho-L-serine or LPS) and lysophosphatidylethanolamine (1-
CC acyl-sn-glycero-3-phosphoethanolamine or LPE), and to a lesser extend
CC lysophosphatidylcholine (PubMed:18287005). Prefers oleoyl-CoA as the
CC acyl donor and 1-oleoyl-LPE as acceptor (PubMed:18287005). May play a
CC role in neurite outgrowth during neuronal differentiation
CC (PubMed:27048541). {ECO:0000269|PubMed:18287005,
CC ECO:0000269|PubMed:27048541}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphoethanolamine + an acyl-CoA = a
CC 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CoA;
CC Xref=Rhea:RHEA:32995, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:64381, ChEBI:CHEBI:64612; EC=2.3.1.n7;
CC Evidence={ECO:0000269|PubMed:18287005};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32996;
CC Evidence={ECO:0000305|PubMed:18287005};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phospho-L-serine + an acyl-CoA = a 1,2-
CC diacyl-sn-glycero-3-phospho-L-serine + CoA; Xref=Rhea:RHEA:33191,
CC ChEBI:CHEBI:57262, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:64379; EC=2.3.1.n6;
CC Evidence={ECO:0000269|PubMed:18287005};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33192;
CC Evidence={ECO:0000305|PubMed:18287005};
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:0000250|UniProtKB:Q6ZNC8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12938;
CC Evidence={ECO:0000250|UniProtKB:Q6ZNC8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-O-(1Z-alkenyl)-sn-glycero-3-
CC phosphoethanolamine = 1-O-(1Z)-alkenyl-2-(9Z)-octadecenoyl-sn-
CC glycero-3-phosphoethanolamine + CoA; Xref=Rhea:RHEA:37631,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:77288,
CC ChEBI:CHEBI:77291; Evidence={ECO:0000269|PubMed:18287005};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37632;
CC Evidence={ECO:0000305|PubMed:18287005};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-octadecanoyl-sn-glycero-3-
CC phosphoethanolamine = 1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-
CC 3-phosphoethanolamine + CoA; Xref=Rhea:RHEA:37523, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:75036, ChEBI:CHEBI:75038;
CC Evidence={ECO:0000269|PubMed:18287005};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37524;
CC Evidence={ECO:0000305|PubMed:18287005};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-
CC phospho-L-serine = 1,2-di-(9Z)-octadecenoyl-sn-glycero-3-phospho-L-
CC serine + CoA; Xref=Rhea:RHEA:37407, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:74617, ChEBI:CHEBI:74905;
CC Evidence={ECO:0000269|PubMed:18287005};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37408;
CC Evidence={ECO:0000305|PubMed:18287005};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine + CoA; Xref=Rhea:RHEA:37499, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:74971, ChEBI:CHEBI:74986;
CC Evidence={ECO:0000269|PubMed:18287005};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37500;
CC Evidence={ECO:0000305|PubMed:18287005};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-
CC phosphoethanolamine = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-
CC 3-phosphoethanolamine + CoA; Xref=Rhea:RHEA:36015, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:73004, ChEBI:CHEBI:73007;
CC Evidence={ECO:0000269|PubMed:18287005};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36016;
CC Evidence={ECO:0000305|PubMed:18287005};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(10Z-heptadecenoyl)-sn-glycero-3-phosphoethanolamine +
CC hexadecanoyl-CoA = 1-(10Z-heptadecenoyl)-2-hexadecanoyl-sn-glycero-3-
CC phosphoethanolamine + CoA; Xref=Rhea:RHEA:65128, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57379, ChEBI:CHEBI:149768, ChEBI:CHEBI:156345;
CC Evidence={ECO:0000269|PubMed:27048541};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65129;
CC Evidence={ECO:0000305|PubMed:27048541};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine +
