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Protein

Glycerol-3-phosphate acyltransferase 3

Gene

Gpat3

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 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) (By similarity).By similarity

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.

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 3 (Gpat3), Glycerol-3-phosphate acyltransferase 1, mitochondrial (Gpam)
  2. 1-acyl-sn-glycerol-3-phosphate acyltransferase delta (Agpat4)
  3. Phosphatidate cytidylyltransferase 2 (Cds2), Phosphatidate cytidylyltransferase (Cds2), Phosphatidate cytidylyltransferase 1 (Cds1), Phosphatidate cytidylyltransferase, mitochondrial (Tamm41)
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

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Enzyme and pathway databases

ReactomeiR-RNO-1483166. Synthesis of PA.
R-RNO-75109. Triglyceride Biosynthesis.
UniPathwayiUPA00282.
UPA00557; UER00612.

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 9 (EC:2.3.1.51)
Short name:
1-AGP acyltransferase 9
Short name:
1-AGPAT 9
Lysophosphatidic acid acyltransferase theta
Short name:
LPAAT-theta
Gene namesi
Name:Gpat3Imported
Synonyms:Agpat9
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 14

Organism-specific databases

RGDi1565703. Gpat3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei14 – 3421HelicalSequence analysisAdd
BLAST
Transmembranei137 – 15721HelicalSequence analysisAdd
BLAST
Transmembranei161 – 18121HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 457457Glycerol-3-phosphate acyltransferase 3PRO_0000291572Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei68 – 681PhosphoserineCombined sources
Modified residuei77 – 771PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ4V8J4.

PTM databases

iPTMnetiQ4V8J4.
PhosphoSiteiQ4V8J4.

Expressioni

Gene expression databases

GenevisibleiQ4V8J4. RN.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000002936.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi229 – 2346HXXXXD motif

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.
InParanoidiQ4V8J4.
KOiK13506.
OMAiEVYMKIL.
OrthoDBiEOG70GMFG.
PhylomeDBiQ4V8J4.
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.

Q4V8J4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEGTDLVVKL LSTWLTLVGS LILLPSAFGL SLGISEIYMK ILVKTLEWAT
60 70 80 90 100
LRIEKGAPKE SVLKSPASMG IIQRDESPME KGLSGLRGRD FELSDVFYFS
110 120 130 140 150
KKGLEAIVED EVTQRFSSEE LVSWNLLTRT NVNFHYISPK LTIVWVLGVL
160 170 180 190 200
VRYCFLLPLR VTLAFIGISL LIIGTTLVGQ LPDSSLKNWL SELVHLTCCR
210 220 230 240 250
ICVRSLSGTI HYHNKQYRPQ KGGICVANHT SPIDVLILAT DGCYAMVGQV
260 270 280 290 300
HGGLMGIIQR AMVKACPHVW FERSEIKDRH LVTKRLKEHI ADKKKLPILI
310 320 330 340 350
FPEGTCINNT SVMMFKKGSF EIGGTIYPVA IKYNPQFGDA FWNSSKYNLV
360 370 380 390 400
SYLLRIMTSW AIVCDVWYMP PMTREEGEDA VQFANRVKSA IAVQGGLTEL
410 420 430 440 450
PWDGGLKRAK VKDTFKEEQQ KTYSKMIVGN GSPSLALDSS TVDNHGSPEP

AFRSESL
Length:457
Mass (Da):51,012
Last modified:July 5, 2005 - v1
Checksum:iBC8A63BF240137A9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC097362 mRNA. Translation: AAH97362.1.
RefSeqiNP_001020841.1. NM_001025670.1.
XP_008768241.1. XM_008770019.1.
XP_008768242.1. XM_008770020.1.
XP_008768243.1. XM_008770021.1.
UniGeneiRn.214521.

Genome annotation databases

EnsembliENSRNOT00000002936; ENSRNOP00000002936; ENSRNOG00000002159.
GeneIDi305166.
KEGGirno:305166.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC097362 mRNA. Translation: AAH97362.1.
RefSeqiNP_001020841.1. NM_001025670.1.
XP_008768241.1. XM_008770019.1.
XP_008768242.1. XM_008770020.1.
XP_008768243.1. XM_008770021.1.
UniGeneiRn.214521.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000002936.

PTM databases

iPTMnetiQ4V8J4.
PhosphoSiteiQ4V8J4.

Proteomic databases

PaxDbiQ4V8J4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000002936; ENSRNOP00000002936; ENSRNOG00000002159.
GeneIDi305166.
KEGGirno:305166.

Organism-specific databases

CTDi84803.
RGDi1565703. Gpat3.

Phylogenomic databases

eggNOGiKOG2898. Eukaryota.
COG0204. LUCA.
GeneTreeiENSGT00390000000536.
HOGENOMiHOG000265725.
InParanoidiQ4V8J4.
KOiK13506.
OMAiEVYMKIL.
OrthoDBiEOG70GMFG.
PhylomeDBiQ4V8J4.
TreeFamiTF315039.

Enzyme and pathway databases

UniPathwayiUPA00282.
UPA00557; UER00612.
ReactomeiR-RNO-1483166. Synthesis of PA.
R-RNO-75109. Triglyceride Biosynthesis.

Miscellaneous databases

PROiQ4V8J4.

Gene expression databases

GenevisibleiQ4V8J4. RN.

Family and domain databases

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

Publicationsi

  1. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Placenta.
  2. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiGPAT3_RAT
AccessioniPrimary (citable) accession number: Q4V8J4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: July 5, 2005
Last modified: June 8, 2016
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Despite its name, the human ortholog of 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.