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Protein

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

Gene

AGPAT5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 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. 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.

Kineticsi

  1. KM=5.52 µM for LPA sn-1 C18:1
  2. KM=16.30 µM for C18:1-CoA
  1. Vmax=2.42 nmol/min/mg enzyme toward LPA sn-1 C18:1
  2. Vmax=1.22 nmol/min/mg enzyme toward C18:1-CoA

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 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

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

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

BioCyciMetaCyc:HS08034-MONOMER.
ZFISH:HS08034-MONOMER.
BRENDAi2.3.1.51. 2681.
ReactomeiR-HSA-1483166. Synthesis of PA.
R-HSA-75109. Triglyceride Biosynthesis.
UniPathwayiUPA00557; UER00613.

Chemistry databases

SwissLipidsiSLP:000000822.

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:20886. AGPAT5.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei15 – 35HelicalSequence analysisAdd BLAST21
Transmembranei61 – 81HelicalSequence analysisAdd BLAST21
Transmembranei344 – 364HelicalSequence analysisAdd BLAST21

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Mitochondrion, Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi55326.
OpenTargetsiENSG00000155189.
PharmGKBiPA134952751.

Polymorphism and mutation databases

BioMutaiAGPAT5.
DMDMi30923427.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002082001 – 3641-acyl-sn-glycerol-3-phosphate acyltransferase epsilonAdd BLAST364

Proteomic databases

EPDiQ9NUQ2.
MaxQBiQ9NUQ2.
PaxDbiQ9NUQ2.
PeptideAtlasiQ9NUQ2.
PRIDEiQ9NUQ2.

PTM databases

iPTMnetiQ9NUQ2.
PhosphoSitePlusiQ9NUQ2.
SwissPalmiQ9NUQ2.

Expressioni

Tissue specificityi

Widely expressed.2 Publications

Gene expression databases

BgeeiENSG00000155189.
CleanExiHS_AGPAT5.
ExpressionAtlasiQ9NUQ2. baseline and differential.
GenevisibleiQ9NUQ2. HS.

Organism-specific databases

HPAiHPA010644.
HPA010950.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
UBQLN1Q9UMX03EBI-6916385,EBI-741480

Protein-protein interaction databases

BioGridi120607. 9 interactors.
IntActiQ9NUQ2. 2 interactors.
MINTiMINT-4725223.
STRINGi9606.ENSP00000285518.

Structurei

3D structure databases

ProteinModelPortaliQ9NUQ2.
SMRiQ9NUQ2.
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.
GeneTreeiENSGT00530000062943.
HOGENOMiHOG000007801.
HOVERGENiHBG039632.
InParanoidiQ9NUQ2.
KOiK19007.
OMAiWFPATIM.
OrthoDBiEOG091G0C4Z.
PhylomeDBiQ9NUQ2.
TreeFamiTF314346.

Family and domain databases

InterProiIPR032098. Acyltransf_C.
IPR002123. Plipid/glycerol_acylTrfase.
[Graphical view]
PfamiPF16076. Acyltransf_C. 1 hit.
PF01553. Acyltransferase. 1 hit.
[Graphical view]
SMARTiSM00563. PlsC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9NUQ2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLLSLVLHTY SMRYLLPSVV LLGTAPTYVL AWGVWRLLSA FLPARFYQAL
60 70 80 90 100
DDRLYCVYQS MVLFFFENYT GVQILLYGDL PKNKENIIYL ANHQSTVDWI
110 120 130 140 150
VADILAIRQN ALGHVRYVLK EGLKWLPLYG CYFAQHGGIY VKRSAKFNEK
160 170 180 190 200
EMRNKLQSYV DAGTPMYLVI FPEGTRYNPE QTKVLSASQA FAAQRGLAVL
210 220 230 240 250
KHVLTPRIKA THVAFDCMKN YLDAIYDVTV VYEGKDDGGQ RRESPTMTEF
260 270 280 290 300
LCKECPKIHI HIDRIDKKDV PEEQEHMRRW LHERFEIKDK MLIEFYESPD
310 320 330 340 350
PERRKRFPGK SVNSKLSIKK TLPSMLILSG LTAGMLMTDA GRKLYVNTWI
360
YGTLLGCLWV TIKA
Length:364
Mass (Da):42,072
Last modified:May 16, 2003 - v3
Checksum:i90A0F87FC7C78081
GO

Sequence cautioni

The sequence BAA92069 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti156L → V in BAA92069 (PubMed:11230166).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02269677Y → C.Corresponds to variant rs17077958dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF375789 mRNA. Translation: AAK54809.1.
AL136587 mRNA. Translation: CAB66522.1.
BC023550 mRNA. Translation: AAH23550.1.
BC080537 mRNA. Translation: AAH80537.1.
AK002072 mRNA. Translation: BAA92069.1. Different initiation.
CCDSiCCDS34796.1.
RefSeqiNP_060831.2. NM_018361.3.
UniGeneiHs.624002.

