Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Dihydroxyacetone phosphate acyltransferase

Gene

Gnpat

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Acyl-CoA + glycerone phosphate = CoA + acylglycerone phosphate.

Pathwayi: glycerophospholipid metabolism

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

GO - Molecular functioni

  • glycerone-phosphate O-acyltransferase activity Source: RGD
  • palmitoyl-CoA hydrolase activity Source: Ensembl

GO - Biological processi

  • cerebellum morphogenesis Source: Ensembl
  • ether lipid biosynthetic process Source: Ensembl
  • glycerophospholipid metabolic process Source: UniProtKB-UniPathway
  • membrane organization Source: Ensembl
  • paranodal junction assembly Source: Ensembl
  • response to drug Source: RGD
  • response to fatty acid Source: RGD
  • response to nutrient Source: RGD
  • response to starvation Source: RGD
  • synapse assembly Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Enzyme and pathway databases

BRENDAi2.3.1.42. 5301.
ReactomeiR-RNO-1483166. Synthesis of PA.
R-RNO-75896. Plasmalogen biosynthesis.
SABIO-RKQ9ES71.
UniPathwayiUPA00940.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydroxyacetone phosphate acyltransferase (EC:2.3.1.42)
Short name:
DAP-AT
Short name:
DHAP-AT
Alternative name(s):
Acyl-CoA:dihydroxyacetonephosphateacyltransferase
Glycerone-phosphate O-acyltransferase
Gene namesi
Name:Gnpat
Synonyms:Dhapat
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 19

Organism-specific databases

RGDi620179. Gnpat.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: RGD
  • peroxisomal membrane Source: UniProtKB
  • peroxisome Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 678678Dihydroxyacetone phosphate acyltransferasePRO_0000195248Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei12 – 121PhosphoserineCombined sources
Modified residuei17 – 171PhosphoserineCombined sources
Modified residuei641 – 6411N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ9ES71.
PRIDEiQ9ES71.

PTM databases

iPTMnetiQ9ES71.
PhosphoSiteiQ9ES71.

Expressioni

Gene expression databases

GenevisibleiQ9ES71. RN.

Interactioni

Subunit structurei

May be part of a heterotrimeric complex composed of DAP-AT, ADAP-S and a modified form of DAP-AT.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000026617.

Structurei

3D structure databases

ProteinModelPortaliQ9ES71.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi161 – 1666HXXXXD motif
Motifi676 – 6783Microbody targeting signalSequence analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi5 – 95Poly-Ser

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

Phylogenomic databases

eggNOGiKOG3730. Eukaryota.
COG2937. LUCA.
GeneTreeiENSGT00520000055570.
HOGENOMiHOG000112751.
HOVERGENiHBG051749.
InParanoidiQ9ES71.
KOiK00649.
OMAiPRYIPQK.
OrthoDBiEOG7CCBQT.
PhylomeDBiQ9ES71.
TreeFamiTF313360.

