MBOA2_MOUSE
ID MBOA2_MOUSE Reviewed; 519 AA.
AC Q8R3I2; A9EDS7; Q8BHH5; Q8BM56; Q8R192; Q9CZ73;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Lysophospholipid acyltransferase 2 {ECO:0000305};
DE Short=LPLAT 2;
DE EC=2.3.1.- {ECO:0000269|PubMed:18287005};
DE AltName: Full=1-acylglycerophosphocholine O-acyltransferase;
DE EC=2.3.1.23 {ECO:0000269|PubMed:18287005};
DE AltName: Full=1-acylglycerophosphoethanolamine O-acyltransferase;
DE EC=2.3.1.n7 {ECO:0000269|PubMed:18287005};
DE AltName: Full=Lysophosphatidylcholine acyltransferase;
DE Short=LPCAT;
DE Short=Lyso-PC acyltransferase;
DE AltName: Full=Lysophosphatidylcholine acyltransferase 4 {ECO:0000303|PubMed:29196633};
DE Short=Lyso-PC acyltransferase 4;
DE Short=mLPCAT4;
DE AltName: Full=Lysophosphatidylethanolamine acyltransferase;
DE Short=LPEAT;
DE Short=Lyso-PE acyltransferase;
DE AltName: Full=Membrane-bound O-acyltransferase domain-containing protein 2;
DE Short=O-acyltransferase domain-containing protein 2;
GN Name=Mboat2 {ECO:0000312|MGI:MGI:1914466};
GN Synonyms=Lpcat4 {ECO:0000303|PubMed:29196633}, Oact2;
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).
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] (ISOFORM 1), FUNCTION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND CATALYTIC
RP 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] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Embryoid bodies, Medulla oblongata, and Testis;
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).
RC STRAIN=Czech II; TISSUE=Eye, 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, and Lung;
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).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION.
RX PubMed=29196633; DOI=10.1038/s41598-017-16902-4;
RA Tabe S., Hikiji H., Ariyoshi W., Hashidate-Yoshida T., Shindou H.,
RA Shimizu T., Okinaga T., Seta Y., Tominaga K., Nishihara T.;
RT "Lysophosphatidylcholine acyltransferase 4 is involved in chondrogenic
RT differentiation of ATDC5 cells.";
RL Sci. Rep. 7:16701-16701(2017).
CC -!- FUNCTION: Acyltransferase which catalyzes the transfert of an acyl
CC group from an acyl-CoA to a lysophospholipid leading to the production
CC of a phospholipid and participates in the reacylation step of the
CC phospholipid remodeling pathway also known as the Lands cycle
CC (PubMed:18287005, PubMed:29196633). Catalyzes the acylation of
CC lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine or LPC) and
CC to a lesser extend lysophosphatidylethanolamine (1-acyl-sn-glycero-3-
CC phosphoethanolamine or LPE) (PubMed:18287005, PubMed:29196633). Does
CC not acylates lysophosphatidic acid (LPA) and lysophosphatidylserine
CC (PubMed:18287005). Prefers oleoyl-CoA as the acyl donor
CC (PubMed:18287005, PubMed:29196633). May be involved in chondrocyte
CC differentiation (PubMed:29196633). {ECO:0000269|PubMed:18287005,
CC ECO:0000269|PubMed:29196633}.
