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Protein

1-acyl-sn-glycerol-3-phosphate acyltransferase epsilon

Gene

Agpat5

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

Functioni

Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone. Acts on LPA containing saturated or unsaturated fatty acids C15:0-C20:4 at the sn-1 position using C18:1-CoA as the acyl donor. Also acts on lysophosphatidylethanolamine using oleoyl-CoA, but not arachidonoyl-CoA, and lysophosphatidylinositol using arachidonoyl-CoA, but not oleoyl-CoA. Activity toward lysophosphatidylglycerol not detectable.1 Publication

Catalytic activityi

Acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate.

Pathwayi: CDP-diacylglycerol biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes CDP-diacylglycerol from sn-glycerol 3-phosphate.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Glycerol-3-phosphate acyltransferase 1, mitochondrial (Gpam), Glycerol-3-phosphate acyltransferase 4 (Gpat4), Glycerol-3-phosphate acyltransferase 3 (Gpat3), Glycerol-3-phosphate acyltransferase 2, mitochondrial (Gpat2)
  2. 1-acyl-sn-glycerol-3-phosphate acyltransferase gamma (Agpat3), 1-acyl-sn-glycerol-3-phosphate acyltransferase beta (Agpat2), 1-acyl-sn-glycerol-3-phosphate acyltransferase alpha (Agpat1), Lysocardiolipin acyltransferase 1 (Lclat1), 1-acyl-sn-glycerol-3-phosphate acyltransferase epsilon (Agpat5), 1-acyl-sn-glycerol-3-phosphate acyltransferase delta (Agpat4)
  3. Phosphatidate cytidylyltransferase, mitochondrial (Tamm41), Phosphatidate cytidylyltransferase (Cds2), Phosphatidate cytidylyltransferase, mitochondrial (Tamm41), Phosphatidate cytidylyltransferase (Cds2), Phosphatidate cytidylyltransferase 2 (Cds2), Phosphatidate cytidylyltransferase (Cds2), Phosphatidate cytidylyltransferase 1 (Cds1)
This subpathway is part of the pathway CDP-diacylglycerol biosynthesis, which is itself part of Phospholipid metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes CDP-diacylglycerol from sn-glycerol 3-phosphate, the pathway CDP-diacylglycerol biosynthesis and in Phospholipid metabolism.

GO - Molecular functioni

  • 1-acylglycerol-3-phosphate O-acyltransferase activity Source: MGI

GO - Biological processi

  • acylglycerol metabolic process Source: MGI
  • CDP-diacylglycerol biosynthetic process Source: UniProtKB-UniPathway
  • hematopoietic progenitor cell differentiation Source: MGI

Keywordsi

Molecular functionAcyltransferase, Transferase
Biological processLipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Enzyme and pathway databases

ReactomeiR-MMU-1483166. Synthesis of PA.
UniPathwayiUPA00557; UER00613.

Names & Taxonomyi

Protein namesi
Recommended name:
1-acyl-sn-glycerol-3-phosphate acyltransferase epsilon (EC:2.3.1.51)
Alternative name(s):
1-acylglycerol-3-phosphate O-acyltransferase 5
Short name:
1-AGP acyltransferase 5
Short name:
1-AGPAT 5
Lysophosphatidic acid acyltransferase epsilon
Short name:
LPAAT-epsilon
Gene namesi
Name:Agpat5
Synonyms:D8Ertd319e
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:1196345. Agpat5.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei15 – 35HelicalSequence analysisAdd BLAST21
Transmembranei345 – 365HelicalSequence analysisAdd BLAST21

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Mitochondrion, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002082011 – 3651-acyl-sn-glycerol-3-phosphate acyltransferase epsilonAdd BLAST365

Proteomic databases

EPDiQ9D1E8.
MaxQBiQ9D1E8.
PaxDbiQ9D1E8.
PRIDEiQ9D1E8.

