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Protein

Glycerol-3-phosphate acyltransferase 1, mitochondrial

Gene

Gpam

Organism
Rattus norvegicus (Rat)
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.1 Publication

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), Glycerol-3-phosphate acyltransferase 1, mitochondrial (Gpam), 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

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

GO - Biological processi

  • CDP-diacylglycerol biosynthetic process Source: UniProtKB-UniPathway
  • cellular response to insulin stimulus Source: RGD
  • positive regulation of triglyceride biosynthetic process Source: RGD
  • response to activity Source: RGD
  • response to cadmium ion Source: RGD
  • response to fructose Source: RGD
  • response to nutrient levels Source: RGD
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. 5301.
SABIO-RKP97564.
UniPathwayiUPA00557; UER00612.

Chemistry databases

SwissLipidsiSLP:000000284.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycerol-3-phosphate acyltransferase 1, mitochondrial (EC:2.3.1.15)
Short name:
GPAT-1
Gene namesi
Name:Gpam
Synonyms:Gpat1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi61847. Gpam.

Subcellular locationi

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 – 828Mitochondrial intermembraneSequence analysisAdd BLAST235

GO - Cellular componenti

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

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion outer membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000024692? – 828Glycerol-3-phosphate acyltransferase 1, mitochondrial
Transit peptidei1 – ?MitochondrionSequence analysis

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei380PhosphoserineCombined sources1
Modified residuei688PhosphoserineCombined sources1
Modified residuei695PhosphoserineCombined sources1
Modified residuei780N6-acetyllysineBy similarity1
Modified residuei784N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP97564.
PRIDEiP97564.

PTM databases

iPTMnetiP97564.
PhosphoSitePlusiP97564.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000050050.

Structurei

3D structure databases

ProteinModelPortaliP97564.
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.
HOGENOMiHOG000112780.
InParanoidiP97564.
KOiK00629.
PhylomeDBiP97564.

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.

P97564-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEESSVTIGT IDVSYLPNSS EYSLGRCKHT NEDWVDCGFK PTFFRSATLK
60 70 80 90 100
WKESLMSRKR PFVGRCCYSC TPQSWERFFN PSIPSLGLRN VIYINETHTR
110 120 130 140 150
HRGWLARRLS YILFVQERDV HKGMFATSIT DNVLNSSRVQ 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 IPIFSTLIHK LGGFFIRRRL DETPDGRKDI LYRALLHGHI
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 AILPSRPDAA AAEHEDMSSN
460 470 480 490 500
ESRNAADEAF RRRLIANLAE HILFTASKSC AIMSTHIVAC LLLYRHRQGI
510 520 530 540 550
HLSTLVEDFF VMKEEVLARD FDLGFSGNSE DVVMHAIQLL GNCVTITHTS
560 570 580 590 600
RKDEFFITPS TTVPSVFELN FYSNGVLHVF IMEAIIACSI YAVQNKRGSG
610 620 630 640 650
GSAGGLGNLI SQEQLVRKAA SLCYLLSNEG TISLPCQTFY QVCQETVGKF
660 670 680 690 700
IQYGILTVAE QDDQEDVSPG LAEQQWNKKL PEPLNWRSDE EDEDSDFGEE
710 720 730 740 750
QRDCYLKVSQ AKEHQQFITF LQRLLGPLLE AYSSAAIFVH TFRGPVPESE
760 770 780 790 800
YLQKLHRYLL TRTERNVAVY AESATYCLVK NAVKMFKDIG VFKETKQKRA
810 820
SVLELSTTFL PQGSRQKLLE YILSFVVL
Length:828
Mass (Da):93,715
Last modified:December 15, 1998 - v3
Checksum:iACA4A087E7DEB12C
GO

Sequence cautioni

The sequence AAB39470 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti37C → F (PubMed:10924502).Curated1
Sequence conflicti85S → P in AAB39470 (PubMed:10924502).Curated1
Sequence conflicti300I → V in AAB39470 (PubMed:10924502).Curated1
Sequence conflicti331L → V in AAB39470 (PubMed:10924502).Curated1
Sequence conflicti472 – 474ILF → NLL in AAB39470 (PubMed:10924502).Curated3
Sequence conflicti497R → W in AAB39470 (PubMed:10924502).Curated1
Sequence conflicti602 – 606SAGGL → LPEP in AAB39470 (PubMed:10924502).Curated5
Sequence conflicti644Q → H in AAB39470 (PubMed:10924502).Curated1
Sequence conflicti744G → A in AAB39470 (PubMed:10924502).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF021348 mRNA. Translation: AAB71605.1.
U36771 mRNA. Translation: AAB39470.2. Different initiation.
RefSeqiNP_058970.1. NM_017274.1.
UniGeneiRn.44456.

Genome annotation databases

GeneIDi29653.
KEGGirno:29653.
UCSCiRGD:61847. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF021348 mRNA. Translation: AAB71605.1.
U36771 mRNA. Translation: AAB39470.2. Different initiation.
RefSeqiNP_058970.1. NM_017274.1.
UniGeneiRn.44456.

3D structure databases

ProteinModelPortaliP97564.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000050050.

Chemistry databases

SwissLipidsiSLP:000000284.

PTM databases

iPTMnetiP97564.
PhosphoSitePlusiP97564.

Proteomic databases

PaxDbiP97564.
PRIDEiP97564.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi29653.
KEGGirno:29653.
UCSCiRGD:61847. rat.

Organism-specific databases

CTDi57678.
RGDi61847. Gpam.

Phylogenomic databases

eggNOGiKOG3729. Eukaryota.
COG2937. LUCA.
HOGENOMiHOG000112780.
InParanoidiP97564.
KOiK00629.
PhylomeDBiP97564.

Enzyme and pathway databases

UniPathwayiUPA00557; UER00612.
BRENDAi2.3.1.15. 5301.
SABIO-RKP97564.

Miscellaneous databases

PROiP97564.

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_RAT
AccessioniPrimary (citable) accession number: P97564
Secondary accession number(s): O35349, P97565, P97566
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: December 15, 1998
Last modified: November 2, 2016
This is version 117 of the entry and version 3 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. 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.