ID G1L746_AILME Unreviewed; 652 AA.
AC G1L746;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 62.
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|Ensembl:ENSAMEP00000002712.2};
OS Ailuropoda melanoleuca (Giant panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646 {ECO:0000313|Ensembl:ENSAMEP00000002712.2, ECO:0000313|Proteomes:UP000008912};
RN [1] {ECO:0000313|Ensembl:ENSAMEP00000002712.2, ECO:0000313|Proteomes:UP000008912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20010809; DOI=10.1038/nature08696;
RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA Wang J.;
RT "The sequence and de novo assembly of the giant panda genome.";
RL Nature 463:311-317(2010).
RN [2] {ECO:0000313|Ensembl:ENSAMEP00000002712.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 AlphaFoldDB; G1L746; -.
DR STRING; 9646.ENSAMEP00000002712; -.
DR Ensembl; ENSAMET00000002829.2; ENSAMEP00000002712.2; ENSAMEG00000002552.2.
DR eggNOG; KOG3730; Eukaryota.
DR GeneTree; ENSGT00520000055570; -.
DR HOGENOM; CLU_017332_0_1_1; -.
DR InParanoid; G1L746; -.
DR TreeFam; TF313360; -.
DR UniPathway; UPA00940; -.
DR Proteomes; UP000008912; 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:0021587; P:cerebellum morphogenesis; IEA:Ensembl.
DR GO; GO:0008611; P:ether lipid biosynthetic process; IEA:Ensembl.
DR GO; GO:0006650; P:glycerophospholipid metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0061024; P:membrane organization; IEA:Ensembl.
DR GO; GO:0030913; P:paranodal junction assembly; IEA:Ensembl.
DR GO; GO:0007416; P:synapse assembly; IEA:Ensembl.
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; 2.
DR PIRSF; PIRSF500063; DHAPAT; 2.
DR PIRSF; PIRSF000437; GPAT_DHAPAT; 2.
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:UP000008912};
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 652 AA; 73852 MW; 0397F70C39663336 CRC64;
MDSSSSSNSF SVGSASPGTV VLLYSKELKK WDEFEDILEE RRHVSDLKFA MKCYTPLVYK
GITPCKPSDI KSSVLSSEEV RYVIKQLSKE SLQSADVLRE EVCEILDEMS HKLRLGAIRF
FAFALSKIFK QIFSKVCVNE EGIQKLQRAI QEHPVVLLPS HRSYIDFLML SFLLYNYDLP
VPVIAAGMDF LGMKMVGELL RMSGAFFMRR TFGGDKLYWA VFSEYVKTML RNGYAPVEFF
LEGTRSRSSK TLTPKFGLLN IVMEPFFKRE VFDTYLVPIS ISYDKILEET LYVYELLGVP
KPKESTTGLL KARKILSENF GNIHVYFGDP VSLRSLAAGR MSQSPYNLVP RYIPQRQSED
VHAFVTEVAY KMELLQIQNL VLSPWALTVA VLLQNRPSMD FDALVEKTLW LKGLTQAFGG
FLTWPDNEPA EEVLQSNILL HSNIASLVKD QVVLNMDSGD SEVVNGLIFQ HITLLMCSAY
RNQLLNIFVR PSLVAMALQM APGFRKDFEE GCYLLCKNET IQVTTRDILV TEKGNTVLEF
LIGLFKPFVE CYQIICKYLL NEEEDDFTEK QYLAGVRKFT SQLLDQGASQ CYDVLSCDVQ
KNALAAFVRL GVVEKKKVNS DSVFNVNEPA MTKLEEMLGC KTPVGKPATA KL
//
