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Lysophospholipid acyltransferase 2 (LPLAT 2) (EC 2.3.1.-) (1-acylglycerophosphocholine O-acyltransferase) (EC 2.3.1.23) (1-acylglycerophosphoethanolamine O-acyltransferase) (EC 2.3.1.n7) (Lysophosphatidylcholine acyltransferase) (LPCAT) (Lyso-PC acyltransferase) (Lysophosphatidylcholine acyltransferase 4) (Lyso-PC acyltransferase 4) (mLPCAT4) (Lysophosphatidylethanolamine acyltransferase) (LPEAT) (Lyso-PE acyltransferase) (Membrane-bound O-acyltransferase domain-containing protein 2) (O-acyltransferase domain-containing protein 2)

 MBOA2_MOUSE             Reviewed;         519 AA.
Q8R3I2; A9EDS7; Q8BHH5; Q8BM56; Q8R192; Q9CZ73;
23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
01-JUN-2002, sequence version 1.
23-MAY-2018, entry version 98.
RecName: Full=Lysophospholipid acyltransferase 2;
Short=LPLAT 2;
EC=2.3.1.-;
AltName: Full=1-acylglycerophosphocholine O-acyltransferase;
EC=2.3.1.23;
AltName: Full=1-acylglycerophosphoethanolamine O-acyltransferase;
EC=2.3.1.n7;
AltName: Full=Lysophosphatidylcholine acyltransferase;
Short=LPCAT;
Short=Lyso-PC acyltransferase;
AltName: Full=Lysophosphatidylcholine acyltransferase 4;
Short=Lyso-PC acyltransferase 4;
Short=mLPCAT4;
AltName: Full=Lysophosphatidylethanolamine acyltransferase;
Short=LPEAT;
Short=Lyso-PE acyltransferase;
AltName: Full=Membrane-bound O-acyltransferase domain-containing protein 2;
Short=O-acyltransferase domain-containing protein 2;
Name=Mboat2; Synonyms=Lpcat4, Oact2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=17890783; DOI=10.1074/jbc.M704509200;
Tamaki H., Shimada A., Itoh Y., Ohya M., Takase J., Miyashita M.,
Miyagawa H., Nozaki H., Nakayama R., Kumagai H.;
"LPT1 encodes a membrane-bound O-acyltransferase involved in the
acylation of lysophospholipids in the yeast Saccharomyces
cerevisiae.";
J. Biol. Chem. 282:34288-34298(2007).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, BIOPHYSICOCHEMICAL
PROPERTIES, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=18287005; DOI=10.1073/pnas.0712245105;
Hishikawa D., Shindou H., Kobayashi S., Nakanishi H., Taguchi R.,
Shimizu T.;
"Discovery of a lysophospholipid acyltransferase family essential for
membrane asymmetry and diversity.";
Proc. Natl. Acad. Sci. U.S.A. 105:2830-2835(2008).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
STRAIN=C57BL/6J;
TISSUE=Embryoid bodies, Medulla oblongata, and Testis;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=Czech II; TISSUE=Eye, and Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Heart, Kidney, and Lung;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Acyltransferase which mediates the conversion of
lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine or
LPC) into phosphatidylcholine (1,2-diacyl-sn-glycero-3-
phosphocholine or PC) (LPCAT activity). To a lesser extent, also
catalyzes the acylation of lysophosphatidylethanolamine (1-acyl-
sn-glycero-3-phosphoethanolamine or LPE) into
phosphatidylethanolamine (1,2-diacyl-sn-glycero-3-
phosphoethanolamine or PE) (LPEAT activity). Prefers oleoyl-CoA as
the acyl donor. Lysophospholipid acyltransferases (LPLATs)
catalyze the reacylation step of the phospholipid remodeling
pathway also known as the Lands cycle.
{ECO:0000269|PubMed:18287005}.
-!- CATALYTIC ACTIVITY: Acyl-CoA + 1-acyl-sn-glycero-3-phosphocholine
= CoA + 1,2-diacyl-sn-glycero-3-phosphocholine.
-!- CATALYTIC ACTIVITY: Acyl-CoA + 1-acyl-sn-glycero-3-
phosphoethanolamine = CoA + 1,2-diacyl-sn-glycero-3-
phosphoethanolamine.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=5.3 uM for oleoyl-CoA (in the presence of LPC C16:0 as
cosubstrate) {ECO:0000269|PubMed:18287005};
KM=48.15 uM for oleoyl-CoA (in the presence of LPE C16:0 as
cosubstrate) {ECO:0000269|PubMed:18287005};
KM=7.9 uM for LPC C16:0 (in the presence of oleoyl-CoA as
cosubstrate) {ECO:0000269|PubMed:18287005};
KM=27.7 uM for LPE C16:0 (in the presence of oleoyl-CoA as
cosubstrate) {ECO:0000269|PubMed:18287005};
Vmax=24.24 nmol/min/mg enzyme with oleoyl-CoA and LPC C16:0 as
substrates {ECO:0000269|PubMed:18287005};
Vmax=26.3 nmol/min/mg enzyme with oleoyl-CoA and LPE C16:0 as
substrates {ECO:0000269|PubMed:18287005};
-!- PATHWAY: Lipid metabolism; phospholipid metabolism.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
protein {ECO:0000305}. Endoplasmic reticulum
{ECO:0000269|PubMed:18287005}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q8R3I2-1; Sequence=Displayed;
Name=2;
IsoId=Q8R3I2-2; Sequence=VSP_022458;
Name=3;
IsoId=Q8R3I2-3; Sequence=VSP_022457, VSP_022459;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highly expressed in epididymis, brain, testis,
and ovary. {ECO:0000269|PubMed:18287005}.
