ID Q3TKG9_MOUSE Unreviewed; 678 AA.
AC Q3TKG9;
DT 11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT 11-OCT-2005, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE RecName: Full=Dihydroxyacetone phosphate acyltransferase {ECO:0000256|ARBA:ARBA00044178, ECO:0000256|PIRNR:PIRNR000437};
DE Short=DAP-AT {ECO:0000256|PIRNR:PIRNR000437};
DE Short=DHAP-AT {ECO:0000256|PIRNR:PIRNR000437};
DE EC=2.3.1.42 {ECO:0000256|ARBA:ARBA00044061, ECO:0000256|PIRNR:PIRNR000437};
GN Name=Gnpat {ECO:0000313|MGI:MGI:1343460};
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 {ECO:0000313|EMBL:BAE39176.1};
RN [1] {ECO:0000313|EMBL:BAE39176.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE39176.1};
RX PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA Carninci P., Hayashizaki Y.;
RT "High-efficiency full-length cDNA cloning.";
RL Methods Enzymol. 303:19-44(1999).
RN [2] {ECO:0000313|EMBL:BAE39176.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE39176.1};
RX PubMed=11042159; DOI=10.1101/gr.145100;
RA Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT "Normalization and subtraction of cap-trapper-selected cDNAs to prepare
RT full-length cDNA libraries for rapid discovery of new genes.";
RL Genome Res. 10:1617-1630(2000).
RN [3] {ECO:0000313|EMBL:BAE39176.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE39176.1};
RX PubMed=11076861; DOI=10.1101/gr.152600;
RA Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M., Sumi N.,
RA Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A., Yamamoto R.,
RA Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K., Fujiwake S.,
RA Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M., Yoneda Y.,
RA Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J., Okazaki Y.,
RA Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT "RIKEN integrated sequence analysis (RISA) system--384-format sequencing
RT pipeline with 384 multicapillary sequencer.";
RL Genome Res. 10:1757-1771(2000).
RN [4] {ECO:0000313|EMBL:BAE39176.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE39176.1};
RX PubMed=11217851; DOI=10.1038/35055500;
RG The RIKEN Genome Exploration Research Group Phase II Team and the FANTOM Consortium;
RT "Functional annotation of a full-length mouse cDNA collection.";
RL Nature 409:685-690(2001).
RN [5] {ECO:0000313|EMBL:BAE39176.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE39176.1};
RX PubMed=12466851; DOI=10.1038/nature01266;
RG The FANTOM Consortium and the RIKEN Genome Exploration Research Group Phase I and II Team;
RT "Analysis of the mouse transcriptome based on functional annotation of
RT 60,770 full-length cDNAs.";
RL Nature 420:563-573(2002).
RN [6] {ECO:0000313|EMBL:BAE39176.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE39176.1};
RA Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K., Hori F.,
RA Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S., Kawai J., Kojima M.,
RA Konno H., Murata M., Nakamura M., Ninomiya N., Nishiyori H., Nomura K.,
RA Ohno M., Sakazume N., Sano H., Sasaki D., Shibata K., Shiraki T.,
RA Tagami M., Tagami Y., Waki K., Watahiki A., Muramatsu M., Hayashizaki Y.;
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [7] {ECO:0000313|EMBL:BAE39176.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE39176.1};
RG The FANTOM Consortium;
RG Riken Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group);
RT "The Transcriptional Landscape of the Mammalian Genome.";
RL Science 309:1559-1563(2005).
RN [8] {ECO:0000313|EMBL:BAE39176.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE39176.1};
RX PubMed=16141073; DOI=10.1126/science.1112009;
RG RIKEN Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group) and the FANTOM Consortium;
RT "Antisense Transcription in the Mammalian Transcriptome.";
RL Science 309:1564-1566(2005).
CC -!- FUNCTION: Dihydroxyacetonephosphate acyltransferase catalyzing the
CC first step in the biosynthesis of plasmalogens, a subset of
CC phospholipids that differ from other glycerolipids by having an alkyl
CC chain attached through a vinyl ether linkage at the sn-1 position of
CC the glycerol backbone, and which unique physical properties have an
CC impact on various aspects of cell signaling and membrane biology.
CC {ECO:0000256|ARBA:ARBA00043888}.
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 Evidence={ECO:0000256|ARBA:ARBA00043791};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17658;
CC Evidence={ECO:0000256|ARBA:ARBA00043791};
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:0000256|ARBA:ARBA00043732};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40716;
CC Evidence={ECO:0000256|ARBA:ARBA00043732};
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism.
CC {ECO:0000256|ARBA:ARBA00037925, ECO:0000256|PIRNR:PIRNR000437}.
CC -!- PATHWAY: Phospholipid metabolism. {ECO:0000256|ARBA:ARBA00025707}.
CC -!- SUBUNIT: Part of a heterotrimeric complex composed of GNPAT, AGPS and a
CC modified form of GNPAT. {ECO:0000256|ARBA:ARBA00044003}.
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane
CC {ECO:0000256|ARBA:ARBA00043943, ECO:0000256|PIRNR:PIRNR000437};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00043943,
CC ECO:0000256|PIRNR:PIRNR000437}; Matrix side
CC {ECO:0000256|ARBA:ARBA00043943, ECO:0000256|PIRNR:PIRNR000437}.
CC -!- SIMILARITY: Belongs to the GPAT/DAPAT family.
CC {ECO:0000256|ARBA:ARBA00007937, ECO:0000256|PIRNR:PIRNR000437}.
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DR EMBL; AK166997; BAE39176.1; -; mRNA.
DR AlphaFoldDB; Q3TKG9; -.
DR PeptideAtlas; Q3TKG9; -.
DR AGR; MGI:1343460; -.
DR MGI; MGI:1343460; Gnpat.
DR UniPathway; UPA00940; -.
DR ChiTaRS; Gnpat; mouse.
DR GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016287; F:glycerone-phosphate O-acyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008611; P:ether lipid biosynthetic process; IEA:InterPro.
DR GO; GO:0006650; P:glycerophospholipid metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd07993; LPLAT_DHAPAT-like; 1.
DR InterPro; IPR028353; DHAPAT.
DR InterPro; IPR022284; GPAT/DHAPAT.
DR InterPro; IPR045520; GPAT/DHAPAT_C.
DR InterPro; IPR041728; GPAT/DHAPAT_LPLAT.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR PANTHER; PTHR12563:SF17; DIHYDROXYACETONE PHOSPHATE ACYLTRANSFERASE; 1.
DR PANTHER; PTHR12563; GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR Pfam; PF19277; GPAT_C; 1.
DR PIRSF; PIRSF500063; DHAPAT; 1.
DR PIRSF; PIRSF000437; GPAT_DHAPAT; 2.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
PE 2: Evidence at transcript level;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000256|PIRNR:PIRNR000437};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR000437};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140, ECO:0000256|PIRNR:PIRNR000437};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000437}.
FT DOMAIN 155..284
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 678 AA; 76900 MW; FA6F9862C00CB4FF 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 DQSSSQCYDA LSSELQKNAL AAFVRLGVVE KKKVDSKYVY YVNGPATSKL
EEMLGCKKPI GKPATAKL
//