CC octadecanoyl-CoA = 1-(9Z-octadecenoyl)-2-octadecanoyl-sn-glycero-3-
CC phospho-L-serine + CoA; Xref=Rhea:RHEA:37403, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57394, ChEBI:CHEBI:74617, ChEBI:CHEBI:74902;
CC Evidence={ECO:0000250|UniProtKB:Q6ZNC8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37404;
CC Evidence={ECO:0000250|UniProtKB:Q6ZNC8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-hexadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-
CC phospho-L-serine = 1-(9Z-octadecenoyl)-2-(9Z-hexadecenoyl)-sn-
CC glycero-3-phospho-L-serine + CoA; Xref=Rhea:RHEA:37399,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:61540, ChEBI:CHEBI:74617,
CC ChEBI:CHEBI:74901; Evidence={ECO:0000250|UniProtKB:Q6ZNC8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37400;
CC Evidence={ECO:0000250|UniProtKB:Q6ZNC8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-
CC 3-phospho-L-serine = 1-(9Z-octadecenoyl)-2-(9Z,12Z-octadienoyl)-sn-
CC glycero-3-phospho-L-serine + CoA; Xref=Rhea:RHEA:37375,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57383, ChEBI:CHEBI:74617,
CC ChEBI:CHEBI:74892; Evidence={ECO:0000250|UniProtKB:Q6ZNC8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37376;
CC Evidence={ECO:0000250|UniProtKB:Q6ZNC8};
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:Q6ZNC8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35992;
CC Evidence={ECO:0000250|UniProtKB:Q6ZNC8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-(10Z-heptadecenoyl)-sn-glycero-3-
CC phosphoethanolamine = 1-(10Z-heptadecenoyl)-2-(9Z-octadecenoyl)-sn-
CC glycero-3-phosphoethanolamine + CoA; Xref=Rhea:RHEA:65136,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:149768,
CC ChEBI:CHEBI:156344; Evidence={ECO:0000269|PubMed:27048541};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65137;
CC Evidence={ECO:0000305|PubMed:27048541};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.7 uM for oleoyl-CoA (in the presence of LPE C18:1 as
CC cosubstrate) {ECO:0000269|PubMed:18287005};
CC KM=3.9 uM for oleoyl-CoA (in the presence of LPS C18:1 as
CC cosubstrate) {ECO:0000269|PubMed:18287005};
CC KM=7.75 uM for LPE C18:1 (in the presence of oleoyl-CoA as
CC cosubstrate) {ECO:0000269|PubMed:18287005};
CC KM=2.25 uM for LPS C18:1 (in the presence of oleoyl-CoA as
CC cosubstrate) {ECO:0000269|PubMed:18287005};
CC Vmax=9.125 nmol/min/mg enzyme with oleoyl-CoA and LPE C18:1 as
CC substrates {ECO:0000269|PubMed:18287005};
CC Vmax=4.7 nmol/min/mg enzyme with oleoyl-CoA and LPS C18:1 as
CC substrates {ECO:0000269|PubMed:18287005};
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC {ECO:0000269|PubMed:18287005}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}. Endoplasmic reticulum
CC {ECO:0000269|PubMed:18287005}.
CC -!- TISSUE SPECIFICITY: Highly expressed in stomach, epididymis, and colon.
CC {ECO:0000269|PubMed:18287005}.
CC -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AB305045; BAF93901.1; -; mRNA.
DR EMBL; AB297382; BAG12121.1; -; mRNA.
DR EMBL; AK033388; BAC28261.1; -; mRNA.
DR EMBL; AK146984; BAE27587.1; -; mRNA.
DR EMBL; AL645749; CAI24381.1; -; Genomic_DNA.
DR EMBL; AL450321; CAI24381.1; JOINED; Genomic_DNA.
DR EMBL; AL450321; CAI24665.1; -; Genomic_DNA.
DR EMBL; AL645749; CAI24665.1; JOINED; Genomic_DNA.
DR EMBL; CH466561; EDL32389.1; -; Genomic_DNA.
DR EMBL; CH466561; EDL32390.1; -; Genomic_DNA.
DR EMBL; BC023845; AAH23845.1; -; mRNA.
DR EMBL; BC024653; AAH24653.1; -; mRNA.
DR CCDS; CCDS26414.1; -.
DR RefSeq; NP_705774.1; NM_153546.4.
DR AlphaFoldDB; Q8BH98; -.
DR SMR; Q8BH98; -.
DR STRING; 10090.ENSMUSP00000045441; -.
DR ChEMBL; CHEMBL1255152; -.
DR SwissLipids; SLP:000000288; -.
DR iPTMnet; Q8BH98; -.
DR PhosphoSitePlus; Q8BH98; -.
DR EPD; Q8BH98; -.
DR MaxQB; Q8BH98; -.
DR PaxDb; Q8BH98; -.
DR PRIDE; Q8BH98; -.
DR ProteomicsDB; 293417; -.
DR Antibodypedia; 25215; 29 antibodies from 13 providers.
