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Protein

Glycerol-3-phosphate acyltransferase 1, mitochondrial

Gene

Gpam

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.By similarity

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: MGI

GO - Biological processi

  • acyl-CoA metabolic process Source: MGI
  • CDP-diacylglycerol biosynthetic process Source: UniProtKB-UniPathway
  • defense response to virus Source: MGI
  • fatty acid homeostasis Source: MGI
  • fatty acid metabolic process Source: MGI
  • glycerophospholipid metabolic process Source: MGI
  • interleukin-2 secretion Source: MGI
  • negative regulation of activation-induced cell death of T cells Source: MGI
  • phospholipid homeostasis Source: MGI
  • positive regulation of activated T cell proliferation Source: MGI
  • positive regulation of multicellular organism growth Source: MGI
  • regulation of cytokine secretion Source: MGI
  • response to glucose Source: MGI
  • triglyceride biosynthetic process Source: MGI
  • 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-2426168. Activation of gene expression by SREBF (SREBP).
R-MMU-75109. Triglyceride Biosynthesis.
SABIO-RKQ61586.
UniPathwayiUPA00557; UER00612.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycerol-3-phosphate acyltransferase 1, mitochondrial (EC:2.3.1.15)
Short name:
GPAT-1
Alternative name(s):
P90
Gene namesi
Name:Gpam
Synonyms:Gpat1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:109162. Gpam.

Subcellular locationi

  • Mitochondrion outer membrane By similarity; Multi-pass membrane protein By similarity

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini? – 471Mitochondrial intermembraneSequence analysis
Transmembranei472 – 494HelicalSequence analysisAdd BLAST23
Topological domaini495 – 574CytoplasmicSequence analysisAdd BLAST80
Transmembranei575 – 593HelicalSequence analysisAdd BLAST19
Topological domaini594 – 827Mitochondrial intermembraneSequence analysisAdd BLAST234

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • mitochondrial inner membrane Source: MGI
  • mitochondrial outer membrane Source: UniProtKB-SubCell
  • mitochondrion Source: MGI
  • plasma membrane Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion outer membrane

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3580525.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000024691? – 827Glycerol-3-phosphate acyltransferase 1, mitochondrial
Transit peptidei1 – ?MitochondrionSequence analysis

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei380PhosphoserineBy similarity1
Modified residuei687PhosphoserineCombined sources1
Modified residuei694PhosphoserineCombined sources1
Modified residuei779N6-acetyllysineCombined sources1
Modified residuei783N6-acetyllysineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ61586.
PaxDbiQ61586.
PeptideAtlasiQ61586.
PRIDEiQ61586.

PTM databases

iPTMnetiQ61586.
PhosphoSitePlusiQ61586.

Expressioni

Tissue specificityi

Highest levels in liver, intermediate levels in muscle and kidney, and lowest levels in lung and brain.

Gene expression databases

BgeeiENSMUSG00000024978.
GenevisibleiQ61586. MM.

Interactioni

Protein-protein interaction databases

BioGridi200011. 1 interactor.
IntActiQ61586. 1 interactor.
MINTiMINT-4119610.
STRINGi10090.ENSMUSP00000057635.

Structurei

3D structure databases

ProteinModelPortaliQ61586.
SMRiQ61586.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi230 – 235HXXXXD 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

Belongs to the GPAT/DAPAT family.Curated

Keywords - Domaini

Transit peptide, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3729. Eukaryota.
COG2937. LUCA.
GeneTreeiENSGT00520000055570.
HOVERGENiHBG000102.
InParanoidiQ61586.
KOiK00629.
OMAiKPCMPKG.
OrthoDBiEOG091G0IKA.
TreeFamiTF313360.

