GPAT1_RAT
ID GPAT1_RAT Reviewed; 828 AA.
AC P97564; O35349; P97565; P97566;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 3.
DT 25-MAY-2022, entry version 136.
DE RecName: Full=Glycerol-3-phosphate acyltransferase 1, mitochondrial {ECO:0000305};
DE Short=GPAT-1;
DE EC=2.3.1.15 {ECO:0000269|PubMed:10446428};
DE Flags: Precursor;
GN Name=Gpam {ECO:0000312|RGD:61847}; Synonyms=Gpat1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, AND FUNCTION.
RC TISSUE=Liver;
RX PubMed=10446428; DOI=10.1016/s1388-1981(99)00103-1;
RA Bhat B.G., Wang P., Kim J.-H., Black T.M., Lewin T.M., Fiedorek F.T. Jr.,
RA Coleman R.A.;
RT "Rat sn-glycerol-3-phosphate acyltransferase: molecular cloning and
RT characterization of the cDNA and expressed protein.";
RL Biochim. Biophys. Acta 1439:415-423(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TOPOLOGY.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=10924502; DOI=10.1074/jbc.m002963200;
RA Balija V.S., Chakraborty T.R., Nikonov A.V., Morimoto T., Haldar D.;
RT "Identification of two transmembrane regions and a cytosolic domain of rat
RT mitochondrial glycerophosphate acyltransferase.";
RL J. Biol. Chem. 275:31668-31673(2000).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-380, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [4]
RP CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=22905194; DOI=10.1371/journal.pone.0042986;
RA Cattaneo E.R., Pellon-Maison M., Rabassa M.E., Lacunza E., Coleman R.A.,
RA Gonzalez-Baro M.R.;
RT "Glycerol-3-phosphate acyltransferase-2 is expressed in spermatic germ
RT cells and incorporates arachidonic acid into triacylglycerols.";
RL PLoS ONE 7:e42986-e42986(2012).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-688 AND SER-695, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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:0000269|PubMed:10446428, ECO:0000269|PubMed:22905194}.
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:0000269|PubMed:10446428};
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:0000269|PubMed:22905194};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35724;
CC Evidence={ECO:0000305|PubMed:22905194};
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=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:0000269|PubMed:10446428}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:10924502}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:10924502}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB39470.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF021348; AAB71605.1; -; mRNA.
DR EMBL; U36771; AAB39470.2; ALT_INIT; mRNA.
DR RefSeq; NP_058970.1; NM_017274.1.
DR AlphaFoldDB; P97564; -.
DR STRING; 10116.ENSRNOP00000050050; -.
DR SwissLipids; SLP:000000284; -.
DR iPTMnet; P97564; -.
DR PhosphoSitePlus; P97564; -.
DR jPOST; P97564; -.
DR PaxDb; P97564; -.
DR PRIDE; P97564; -.
DR GeneID; 29653; -.
DR KEGG; rno:29653; -.
DR UCSC; RGD:61847; rat.
DR CTD; 57678; -.
DR RGD; 61847; Gpam.
DR eggNOG; KOG3729; Eukaryota.
DR InParanoid; P97564; -.
DR PhylomeDB; P97564; -.
DR BRENDA; 2.3.1.15; 5301.
DR Reactome; R-RNO-1483166; Synthesis of PA.
DR Reactome; R-RNO-75109; Triglyceride biosynthesis.
DR SABIO-RK; P97564; -.
DR UniPathway; UPA00557; UER00612.
DR PRO; PR:P97564; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:RGD.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:RGD.
DR GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR GO; GO:0004366; F:glycerol-3-phosphate O-acyltransferase activity; IDA:RGD.
DR GO; GO:0102420; F:sn-1-glycerol-3-phosphate C16:0-DCA-CoA acyl transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006637; P:acyl-CoA metabolic process; ISO:RGD.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IDA:RGD.
DR GO; GO:0051607; P:defense response to virus; ISO:RGD.
DR GO; GO:0006651; P:diacylglycerol biosynthetic process; IMP:UniProtKB.
DR GO; GO:0055089; P:fatty acid homeostasis; ISO:RGD.
DR GO; GO:0006631; P:fatty acid metabolic process; ISO:RGD.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006650; P:glycerophospholipid metabolic process; ISO:RGD.
DR GO; GO:0070236; P:negative regulation of activation-induced cell death of T cells; ISO:RGD.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IMP: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:0055091; P:phospholipid homeostasis; ISO:RGD.
