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   10-JUN-2026, entry version 149.
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};
GN   Name=Gpam {ECO:0000312|RGD:61847};
GN   Synonyms=Gpat1 {ECO:0000250|UniProtKB:Q9HCL2};
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: Mitochondrial membrane protein that catalyzes the essential
CC       first step of biosynthesis of glycerolipids such as triglycerides,
CC       phosphatidic acids and lysophosphatidic acids (PubMed:10446428,
CC       PubMed:22905194). Esterifies acyl-group from acyl-coenzyme A (acyl-CoA)
CC       to the sn-1 position of glycerol-3-phosphate, to produce
CC       lysophosphatidic acid (PubMed:10446428, PubMed:22905194). Has a narrow
CC       hydrophobic binding cleft that selects for a linear acyl chain (By
CC       similarity). Catalytic activity is higher for substrates with a 16-
CC       carbon acyl chain (By similarity). {ECO:0000250|UniProtKB:Q9HCL2,
CC       ECO:0000269|PubMed:10446428, ECO:0000269|PubMed:22905194}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=sn-glycerol 3-phosphate + an acyl-CoA = 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=sn-glycerol 3-phosphate + hexadecanoyl-CoA = 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=sn-glycerol 3-phosphate + (9Z)-octadecenoyl-CoA = 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=sn-glycerol 3-phosphate + octadecanoyl-CoA = 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 = a
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}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q9HCL2}. Note=Associated with the mitochondrion
CC       outer membrane of hepatic cells via a patch of basic residues.
CC       {ECO:0000250|UniProtKB:Q9HCL2}.
CC   -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity and
CC       contributes to the binding of the cysteamine moiety of the acyl-CoA and
CC       the phosphate moiety of the glycerol-3-phosphate.
CC       {ECO:0000250|UniProtKB:Q9HCL2}.
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   SMR; P97564; -.
DR   FunCoup; P97564; 1202.
DR   STRING; 10116.ENSRNOP00000069320; -.
DR   SwissLipids; SLP:000000284; -.
DR   GlyGen; P97564; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P97564; -.
DR   PhosphoSitePlus; P97564; -.
DR   jPOST; P97564; -.
DR   PaxDb; 10116-ENSRNOP00000069320; -.
DR   GeneID; 29653; -.
DR   KEGG; rno:29653; -.
DR   UCSC; RGD:61847; rat.
DR   AGR; RGD:61847; -.
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:0031966; C:mitochondrial membrane; IDA:RGD.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IDA:MGI.
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: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: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: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:0007584; P:response to nutrient; IEP: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; 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   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.
FT   CHAIN           1..828
FT                   /note="Glycerol-3-phosphate acyltransferase 1,
FT                   mitochondrial"
FT                   /id="PRO_0000024692"
FT   TOPO_DOM        1..87
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HCL2"
FT   INTRAMEM        88..118
FT                   /evidence="ECO:0000250|UniProtKB:Q9HCL2"
FT   TOPO_DOM        119..828
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HCL2"
FT   REGION          80..120
FT                   /note="Important for mitochondrial localization"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HCL2"
FT   MOTIF           230..235
FT                   /note="HXXXXD motif"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HCL2"
FT   BINDING         278
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HCL2"
FT   BINDING         279
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HCL2"
FT   BINDING         288
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HCL2"
FT   BINDING         293
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HCL2"
FT   BINDING         328
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HCL2"
FT   BINDING         462
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HCL2"
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
//