Family and domain databases

InterProiIPR022284. GPAT/DHAPAT.
IPR028354. GPAT_PlsB.
IPR002123. Plipid/glycerol_acylTrfase.
[Graphical view]
PANTHERiPTHR12563. PTHR12563. 1 hit.
PfamiPF01553. Acyltransferase. 1 hit.
[Graphical view]
PIRSFiPIRSF500064. GPAT. 1 hit.
PIRSF000437. GPAT_DHAPAT. 1 hit.
SMARTiSM00563. PlsC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q61586-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEESSVTVGT IDVSYLPSSS EYSLGRCKHT SEDWVDCGFK PTFFRSATLK
60 70 80 90 100
WKESLMSRKR PFVGRCCYSC TPQSWERFFN PSIPSLGLRN VIYINETHTR
110 120 130 140 150
HRGWLARRLS YILFVQERDV HKGMFATSVT ENVLSSSRVQ EAIAEVAAEL
160 170 180 190 200
NPDGSAQQQS KAIQKVKRKA RKILQEMVAT VSPGMIRLTG WVLLKLFNSF
210 220 230 240 250
FWNIQIHKGQ LEMVKAATET NLPLLFLPVH RSHIDYLLLT FILFCHNIKA
260 270 280 290 300
PYIASGNNLN IPVFSTLIHK LGGFFIRRRL DETPDGRKDI LYRALLHGHV
310 320 330 340 350
VELLRQQQFL EIFLEGTRSR SGKTSCARAG LLSVVVDTLS SNTIPDILVI
360 370 380 390 400
PVGISYDRII EGHYNGEQLG KPKKNESLWS VARGVIRMLR KNYGYVRVDF
410 420 430 440 450
AQPFSLKEYL EGQSQKPVSA PLSLEQALLP AILPSRPNDV ADEHQDLSSN
460 470 480 490 500
ESRNPADEAF RRRLIANLAE HILFTASKSC AIMSTHIVAC LLLYRHRQGI
510 520 530 540 550
HLSTLVEDFF VMKEEVLARD FDLGFSGNSE DVVMHAIQLL GNCVTITHTS
560 570 580 590 600
RKDEFFITPS TTVPSVFELN FYSNGVLHVF IMEAIIACSI YAVLNKRCSG
610 620 630 640 650
GSAGGLGNLI SQEQLVRKAA SLCYLLSNEG TISLPCQTFY QVCHETVGKF
660 670 680 690 700
IQYGILTVAE QDDQEDVSPG LAEQQWDKKL PELNWRSDEE DEDSDFGEEQ
710 720 730 740 750
RDCYLKVSQS KEHQQFITFL QRLLGPLLEA YSSAAIFVHN FSGPVPESEY
760 770 780 790 800
LQKLHRYLIT RTERNVAVYA ESATYCLVKN AVKMFKDIGV FKETKQKRVS
810 820
VLELSSTFLP QCNRQKLLEY ILSFVVL
Length:827
Mass (Da):93,705
Last modified:July 27, 2011 - v2
Checksum:i4C177AA15374EE9B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti331L → V in AAA37647 (PubMed:1721057).Curated1
Sequence conflicti337D → N in AAA37647 (PubMed:1721057).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M77003 mRNA. Translation: AAA37647.1.
DQ479922 Genomic DNA. Translation: ABF48501.1.
AK137067 mRNA. Translation: BAE23226.1.
CH466585 Genomic DNA. Translation: EDL01718.1.
CH466585 Genomic DNA. Translation: EDL01719.1.
BC019201 mRNA. Translation: AAH19201.1.
CCDSiCCDS29906.1.
PIRiA41672.
RefSeqiNP_032175.2. NM_008149.3.
XP_006526755.1. XM_006526692.3.
XP_006526756.1. XM_006526693.3.
XP_006526757.1. XM_006526694.1.
XP_011245449.1. XM_011247147.1.
UniGeneiMm.210196.

Genome annotation databases

EnsembliENSMUST00000061856; ENSMUSP00000057635; ENSMUSG00000024978.
GeneIDi14732.
KEGGimmu:14732.
UCSCiuc008hxk.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M77003 mRNA. Translation: AAA37647.1.
DQ479922 Genomic DNA. Translation: ABF48501.1.
AK137067 mRNA. Translation: BAE23226.1.
CH466585 Genomic DNA. Translation: EDL01718.1.
CH466585 Genomic DNA. Translation: EDL01719.1.
BC019201 mRNA. Translation: AAH19201.1.
CCDSiCCDS29906.1.
PIRiA41672.
RefSeqiNP_032175.2. NM_008149.3.
XP_006526755.1. XM_006526692.3.
XP_006526756.1. XM_006526693.3.
XP_006526757.1. XM_006526694.1.
XP_011245449.1. XM_011247147.1.
UniGeneiMm.210196.

3D structure databases

ProteinModelPortaliQ61586.
SMRiQ61586.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200011. 1 interactor.
IntActiQ61586. 1 interactor.
MINTiMINT-4119610.
STRINGi10090.ENSMUSP00000057635.

Chemistry databases

ChEMBLiCHEMBL3580525.

PTM databases

iPTMnetiQ61586.
PhosphoSitePlusiQ61586.

Proteomic databases

MaxQBiQ61586.
PaxDbiQ61586.
PeptideAtlasiQ61586.
PRIDEiQ61586.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000061856; ENSMUSP00000057635; ENSMUSG00000024978.
GeneIDi14732.
KEGGimmu:14732.
UCSCiuc008hxk.1. mouse.

Organism-specific databases

CTDi57678.
MGIiMGI:109162. Gpam.

Phylogenomic databases

eggNOGiKOG3729. Eukaryota.
COG2937. LUCA.
GeneTreeiENSGT00520000055570.
HOVERGENiHBG000102.
InParanoidiQ61586.
KOiK00629.
OMAiKPCMPKG.
OrthoDBiEOG091G0IKA.
TreeFamiTF313360.

Enzyme and pathway databases

UniPathwayiUPA00557; UER00612.
BRENDAi2.3.1.15. 3474.
ReactomeiR-MMU-1483166. Synthesis of PA.
R-MMU-2426168. Activation of gene expression by SREBF (SREBP).
R-MMU-75109. Triglyceride Biosynthesis.
SABIO-RKQ61586.

Miscellaneous databases

PROiQ61586.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000024978.
GenevisibleiQ61586. MM.

Family and domain databases

InterProiIPR022284. GPAT/DHAPAT.
IPR028354. GPAT_PlsB.
IPR002123. Plipid/glycerol_acylTrfase.
[Graphical view]
PANTHERiPTHR12563. PTHR12563. 1 hit.
PfamiPF01553. Acyltransferase. 1 hit.
[Graphical view]
PIRSFiPIRSF500064. GPAT. 1 hit.
PIRSF000437. GPAT_DHAPAT. 1 hit.
SMARTiSM00563. PlsC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGPAT1_MOUSE
AccessioniPrimary (citable) accession number: Q61586
Secondary accession number(s): Q8VCT2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 27, 2011
Last modified: November 30, 2016
This is version 140 of the entry and version 2 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.