PTM databases

iPTMnetiQ9D1E8.
PhosphoSitePlusiQ9D1E8.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiENSMUSG00000031467.
ExpressionAtlasiQ9D1E8. baseline and differential.
GenevisibleiQ9D1E8. MM.

Interactioni

Protein-protein interaction databases

BioGridi206392. 2 interactors.
IntActiQ9D1E8. 2 interactors.
STRINGi10090.ENSMUSP00000117025.

Structurei

3D structure databases

ProteinModelPortaliQ9D1E8.
SMRiQ9D1E8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi93 – 98HXXXXD motif6

Domaini

The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.By similarity

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1505. Eukaryota.
COG0204. LUCA.
GeneTreeiENSGT00890000139404.
HOGENOMiHOG000007801.
HOVERGENiHBG039632.
InParanoidiQ9D1E8.
KOiK19007.
OMAiDWIIADM.
OrthoDBiEOG091G0C4Z.
PhylomeDBiQ9D1E8.
TreeFamiTF314346.

Family and domain databases

InterProiView protein in InterPro
IPR032098. Acyltransf_C.
IPR002123. Plipid/glycerol_acylTrfase.
PfamiView protein in Pfam
PF16076. Acyltransf_C. 1 hit.
PF01553. Acyltransferase. 1 hit.
SMARTiView protein in SMART
SM00563. PlsC. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9D1E8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLLSLVLHTY SMRYLLPSVL LLGSAPTYLL AWTLWRVLSA LMPARLYQRV
60 70 80 90 100
DDRLYCVYQN MVLFFFENYT GVQILLYGDL PKNKENVIYL ANHQSTVDWI
110 120 130 140 150
VADMLAARQD ALGHVRYVLK DKLKWLPLYG FYFAQHGGIY VKRSAKFNDK
160 170 180 190 200
EMRSKLQSYV NAGTPMYLVI FPEGTRYNAT YTKLLSASQA FAAQRGLAVL
210 220 230 240 250
KHVLTPRIKA THVAFDSMKS HLDAIYDVTV VYEGNEKGSG KYSNPPSMTE
260 270 280 290 300
FLCKQCPKLH IHFDRIDRNE VPEEQEHMKK WLHERFEIKD RLLIEFYDSP
310 320 330 340 350
DPERRNKFPG KSVHSRLSVK KTLPSVLILG SLTAVMLMTE SGRKLYMGTW
360
LYGTLLGCLW FVIKA
Length:365
Mass (Da):42,202
Last modified:May 16, 2003 - v2
Checksum:iC13E14759610E19B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti80L → W in AAN75571 (Ref. 1) Curated1
Sequence conflicti128L → M in AAN75571 (Ref. 1) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY161042 mRNA. Translation: AAN75571.1.
AK003649 mRNA. Translation: BAB22915.2.
AK082137 mRNA. Translation: BAC38421.1.
AK089885 mRNA. Translation: BAC40983.1.
AK152709 mRNA. Translation: BAE31436.1.
AK152889 mRNA. Translation: BAE31572.1.
AK155378 mRNA. Translation: BAE33229.1.
BC031987 mRNA. Translation: AAH31987.2.
CCDSiCCDS22126.1.
RefSeqiNP_081068.1. NM_026792.3.
UniGeneiMm.24117.

Genome annotation databases

EnsembliENSMUST00000149565; ENSMUSP00000117025; ENSMUSG00000031467.
GeneIDi52123.
KEGGimmu:52123.
UCSCiuc009kzv.1. mouse.

Similar proteinsi

Entry informationi

Entry nameiPLCE_MOUSE
AccessioniPrimary (citable) accession number: Q9D1E8
Secondary accession number(s): Q3U702, Q8BG61, Q8CGN6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: May 16, 2003
Last modified: October 25, 2017
This is version 117 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

It is uncertain whether Met-1 or Met-12 is the initiator.Curated

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