ID A0A091DVD8_FUKDA Unreviewed; 676 AA.
AC A0A091DVD8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
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 ORFNames=H920_04354 {ECO:0000313|EMBL:KFO34225.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO34225.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO34225.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO34225.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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; KN122008; KFO34225.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091DVD8; -.
DR STRING; 885580.ENSFDAP00000023222; -.
DR eggNOG; KOG3730; Eukaryota.
DR UniPathway; UPA00940; -.
DR Proteomes; UP000028990; Unassembled WGS sequence.
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; 1.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
PE 3: Inferred from homology;
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 Reference proteome {ECO:0000313|Proteomes:UP000028990};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000437}.
FT DOMAIN 152..281
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 676 AA; 77008 MW; E13702FE51FDE9DC CRC64;
MVALPDTISG LYLILKEVGV IQKELKKWDE FEDMLEERKH VSDLKFAMKC YTPLVYKGIT
PCKPSDIKGS VLNSEEIHYV IKQLAKESSQ PVDVLREEAS EILDEMSHKL RVGAIRFFAF
TLSKIFKQIF SKVCVNEEGI QKLQSVIQEY PAVLLPSHRS YIDFLMLSFL LYSYDLPVPV
IAAGMDFLGM KIIGELLRMS GAFFMRRTFG GDKLYWAVFS EYVKTMLRNG YAPVEFFLEG
TRSRSAKTLT PKLGLLNIVM EPFFKREVFD IYLVPISISY DKVLEETLYA YELLGVPKPK
ESTTGLLKAR RILSEHFGSI HVYFGDPVSL RSLAAGRMSR SPYNLVPRYI PQKPSEEMHA
FVTEVAYKMQ LLQIENLVLS PWVLAVAVLL QNRPSMDFDT LVEKTLWLKA LTQAFGGFLR
WPDNEPAEEV VRSNILLHSN LASLVKDQVI LKVDCGDSEV VNGLIFQHIT LLMCSAYRNQ
LLNIFVRPSL VAVALQMTPG FRKEDVYSCF HFLCSVFSDE FIFLPGNTLK DFEEGCYLLC
KSETIQVTTK DILVTEKGNA VLEFLVGLFK PFVECYQIIC KYLLHEEEDH FTEKYYLAAV
RKFTNQLLDQ GSCQCYDVLS SDVQKNALAA CVRLGVVERK KLNNDYRYSV NEPAVSKLEE
MLGCKTPIGK PATAKL
//
