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Protein

Glycerol-3-phosphate acyltransferase 3

Gene

GPAT3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May transfer the acyl-group from acyl-coA to the sn-1 position of glycerol-3-phosphate, an essential step in glycerolipid biosynthesis. Also transfers the acyl-group from acyl-coA to the sn-2 position of 1-acyl-sn-glycerol-3-phosphate (lysophosphatidic acid, or LPA), forming 1,2-diacyl-sn-glycerol-3-phosphate (phosphatidic acid, or PA).3 Publications

Catalytic activityi

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

Enzyme regulationi

Inhibited by N-ethylmaleimide (NEM).1 Publication

Pathwayi: triacylglycerol biosynthesis

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

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 2, mitochondrial (GPAT2), Glycerol-3-phosphate acyltransferase 1, mitochondrial (GPAM), Glycerol-3-phosphate acyltransferase 1, mitochondrial (GPAM), Glycerol-3-phosphate acyltransferase 4 (GPAT4), Glycerol-3-phosphate acyltransferase 3 (GPAT3), Glycerol-3-phosphate acyltransferase 1, mitochondrial, Glycerol-3-phosphate acyltransferase 1, mitochondrial (GPAM), Glycerol-3-phosphate acyltransferase 1, mitochondrial (DKFZp451B1115)
  2. 1-acyl-sn-glycerol-3-phosphate acyltransferase beta (AGPAT2), 1-acyl-sn-glycerol-3-phosphate acyltransferase delta (AGPAT4), 1-acyl-sn-glycerol-3-phosphate acyltransferase gamma (AGPAT3), 1-acyl-sn-glycerol-3-phosphate acyltransferase epsilon (AGPAT5), 1-acyl-sn-glycerol-3-phosphate acyltransferase alpha (AGPAT1), Lysocardiolipin acyltransferase 1 (LCLAT1)
  3. Phosphatidate cytidylyltransferase 1 (CDS1), Phosphatidate cytidylyltransferase 2 (CDS2), Phosphatidate cytidylyltransferase, mitochondrial (TAMM41), Phosphatidate cytidylyltransferase (CDS1), Phosphatidate cytidylyltransferase, Phosphatidate cytidylyltransferase, Phosphatidate cytidylyltransferase, Phosphatidate cytidylyltransferase
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

GO - Biological processi

  • CDP-diacylglycerol biosynthetic process Source: UniProtKB-UniPathway
  • phosphatidic acid biosynthetic process Source: Reactome
  • regulation of TOR signaling Source: UniProtKB
  • triglyceride biosynthetic process Source: UniProtKB

Keywordsi

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

Enzyme and pathway databases

BRENDAi2.3.1.15. 2681.
ReactomeiR-HSA-1483166. Synthesis of PA.
UniPathwayiUPA00282.
UPA00557; UER00612.

Chemistry databases

SwissLipidsiSLP:000000290.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycerol-3-phosphate acyltransferase 3Imported (EC:2.3.1.15)
Short name:
GPAT-3
Alternative name(s):
1-acyl-sn-glycerol-3-phosphate O-acyltransferase 10
Short name:
AGPAT 10
1-acyl-sn-glycerol-3-phosphate O-acyltransferase 9 (EC:2.3.1.51)
Short name:
1-AGP acyltransferase 9
Short name:
1-AGPAT 9
Acyl-CoA:glycerol-3-phosphate acyltransferase 3
Short name:
hGPAT3
Lung cancer metastasis-associated protein 1
Lysophosphatidic acid acyltransferase theta
Short name:
LPAAT-theta
MAG-1
Gene namesi
Name:GPAT3Imported
Synonyms:AGPAT9, MAG1
ORF Names:HMFN0839, UNQ2753/PRO6492
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

EuPathDBiHostDB:ENSG00000138678.10.
HGNCiHGNC:28157. GPAT3.

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
Transmembranei14 – 34HelicalSequence analysisAdd BLAST21
Transmembranei137 – 157HelicalSequence analysisAdd BLAST21
Transmembranei161 – 181HelicalSequence analysisAdd BLAST21

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Organism-specific databases

DisGeNETi84803.
OpenTargetsiENSG00000138678.
PharmGKBiPA162375888.

Polymorphism and mutation databases

BioMutaiAGPAT9.
DMDMi150403919.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002915701 – 434Glycerol-3-phosphate acyltransferase 3Add BLAST434

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei68PhosphoserineCombined sources1
Modified residuei77PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ53EU6.
MaxQBiQ53EU6.
PaxDbiQ53EU6.
PeptideAtlasiQ53EU6.
PRIDEiQ53EU6.

