GNPAT_MOUSE
ID GNPAT_MOUSE Reviewed; 678 AA.
AC P98192; Q9WUT6;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Dihydroxyacetone phosphate acyltransferase {ECO:0000305};
DE Short=DAP-AT;
DE Short=DHAP-AT;
DE EC=2.3.1.42;
DE AltName: Full=Acyl-CoA:dihydroxyacetonephosphateacyltransferase;
DE AltName: Full=Glycerone-phosphate O-acyltransferase;
GN Name=Gnpat {ECO:0000312|MGI:MGI:1343460}; Synonyms=Dhapat;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Fibroblast;
RX PubMed=10395968; DOI=10.1016/s1388-1981(99)00081-5;
RA Ofman R., Hogenhout E.M., Wanders R.J.A.;
RT "Identification and characterization of the mouse cDNA encoding acyl-
RT CoA:dihydroxyacetone phosphate acyltransferase.";
RL Biochim. Biophys. Acta 1439:89-94(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10456321; DOI=10.1016/s0014-5793(99)00968-0;
RA Thai T.P., Rodemer C., Worsch J., Hunziker A., Gorgas K., Just W.W.;
RT "Synthesis of plasmalogens in eye lens epithelial cells.";
RL FEBS Lett. 456:263-268(1999).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Dihydroxyacetonephosphate acyltransferase involved in
CC plasmalogen biosynthesis. {ECO:0000250|UniProtKB:O15228}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acyl-CoA + dihydroxyacetone phosphate = a 1-acylglycerone
CC 3-phosphate + CoA; Xref=Rhea:RHEA:17657, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57534, ChEBI:CHEBI:57642, ChEBI:CHEBI:58342; EC=2.3.1.42;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dihydroxyacetone phosphate + hexadecanoyl-CoA = 1-
CC hexadecanoylglycerone 3-phosphate + CoA; Xref=Rhea:RHEA:40715,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:57642,
CC ChEBI:CHEBI:58303; Evidence={ECO:0000250|UniProtKB:O15228};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40716;
CC Evidence={ECO:0000250|UniProtKB:O15228};
CC -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism.
CC -!- SUBUNIT: May be part of a heterotrimeric complex composed of DAP-AT,
CC ADAP-S and a modified form of DAP-AT.
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane
CC {ECO:0000250|UniProtKB:Q9ES71}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9ES71}; Matrix side
CC {ECO:0000250|UniProtKB:Q9ES71}. Note=Exclusively localized to the
CC lumenal side of the peroxisomal membrane. {ECO:0000250,
CC ECO:0000250|UniProtKB:Q9ES71}.
CC -!- TISSUE SPECIFICITY: Highly expressed in liver and testis. Lower levels
CC in heart, brain, lung and kidney. Detected in spleen.
CC -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity and
CC may constitute the binding site for the phosphate moiety of the
CC glycerol-3-phosphate. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GPAT/DAPAT family. {ECO:0000305}.
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DR EMBL; AF110769; AAD55351.1; -; mRNA.
DR EMBL; AJ132012; CAB41975.1; -; mRNA.
DR CCDS; CCDS22776.1; -.
DR RefSeq; NP_034452.3; NM_010322.3.
DR AlphaFoldDB; P98192; -.
DR BioGRID; 199996; 1.
DR IntAct; P98192; 2.
DR MINT; P98192; -.
DR STRING; 10090.ENSMUSP00000034466; -.
DR iPTMnet; P98192; -.
DR PhosphoSitePlus; P98192; -.
DR EPD; P98192; -.
DR jPOST; P98192; -.
DR PaxDb; P98192; -.
DR PeptideAtlas; P98192; -.
DR PRIDE; P98192; -.
DR ProteomicsDB; 267739; -.
DR Antibodypedia; 34685; 289 antibodies from 30 providers.
DR DNASU; 14712; -.
DR Ensembl; ENSMUST00000034466; ENSMUSP00000034466; ENSMUSG00000031985.
DR GeneID; 14712; -.
DR KEGG; mmu:14712; -.
DR UCSC; uc009nxv.2; mouse.
DR CTD; 8443; -.
DR MGI; MGI:1343460; Gnpat.
DR VEuPathDB; HostDB:ENSMUSG00000031985; -.
DR eggNOG; KOG3730; Eukaryota.
DR GeneTree; ENSGT00520000055570; -.
DR InParanoid; P98192; -.
DR OMA; RFNLEWY; -.
DR OrthoDB; 198209at2759; -.
DR PhylomeDB; P98192; -.
DR TreeFam; TF313360; -.