-!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAC27567.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AB305046; BAF93902.1; -; mRNA.
EMBL; AB297383; BAG12122.1; -; mRNA.
EMBL; AK012931; BAB28556.1; -; mRNA.
EMBL; AK031824; BAC27567.1; ALT_INIT; mRNA.
EMBL; AK033106; BAC28154.1; -; mRNA.
EMBL; AK034873; BAC28863.1; -; mRNA.
EMBL; AK076045; BAC36144.1; -; mRNA.
EMBL; BC025020; AAH25020.1; -; mRNA.
CCDS; CCDS25845.1; -. [Q8R3I2-1]
CCDS; CCDS36423.1; -. [Q8R3I2-2]
RefSeq; NP_001076810.1; NM_001083341.1. [Q8R3I2-2]
RefSeq; NP_080313.2; NM_026037.3. [Q8R3I2-1]
RefSeq; XP_006515232.1; XM_006515169.2. [Q8R3I2-3]
RefSeq; XP_006515233.1; XM_006515170.3. [Q8R3I2-3]
UniGene; Mm.167671; -.
ProteinModelPortal; Q8R3I2; -.
STRING; 10090.ENSMUSP00000106567; -.
ChEMBL; CHEMBL1255156; -.
SwissLipids; SLP:000000287; -.
iPTMnet; Q8R3I2; -.
PhosphoSitePlus; Q8R3I2; -.
SwissPalm; Q8R3I2; -.
PaxDb; Q8R3I2; -.
PeptideAtlas; Q8R3I2; -.
PRIDE; Q8R3I2; -.
Ensembl; ENSMUST00000110942; ENSMUSP00000106567; ENSMUSG00000020646. [Q8R3I2-1]
Ensembl; ENSMUST00000221952; ENSMUSP00000152348; ENSMUSG00000020646. [Q8R3I2-2]
GeneID; 67216; -.
KEGG; mmu:67216; -.
UCSC; uc007neu.1; mouse. [Q8R3I2-1]
UCSC; uc007nev.1; mouse. [Q8R3I2-2]
UCSC; uc007nex.1; mouse. [Q8R3I2-3]
CTD; 129642; -.
MGI; MGI:1914466; Mboat2.
eggNOG; KOG2704; Eukaryota.
eggNOG; COG5202; LUCA.
GeneTree; ENSGT00550000074565; -.
HOGENOM; HOG000015994; -.
HOVERGEN; HBG058823; -.
InParanoid; Q8R3I2; -.
KO; K13517; -.
OMA; RHYFIEP; -.
OrthoDB; EOG091G06A8; -.
PhylomeDB; Q8R3I2; -.
TreeFam; TF314906; -.
BRENDA; 2.3.1.23; 3474.
Reactome; R-MMU-1482788; Acyl chain remodelling of PC.
Reactome; R-MMU-1482839; Acyl chain remodelling of PE.
UniPathway; UPA00085; -.
PRO; PR:Q8R3I2; -.
Proteomes; UP000000589; Chromosome 12.
Bgee; ENSMUSG00000020646; -.
ExpressionAtlas; Q8R3I2; baseline and differential.
Genevisible; Q8R3I2; MM.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0047184; F:1-acylglycerophosphocholine O-acyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
InterPro; IPR004299; MBOAT_fam.
Pfam; PF03062; MBOAT; 1.
1: Evidence at protein level;
Acyltransferase; Alternative splicing; Complete proteome;
Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism; Membrane;
Phospholipid biosynthesis; Phospholipid metabolism;
Reference proteome; Transferase; Transmembrane; Transmembrane helix.
CHAIN 1 519 Lysophospholipid acyltransferase 2.
/FTId=PRO_0000273021.
TRANSMEM 22 42 Helical. {ECO:0000255}.
TRANSMEM 61 81 Helical. {ECO:0000255}.
TRANSMEM 88 108 Helical. {ECO:0000255}.
TRANSMEM 184 204 Helical. {ECO:0000255}.
TRANSMEM 236 256 Helical. {ECO:0000255}.
TRANSMEM 263 283 Helical. {ECO:0000255}.
TRANSMEM 365 385 Helical. {ECO:0000255}.
TRANSMEM 415 435 Helical. {ECO:0000255}.
TRANSMEM 443 463 Helical. {ECO:0000255}.
ACT_SITE 341 341 {ECO:0000250}.
ACT_SITE 372 372 {ECO:0000250}.
VAR_SEQ 1 141 Missing (in isoform 3).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_022457.
VAR_SEQ 100 132 QCCFVFALGYLSVCQITRVYIFDYGQYSADFSG -> H
(in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_022458.
VAR_SEQ 142 150 TSLAYEIHD -> MDNILLIFQ (in isoform 3).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_022459.
CONFLICT 28 28 F -> S (in Ref. 3; BAB28556).
{ECO:0000305}.
CONFLICT 40 40 V -> L (in Ref. 3; BAB28556).
{ECO:0000305}.
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


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