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:18287005};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12938;
CC Evidence={ECO:0000269|PubMed:18287005};
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:0000269|PubMed:18287005};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-O-(1Z-alkenyl)-sn-glycero-3-
CC phosphocholine = 1-O-(1Z)-alkenyl-2-(9Z)-octadecenoyl-sn-glycero-3-
CC phosphocholine + CoA; Xref=Rhea:RHEA:37627, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:77287, ChEBI:CHEBI:77294;
CC Evidence={ECO:0000269|PubMed:18287005};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37628;
CC Evidence={ECO:0000269|PubMed:18287005};
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:0000269|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:0000269|PubMed:18287005};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-octadecanoyl-sn-glycero-3-
CC phosphocholine = 1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphocholine + CoA; Xref=Rhea:RHEA:37519, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:73858, ChEBI:CHEBI:75034;
CC Evidence={ECO:0000269|PubMed:18287005};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37520;
CC Evidence={ECO:0000269|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:0000269|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:0000269|PubMed:18287005};
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:18287005, ECO:0000269|PubMed:29196633};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35992;
CC Evidence={ECO:0000269|PubMed:18287005, ECO:0000269|PubMed:29196633};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-hexadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-
CC phosphocholine = 1-hexadecanoyl-2-(9Z-hexadecenoyl)-sn-glycero-3-
CC phosphocholine + CoA; Xref=Rhea:RHEA:37207, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:61540, ChEBI:CHEBI:72998, ChEBI:CHEBI:74000;
CC Evidence={ECO:0000250|UniProtKB:Q6ZWT7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37208;
CC Evidence={ECO:0000250|UniProtKB:Q6ZWT7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-hexadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-
CC phosphoethanolamine = 1-hexadecanoyl-2-(9Z)-hexadecenoyl-sn-glycero-
CC 3-phosphoethanolamine + CoA; Xref=Rhea:RHEA:37419, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:61540, ChEBI:CHEBI:73004, ChEBI:CHEBI:73999;
CC Evidence={ECO:0000250|UniProtKB:Q6ZWT7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37420;
CC Evidence={ECO:0000250|UniProtKB:Q6ZWT7};
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:Q6ZWT7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35996;
CC Evidence={ECO:0000250|UniProtKB:Q6ZWT7};
CC -!- ACTIVITY REGULATION: Partially inhibited by thimerosal.
CC {ECO:0000250|UniProtKB:Q6ZWT7}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.3 uM for oleoyl-CoA (in the presence of LPC C16:0 as
CC cosubstrate) {ECO:0000269|PubMed:18287005};
CC KM=48.15 uM for oleoyl-CoA (in the presence of LPE C16:0 as
CC cosubstrate) {ECO:0000269|PubMed:18287005};
CC KM=7.9 uM for LPC C16:0 (in the presence of oleoyl-CoA as
CC cosubstrate) {ECO:0000269|PubMed:18287005};
CC KM=27.7 uM for LPE C16:0 (in the presence of oleoyl-CoA as
CC cosubstrate) {ECO:0000269|PubMed:18287005};
CC Vmax=24.24 nmol/min/mg enzyme with oleoyl-CoA and LPC C16:0 as
CC substrates {ECO:0000269|PubMed:18287005};
CC Vmax=26.3 nmol/min/mg enzyme with oleoyl-CoA and LPE C16:0 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8R3I2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8R3I2-2; Sequence=VSP_022458;
CC Name=3;
CC IsoId=Q8R3I2-3; Sequence=VSP_022457, VSP_022459;
CC -!- TISSUE SPECIFICITY: Highly expressed in epididymis, brain, testis, and
CC ovary. {ECO:0000269|PubMed:18287005}.
CC -!- INDUCTION: Increased during chondrogenic differentiation.
CC {ECO:0000269|PubMed:29196633}.
CC -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC27567.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB305046; BAF93902.1; -; mRNA.
DR EMBL; AB297383; BAG12122.1; -; mRNA.
DR EMBL; AK012931; BAB28556.1; -; mRNA.
DR EMBL; AK031824; BAC27567.1; ALT_INIT; mRNA.
DR EMBL; AK033106; BAC28154.1; -; mRNA.
DR EMBL; AK034873; BAC28863.1; -; mRNA.
DR EMBL; AK076045; BAC36144.1; -; mRNA.
DR EMBL; BC025020; AAH25020.1; -; mRNA.
DR CCDS; CCDS25845.1; -. [Q8R3I2-1]
DR CCDS; CCDS36423.1; -. [Q8R3I2-2]
DR RefSeq; NP_001076810.1; NM_001083341.1. [Q8R3I2-2]
DR RefSeq; NP_080313.2; NM_026037.3. [Q8R3I2-1]
DR RefSeq; XP_006515232.1; XM_006515169.2.
DR RefSeq; XP_006515233.1; XM_006515170.3. [Q8R3I2-3]
DR AlphaFoldDB; Q8R3I2; -.
DR SMR; Q8R3I2; -.
DR STRING; 10090.ENSMUSP00000106567; -.
DR ChEMBL; CHEMBL1255156; -.
DR SwissLipids; SLP:000000287; -.
DR iPTMnet; Q8R3I2; -.
DR PhosphoSitePlus; Q8R3I2; -.
DR SwissPalm; Q8R3I2; -.
DR MaxQB; Q8R3I2; -.
DR PaxDb; Q8R3I2; -.
DR PeptideAtlas; Q8R3I2; -.
DR PRIDE; Q8R3I2; -.