DR Reactome; R-MMU-1483166; Synthesis of PA.
DR Reactome; R-MMU-75896; Plasmalogen biosynthesis.
DR Reactome; R-MMU-9033241; Peroxisomal protein import.
DR UniPathway; UPA00940; -.
DR BioGRID-ORCS; 14712; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Gnpat; mouse.
DR PRO; PR:P98192; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; P98192; protein.
DR Bgee; ENSMUSG00000031985; Expressed in embryonic post-anal tail and 271 other tissues.
DR ExpressionAtlas; P98192; baseline and differential.
DR Genevisible; P98192; MM.
DR GO; GO:0031966; C:mitochondrial membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005782; C:peroxisomal matrix; TAS:MGI.
DR GO; GO:0005778; C:peroxisomal membrane; ISO:MGI.
DR GO; GO:0005777; C:peroxisome; ISO:MGI.
DR GO; GO:0003824; F:catalytic activity; IDA:MGI.
DR GO; GO:0016287; F:glycerone-phosphate O-acyltransferase activity; IDA:MGI.
DR GO; GO:0021587; P:cerebellum morphogenesis; IMP:MGI.
DR GO; GO:0008611; P:ether lipid biosynthetic process; IMP:MGI.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR GO; GO:0006650; P:glycerophospholipid metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0061024; P:membrane organization; IMP:MGI.
DR GO; GO:0042552; P:myelination; IMP:MGI.
DR GO; GO:0030913; P:paranodal junction assembly; IMP:MGI.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IBA:GO_Central.
DR GO; GO:0070542; P:response to fatty acid; IEA:Ensembl.
DR GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
DR GO; GO:0042594; P:response to starvation; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0007416; P:synapse assembly; IMP:MGI.
DR CDD; cd07993; LPLAT_DHAPAT-like; 1.
DR InterPro; IPR028353; DHAPAT.
DR InterPro; IPR022284; GPAT/DHAPAT.
DR InterPro; IPR041728; GPAT/DHAPAT_LPLAT.
DR InterPro; IPR045520; GPAT_C.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR PANTHER; PTHR12563; PTHR12563; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR Pfam; PF19277; GPAT_C; 1.
DR PIRSF; PIRSF500063; DHAPAT; 1.
DR PIRSF; PIRSF000437; GPAT_DHAPAT; 1.
DR SMART; SM00563; PlsC; 1.
PE 1: Evidence at protein level;
KW Acetylation; Acyltransferase; Membrane; Peroxisome; Phosphoprotein;
KW Reference proteome; Transferase.
FT CHAIN 1..678
FT /note="Dihydroxyacetone phosphate acyltransferase"
FT /id="PRO_0000195247"
FT MOTIF 161..166
FT /note="HXXXXD motif"
FT MOTIF 676..678
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ES71"
FT MOD_RES 641
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O15228"
SQ SEQUENCE 678 AA; 76870 MW; FA7245A2DDD174FF CRC64;
MDVPSSSSSR FSVGSASPSS VLLYAKDLKK WDEFEDLLEE RRHISDFKFA MKCYTPPLYR
GITPCKPGDI KSIVLSSEEI NYVIKQLSRE SLTGVDVLRE EASEILEEMS HKLRIGAIRF
FAFVLSKIFK QIFSKVCVNE EGIQKLQRAV QEHPVVLLPS HRSYIDFLML SFILYSYDLP
VPVIAAGMDF LGMRVVSELL RMSGAFFMRR TFGGNKLYWA VFSEYVKTML RCGYAPVEFF
LEGTRSRAAK TLTPKFGLLN IVMEPFFKRE VFDTYFVPIS ISYDKILEES LYAYEILGVP
KPKESTTGLL KARRILSENF GSIHVYFGDP VSLRSLAAGR LNRNTYNLVP RCIPQKQPED
VQAFVTEVAY KMQLLQIENL ALSPWLLVVT ILLQNQLSMD FDALVEKTLW LKGVTQVFGG
FLLWPDNKLP EEVVQSSILL HSNLASLVKD QVVLKMNSGS SQVVNGLVPE HIALLMCSAY
RNQLLNIFAR PSLVALALHM TPGLRKEDVF SCFSFLRNVF SDEFIFLPGN TLRDFEEGCY
LLCKAEAMQM AGKDIILTDK GTAVLQFLTS LFKPFVESYQ LLCRYLLHEE DYFGEKEYLV
AARKFTRQLL DQGSSQCYDA LSSELQKNAL AAFVRLGVVE KKKVDSKYVY YVNGPATSKL
EEMLGCKKPI GKPATAKL
