ID K7G5N4_PELSI Unreviewed; 635 AA.
AC K7G5N4;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
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:ENSPSIP00000015595.1};
OS Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Trionychia;
OC Trionychidae; Pelodiscus.
OX NCBI_TaxID=13735 {ECO:0000313|Ensembl:ENSPSIP00000015595.1, ECO:0000313|Proteomes:UP000007267};
RN [1] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RG Soft-shell Turtle Genome Consortium;
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
RN [3] {ECO:0000313|Ensembl:ENSPSIP00000015595.1}
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 EMBL; AGCU01078443; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01078444; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01078445; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01078446; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01078447; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01078448; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01078449; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01078450; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; K7G5N4; -.
DR Ensembl; ENSPSIT00000015669.1; ENSPSIP00000015595.1; ENSPSIG00000013801.1.
DR GeneTree; ENSGT00520000055570; -.
DR HOGENOM; CLU_017332_0_1_1; -.
DR UniPathway; UPA00940; -.
DR Proteomes; UP000007267; 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:UP000007267};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000437}.
FT DOMAIN 144..273
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 635 AA; 72807 MW; 0F20F0D3C5F15921 CRC64;
MYNQRRDWAP DLKELTSKKR DEFEDILEER RQSSDLRYAM KCYTPVIYKG LSACKPSAIK
NSVLQSEQVQ YVIKQLSKEM GESADIIQEE ATEILDEMGH NLHIGAIRFF AFSLSKIFKR
LFQRVCVNEE GIQKLQQAIQ EHPVVLLPSH RSYIDFLMLS YLLYTYDLAL PVIAAGMDFL
GMKIVGELLR RSGAFFMRRS FGGNRLYWAV FAEYVKTMLR NGYAPIEFFL EGTRSRTSKT
LTPKFGLLSI VMEPFFKREV FDTYLVPISI SYERILEESL YAYELLGVPK PKESTSGLLK
ARKILSDNFG SIHVYFGQPV SLRTLASGRI NRCPYNLVPR HLPQRLSEDI QEFVTDVAYK
MELLQIENMV LSPWVLIASV LLQNLPAIDF DVLVEKTLWL KGITQVFGGF FEWPDNLCAN
KAVTSSLALH TNIVSLVNGQ VVLNDMGIED GATEELIFKQ ALSILMCGAY RNQLLNVFVR
PSLVAVALQM TQSFRKEEIY NCFNFLRNMF SDEFIFFPGI ALKDFEEGCF LLTKCDVIQV
TPQEILVTEK GNSAASFLAA MFRPFMEGYQ IICRYLSKET KETFTEKQFI LGIRNFAFQL
LETGSTQCYE VLSSDLQKNA LAAFVRLNVM KKMKM
//
