ID A0A0N4SWI8_PIG Unreviewed; 825 AA.
AC A0A0N4SWI8;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Glycerol-3-phosphate acyltransferase 1, mitochondrial {ECO:0000256|ARBA:ARBA00017577, ECO:0000256|PIRNR:PIRNR000437};
DE EC=2.3.1.15 {ECO:0000256|ARBA:ARBA00013113, ECO:0000256|PIRNR:PIRNR000437};
GN Name=GPAM {ECO:0000313|Ensembl:ENSSSCP00000011325.3,
GN ECO:0000313|VGNC:VGNC:88570};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000011325.3, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000011325.3, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000011325.3,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000011325.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Esterifies acyl-group from acyl-ACP to the sn-1 position of
CC glycerol-3-phosphate, an essential step in glycerolipids biosynthesis
CC such as triglycerides, phosphatidic acids and lysophosphatidic acids.
CC {ECO:0000256|ARBA:ARBA00023435}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + sn-glycerol 3-phosphate = 1-(9Z-
CC octadecenoyl)-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37199,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:57597,
CC ChEBI:CHEBI:74544; Evidence={ECO:0000256|ARBA:ARBA00023362};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37200;
CC Evidence={ECO:0000256|ARBA:ARBA00023362};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + sn-glycerol 3-phosphate = 1-
CC (9Z,12Z)-octadecadienoyl-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37203, ChEBI:CHEBI:57287, ChEBI:CHEBI:57383,
CC ChEBI:CHEBI:57597, ChEBI:CHEBI:74547;
CC Evidence={ECO:0000256|ARBA:ARBA00023344};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37204;
CC Evidence={ECO:0000256|ARBA:ARBA00023344};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-acyl-sn-glycero-3-phospho-(1'-sn-glycerol) + an acyl-CoA =
CC 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + CoA;
CC Xref=Rhea:RHEA:33203, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:64716, ChEBI:CHEBI:64840;
CC Evidence={ECO:0000256|ARBA:ARBA00023355};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33204;
CC Evidence={ECO:0000256|ARBA:ARBA00023355};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acyl-CoA + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-
CC phosphate + CoA; Xref=Rhea:RHEA:15325, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57597, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342; EC=2.3.1.15;
CC Evidence={ECO:0000256|PIRNR:PIRNR000437};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dodecanoyl-CoA + sn-glycerol 3-phosphate = 1-dodecanoyl-sn-
CC glycerol 3-phosphate + CoA; Xref=Rhea:RHEA:35727, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57375, ChEBI:CHEBI:57597, ChEBI:CHEBI:72682;
CC Evidence={ECO:0000256|ARBA:ARBA00023335};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35728;
CC Evidence={ECO:0000256|ARBA:ARBA00023335};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanoyl-CoA + sn-glycerol 3-phosphate = 1-hexadecanoyl-
CC sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:35723,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:57518,
CC ChEBI:CHEBI:57597; Evidence={ECO:0000256|ARBA:ARBA00023405};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35724;
CC Evidence={ECO:0000256|ARBA:ARBA00023405};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=octadecanoyl-CoA + sn-glycerol 3-phosphate = 1-octadecanoyl-
CC sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37195,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57394, ChEBI:CHEBI:57597,
CC ChEBI:CHEBI:74565; Evidence={ECO:0000256|ARBA:ARBA00023374};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37196;
CC Evidence={ECO:0000256|ARBA:ARBA00023374};
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
CC {ECO:0000256|ARBA:ARBA00004765, ECO:0000256|PIRNR:PIRNR000437}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion
CC outer membrane {ECO:0000256|ARBA:ARBA00004374}; Multi-pass membrane
CC protein {ECO:0000256|ARBA:ARBA00004374}.
CC -!- SIMILARITY: Belongs to the GPAT/DAPAT family.
CC {ECO:0000256|ARBA:ARBA00007937, ECO:0000256|PIRNR:PIRNR000437}.
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DR AlphaFoldDB; A0A0N4SWI8; -.
DR Ensembl; ENSSSCT00000011627.5; ENSSSCP00000011325.3; ENSSSCG00000010631.5.
DR VGNC; VGNC:88570; GPAM.
DR GeneTree; ENSGT00520000055570; -.
DR InParanoid; A0A0N4SWI8; -.
DR OMA; RCKHTNE; -.
DR Reactome; R-SSC-1483166; Synthesis of PA.
DR Reactome; R-SSC-75109; Triglyceride biosynthesis.
DR UniPathway; UPA00557; UER00612.
DR Proteomes; UP000008227; Chromosome 14.
DR Bgee; ENSSSCG00000010631; Expressed in epididymis and 45 other cell types or tissues.