DR ProteomicsDB; 293418; -. [Q8R3I2-1]
DR ProteomicsDB; 293419; -. [Q8R3I2-2]
DR ProteomicsDB; 293420; -. [Q8R3I2-3]
DR Antibodypedia; 12361; 79 antibodies from 19 providers.
DR Ensembl; ENSMUST00000110942; ENSMUSP00000106567; ENSMUSG00000020646. [Q8R3I2-1]
DR Ensembl; ENSMUST00000221952; ENSMUSP00000152348; ENSMUSG00000020646. [Q8R3I2-2]
DR GeneID; 67216; -.
DR KEGG; mmu:67216; -.
DR UCSC; uc007neu.1; mouse. [Q8R3I2-1]
DR UCSC; uc007nev.1; mouse. [Q8R3I2-2]
DR UCSC; uc007nex.1; mouse. [Q8R3I2-3]
DR CTD; 129642; -.
DR MGI; MGI:1914466; Mboat2.
DR VEuPathDB; HostDB:ENSMUSG00000020646; -.
DR eggNOG; KOG2704; Eukaryota.
DR GeneTree; ENSGT01030000234564; -.
DR HOGENOM; CLU_011340_3_0_1; -.
DR InParanoid; Q8R3I2; -.
DR OMA; WAISIFE; -.
DR PhylomeDB; Q8R3I2; -.
DR TreeFam; TF314906; -.
DR BRENDA; 2.3.1.23; 3474.
DR Reactome; R-MMU-1482788; Acyl chain remodelling of PC.
DR Reactome; R-MMU-1482839; Acyl chain remodelling of PE.
DR UniPathway; UPA00085; -.
DR BioGRID-ORCS; 67216; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Mboat2; mouse.
DR PRO; PR:Q8R3I2; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q8R3I2; protein.
DR Bgee; ENSMUSG00000020646; Expressed in umbilical cord and 245 other tissues.
DR ExpressionAtlas; Q8R3I2; baseline and differential.
DR Genevisible; Q8R3I2; 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; IDA:UniProtKB.
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:0036151; P:phosphatidylcholine acyl-chain remodeling; IMP:UniProtKB.
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; IEA:UniProtKB-KW.
DR GO; GO:0032330; P:regulation of chondrocyte differentiation; IMP:UniProtKB.
DR InterPro; IPR004299; MBOAT_fam.
DR Pfam; PF03062; MBOAT; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Alternative splicing; Endoplasmic reticulum;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..519
FT /note="Lysophospholipid acyltransferase 2"
FT /id="PRO_0000273021"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 365..385
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 415..435
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 443..463
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 497..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 341
FT /evidence="ECO:0000250"
FT ACT_SITE 372
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..141
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_022457"
FT VAR_SEQ 100..132
FT /note="QCCFVFALGYLSVCQITRVYIFDYGQYSADFSG -> H (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_022458"
FT VAR_SEQ 142..150
FT /note="TSLAYEIHD -> MDNILLIFQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_022459"
FT CONFLICT 28
FT /note="F -> S (in Ref. 3; BAB28556)"
FT /evidence="ECO:0000305"
FT CONFLICT 40
FT /note="V -> L (in Ref. 3; BAB28556)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 519 AA; 58995 MW; A21F3947612314EE CRC64;
MATTSTTGST LLQPLSNAVQ LPIDQVNFVV CQLFALLAAV WFRTYLHSSK TSSFIRHVVA
TLLGLYLAFF CFGWYALHFL VQSGISYCIM IIAGVESMQQ CCFVFALGYL SVCQITRVYI
FDYGQYSADF SGPMMIITQK ITSLAYEIHD GMFRKDEELT PSQRGLAVRR MPSLLEYVSY
TCNFMGILAG PLCSYKDYIA FIEGRASHVA QPSENGKDEQ HGKADPSPNA AVTEKLLVCG
LSLLFHLTIS NMLPVEYNID EHFQATASWP TKATYLYVSL LAARPKYYFA WTLADAINNA
AGFGFRGYDK NGVARWDLIS NLRIQQIEMS TSFKMFLDNW NIQTALWLKR VCYERATFSP
TIQTFFLSAI WHGVYPGYYL TFLTGVLMTL AARAVRNNFR HYFLEPPQLK LFYDLITWVA
TQITISYTVV PFVLLSIKPS FTFYSSWYYC LHVCSILVLL LLPVKKSQRR TSTQENVHLS
QAKKFDERDN PLGQNSFSTM NNVCNQNRDT GSRHSSLTQ