ID   GPAT1_HUMAN             Reviewed;         828 AA.
AC   Q9HCL2; Q5VW51; Q86TA3;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 3.
DT   02-SEP-2026, entry version 192.
DE   RecName: Full=Glycerol-3-phosphate acyltransferase 1, mitochondrial {ECO:0000305};
DE            Short=GPAT-1;
DE            EC=2.3.1.15 {ECO:0000269|PubMed:18238778, ECO:0000269|PubMed:36522428};
GN   Name=GPAM {ECO:0000312|HGNC:HGNC:24865};
GN   Synonyms=GPAT1 {ECO:0000303|PubMed:36522428}, KIAA1560;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Spinal cord;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164054; DOI=10.1038/nature02462;
RA   Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA   Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA   Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA   Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA   Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA   Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA   Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA   Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA   Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA   Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA   Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA   Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA   McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA   Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA   Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA   Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA   Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA   Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA   Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA   Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA   Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 10.";
RL   Nature 429:375-381(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 167-828.
RC   TISSUE=Brain;
RX   PubMed=10997877; DOI=10.1093/dnares/7.4.271;
RA   Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XVIII. The
RT   complete sequences of 100 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 7:273-281(2000).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT   networks.";
RL   Cell 127:635-648(2006).
RN   [5]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=18238778; DOI=10.1074/jbc.m708151200;
RA   Chen Y.Q., Kuo M.-S., Li S., Bui H.H., Peake D.A., Sanders P.E.,
RA   Thibodeaux S.J., Chu S., Qian Y.-W., Zhao Y., Bredt D.S., Moller D.E.,
RA   Konrad R.J., Beigneux A.P., Young S.G., Cao G.;
RT   "AGPAT6 is a novel microsomal glycerol-3-phosphate acyltransferase.";
RL   J. Biol. Chem. 283:10048-10057(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-695, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=18318008; DOI=10.1002/pmic.200700884;
RA   Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA   Zou H., Gu J.;
RT   "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT   and fractionation of phosphopeptides with strong anion exchange
RT   chromatography.";
RL   Proteomics 8:1346-1361(2008).
RN   [7]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=19075029; DOI=10.1194/jlr.m800567-jlr200;
RA   Zhao Y., Chen Y.-Q., Li S., Konrad R.J., Cao G.;
RT   "The microsomal cardiolipin remodeling enzyme acyl-CoA lysocardiolipin
RT   acyltransferase is an acyltransferase of multiple anionic
RT   lysophospholipids.";
RL   J. Lipid Res. 50:945-956(2009).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-695, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [9] {ECO:0007744|PDB:8E4Y, ECO:0007744|PDB:8E50}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS) OF 80-828, FUNCTION,
RP   CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION, DOMAIN,
RP   TOPOLOGY, AND MUTAGENESIS OF ARG-89; HIS-98; ARG-100; HIS-101; ARG-102;
RP   ARG-107; ARG-108; ARG-118; HIS-230; HIS-233; GLY-273; ARG-278; PHE-313;
RP   ARG-318 AND MET-388.
RX   PubMed=36522428; DOI=10.1038/s41594-022-00884-7;
RA   Johnson Z.L., Ammirati M., Wasilko D.J., Chang J.S., Noell S., Foley T.L.,
RA   Yoon H., Smith K., Asano S., Hales K., Wan M., Yang Q., Piotrowski M.A.,
RA   Farley K.A., Gilbert T., Aschenbrenner L.M., Fennell K.F., Dutra J.K.,
RA   Xu M., Guo C., Varghese A.E., Bellenger J., Quinn A., Am Ende C.W.,
RA   West G.M., Griffor M.C., Bennett D., Calabrese M., Steppan C.M., Han S.,
RA   Wu H.;
RT   "Structural basis of the acyl-transfer mechanism of human GPAT1.";
RL   Nat. Struct. Mol. Biol. 30:22-30(2023).