Family and domain databases

InterProiIPR028353. DHAPAT.
IPR022284. GPAT/DHAPAT.
IPR002123. Plipid/glycerol_acylTrfase.
[Graphical view]
PANTHERiPTHR12563. PTHR12563. 1 hit.
PfamiPF01553. Acyltransferase. 1 hit.
[Graphical view]
PIRSFiPIRSF500063. DHAPAT. 1 hit.
PIRSF000437. GPAT_DHAPAT. 1 hit.
SMARTiSM00563. PlsC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9ES71-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDVPSSSSSR FSVGSASPSS VLLYAKDLKK WDEFEDLLEE RRQVSDFKFA
60 70 80 90 100
MKCYTPPLYR GITPCKPSDI KSIVLNSEEI NYVIKQLSRE SLTGVDVLRE
110 120 130 140 150
EANEILEEMS HKLRIGAIRF FAFVLSKVFK QIFSKVCVNE EGIQKLQRAI
160 170 180 190 200
QEHPVILLPS HRSYIDFLML SFVLYNYDLP VPVIAAGMDF LGMRVVSELL
210 220 230 240 250
RMSGAFFMRR TFGGNKLYWA VFSEYVKTML RSGYAPVEFF LEGTRSRAAK
260 270 280 290 300
TLTPKFGLLN IVMEPFFKRE VFDTYFVPIS ISYDKILEES LYAYELLGIP
310 320 330 340 350
KPKESTTGLL KARRILSENF GSIHVYFGDP VSLRSLAAGR LSRNTYNLVP
360 370 380 390 400
RCIPQKQPED VQAFVTEVAY KMQLLQIENL ALSPWLLVVA ILLQNQLCMD
410 420 430 440 450
FDALVEKTLW LKGLTQVFGG FLLWPDNKLP EEVVQSSILL HSNLATLVKD
460 470 480 490 500
QVVLKVDSES SQMVNGLVPQ HIAFLMCSAY RNQLLNVFAR PSLVAVALHM
510 520 530 540 550
TPGLRKEDVF SCFSFLRNVF SDEFIFLPGN TLRDFEEGCY LLCKTEVMQM
560 570 580 590 600
TGKDIILTDK GNAVLQFLTG LFKPFVESYQ ILSKCLLHEE DYFSEKEYLV
610 620 630 640 650
TARKFTRQLL DQDASQCYDA LSSELQKNAL AAFVRLGVVE KNKVDSKYVY
660 670
YVNGPATSKL EEMLGCKKPI GKPATAKL
Length:678
Mass (Da):77,076
Last modified:March 1, 2001 - v1
Checksum:iF825A2728D534B68
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF218826 mRNA. Translation: AAG17548.1.
RefSeqiNP_445862.1. NM_053410.1.
UniGeneiRn.1739.

Genome annotation databases

EnsembliENSRNOT00000026617; ENSRNOP00000026617; ENSRNOG00000019205.
GeneIDi84470.
KEGGirno:84470.
UCSCiRGD:620179. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF218826 mRNA. Translation: AAG17548.1.
RefSeqiNP_445862.1. NM_053410.1.
UniGeneiRn.1739.

3D structure databases

ProteinModelPortaliQ9ES71.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000026617.

PTM databases

iPTMnetiQ9ES71.
PhosphoSiteiQ9ES71.

Proteomic databases

PaxDbiQ9ES71.
PRIDEiQ9ES71.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000026617; ENSRNOP00000026617; ENSRNOG00000019205.
GeneIDi84470.
KEGGirno:84470.
UCSCiRGD:620179. rat.

Organism-specific databases

CTDi8443.
RGDi620179. Gnpat.

Phylogenomic databases

eggNOGiKOG3730. Eukaryota.
COG2937. LUCA.
GeneTreeiENSGT00520000055570.
HOGENOMiHOG000112751.
HOVERGENiHBG051749.
InParanoidiQ9ES71.
KOiK00649.
OMAiPRYIPQK.
OrthoDBiEOG7CCBQT.
PhylomeDBiQ9ES71.
TreeFamiTF313360.

Enzyme and pathway databases

UniPathwayiUPA00940.
BRENDAi2.3.1.42. 5301.
ReactomeiR-RNO-1483166. Synthesis of PA.
R-RNO-75896. Plasmalogen biosynthesis.
SABIO-RKQ9ES71.

Miscellaneous databases

PROiQ9ES71.

Gene expression databases

GenevisibleiQ9ES71. RN.

Family and domain databases

InterProiIPR028353. DHAPAT.
IPR022284. GPAT/DHAPAT.
IPR002123. Plipid/glycerol_acylTrfase.
[Graphical view]
PANTHERiPTHR12563. PTHR12563. 1 hit.
PfamiPF01553. Acyltransferase. 1 hit.
[Graphical view]
PIRSFiPIRSF500063. DHAPAT. 1 hit.
PIRSF000437. GPAT_DHAPAT. 1 hit.
SMARTiSM00563. PlsC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA encoding rat dihydroxyacetonephosphate acyltransferase (DHAP-AT)."
    Ofman R., Lajmir S., Wanders R.J.A.
    Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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-12 AND SER-17, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiGNPAT_RAT
AccessioniPrimary (citable) accession number: Q9ES71
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: March 1, 2001
Last modified: June 8, 2016
This is version 103 of the entry and version 1 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.