DR DNASU; 218121; -.
DR Ensembl; ENSMUST00000047311; ENSMUSP00000045441; ENSMUSG00000038732.
DR GeneID; 218121; -.
DR KEGG; mmu:218121; -.
DR UCSC; uc007pyt.1; mouse.
DR CTD; 154141; -.
DR MGI; MGI:2387184; Mboat1.
DR VEuPathDB; HostDB:ENSMUSG00000038732; -.
DR eggNOG; KOG2704; Eukaryota.
DR GeneTree; ENSGT01030000234564; -.
DR HOGENOM; CLU_011340_3_0_1; -.
DR InParanoid; Q8BH98; -.
DR OMA; WHGTRPG; -.
DR OrthoDB; 881262at2759; -.
DR PhylomeDB; Q8BH98; -.
DR TreeFam; TF314906; -.
DR Reactome; R-MMU-1482801; Acyl chain remodelling of PS.
DR Reactome; R-MMU-1482839; Acyl chain remodelling of PE.
DR UniPathway; UPA00085; -.
DR BioGRID-ORCS; 218121; 2 hits in 76 CRISPR screens.
DR ChiTaRS; Mboat1; mouse.
DR PRO; PR:Q8BH98; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q8BH98; protein.
DR Bgee; ENSMUSG00000038732; Expressed in left colon and 170 other tissues.
DR Genevisible; Q8BH98; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0047184; F:1-acylglycerophosphocholine O-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0106262; F:1-acylglycerophosphoethanolamine O-acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0106263; F:1-acylglycerophosphoserine O-acyltransferase activity; ISS:UniProtKB.
DR GO; GO:0016746; F:acyltransferase activity; IBA:GO_Central.
DR GO; GO:0030258; P:lipid modification; IBA:GO_Central.
DR GO; GO:0036152; P:phosphatidylethanolamine acyl-chain remodeling; IMP:UniProtKB.
DR GO; GO:0036150; P:phosphatidylserine acyl-chain remodeling; ISS:UniProtKB.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IMP:UniProtKB.
DR GO; GO:0010975; P:regulation of neuron projection development; IMP:UniProtKB.
DR InterPro; IPR004299; MBOAT_fam.
DR Pfam; PF03062; MBOAT; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Endoplasmic reticulum; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Phospholipid biosynthesis;
KW Phospholipid metabolism; Phosphoprotein; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..492
FT /note="Lysophospholipid acyltransferase 1"
FT /id="PRO_0000273019"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 296..316
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 423..443
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 452..472
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 349
FT /evidence="ECO:0000250"
FT ACT_SITE 380
FT /evidence="ECO:0000250"
FT MOD_RES 486
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZNC8"
FT CONFLICT 99
FT /note="T -> S (in Ref. 6; AAH24653)"
FT /evidence="ECO:0000305"
FT CONFLICT 237
FT /note="M -> T (in Ref. 6; AAH24653)"
FT /evidence="ECO:0000305"
FT CONFLICT 365
FT /note="P -> S (in Ref. 6; AAH24653)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 492 AA; 56160 MW; 3DD8D88F46250B8D CRC64;
MAARPPASLS YRTTGSTCLH PLSQLLGIPL DQVNFVACQL FALSAAFWFR IYLHPGKASP
EVRHTLATIL GIYFVVFCFG WYAVHLFVLV LMCYGVMVTA SVSNIHRYSF FVAMGYLTIC
HISRIYIFHY GILTTDFSGP LMIVTQKITT LAFQVHDGLG RKAEDLSAEQ HRLAVKAKPS
LLEYLSYHLN FMSVIAGPCN NFKDYVAFIE GRHIHMKLLE VNWTQRGFQS LPEPSPMGAV
IQKLCVTLMS LLLFLTLSKS FPVTFLIDDW FVHKANFLSR LWYLYVVMQA AKPKYYFAWT
LADAVHNAAG FGFNGMDTDG KSRWDLLSNL NIWKIETATS FKMYLENWNI QTSTWLKCVC
YERVPWYPTV LTFLLSALWH GVYPGYYFTF LTGVPVTLAA RAVRNNYRHH FLSSKARKIA
YDVVTWAVTQ LAVSYTAAPF VMLAVEPTIS LYKSVFFFLH IICLLIILFL PIKPHQPQRQ
SRSPNSVKKK AD
