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Lysophospholipid acyltransferase 5 (LPLAT 5) (EC 2.3.1.-) (1-acylglycerophosphocholine O-acyltransferase) (EC 2.3.1.23) (1-acylglycerophosphoethanolamine O-acyltransferase) (EC 2.3.1.n7) (1-acylglycerophosphoserine O-acyltransferase) (EC 2.3.1.n6) (Lysophosphatidylcholine acyltransferase) (LPCAT) (Lyso-PC acyltransferase) (Lysophosphatidylcholine acyltransferase 3) (Lyso-PC acyltransferase 3) (mLPCAT3) (Lysophosphatidylethanolamine acyltransferase) (LPEAT) (Lyso-PE acyltransferase) (Lysophosphatidylserine acyltransferase) (LPSAT) (Lyso-PS acyltransferase) (Membrane-bound O-acyltransferase domain-containing protein 5) (O-acyltransferase domain-containing protein 5)

 MBOA5_MOUSE             Reviewed;         487 AA.
Q91V01; B1B362; O35131; Q8BNH6;
02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
12-SEP-2018, entry version 119.
RecName: Full=Lysophospholipid acyltransferase 5;
Short=LPLAT 5;
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=1-acylglycerophosphoserine O-acyltransferase;
EC=2.3.1.n6;
AltName: Full=Lysophosphatidylcholine acyltransferase;
Short=LPCAT;
Short=Lyso-PC acyltransferase;
AltName: Full=Lysophosphatidylcholine acyltransferase 3;
Short=Lyso-PC acyltransferase 3;
Short=mLPCAT3;
AltName: Full=Lysophosphatidylethanolamine acyltransferase;
Short=LPEAT;
Short=Lyso-PE acyltransferase;
AltName: Full=Lysophosphatidylserine acyltransferase;
Short=LPSAT;
Short=Lyso-PS acyltransferase;
AltName: Full=Membrane-bound O-acyltransferase domain-containing protein 5;
Short=O-acyltransferase domain-containing protein 5;
Name=Lpcat3;
Synonyms=Grcc3f {ECO:0000312|MGI:MGI:1315211}, Mboat5, Oact5;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1] {ECO:0000312|EMBL:AAK20915.1}
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6J {ECO:0000312|EMBL:AAK20915.1};
TISSUE=Liver {ECO:0000312|EMBL:AAK20915.1};
Zhu Y., Han Y., Reddy J.K.;
"Cloning and initial characterization of mouse PTG cDNA, whose
expression is in a PPAR alpha dependent manner.";
Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA], 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] {ECO:0000312|EMBL:AAK20915.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4] {ECO:0000312|EMBL:AAH06753.2}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N {ECO:0000312|EMBL:AAH06753.2};
TISSUE=Mammary gland {ECO:0000312|EMBL:AAH06753.2};
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] {ECO:0000305, ECO:0000312|EMBL:AAC36007.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 48-487.
PubMed=9445485;
Ansari-Lari M.A., Oeltjen J.C., Schwartz S., Zhang Z., Muzny D.M.,
Lu J., Gorrell J.H., Chinault A.C., Belmont J.W., Miller W.,
Gibbs R.A.;
"Comparative sequence analysis of a gene-rich cluster at human
chromosome 12p13 and its syntenic region in mouse chromosome 6.";
Genome Res. 8:29-40(1998).
[6] {ECO:0000305, ECO:0000312|EMBL:BAC38993.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 114-487.
STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC38993.1};
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).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
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), and the conversion of
lysophosphatidylserine (1-acyl-2-hydroxy-sn-glycero-3-phospho-L-
serine or LPS) into phosphatidylserine (1,2-diacyl-sn-glycero-3-
phospho-L-serine or PS) (LPSAT activity). Favors polyunsaturated
fatty acyl-CoAs as acyl donors compared to saturated fatty acyl-
CoAs. Seems to be the major enzyme contributing to LPCAT activity
in the liver. 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.
-!- CATALYTIC ACTIVITY: Acyl-CoA + 1-acyl-sn-glycero-3-
phosphatidylserine = CoA + 1,2-diacyl-sn-glycero-3-
phosphatidylserine.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=7.8 uM for arachidonoyl-CoA (in the presence of LPC C16:0 as
cosubstrate) {ECO:0000269|PubMed:18287005};
KM=44.1 uM for arachidonoyl-CoA (in the presence of LPE C18:1 as
cosubstrate) {ECO:0000269|PubMed:18287005};
KM=28 uM for arachidonoyl-CoA (in the presence of LPS C18:1 as
cosubstrate) {ECO:0000269|PubMed:18287005};
KM=34.5 uM for LPC C16:0 (in the presence of arachidonoyl-CoA as
cosubstrate) {ECO:0000269|PubMed:18287005};
KM=29.7 uM for LPE C18:1 (in the presence of arachidonoyl-CoA as
cosubstrate) {ECO:0000269|PubMed:18287005};
KM=22.3 uM for LPS C18:1 (in the presence of arachidonoyl-CoA as
cosubstrate) {ECO:0000269|PubMed:18287005};
Vmax=1085.5 nmol/min/mg enzyme with arachidonoyl-CoA and LPC
C16:0 as substrates {ECO:0000269|PubMed:18287005};
Vmax=389.25 nmol/min/mg enzyme with arachidonoyl-CoA and LPE
C18:1 as substrates {ECO:0000269|PubMed:18287005};
Vmax=335.75 nmol/min/mg enzyme with arachidonoyl-CoA and LPS
C18:1 as substrates {ECO:0000269|PubMed:18287005};
-!- PATHWAY: Lipid metabolism; phospholipid metabolism.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:18287005}; Multi-pass membrane protein
{ECO:0000269|PubMed:18287005}.