DR ExpressionAtlas; A0A0N4SWI8; baseline and differential.
DR GO; GO:0031966; C:mitochondrial membrane; IBA:GO_Central.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR GO; GO:0004366; F:glycerol-3-phosphate O-acyltransferase activity; IBA:GO_Central.
DR GO; GO:0102420; F:sn-1-glycerol-3-phosphate C16:0-DCA-CoA acyl transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0050798; P:activated T cell proliferation; IEA:Ensembl.
DR GO; GO:0006924; P:activation-induced cell death of T cells; IEA:Ensembl.
DR GO; GO:0006637; P:acyl-CoA metabolic process; IEA:Ensembl.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0051607; P:defense response to virus; IEA:Ensembl.
DR GO; GO:0055089; P:fatty acid homeostasis; IEA:Ensembl.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IBA:GO_Central.
DR GO; GO:0070236; P:negative regulation of activation-induced cell death of T cells; IEA:Ensembl.
DR GO; GO:0006655; P:phosphatidylglycerol biosynthetic process; IEA:Ensembl.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IBA:GO_Central.
DR GO; GO:0055091; P:phospholipid homeostasis; IEA:Ensembl.
DR GO; GO:0042104; P:positive regulation of activated T cell proliferation; IEA:Ensembl.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IEA:Ensembl.
DR GO; GO:0001817; P:regulation of cytokine production; IEA:Ensembl.
DR GO; GO:0009749; P:response to glucose; IEA:Ensembl.
DR GO; GO:0019432; P:triglyceride biosynthetic process; IBA:GO_Central.
DR CDD; cd07993; LPLAT_DHAPAT-like; 1.
DR InterPro; IPR022284; GPAT/DHAPAT.
DR InterPro; IPR045520; GPAT/DHAPAT_C.
DR InterPro; IPR041728; GPAT/DHAPAT_LPLAT.
DR InterPro; IPR028354; GPAT_PlsB.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR PANTHER; PTHR12563; GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE; 1.
DR PANTHER; PTHR12563:SF16; GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE 1, MITOCHONDRIAL; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR Pfam; PF19277; GPAT_C; 1.
DR PIRSF; PIRSF500064; GPAT; 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 Lipid biosynthesis {ECO:0000256|PIRNR:PIRNR000437};
KW Lipid metabolism {ECO:0000256|PIRNR:PIRNR000437};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR000437};
KW Mitochondrion {ECO:0000256|PIRNR:PIRNR000437};
KW Phospholipid biosynthesis {ECO:0000256|PIRNR:PIRNR000437};
KW Phospholipid metabolism {ECO:0000256|PIRNR:PIRNR000437};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000437};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 224..357
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 825 AA; 93506 MW; 6D3DAB9B28147405 CRC64;
MDESALTLGT IDVSYLPNSS EYSIGRCKHA SEEWGECGFR PPVFRSATLK WKESLMSRKR
PFVGRCCYSC TPQSWDRFFN PSIPSLGLRN VIYINETHTR HRGWLARRLS YVLFIQERDV
HKGMFATNVT ENVLNSSRVQ EAIAEVAAEL NPDGSAQQQS KAVNKVKKKA KKILQEMVAT
VSPAMIRLTG WVLLKLFNSF FWNIQIHKGQ LEMVKAATEM NLPLIFLPVH RSHIDYLLLT
FILFCHNIKA PYIASGNNLN IPIFSTLIHK LGGFFIRRRL DETPDGQKDI LYRALLHGHI
VELLRQQQFL EIFLEGTRSR SGKTSCARAG LLSVVVDTLS TNTIPDILII PVGISYDRII
EGHYNGEQLG KPKKNESLWS VARGVIRMLR KNYGCVRVDF AQPFSLKEYL ESQSQKPVSA
PLSLEQALLP AILPSRPSDA VDEGTDMSIN ESRNADESFR RRLIANLAEH ILFTASKSCA
IMSTHIVACL LLYRHRQGID LSTLVEDFFV MKEEVLARDF DLGFSGNSED VVMHAIQLLG
NCITITHTSR NDEFFITPST TVPSVFELNF YSNGVLHVFI MEAIIACSLY AVLKKRGSGG
PASPSLISQE QLVRKAASLC YLLSNEGTIS LPCQTFYQIC HETVGRFIQY GILTVAEQDD
QEDISPSLAE QHWDKKLPEP LSWRSDEEDE DSDFGEEQRD CYLKVSQSKE HQQFITFLQR
LLGPLLEAYS SAAIFIHNFS GPVPEPEYLQ KLHKYLINRT ERRVAVYAES ATYCLVKNAV
KMFKDIGVFK ETKQKKVSVL ELSSTFLPQC NRQKLLEYIL SFVVL
//