DR GO; GO:0042104; P:positive regulation of activated T cell proliferation; ISO:RGD.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; ISO:RGD.
DR GO; GO:0010867; P:positive regulation of triglyceride biosynthetic process; IDA:RGD.
DR GO; GO:0001817; P:regulation of cytokine production; ISO:RGD.
DR GO; GO:0014823; P:response to activity; IDA:RGD.
DR GO; GO:0046686; P:response to cadmium ion; IEP:RGD.
DR GO; GO:0009750; P:response to fructose; IEP:RGD.
DR GO; GO:0009749; P:response to glucose; ISO:RGD.
DR GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
DR GO; GO:0019432; P:triglyceride biosynthetic process; ISO:RGD.
DR GO; GO:0006641; P:triglyceride metabolic process; ISO:RGD.
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 1: Evidence at protein 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:0000255"
FT CHAIN ?..828
FT /note="Glycerol-3-phosphate acyltransferase 1,
FT mitochondrial"
FT /id="PRO_0000024692"
FT TOPO_DOM ?..471
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 472..494
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 495..574
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 575..593
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 594..828
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT MOTIF 230..235
FT /note="HXXXXD motif"
FT MOD_RES 380
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT MOD_RES 688
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 695
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 780
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q61586"
FT MOD_RES 784
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q61586"
FT CONFLICT 37
FT /note="C -> F (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 85
FT /note="S -> P (in Ref. 2; AAB39470)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="I -> V (in Ref. 2; AAB39470)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="L -> V (in Ref. 2; AAB39470)"
FT /evidence="ECO:0000305"
FT CONFLICT 472..474
FT /note="ILF -> NLL (in Ref. 2; AAB39470)"
FT /evidence="ECO:0000305"
FT CONFLICT 497
FT /note="R -> W (in Ref. 2; AAB39470)"
FT /evidence="ECO:0000305"
FT CONFLICT 602..606
FT /note="SAGGL -> LPEP (in Ref. 2; AAB39470)"
FT /evidence="ECO:0000305"
FT CONFLICT 644
FT /note="Q -> H (in Ref. 2; AAB39470)"
FT /evidence="ECO:0000305"
FT CONFLICT 744
FT /note="G -> A (in Ref. 2; AAB39470)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 828 AA; 93715 MW; ACA4A087E7DEB12C CRC64;
MEESSVTIGT IDVSYLPNSS EYSLGRCKHT NEDWVDCGFK PTFFRSATLK WKESLMSRKR
PFVGRCCYSC TPQSWERFFN PSIPSLGLRN VIYINETHTR HRGWLARRLS YILFVQERDV
HKGMFATSIT DNVLNSSRVQ EAIAEVAAEL NPDGSAQQQS KAIQKVKRKA RKILQEMVAT
VSPGMIRLTG WVLLKLFNSF FWNIQIHKGQ LEMVKAATET NLPLLFLPVH RSHIDYLLLT
FILFCHNIKA PYIASGNNLN IPIFSTLIHK LGGFFIRRRL DETPDGRKDI LYRALLHGHI
VELLRQQQFL EIFLEGTRSR SGKTSCARAG LLSVVVDTLS SNTIPDILVI PVGISYDRII
EGHYNGEQLG KPKKNESLWS VARGVIRMLR KNYGYVRVDF AQPFSLKEYL EGQSQKPVSA
PLSLEQALLP AILPSRPDAA AAEHEDMSSN ESRNAADEAF RRRLIANLAE HILFTASKSC
AIMSTHIVAC LLLYRHRQGI HLSTLVEDFF VMKEEVLARD FDLGFSGNSE DVVMHAIQLL
GNCVTITHTS RKDEFFITPS TTVPSVFELN FYSNGVLHVF IMEAIIACSI YAVQNKRGSG
GSAGGLGNLI SQEQLVRKAA SLCYLLSNEG TISLPCQTFY QVCQETVGKF IQYGILTVAE
QDDQEDVSPG LAEQQWNKKL PEPLNWRSDE EDEDSDFGEE QRDCYLKVSQ AKEHQQFITF
LQRLLGPLLE AYSSAAIFVH TFRGPVPESE YLQKLHRYLL TRTERNVAVY AESATYCLVK
NAVKMFKDIG VFKETKQKRA SVLELSTTFL PQGSRQKLLE YILSFVVL