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:18238778,
CC       PubMed:19075029, PubMed:36522428). Esterifies acyl-group from acyl-
CC       coenzyme A (acyl-CoA) to the sn-1 position of glycerol-3-phosphate, to
CC       produce lysophosphatidic acid (PubMed:18238778). Has a narrow
CC       hydrophobic binding cleft that selects for a linear acyl chain
CC       (PubMed:36522428). Catalytic activity is higher for substrates with a
CC       16-carbon acyl chain (PubMed:36522428). {ECO:0000269|PubMed:18238778,
CC       ECO:0000269|PubMed:19075029, ECO:0000269|PubMed:36522428}.
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:18238778, ECO:0000269|PubMed:36522428};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15326;
CC         Evidence={ECO:0000305|PubMed:18238778, ECO:0000305|PubMed:36522428};
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:0000269|PubMed:18238778, ECO:0000269|PubMed:36522428};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37204;
CC         Evidence={ECO:0000305|PubMed:18238778, ECO:0000305|PubMed:36522428};
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:0000269|PubMed:18238778,
CC         ECO:0000269|PubMed:36522428};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37200;
CC         Evidence={ECO:0000305|PubMed:18238778, ECO:0000305|PubMed:36522428};
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:0000269|PubMed:18238778};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37196;
CC         Evidence={ECO:0000305|PubMed:18238778};
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:18238778};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35724;
CC         Evidence={ECO:0000305|PubMed:18238778};
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:0000269|PubMed:18238778};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35728;
CC         Evidence={ECO:0000305|PubMed:18238778};
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:0000269|PubMed:19075029};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33204;
CC         Evidence={ECO:0000269|PubMed:19075029};
CC   -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC       diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
CC       {ECO:0000269|PubMed:18238778}.
CC   -!- INTERACTION:
CC       Q9HCL2; Q9UHD4: CIDEB; NbExp=3; IntAct=EBI-7600236, EBI-7062247;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC       {ECO:0000269|PubMed:36522428}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:36522428}. Note=Associated with the mitochondrion
CC       outer membrane of hepatic cells via a patch of basic residues.
CC       {ECO:0000269|PubMed:36522428}.
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:0000269|PubMed:36522428}.
CC   -!- SIMILARITY: Belongs to the GPAT/DAPAT family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AL833093; CAD89932.1; -; mRNA.
DR   EMBL; AL391986; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AB046780; BAB13386.1; -; mRNA.
DR   CCDS; CCDS7570.1; -.
DR   RefSeq; NP_001231878.1; NM_001244949.2.
DR   RefSeq; NP_065969.3; NM_020918.6.
DR   RefSeq; XP_005270055.1; XM_005269998.2.
DR   RefSeq; XP_024303857.1; XM_024448089.2.
DR   RefSeq; XP_047281520.1; XM_047425564.1.
DR   PDB; 8E4Y; EM; 3.40 A; A=80-828.
DR   PDB; 8E50; EM; 3.67 A; A=80-828.
DR   AlphaFoldDB; Q9HCL2; -.
DR   EMDB; EMD-27898; -.
DR   EMDB; EMD-27899; -.
DR   SMR; Q9HCL2; -.
DR   BioGRID; 121707; 39.
DR   FunCoup; Q9HCL2; 937.
DR   IntAct; Q9HCL2; 25.
DR   MINT; Q9HCL2; -.
DR   NDEx; IQUERY-CP-GPAM; 7 NDEx IQuery Curated Pathways.
DR   STRING; 9606.ENSP00000265276; -.
DR   BindingDB; Q9HCL2; -.
DR   ChEMBL; CHEMBL3734642; -.
DR   SwissLipids; SLP:000000094; -.
DR   GlyGen; Q9HCL2; 2 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9HCL2; -.
DR   PhosphoSitePlus; Q9HCL2; -.
DR   SwissPalm; Q9HCL2; -.
DR   BioMuta; GPAM; -.
DR   DMDM; 59803040; -.
DR   jPOST; Q9HCL2; -.
DR   MassIVE; Q9HCL2; -.
DR   PaxDb; 9606-ENSP00000265276; -.
DR   PeptideAtlas; Q9HCL2; -.
DR   ProteomicsDB; 81752; -.
DR   Pumba; Q9HCL2; -.
DR   Antibodypedia; 31772; 248 antibodies from 31 providers.
DR   DNASU; 57678; -.