PTM databases

iPTMnetiQ53EU6.
PhosphoSitePlusiQ53EU6.

Expressioni

Tissue specificityi

Widely expressed. Expressed in liver, kidney, testis, brain, heart, skeletal muscle, thyroid, prostate, thymus and placenta. Also expressed lung and adipose tissue.2 Publications

Gene expression databases

BgeeiENSG00000138678.
CleanExiHS_AGPAT9.
ExpressionAtlasiQ53EU6. baseline and differential.
GenevisibleiQ53EU6. HS.

Organism-specific databases

HPAiCAB033749.
HPA029414.

Interactioni

Protein-protein interaction databases

BioGridi124267. 15 interactors.
IntActiQ53EU6. 4 interactors.
STRINGi9606.ENSP00000264409.

Structurei

3D structure databases

ProteinModelPortaliQ53EU6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi229 – 234HXXXXD 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

eggNOGiKOG2898. Eukaryota.
COG0204. LUCA.
GeneTreeiENSGT00390000000536.
HOGENOMiHOG000265725.
InParanoidiQ53EU6.
KOiK13506.
OMAiNINFQYI.
OrthoDBiEOG091G04E8.
PhylomeDBiQ53EU6.
TreeFamiTF315039.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Q53EU6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEGAELAGKI LSTWLTLVLG FILLPSVFGV SLGISEIYMK ILVKTLEWAT
60 70 80 90 100
IRIEKGTPKE SILKNSASVG IIQRDESPME KGLSGLRGRD FELSDVFYFS
110 120 130 140 150
KKGLEAIVED EVTQRFSSEE LVSWNLLTRT NVNFQYISLR LTMVWVLGVI
160 170 180 190 200
VRYCVLLPLR VTLAFIGISL LVIGTTLVGQ LPDSSLKNWL SELVHLTCCR
210 220 230 240 250
ICVRALSGTI HYHNKQYRPQ KGGICVANHT SPIDVLILTT DGCYAMVGQV
260 270 280 290 300
HGGLMGIIQR AMVKACPHVW FERSEMKDRH LVTKRLKEHI ADKKKLPILI
310 320 330 340 350
FPEGTCINNT SVMMFKKGSF EIGGTIHPVA IKYNPQFGDA FWNSSKYNMV
360 370 380 390 400
SYLLRMMTSW AIVCDVWYMP PMTREEGEDA VQFANRVKSA IAIQGGLTEL
410 420 430
PWDGGLKRAK VKDIFKEEQQ KNYSKMIVGN GSLS
Length:434
Mass (Da):48,705
Last modified:June 26, 2007 - v2
Checksum:i80DD5423E5E7847A
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti156L → I in BAD97263 (Ref. 5) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ324782 mRNA. Translation: ABC55674.1.
DQ345298 mRNA. Translation: ABC70186.1.
AY358100 mRNA. Translation: AAQ88467.1.
AK055749 mRNA. Translation: BAB71002.1.
AK223543 mRNA. Translation: BAD97263.1.
BC073136 mRNA. Translation: AAH73136.1.
BC090956 mRNA. Translation: AAH90956.1.
AB075872 mRNA. Translation: BAD38654.1.
CCDSiCCDS3606.1.
RefSeqiNP_001243350.1. NM_001256421.1.
NP_001243351.1. NM_001256422.1.
NP_116106.2. NM_032717.4.
XP_016864270.1. XM_017008781.1.
UniGeneiHs.99196.

Genome annotation databases

EnsembliENST00000264409; ENSP00000264409; ENSG00000138678.
ENST00000395226; ENSP00000378651; ENSG00000138678.
ENST00000611707; ENSP00000482571; ENSG00000138678.
GeneIDi84803.
KEGGihsa:84803.
UCSCiuc003how.5. human.

Similar proteinsi

Entry informationi

Entry nameiGPAT3_HUMAN
AccessioniPrimary (citable) accession number: Q53EU6
Secondary accession number(s): Q68CJ4, Q6GPI6, Q96NA3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: June 26, 2007
Last modified: September 27, 2017
This is version 105 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Caution

Despite its name, this protein appears to lack measurable glycerol-3-phosphate acyltransferase activity under some conditions (PMID:19318427).Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. SIMILARITY comments
    Index of protein domains and families