GNPAT_RAT
ID GNPAT_RAT Reviewed; 678 AA.
AC Q9ES71;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 131.
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|RGD:620179}; Synonyms=Dhapat;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Ofman R., Lajmir S., Wanders R.J.A.;
RT "cDNA encoding rat dihydroxyacetonephosphate acyltransferase (DHAP-AT).";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=9459311; DOI=10.1016/s0014-5793(97)01495-6;
RA Thai T.-P., Heid H., Rackwitz H.-R., Hunziker A., Gorgas K., Just W.W.;
RT "Ether lipid biosynthesis: isolation and molecular characterization of
RT human dihydroxyacetonephosphate acyltransferase.";
RL FEBS Lett. 420:205-211(1997).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12 AND SER-17, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000269|PubMed:9459311};
CC Peripheral membrane protein {ECO:0000269|PubMed:9459311}; Matrix side
CC {ECO:0000269|PubMed:9459311}. Note=Exclusively localized to the lumenal
CC side of the peroxisomal membrane. {ECO:0000250,
CC ECO:0000269|PubMed:9459311}.
CC -!- TISSUE SPECIFICITY: Expressed in liver (at protein level).
CC {ECO:0000269|PubMed:9459311}.
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; AF218826; AAG17548.1; -; mRNA.
DR RefSeq; NP_445862.1; NM_053410.1.
DR AlphaFoldDB; Q9ES71; -.
DR SMR; Q9ES71; -.
DR STRING; 10116.ENSRNOP00000026617; -.
DR iPTMnet; Q9ES71; -.
DR PhosphoSitePlus; Q9ES71; -.
DR PaxDb; Q9ES71; -.
DR PRIDE; Q9ES71; -.
DR Ensembl; ENSRNOT00000026617; ENSRNOP00000026617; ENSRNOG00000019205.
DR GeneID; 84470; -.
DR KEGG; rno:84470; -.
DR UCSC; RGD:620179; rat.
DR CTD; 8443; -.
DR RGD; 620179; Gnpat.
DR eggNOG; KOG3730; Eukaryota.
DR GeneTree; ENSGT00520000055570; -.
DR HOGENOM; CLU_017332_0_1_1; -.
DR InParanoid; Q9ES71; -.
DR OMA; RFNLEWY; -.
DR OrthoDB; 198209at2759; -.
DR PhylomeDB; Q9ES71; -.
DR TreeFam; TF313360; -.
DR BRENDA; 2.3.1.42; 5301.
DR Reactome; R-RNO-1483166; Synthesis of PA.
DR Reactome; R-RNO-75896; Plasmalogen biosynthesis.
DR Reactome; R-RNO-9033241; Peroxisomal protein import.
DR SABIO-RK; Q9ES71; -.
DR UniPathway; UPA00940; -.
DR PRO; PR:Q9ES71; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Bgee; ENSRNOG00000019205; Expressed in skeletal muscle tissue and 20 other tissues.
DR Genevisible; Q9ES71; RN.
DR GO; GO:0031966; C:mitochondrial membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0005778; C:peroxisomal membrane; IDA:UniProtKB.
DR GO; GO:0005777; C:peroxisome; IDA:HGNC-UCL.
DR GO; GO:0003824; F:catalytic activity; ISO:RGD.
DR GO; GO:0016287; F:glycerone-phosphate O-acyltransferase activity; ISO:RGD.
DR GO; GO:0021587; P:cerebellum morphogenesis; ISO:RGD.
DR GO; GO:0008611; P:ether lipid biosynthetic process; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0042552; P:myelination; ISO:RGD.
DR GO; GO:0030913; P:paranodal junction assembly; ISO:RGD.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IBA:GO_Central.
DR GO; GO:0070542; P:response to fatty acid; IEP:RGD.
DR GO; GO:0007584; P:response to nutrient; IEP:RGD.
DR GO; GO:0042594; P:response to starvation; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0007416; P:synapse assembly; ISO:RGD.
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_0000195248"
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:22673903"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 641
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O15228"
SQ SEQUENCE 678 AA; 77076 MW; F825A2728D534B68 CRC64;
MDVPSSSSSR FSVGSASPSS VLLYAKDLKK WDEFEDLLEE RRQVSDFKFA MKCYTPPLYR
GITPCKPSDI KSIVLNSEEI NYVIKQLSRE SLTGVDVLRE EANEILEEMS HKLRIGAIRF
FAFVLSKVFK QIFSKVCVNE EGIQKLQRAI QEHPVILLPS HRSYIDFLML SFVLYNYDLP
VPVIAAGMDF LGMRVVSELL RMSGAFFMRR TFGGNKLYWA VFSEYVKTML RSGYAPVEFF
LEGTRSRAAK TLTPKFGLLN IVMEPFFKRE VFDTYFVPIS ISYDKILEES LYAYELLGIP
KPKESTTGLL KARRILSENF GSIHVYFGDP VSLRSLAAGR LSRNTYNLVP RCIPQKQPED
VQAFVTEVAY KMQLLQIENL ALSPWLLVVA ILLQNQLCMD FDALVEKTLW LKGLTQVFGG
FLLWPDNKLP EEVVQSSILL HSNLATLVKD QVVLKVDSES SQMVNGLVPQ HIAFLMCSAY
RNQLLNVFAR PSLVAVALHM TPGLRKEDVF SCFSFLRNVF SDEFIFLPGN TLRDFEEGCY
LLCKTEVMQM TGKDIILTDK GNAVLQFLTG LFKPFVESYQ ILSKCLLHEE DYFSEKEYLV
TARKFTRQLL DQDASQCYDA LSSELQKNAL AAFVRLGVVE KNKVDSKYVY YVNGPATSKL
EEMLGCKKPI GKPATAKL
