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Protein

Lysophospholipid acyltransferase 5

Gene

Lpcat3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

Acyl-CoA + 1-acyl-sn-glycero-3-phosphocholine = CoA + 1,2-diacyl-sn-glycero-3-phosphocholine.
Acyl-CoA + 1-acyl-sn-glycero-3-phosphoethanolamine = CoA + 1,2-diacyl-sn-glycero-3-phosphoethanolamine.
Acyl-CoA + 1-acyl-sn-glycero-3-phosphatidylserine = CoA + 1,2-diacyl-sn-glycero-3-phosphatidylserine.

Kineticsi

  1. KM=7.8 µM for arachidonoyl-CoA (in the presence of LPC C16:0 as cosubstrate)1 Publication
  2. KM=44.1 µM for arachidonoyl-CoA (in the presence of LPE C18:1 as cosubstrate)1 Publication
  3. KM=28 µM for arachidonoyl-CoA (in the presence of LPS C18:1 as cosubstrate)1 Publication
  4. KM=34.5 µM for LPC C16:0 (in the presence of arachidonoyl-CoA as cosubstrate)1 Publication
  5. KM=29.7 µM for LPE C18:1 (in the presence of arachidonoyl-CoA as cosubstrate)1 Publication
  6. KM=22.3 µM for LPS C18:1 (in the presence of arachidonoyl-CoA as cosubstrate)1 Publication
  1. Vmax=1085.5 nmol/min/mg enzyme with arachidonoyl-CoA and LPC C16:0 as substrates1 Publication
  2. Vmax=389.25 nmol/min/mg enzyme with arachidonoyl-CoA and LPE C18:1 as substrates1 Publication
  3. Vmax=335.75 nmol/min/mg enzyme with arachidonoyl-CoA and LPS C18:1 as substrates1 Publication

Pathwayi: phospholipid metabolism

This protein is involved in the pathway phospholipid metabolism, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway phospholipid metabolism and in Lipid metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei338 – 3381By similarity
Active sitei374 – 3741By similarity

GO - Molecular functioni

GO - Biological processi

  • phospholipid biosynthetic process Source: UniProtKB-KW
  • regulation of plasma lipoprotein particle levels Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Enzyme and pathway databases

BRENDAi2.3.1.23. 3474.
ReactomeiR-MMU-1482788. Acyl chain remodelling of PC.
R-MMU-1482801. Acyl chain remodelling of PS.
R-MMU-1482839. Acyl chain remodelling of PE.
UniPathwayiUPA00085.

Chemistry

SwissLipidsiSLP:000000286.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysophospholipid acyltransferase 5 (EC:2.3.1.-)
Short name:
LPLAT 5
Alternative name(s):
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
Short name:
LPCAT
Short name:
Lyso-PC acyltransferase
Lysophosphatidylcholine acyltransferase 3
Short name:
Lyso-PC acyltransferase 3
Short name:
mLPCAT3
Lysophosphatidylethanolamine acyltransferase
Short name:
LPEAT
Short name:
Lyso-PE acyltransferase
Lysophosphatidylserine acyltransferase
Short name:
LPSAT
Short name:
Lyso-PS acyltransferase
Membrane-bound O-acyltransferase domain-containing protein 5
Short name:
O-acyltransferase domain-containing protein 5
Gene namesi
Name:Lpcat3
Synonyms:Grcc3fImported, Mboat5, Oact5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:1315211. Lpcat3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei44 – 6421HelicalSequence analysisAdd
BLAST
Transmembranei84 – 10421HelicalSequence analysisAdd
BLAST
Transmembranei111 – 13121HelicalSequence analysisAdd
BLAST
Transmembranei180 – 20021HelicalSequence analysisAdd
BLAST
Transmembranei236 – 25621HelicalSequence analysisAdd
BLAST
Transmembranei285 – 30521HelicalSequence analysisAdd
BLAST
Transmembranei364 – 38421HelicalSequence analysisAdd
BLAST
Transmembranei422 – 44221HelicalSequence analysisAdd
BLAST
Transmembranei453 – 47321HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL1255159.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 487486Lysophospholipid acyltransferase 5PRO_0000233383Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Glycosylationi225 – 2251N-linked (GlcNAc...)Sequence analysis
Glycosylationi308 – 3081N-linked (GlcNAc...)Sequence analysis
Glycosylationi331 – 3311N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Acetylation, Glycoprotein

Proteomic databases

EPDiQ91V01.
MaxQBiQ91V01.
PaxDbiQ91V01.
PRIDEiQ91V01.

PTM databases

iPTMnetiQ91V01.
PhosphoSiteiQ91V01.

Expressioni

Tissue specificityi

Detected ubiquitously, with high expression levels in testis.1 Publication

Gene expression databases

BgeeiQ91V01.
ExpressionAtlasiQ91V01. baseline and differential.
GenevisibleiQ91V01. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000004381.

Structurei

3D structure databases

ProteinModelPortaliQ91V01.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi484 – 4874Di-lysine motif

Domaini

The di-lysine motif confers endoplasmic reticulum localization.By similarity

Sequence similaritiesi

Belongs to the membrane-bound acyltransferase family.Sequence analysis

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2705. Eukaryota.
COG5202. LUCA.
GeneTreeiENSGT00550000074565.
HOGENOMiHOG000019529.
HOVERGENiHBG054659.
InParanoidiQ91V01.
KOiK13515.
OMAiTVLQPFY.
OrthoDBiEOG78SQJ0.
PhylomeDBiQ91V01.
TreeFamiTF106143.

