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Protein

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

Gene

Agpat1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-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.

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: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Enzyme and pathway databases

BRENDAi2.3.1.51. 3474.
UniPathwayiUPA00557; UER00613.

Names & Taxonomyi

Protein namesi
Recommended name:
1-acyl-sn-glycerol-3-phosphate acyltransferase alpha (EC:2.3.1.51)
Alternative name(s):
1-acylglycerol-3-phosphate O-acyltransferase 1
Short name:
1-AGP acyltransferase 1
Short name:
1-AGPAT 1
Lysophosphatidic acid acyltransferase alpha
Short name:
LPAAT-alpha
Gene namesi
Name:Agpat1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1932075. Agpat1.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei35 – 55HelicalSequence analysisAdd BLAST21
Transmembranei125 – 145HelicalSequence analysisAdd BLAST21
Transmembranei190 – 210HelicalSequence analysisAdd BLAST21

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2844.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 28Sequence analysisAdd BLAST28
ChainiPRO_000020819129 – 2851-acyl-sn-glycerol-3-phosphate acyltransferase alphaAdd BLAST257

Proteomic databases

EPDiO35083.
MaxQBiO35083.
PaxDbiO35083.
PeptideAtlasiO35083.
PRIDEiO35083.

PTM databases

PhosphoSitePlusiO35083.
SwissPalmiO35083.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiENSMUSG00000034254.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000048573.

Structurei

3D structure databases

ProteinModelPortaliO35083.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi101 – 106HXXXXD motif6
Motifi175 – 178EGTR 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.
HOVERGENiHBG000676.
InParanoidiO35083.
KOiK13509.
PhylomeDBiO35083.
TreeFamiTF314867.

Family and domain databases

InterProiIPR004552. AGP_acyltrans.
IPR002123. Plipid/glycerol_acylTrfase.
[Graphical view]
PfamiPF01553. Acyltransferase. 1 hit.
[Graphical view]
SMARTiSM00563. PlsC. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00530. AGP_acyltrn. 1 hit.

Sequencei

Sequence statusi: Complete.

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

O35083-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELWPGAWTA LLLLLLLLLS TLWFCSSSAK YFFKMAFYNG WILFLAILAI
60 70 80 90 100
PVCAVRGRNV ENMKILRLLL LHAKYLYGIR VEVRGAHHFP PTQPYVVVSN
110 120 130 140 150
HQSSLDLLGM MEVLPDRCVP IAKRELLWAG SAGLACWLAG IIFIDRKRTG
160 170 180 190 200
DAISVMSEVA QTLLTQDVRV WVFPEGTRNH NGSMLPFKRG AFHLAVQAQV
210 220 230 240 250
PIIPIVMSSY QDFYSKKERR FTSPGRCQVR VLPPVSTEGL TPDDVPALAD
260 270 280
SVRHSMLTIF REISTDGLGG GDCLKKPGGA GEARL
Length:285
Mass (Da):31,709
Last modified:January 1, 1998 - v1
Checksum:i6227A2C3A09009C1
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti73A → V in AAB82009 (PubMed:14656967).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB005623 mRNA. Translation: BAA22599.1.
AF030001 Genomic DNA. Translation: AAB82009.1.
CCDSiCCDS37590.1.
PIRiJC5639.
RefSeqiNP_001156851.1. NM_001163379.1.
NP_061350.3. NM_018862.3.
XP_006524710.1. XM_006524647.2.
XP_006524711.1. XM_006524648.1.
UniGeneiMm.8684.

Genome annotation databases

GeneIDi55979.
KEGGimmu:55979.
UCSCiuc008ccz.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB005623 mRNA. Translation: BAA22599.1.
AF030001 Genomic DNA. Translation: AAB82009.1.
CCDSiCCDS37590.1.
PIRiJC5639.
RefSeqiNP_001156851.1. NM_001163379.1.
NP_061350.3. NM_018862.3.
XP_006524710.1. XM_006524647.2.
XP_006524711.1. XM_006524648.1.
UniGeneiMm.8684.

3D structure databases

ProteinModelPortaliO35083.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000048573.

Chemistry databases

ChEMBLiCHEMBL2844.

PTM databases

PhosphoSitePlusiO35083.
SwissPalmiO35083.

Proteomic databases

EPDiO35083.
MaxQBiO35083.
PaxDbiO35083.
PeptideAtlasiO35083.
PRIDEiO35083.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi55979.
KEGGimmu:55979.
UCSCiuc008ccz.2. mouse.

Organism-specific databases

CTDi10554.
MGIiMGI:1932075. Agpat1.

Phylogenomic databases

eggNOGiKOG2848. Eukaryota.
COG0204. LUCA.
HOVERGENiHBG000676.
InParanoidiO35083.
KOiK13509.
PhylomeDBiO35083.
TreeFamiTF314867.

Enzyme and pathway databases

UniPathwayiUPA00557; UER00613.
BRENDAi2.3.1.51. 3474.

Miscellaneous databases

PROiO35083.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000034254.

Family and domain databases

InterProiIPR004552. AGP_acyltrans.
IPR002123. Plipid/glycerol_acylTrfase.
[Graphical view]
PfamiPF01553. Acyltransferase. 1 hit.
[Graphical view]
SMARTiSM00563. PlsC. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00530. AGP_acyltrn. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiPLCA_MOUSE
AccessioniPrimary (citable) accession number: O35083
Secondary accession number(s): O35446
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 1, 1998
Last modified: November 2, 2016
This is version 123 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.