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Protein

Glycerol-3-phosphate acyltransferase 4

Gene

Gpat4

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

Functioni

Esterifies acyl-group from acyl-ACP to the sn-1 position of glycerol-3-phosphate, an essential step in glycerolipid biosynthesis. Active against both saturated and unsaturated long-chain fatty acyl-CoAs (By similarity).By similarity1 Publication

Catalytic activityi

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

Pathwayi: CDP-diacylglycerol biosynthesis

This protein is involved in step 1 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

  • glycerol-3-phosphate O-acyltransferase activity Source: UniProtKB

GO - Biological processi

  • acyl-CoA metabolic process Source: MGI
  • CDP-diacylglycerol biosynthetic process Source: UniProtKB-UniPathway
  • diacylglycerol metabolic process Source: MGI
  • fatty acid metabolic process Source: MGI
  • glandular epithelial cell maturation Source: MGI
  • lactation Source: UniProtKB
  • lipid biosynthetic process Source: UniProtKB
  • mammary gland development Source: MGI
  • phosphatidylcholine biosynthetic process Source: MGI
  • regulation of multicellular organism growth Source: MGI
  • triglyceride biosynthetic process Source: UniProtKB
  • triglyceride metabolic process 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

BRENDAi2.3.1.15. 3474.
ReactomeiR-MMU-1483166. Synthesis of PA.
R-MMU-75109. Triglyceride Biosynthesis.
UniPathwayiUPA00557; UER00612.

Chemistry databases

SwissLipidsiSLP:000000104.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycerol-3-phosphate acyltransferase 4Imported (EC:2.3.1.15)
Short name:
GPAT4
Alternative name(s):
1-acylglycerol-3-phosphate O-acyltransferase 6
Short name:
1-AGP acyltransferase 6
Short name:
1-AGPAT 6
Acyl-CoA:glycerol-3-phosphate acyltransferase 4
Lysophosphatidic acid acyltransferase zeta
Short name:
LPAAT-zeta
Gene namesi
Name:Gpat4Imported
Synonyms:Agpat6
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:2142716. Gpat4.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei156 – 176HelicalSequence analysisAdd BLAST21
Transmembranei180 – 200HelicalSequence analysisAdd BLAST21

GO - Cellular componenti

  • endoplasmic reticulum Source: UniProtKB
  • integral component of endoplasmic reticulum membrane Source: UniProtKB
  • membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 37Sequence analysisAdd BLAST37
ChainiPRO_000002470438 – 456Glycerol-3-phosphate acyltransferase 4Add BLAST419

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi247N-linked (GlcNAc...)Sequence analysis1
Glycosylationi327N-linked (GlcNAc...)Sequence analysis1
Glycosylationi328N-linked (GlcNAc...)Sequence analysis1
Glycosylationi362N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Glycoprotein

Proteomic databases

EPDiQ8K2C8.
MaxQBiQ8K2C8.
PaxDbiQ8K2C8.
PRIDEiQ8K2C8.

PTM databases

iPTMnetiQ8K2C8.
PhosphoSitePlusiQ8K2C8.

Expressioni

Gene expression databases

BgeeiENSMUSG00000031545.
GenevisibleiQ8K2C8. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000127325.

Structurei

3D structure databases

ProteinModelPortaliQ8K2C8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi248 – 253HXXXXD 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

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2898. Eukaryota.
COG0204. LUCA.
GeneTreeiENSGT00390000000536.
HOGENOMiHOG000265725.
InParanoidiQ8K2C8.
KOiK13506.
OMAiKIFQWAT.
OrthoDBiEOG091G04E8.
PhylomeDBiQ8K2C8.
TreeFamiTF315039.