Family and domain databases

InterProiIPR004299. MBOAT_fam.
[Graphical view]
PfamiPF03062. MBOAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q91V01-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASTADGDMG ETLEQMRGLW PGVEDLSLNK LATSLGASEQ ALRLIFSIFL
60 70 80 90 100
GYPLALFYRH YLFYKDSYLI HLFHTFTGLS IAYFNFGHQF YHSLLCVVLQ
110 120 130 140 150
FLILRLMGRT VTAVITTLCF QMAYLLAGYY YTATGDYDIK WTMPHCVLTL
160 170 180 190 200
KLIGLCIDYY DGGKDGNSLT SEQQKYAIRG VPSLLEVAGF SYFYGAFLVG
210 220 230 240 250
PQFSMNHYMK LVRGQLTDIP GKMPNSTIPA LKRLSLGLVY LVGYTLLSPH
260 270 280 290 300
ITDDYLLTED YDNRPFWFRC MYMLIWGKFV LYKYVTCWLV TEGVCILSGL
310 320 330 340 350
GFNGFDENGT VRWDACANMK VWLFETTPRF NGTIASFNIN TNAWVARYIF
360 370 380 390 400
KRLKFLGNKE LSQGLSLLFL ALWHGLHSGY LICFQMEFLI VIVEKQVSSL
410 420 430 440 450
IRDSPALSSL ASITALQPFY YLVQQTIHWL FMGYSMTAFC LFTWDKWLKV
460 470 480
YRSIYFLGHV FFLSLLFILP YIHKAMVPRK EKLKKRE
Length:487
Mass (Da):56,147
Last modified:December 1, 2001 - v1
Checksum:iEBC51DB3734B17C7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti48 – 492IF → SH in AAC36007 (PubMed:9445485).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY028317 mRNA. Translation: AAK20915.1.
AB294194 mRNA. Translation: BAG12120.1.
CH466523 Genomic DNA. Translation: EDK99746.1.
BC006753 mRNA. Translation: AAH06753.2.
AC002397 Genomic DNA. Translation: AAC36007.1.
AK083687 mRNA. Translation: BAC38993.1.
CCDSiCCDS20523.1.
RefSeqiNP_660112.1. NM_145130.2.
UniGeneiMm.273915.

Genome annotation databases

EnsembliENSMUST00000004381; ENSMUSP00000004381; ENSMUSG00000004270.
GeneIDi14792.
KEGGimmu:14792.
UCSCiuc009drf.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY028317 mRNA. Translation: AAK20915.1.
AB294194 mRNA. Translation: BAG12120.1.
CH466523 Genomic DNA. Translation: EDK99746.1.
BC006753 mRNA. Translation: AAH06753.2.
AC002397 Genomic DNA. Translation: AAC36007.1.
AK083687 mRNA. Translation: BAC38993.1.
CCDSiCCDS20523.1.
RefSeqiNP_660112.1. NM_145130.2.
UniGeneiMm.273915.

3D structure databases

ProteinModelPortaliQ91V01.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000004381.

Chemistry

ChEMBLiCHEMBL1255159.
SwissLipidsiSLP:000000286.

PTM databases

iPTMnetiQ91V01.
PhosphoSiteiQ91V01.

Proteomic databases

EPDiQ91V01.
MaxQBiQ91V01.
PaxDbiQ91V01.
PRIDEiQ91V01.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000004381; ENSMUSP00000004381; ENSMUSG00000004270.
GeneIDi14792.
KEGGimmu:14792.
UCSCiuc009drf.2. mouse.

Organism-specific databases

CTDi10162.
MGIiMGI:1315211. Lpcat3.

Phylogenomic databases

eggNOGiKOG2705. Eukaryota.
COG5202. LUCA.
GeneTreeiENSGT00550000074565.
HOGENOMiHOG000019529.
HOVERGENiHBG054659.
InParanoidiQ91V01.
KOiK13515.
OMAiTVLQPFY.
OrthoDBiEOG78SQJ0.
PhylomeDBiQ91V01.
TreeFamiTF106143.

Enzyme and pathway databases

UniPathwayiUPA00085.
BRENDAi2.3.1.23. 3474.
ReactomeiR-MMU-1482788. Acyl chain remodelling of PC.
R-MMU-1482801. Acyl chain remodelling of PS.
R-MMU-1482839. Acyl chain remodelling of PE.

Miscellaneous databases

ChiTaRSiLpcat3. mouse.
PROiQ91V01.
SOURCEiSearch...

Gene expression databases

BgeeiQ91V01.
ExpressionAtlasiQ91V01. baseline and differential.
GenevisibleiQ91V01. MM.

Family and domain databases

InterProiIPR004299. MBOAT_fam.
[Graphical view]
PfamiPF03062. MBOAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and initial characterization of mouse PTG cDNA, whose expression is in a PPAR alpha dependent manner."
    Zhu Y., Han Y., Reddy J.K.
    Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6JImported.
    Tissue: LiverImported.
  2. "Discovery of a lysophospholipid acyltransferase family essential for membrane asymmetry and diversity."
    Hishikawa D., Shindou H., Kobayashi S., Nakanishi H., Taguchi R., Shimizu T.
    Proc. Natl. Acad. Sci. U.S.A. 105:2830-2835(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/NImported.
    Tissue: Mammary glandImported.
  5. "Comparative sequence analysis of a gene-rich cluster at human chromosome 12p13 and its syntenic region in mouse chromosome 6."
    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.
    Genome Res. 8:29-40(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 48-487.
  6. "The transcriptional landscape of the mammalian genome."
    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.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 114-487.
    Strain: C57BL/6JImported.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiMBOA5_MOUSE
AccessioniPrimary (citable) accession number: Q91V01
Secondary accession number(s): B1B362, O35131, Q8BNH6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: December 1, 2001
Last modified: June 8, 2016
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.