GPAT1_PIG
ID GPAT1_PIG Reviewed; 826 AA.
AC F1S5L4; Q7YS07;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2015, sequence version 3.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Glycerol-3-phosphate acyltransferase 1, mitochondrial {ECO:0000250|UniProtKB:Q9HCL2};
DE Short=GPAT-1 {ECO:0000250|UniProtKB:Q9HCL2};
DE EC=2.3.1.15 {ECO:0000250|UniProtKB:Q9HCL2};
DE Flags: Precursor;
GN Name=GPAM {ECO:0000250|UniProtKB:Q9HCL2}; Synonyms=GPAT, GPAT1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 528-826.
RC TISSUE=Liver;
RX PubMed=14510680; DOI=10.1046/j.1365-2052.2003.01041.x;
RA Tomas A., Estelle J., Clop A., Gomez-Raya L., Noguera J.L., Sanchez A.,
RA Amills M.;
RT "Assignment of the mitochondrial glycerol-3-phosphate acyltransferase
RT (GPAT) gene to porcine chromosome 14.";
RL Anim. Genet. 34:387-387(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:Q9HCL2}.
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:0000250|UniProtKB:Q9HCL2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15326;
CC Evidence={ECO:0000250|UniProtKB:Q9HCL2};
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:0000250|UniProtKB:Q9HCL2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37204;
CC Evidence={ECO:0000250|UniProtKB:Q9HCL2};
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:0000250|UniProtKB:Q9HCL2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37200;
CC Evidence={ECO:0000250|UniProtKB:Q9HCL2};
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:0000250|UniProtKB:Q9HCL2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37196;
CC Evidence={ECO:0000250|UniProtKB:Q9HCL2};
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:0000250|UniProtKB:Q9HCL2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35724;
CC Evidence={ECO:0000250|UniProtKB:Q9HCL2};
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:0000250|UniProtKB:Q9HCL2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35728;
CC Evidence={ECO:0000250|UniProtKB:Q9HCL2};
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:0000250|UniProtKB:Q9HCL2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33204;
CC Evidence={ECO:0000250|UniProtKB:Q9HCL2};
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
CC {ECO:0000250|UniProtKB:Q9HCL2}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:P97564}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P97564}.
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; AY284842; AAP74372.1; -; mRNA.
DR EMBL; CT737200; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT827870; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_001927910.1; XM_001927875.3.
DR RefSeq; XP_005671519.1; XM_005671462.2.
DR RefSeq; XP_005671520.1; XM_005671463.2.
DR AlphaFoldDB; F1S5L4; -.
DR STRING; 9823.ENSSSCP00000011325; -.
DR PaxDb; F1S5L4; -.
DR PRIDE; F1S5L4; -.
DR Ensembl; ENSSSCT00045023945; ENSSSCP00045016515; ENSSSCG00045014059.
DR Ensembl; ENSSSCT00050045061; ENSSSCP00050018517; ENSSSCG00050033629.
DR GeneID; 397629; -.
DR KEGG; ssc:397629; -.
DR CTD; 57678; -.
DR eggNOG; KOG3729; Eukaryota.
DR HOGENOM; CLU_016910_1_1_1; -.
DR InParanoid; F1S5L4; -.
DR OrthoDB; 198209at2759; -.
DR TreeFam; TF313360; -.
DR UniPathway; UPA00557; UER00612.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Genevisible; F1S5L4; SS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; ISS:UniProtKB.
DR GO; GO:0102420; F:sn-1-glycerol-3-phosphate C16:0-DCA-CoA acyl transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006651; P:diacylglycerol biosynthetic process; ISS:UniProtKB.
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:0006654; P:phosphatidic acid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006655; P:phosphatidylglycerol biosynthetic process; ISS:UniProtKB.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IBA:GO_Central.
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; IPR041728; GPAT/DHAPAT_LPLAT.
DR InterPro; IPR045520; GPAT_C.
DR InterPro; IPR028354; GPAT_PlsB.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR PANTHER; PTHR12563; PTHR12563; 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.
PE 2: Evidence at transcript level;
KW Acetylation; Acyltransferase; Lipid biosynthesis; Lipid metabolism;
KW Membrane; Mitochondrion; Mitochondrion outer membrane;
KW Phospholipid biosynthesis; Phospholipid metabolism; Phosphoprotein;
KW Reference proteome; Transferase; Transit peptide; Transmembrane;
KW Transmembrane helix.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:Q9HCL2"
FT CHAIN ?..826
FT /note="Glycerol-3-phosphate acyltransferase 1,
FT mitochondrial"
FT /id="PRO_0000433928"
FT TOPO_DOM ?..471
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305"
FT TRANSMEM 472..492
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 493..573
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 574..594
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 595..826
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305"
FT MOTIF 230..235
FT /note="HXXXXD motif"
FT MOD_RES 380
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97564"
FT MOD_RES 686
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61586"
FT MOD_RES 693
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCL2"
FT MOD_RES 778
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q61586"
FT MOD_RES 782
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q61586"
SQ SEQUENCE 826 AA; 93577 MW; F4E7D2E17F2E40BF 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 ESRNAADESF RRRLIANLAE HILFTASKSC
AIMSTHIVAC LLLYRHRQGI DLSTLVEDFF VMKEEVLARD FDLGFSGNSE DVVMHAIQLL
GNCITITHTS RNDEFFITPS TTVPSVFELN FYSNGVLHVF IMEAIIACSL YAVLKKRGSG
GPASPSLISQ EQLVRKAASL CYLLSNEGTI SLPCQTFYQI CHETVGRFIQ YGILTVAEQD
DQEDISPSLA EQHWDKKLPE PLSWRSDEED EDSDFGEEQR DCYLKVSQSK EHQQFITFLQ
RLLGPLLEAY SSAAIFIHNF SGPVPEPEYL QKLHKYLINR TERRVAVYAE SATYCLVKNA
VKMFKDIGVF KETKQKKVSV LELSSTFLPQ CNRQKLLEYI LSFVVL
