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Protein

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

Gene

Agpat2

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

Functioni

Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone.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, mitochondrial (Tamm41), Phosphatidate cytidylyltransferase (Cds2), 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: UniProtKB

GO - Biological processi

Keywordsi

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

Enzyme and pathway databases

ReactomeiR-MMU-1483166 Synthesis of PA
R-MMU-6798695 Neutrophil degranulation
UniPathwayiUPA00557; UER00613

Names & Taxonomyi

Protein namesi
Recommended name:
1-acyl-sn-glycerol-3-phosphate acyltransferase beta (EC:2.3.1.51)
Alternative name(s):
1-acylglycerol-3-phosphate O-acyltransferase 2
Short name:
1-AGP acyltransferase 2
Short name:
1-AGPAT 2
Lysophosphatidic acid acyltransferase beta
Short name:
LPAAT-beta
Gene namesi
Name:Agpat2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1914762 Agpat2

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
Transmembranei30 – 50HelicalSequence analysisAdd BLAST21
Transmembranei122 – 142HelicalSequence analysisAdd BLAST21
Transmembranei187 – 207HelicalSequence analysisAdd BLAST21

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 23Sequence analysisAdd BLAST23
ChainiPRO_000020819324 – 2781-acyl-sn-glycerol-3-phosphate acyltransferase betaAdd BLAST255

Proteomic databases

MaxQBiQ8K3K7
PaxDbiQ8K3K7
PRIDEiQ8K3K7

PTM databases

iPTMnetiQ8K3K7
PhosphoSitePlusiQ8K3K7

Expressioni

Tissue specificityi

Expressed at high levels in the liver, at intermediate levels in the kidney, gut, heart and skeletal muscles. Undetectable in brain and spleen.1 Publication

Inductioni

Down-regulated in the heart by clofibrate, a PPAR-alpha agonist.1 Publication

Gene expression databases

BgeeiENSMUSG00000026922
ExpressionAtlasiQ8K3K7 baseline and differential
GenevisibleiQ8K3K7 MM

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000028286

Structurei

3D structure databases

ProteinModelPortaliQ8K3K7
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi98 – 103HXXXXD motif6
Motifi172 – 175EGTR motif4

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

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2848 Eukaryota
COG0204 LUCA
GeneTreeiENSGT00390000008726
HOGENOMiHOG000026375
HOVERGENiHBG000676
InParanoidiQ8K3K7
KOiK13509
OMAiMPRPLCY
OrthoDBiEOG091G0ICC
PhylomeDBiQ8K3K7
TreeFamiTF314867

Family and domain databases

InterProiView protein in InterPro
IPR004552 AGP_acyltrans
IPR002123 Plipid/glycerol_acylTrfase
PfamiView protein in Pfam
PF01553 Acyltransferase, 1 hit
SMARTiView protein in SMART
SM00563 PlsC, 1 hit
TIGRFAMsiTIGR00530 AGP_acyltrn, 1 hit

Sequencei

Sequence statusi: Complete.

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

Q8K3K7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDPWPWLTAA LLLLLLLVQL SRTARFYAKV GLYCVLCLSF SAAASIVCLL
60 70 80 90 100
RHGGRTVDNM SIISWFVRSF KYVYGLRFEV SGQKKLEVDG PCVIISNHQS
110 120 130 140 150
ILDMMGLMEI LPKRCVQIAK RELMFTGPVG LIMYLGGVYF INRQQARTAM
160 170 180 190 200
SVMADLGDLM VKENLKVWIY PEGTRNDNGD LLPFKKGAFY LAIQAQVPII
210 220 230 240 250
PVVYSSFSSF YNVKTKLFTS GTIKVQVLDA VPTNGLTDAD VTKLVDTCYQ
260 270
SMRATFLQIS QIPQENSAIK EPGVLPAQ
Length:278
Mass (Da):31,011
Last modified:October 1, 2002 - v1
Checksum:i57A54BFB1A0EFF56
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY072769 mRNA Translation: AAL62337.1
CCDSiCCDS15809.1
RefSeqiNP_080488.1, NM_026212.2
UniGeneiMm.24244

Genome annotation databases

EnsembliENSMUST00000028286; ENSMUSP00000028286; ENSMUSG00000026922
GeneIDi67512
KEGGimmu:67512
UCSCiuc008ivt.2 mouse

Similar proteinsi

Entry informationi

Entry nameiPLCB_MOUSE
AccessioniPrimary (citable) accession number: Q8K3K7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: October 1, 2002
Last modified: April 25, 2018
This is version 117 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health