DR   Ensembl; ENST00000348367.9; ENSP00000265276.4; ENSG00000119927.15.
DR   Ensembl; ENST00000901835.1; ENSP00000571894.1; ENSG00000119927.15.
DR   Ensembl; ENST00000901836.1; ENSP00000571895.1; ENSG00000119927.15.
DR   Ensembl; ENST00000901837.1; ENSP00000571896.1; ENSG00000119927.15.
DR   Ensembl; ENST00000901838.1; ENSP00000571897.1; ENSG00000119927.15.
DR   Ensembl; ENST00000901839.1; ENSP00000571898.1; ENSG00000119927.15.
DR   Ensembl; ENST00000901840.1; ENSP00000571899.1; ENSG00000119927.15.
DR   Ensembl; ENST00000901841.1; ENSP00000571900.1; ENSG00000119927.15.
DR   Ensembl; ENST00000901842.1; ENSP00000571901.1; ENSG00000119927.15.
DR   Ensembl; ENST00000901843.1; ENSP00000571902.1; ENSG00000119927.15.
DR   Ensembl; ENST00000901844.1; ENSP00000571903.1; ENSG00000119927.15.
DR   GeneID; 57678; -.
DR   KEGG; hsa:57678; -.
DR   MANE-Select; ENST00000348367.9; ENSP00000265276.4; NM_001244949.2; NP_001231878.1.
DR   UCSC; uc001kzp.4; human.
DR   AGR; HGNC:24865; -.
DR   ClinPGx; PA134983031; -.
DR   CTD; 57678; -.
DR   DisGeNET; 57678; -.
DR   GeneCards; GPAM; -.
DR   HGNC; HGNC:24865; GPAM.
DR   HPA; ENSG00000119927; Tissue enhanced (adipose tissue, liver).
DR   MIM; 602395; gene.
DR   OpenTargets; ENSG00000119927; -.
DR   VEuPathDB; HostDB:ENSG00000119927; -.
DR   eggNOG; KOG3729; Eukaryota.
DR   GeneTree; ENSGT00520000055570; -.
DR   InParanoid; Q9HCL2; -.
DR   OMA; RCKHTNE; -.
DR   OrthoDB; 5962536at2759; -.
DR   PAN-GO; Q9HCL2; 4 GO annotations based on evolutionary models.
DR   PhylomeDB; Q9HCL2; -.
DR   BioCyc; MetaCyc:57678-MONOMER; -.
DR   BRENDA; 2.3.1.15; 2681.
DR   PathwayCommons; Q9HCL2; -.
DR   Reactome; R-HSA-1483166; Synthesis of PA.
DR   Reactome; R-HSA-2426168; Activation of gene expression by SREBF (SREBP).
DR   Reactome; R-HSA-75109; Triglyceride biosynthesis.
DR   Reactome; R-HSA-8931987; RUNX1 regulates estrogen receptor mediated transcription.
DR   Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
DR   Reactome; R-HSA-9841922; MLL4 and MLL3 complexes regulate expression of PPARG target genes in adipogenesis and hepatic steatosis.
DR   SignaLink; Q9HCL2; -.
DR   UniPathway; UPA00557; UER00612.
DR   Agora; ENSG00000119927; -.
DR   BioGRID-ORCS; 57678; 11 hits in 1159 CRISPR screens.
DR   ChiTaRS; GPAM; human.
DR   GeneWiki; GPAM; -.
DR   GenomeRNAi; 57678; -.
DR   Pharos; Q9HCL2; Tbio.
DR   PRO; PR:Q9HCL2; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   RNAct; Q9HCL2; protein.
DR   Bgee; ENSG00000119927; Expressed in pericardium and 181 other cell types or tissues.
DR   ExpressionAtlas; Q9HCL2; baseline and differential.
DR   GO; GO:0005741; C:mitochondrial outer membrane; TAS:Reactome.
DR   GO; GO:0005739; C:mitochondrion; HTP:FlyBase.
DR   GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR   GO; GO:0004366; F:glycerol-3-phosphate O-acyltransferase activity; IMP:UniProtKB.
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:0006650; P:glycerophospholipid metabolic process; IBA:GO_Central.