-!- TISSUE SPECIFICITY: Detected ubiquitously, with high expression
levels in testis. {ECO:0000269|PubMed:18287005}.
-!- DOMAIN: The di-lysine motif confers endoplasmic reticulum
localization. {ECO:0000250}.
-!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
{ECO:0000255}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AY028317; AAK20915.1; -; mRNA.
EMBL; AB294194; BAG12120.1; -; mRNA.
EMBL; CH466523; EDK99746.1; -; Genomic_DNA.
EMBL; BC006753; AAH06753.2; -; mRNA.
EMBL; AC002397; AAC36007.1; -; Genomic_DNA.
EMBL; AK083687; BAC38993.1; -; mRNA.
CCDS; CCDS20523.1; -.
RefSeq; NP_660112.1; NM_145130.2.
UniGene; Mm.273915; -.
ProteinModelPortal; Q91V01; -.
BioGrid; 200053; 1.
STRING; 10090.ENSMUSP00000004381; -.
ChEMBL; CHEMBL1255159; -.
SwissLipids; SLP:000000286; -.
iPTMnet; Q91V01; -.
PhosphoSitePlus; Q91V01; -.
EPD; Q91V01; -.
MaxQB; Q91V01; -.
PaxDb; Q91V01; -.
PeptideAtlas; Q91V01; -.
PRIDE; Q91V01; -.
Ensembl; ENSMUST00000004381; ENSMUSP00000004381; ENSMUSG00000004270.
GeneID; 14792; -.
KEGG; mmu:14792; -.
UCSC; uc009drf.2; mouse.
CTD; 10162; -.
MGI; MGI:1315211; Lpcat3.
eggNOG; KOG2705; Eukaryota.
eggNOG; COG5202; LUCA.
GeneTree; ENSGT00550000074565; -.
HOGENOM; HOG000019529; -.
HOVERGEN; HBG054659; -.
InParanoid; Q91V01; -.
KO; K13515; -.
OMA; TMPHCIL; -.
OrthoDB; EOG091G062X; -.
PhylomeDB; Q91V01; -.
TreeFam; TF106143; -.
BRENDA; 2.3.1.23; 3474.
Reactome; R-MMU-1482788; Acyl chain remodelling of PC.
Reactome; R-MMU-1482801; Acyl chain remodelling of PS.
Reactome; R-MMU-1482839; Acyl chain remodelling of PE.
UniPathway; UPA00085; -.
ChiTaRS; Lpcat3; mouse.
PRO; PR:Q91V01; -.
Proteomes; UP000000589; Chromosome 6.
Bgee; ENSMUSG00000004270; Expressed in 288 organ(s), highest expression level in jejunum.
ExpressionAtlas; Q91V01; baseline and differential.
Genevisible; Q91V01; MM.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0047184; F:1-acylglycerophosphocholine O-acyltransferase activity; ISO:MGI.
GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0097006; P:regulation of plasma lipoprotein particle levels; IMP:MGI.
InterPro; IPR004299; MBOAT_fam.
Pfam; PF03062; MBOAT; 1.
1: Evidence at protein level;
Acetylation; Acyltransferase; Complete proteome;
Endoplasmic reticulum; Glycoprotein; Lipid biosynthesis;
Lipid metabolism; Membrane; Phospholipid biosynthesis;
Phospholipid metabolism; Reference proteome; Transferase;
Transmembrane; Transmembrane helix.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q6P1A2}.
CHAIN 2 487 Lysophospholipid acyltransferase 5.
/FTId=PRO_0000233383.
TRANSMEM 44 64 Helical. {ECO:0000255}.
TRANSMEM 84 104 Helical. {ECO:0000255}.
TRANSMEM 111 131 Helical. {ECO:0000255}.
TRANSMEM 180 200 Helical. {ECO:0000255}.
TRANSMEM 236 256 Helical. {ECO:0000255}.
TRANSMEM 285 305 Helical. {ECO:0000255}.
TRANSMEM 364 384 Helical. {ECO:0000255}.
TRANSMEM 422 442 Helical. {ECO:0000255}.
TRANSMEM 453 473 Helical. {ECO:0000255}.
MOTIF 484 487 Di-lysine motif.
ACT_SITE 338 338 {ECO:0000250}.
ACT_SITE 374 374 {ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:Q6P1A2}.
CARBOHYD 225 225 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 308 308 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 331 331 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CONFLICT 48 49 IF -> SH (in Ref. 5; AAC36007).
{ECO:0000305}.
SEQUENCE 487 AA; 56147 MW; EBC51DB3734B17C7 CRC64;
MASTADGDMG ETLEQMRGLW PGVEDLSLNK LATSLGASEQ ALRLIFSIFL GYPLALFYRH
YLFYKDSYLI HLFHTFTGLS IAYFNFGHQF YHSLLCVVLQ FLILRLMGRT VTAVITTLCF
QMAYLLAGYY YTATGDYDIK WTMPHCVLTL KLIGLCIDYY DGGKDGNSLT SEQQKYAIRG
VPSLLEVAGF SYFYGAFLVG PQFSMNHYMK LVRGQLTDIP GKMPNSTIPA LKRLSLGLVY
LVGYTLLSPH ITDDYLLTED YDNRPFWFRC MYMLIWGKFV LYKYVTCWLV TEGVCILSGL
GFNGFDENGT VRWDACANMK VWLFETTPRF NGTIASFNIN TNAWVARYIF KRLKFLGNKE
LSQGLSLLFL ALWHGLHSGY LICFQMEFLI VIVEKQVSSL IRDSPALSSL ASITALQPFY
YLVQQTIHWL FMGYSMTAFC LFTWDKWLKV YRSIYFLGHV FFLSLLFILP YIHKAMVPRK
EKLKKRE


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