Genome annotation databases

EnsembliENST00000285518; ENSP00000285518; ENSG00000155189.
GeneIDi55326.
KEGGihsa:55326.
UCSCiuc003wqo.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF375789 mRNA. Translation: AAK54809.1.
AL136587 mRNA. Translation: CAB66522.1.
BC023550 mRNA. Translation: AAH23550.1.
BC080537 mRNA. Translation: AAH80537.1.
AK002072 mRNA. Translation: BAA92069.1. Different initiation.
CCDSiCCDS34796.1.
RefSeqiNP_060831.2. NM_018361.3.
UniGeneiHs.624002.

3D structure databases

ProteinModelPortaliQ9NUQ2.
SMRiQ9NUQ2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120607. 9 interactors.
IntActiQ9NUQ2. 2 interactors.
MINTiMINT-4725223.
STRINGi9606.ENSP00000285518.

Chemistry databases

SwissLipidsiSLP:000000822.

PTM databases

iPTMnetiQ9NUQ2.
PhosphoSitePlusiQ9NUQ2.
SwissPalmiQ9NUQ2.

Polymorphism and mutation databases

BioMutaiAGPAT5.
DMDMi30923427.

Proteomic databases

EPDiQ9NUQ2.
MaxQBiQ9NUQ2.
PaxDbiQ9NUQ2.
PeptideAtlasiQ9NUQ2.
PRIDEiQ9NUQ2.

Protocols and materials databases

DNASUi55326.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000285518; ENSP00000285518; ENSG00000155189.
GeneIDi55326.
KEGGihsa:55326.
UCSCiuc003wqo.4. human.

Organism-specific databases

CTDi55326.
DisGeNETi55326.
GeneCardsiAGPAT5.
HGNCiHGNC:20886. AGPAT5.
HPAiHPA010644.
HPA010950.
MIMi614796. gene.
neXtProtiNX_Q9NUQ2.
OpenTargetsiENSG00000155189.
PharmGKBiPA134952751.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1505. Eukaryota.
COG0204. LUCA.
GeneTreeiENSGT00530000062943.
HOGENOMiHOG000007801.
HOVERGENiHBG039632.
InParanoidiQ9NUQ2.
KOiK19007.
OMAiWFPATIM.
OrthoDBiEOG091G0C4Z.
PhylomeDBiQ9NUQ2.
TreeFamiTF314346.

Enzyme and pathway databases

UniPathwayiUPA00557; UER00613.
BioCyciMetaCyc:HS08034-MONOMER.
ZFISH:HS08034-MONOMER.
BRENDAi2.3.1.51. 2681.
ReactomeiR-HSA-1483166. Synthesis of PA.
R-HSA-75109. Triglyceride Biosynthesis.

Miscellaneous databases

ChiTaRSiAGPAT5. human.
GeneWikiiAGPAT5.
GenomeRNAii55326.
PROiQ9NUQ2.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000155189.
CleanExiHS_AGPAT5.
ExpressionAtlasiQ9NUQ2. baseline and differential.
GenevisibleiQ9NUQ2. HS.

Family and domain databases

InterProiIPR032098. Acyltransf_C.
IPR002123. Plipid/glycerol_acylTrfase.
[Graphical view]
PfamiPF16076. Acyltransf_C. 1 hit.
PF01553. Acyltransferase. 1 hit.
[Graphical view]
SMARTiSM00563. PlsC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPLCE_HUMAN
AccessioniPrimary (citable) accession number: Q9NUQ2
Secondary accession number(s): Q8IZ47, Q9BQG4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: May 16, 2003
Last modified: November 2, 2016
This is version 130 of the entry and version 3 of the sequence. [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

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. 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.