Family and domain databases

InterProiIPR002123. Plipid/glycerol_acylTrfase.
[Graphical view]
PfamiPF01553. Acyltransferase. 1 hit.
[Graphical view]
SMARTiSM00563. PlsC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q8K2C8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFLLLPFDSL IVNLLGISLT VLFTLLLVFI IVPAIFGVSF GIRKLYMKTL
60 70 80 90 100
LKIFAWATLR MERGAKERNH QLYKPYTNGI IAKDPTSLEE EIKEIRRSGS
110 120 130 140 150
SKALDKTPEF ELSDIFYFCR KGMETIMDDE VTKRFSAEEL ESWNLLSRTN
160 170 180 190 200
YNFQYISLRL TILWGLGVLI RYCFLLPLRI ALAFTGIGLL VVGTTMVGYL
210 220 230 240 250
PNGRFKEFLS KHVHLMCYRI CVRALTAIIT YHNRKNRPRN GGICVANHTS
260 270 280 290 300
PIDVIILASD GYYAMVGQVH GGLMGVIQRA MVKACPHVWF ERSEVKDRHL
310 320 330 340 350
VAKRLTEHVQ DKSKLPILIF PEGTCINNTS VMMFKKGSFE IGATVYPVAI
360 370 380 390 400
KYDPQFGDAF WNSSKYGMVT YLLRMMTSWA IVCSVWYLPP MTREKDEDAV
410 420 430 440 450
QFANRVKSAI ARQGGLVDLL WDGGLKREKV KDTFKEEQQK LYSKMIVGNH

EDRSRS
Length:456
Mass (Da):52,181
Last modified:October 1, 2002 - v1
Checksum:i2C3E1C37044C14FA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF406611 mRNA. Translation: AAP97283.1.
AK045235 mRNA. Translation: BAC32273.1.
AK077561 mRNA. Translation: BAC36864.1.
AK083589 mRNA. Translation: BAC38962.1.
AK161270 mRNA. Translation: BAE36282.1.
AK169257 mRNA. Translation: BAE41020.1.
BC031767 mRNA. Translation: AAH31767.1.
CCDSiCCDS22189.1.
RefSeqiNP_061213.2. NM_018743.4.
UniGeneiMm.200898.
Mm.241152.

Genome annotation databases

EnsembliENSMUST00000167004; ENSMUSP00000127325; ENSMUSG00000031545.
GeneIDi102247.
KEGGimmu:102247.
UCSCiuc009leo.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF406611 mRNA. Translation: AAP97283.1.
AK045235 mRNA. Translation: BAC32273.1.
AK077561 mRNA. Translation: BAC36864.1.
AK083589 mRNA. Translation: BAC38962.1.
AK161270 mRNA. Translation: BAE36282.1.
AK169257 mRNA. Translation: BAE41020.1.
BC031767 mRNA. Translation: AAH31767.1.
CCDSiCCDS22189.1.
RefSeqiNP_061213.2. NM_018743.4.
UniGeneiMm.200898.
Mm.241152.

3D structure databases

ProteinModelPortaliQ8K2C8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000127325.

Chemistry databases

SwissLipidsiSLP:000000104.

PTM databases

iPTMnetiQ8K2C8.
PhosphoSitePlusiQ8K2C8.

Proteomic databases

EPDiQ8K2C8.
MaxQBiQ8K2C8.
PaxDbiQ8K2C8.
PRIDEiQ8K2C8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000167004; ENSMUSP00000127325; ENSMUSG00000031545.
GeneIDi102247.
KEGGimmu:102247.
UCSCiuc009leo.2. mouse.

Organism-specific databases

CTDi137964.
MGIiMGI:2142716. Gpat4.

Phylogenomic databases

eggNOGiKOG2898. Eukaryota.
COG0204. LUCA.
GeneTreeiENSGT00390000000536.
HOGENOMiHOG000265725.
InParanoidiQ8K2C8.
KOiK13506.
OMAiKIFQWAT.
OrthoDBiEOG091G04E8.
PhylomeDBiQ8K2C8.
TreeFamiTF315039.

Enzyme and pathway databases

UniPathwayiUPA00557; UER00612.
BRENDAi2.3.1.15. 3474.
ReactomeiR-MMU-1483166. Synthesis of PA.
R-MMU-75109. Triglyceride Biosynthesis.

Miscellaneous databases

ChiTaRSiAgpat6. mouse.
PROiQ8K2C8.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000031545.
GenevisibleiQ8K2C8. MM.

Family and domain databases

InterProiIPR002123. Plipid/glycerol_acylTrfase.
[Graphical view]
PfamiPF01553. Acyltransferase. 1 hit.
[Graphical view]
SMARTiSM00563. PlsC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGPAT4_MOUSE
AccessioniPrimary (citable) accession number: Q8K2C8
Secondary accession number(s): Q3TF78
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: October 1, 2002
Last modified: November 2, 2016
This is version 119 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.