ID   GNPAT_BOVIN             Reviewed;         680 AA.
AC   A4IF87;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Dihydroxyacetone phosphate acyltransferase;
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;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Heart ventricle;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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
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   -!- 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; BC134455; AAI34456.1; -; mRNA.
DR   RefSeq; NP_001096756.1; NM_001103286.1.
DR   AlphaFoldDB; A4IF87; -.
DR   SMR; A4IF87; -.
DR   STRING; 9913.ENSBTAP00000014266; -.
DR   PRIDE; A4IF87; -.
DR   GeneID; 538800; -.
DR   KEGG; bta:538800; -.
DR   CTD; 8443; -.
DR   eggNOG; KOG3730; Eukaryota.
DR   InParanoid; A4IF87; -.
DR   OrthoDB; 198209at2759; -.
DR   UniPathway; UPA00940; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016287; F:glycerone-phosphate O-acyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008611; P:ether lipid biosynthetic process; IEA:InterPro.
DR   GO; GO:0006650; P:glycerophospholipid metabolic process; IEA:UniProtKB-UniPathway.
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   2: Evidence at transcript level;
KW   Acetylation; Acyltransferase; Membrane; Peroxisome; Phosphoprotein;
KW   Reference proteome; Transferase.
FT   CHAIN           1..680
FT                   /note="Dihydroxyacetone phosphate acyltransferase"
FT                   /id="PRO_0000325855"
FT   MOTIF           162..167
FT                   /note="HXXXXD motif"
FT   MOTIF           678..680
FT                   /note="Microbody targeting signal"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         12
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P98192"
FT   MOD_RES         17
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ES71"
FT   MOD_RES         643
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O15228"
SQ   SEQUENCE   680 AA;  77664 MW;  9D80C804CB92854F CRC64;
     MDHSSSSNSC FSVGSTSPGA VVLLYSKELK KWDEFEDVLE ERRHVSDLKF AMKCYTPLVY
     KGITPCKPSD IKCSVLNSEE IHYVIKQLSK ESLQPVEVLR EEACEILDEM SHKLRLGAIR
     FFAFALSKIF KQIFSKVRVN EEGIQKLQRA IQEHPVVLLP SHRSYIDFLM LSFLLYNYDL
     PVPVIAAGMD FLGMKMVGEL LRMSGAFFMR RTFGGNKLYW AVFSEYVKTM LRNGYAPVEF
     FLEGTRSRSA KTLTPKFGLL NIVMEPFFKR EVFDTYLVPI SISYDRILEE TLYAYELLGV
     PKPKESTTGL LKARRILSEK FGNIHVYFGD PVSLRSLAAG RMGRSPYNLV PRYIPQKQSE
     EMHTFVTEVA YKMQLLQIQN LVLSPWPLIV AVLLQNRPSI DFDALLEKTL WLKGLTQAFG
     GFLTWPDNEP AEAVIQSSIL LHSNIVSLVK DRVILKMECG DSELVDGLIF QHITLLMCLA
     YRNQLLNVFV RPSLVAMALQ MTPGFRKEDV YSCFRFLCSV FSDEFIFLPG NALKDFEEGC
     YLLCKSEAIQ VMTRDILVTE KGNSVLEFLI GLFKPFVESY QIICKYLLNE EEDYFTEKQY
     FIRVRKFTSQ LLDQGASQCY DVLSSDVQKN ALAAFVRLGV VEKKKVNNDY IFNVNEPATT
     KLEEMLGCKT PVGKPATAKL