DR   GO; GO:0006654; P:phosphatidic acid biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0006655; P:phosphatidylglycerol biosynthetic process; IMP:UniProtKB.
DR   GO; GO:0019432; P:triglyceride biosynthetic process; IDA:UniProtKB.
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.
DR   PDBsum; 8E4Y; -.
DR   PDBsum; 8E50; -.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Acyltransferase; Lipid biosynthesis;
KW   Lipid metabolism; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW   Phospholipid biosynthesis; Phospholipid metabolism; Phosphoprotein;
KW   Proteomics identification; Reference proteome; Transferase.
FT   CHAIN           1..828
FT                   /note="Glycerol-3-phosphate acyltransferase 1,
FT                   mitochondrial"
FT                   /id="PRO_0000024690"
FT   TOPO_DOM        1..87
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:36522428,
FT                   ECO:0007744|PDB:8E4Y, ECO:0007744|PDB:8E50"
FT   INTRAMEM        88..118
FT                   /evidence="ECO:0000269|PubMed:36522428,
FT                   ECO:0007744|PDB:8E4Y, ECO:0007744|PDB:8E50"
FT   TOPO_DOM        119..828
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:36522428,
FT                   ECO:0007744|PDB:8E4Y, ECO:0007744|PDB:8E50"
FT   REGION          80..120
FT                   /note="Important for mitochondrial localization"
FT   REGION          435..455
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           230..235
FT                   /note="HXXXXD motif"
FT                   /evidence="ECO:0000269|PubMed:36522428"
FT   COMPBIAS        442..455
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         278
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000269|PubMed:36522428,
FT                   ECO:0007744|PDB:8E4Y"
FT   BINDING         279
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000269|PubMed:36522428,
FT                   ECO:0007744|PDB:8E4Y"
FT   BINDING         288
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000269|PubMed:36522428,
FT                   ECO:0007744|PDB:8E4Y"
FT   BINDING         293
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000269|PubMed:36522428,
FT                   ECO:0007744|PDB:8E4Y"
FT   BINDING         328
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000269|PubMed:36522428,
FT                   ECO:0007744|PDB:8E4Y"
FT   BINDING         462
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000269|PubMed:36522428,
FT                   ECO:0007744|PDB:8E4Y"
FT   MOD_RES         380
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P97564"
FT   MOD_RES         688
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q61586"
FT   MOD_RES         695
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18318008,
FT                   ECO:0007744|PubMed:24275569"
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   VARIANT         4
FT                   /note="S -> Y (in dbSNP:rs11549703)"
FT                   /id="VAR_050585"
FT   VARIANT         43
FT                   /note="I -> V (in dbSNP:rs2792751)"
FT                   /id="VAR_050586"
FT   VARIANT         131
FT                   /note="E -> G (in dbSNP:rs10787428)"
FT                   /id="VAR_050587"
FT   VARIANT         386
FT                   /note="I -> T (in dbSNP:rs35019520)"
FT                   /id="VAR_050588"
FT   MUTAGEN         89
FT                   /note="R->E: Abrogates mitochondrial localization; when
FT                   associated with E-98, E-100, E-101, E-102, E-107, E-108 and
FT                   E-118."
FT                   /evidence="ECO:0000269|PubMed:36522428"
FT   MUTAGEN         98
FT                   /note="H->E: Abrogates mitochondrial localization; when
FT                   associated with E-89, E-100, E-101, E-102, E-107, E-108 and
FT                   E-118."
FT                   /evidence="ECO:0000269|PubMed:36522428"
FT   MUTAGEN         100
FT                   /note="R->E: Abrogates mitochondrial localization; when
FT                   associated with E-89, E-98, E-101, E-102, E-107, E-108 and
FT                   E-118."
FT                   /evidence="ECO:0000269|PubMed:36522428"
FT   MUTAGEN         101
FT                   /note="H->E: Abrogates mitochondrial localization; when
FT                   associated with E-89, E-98, E-100, E-102, E-107, E-108 and
FT                   E-118."
FT                   /evidence="ECO:0000269|PubMed:36522428"
FT   MUTAGEN         102
FT                   /note="R->E: Abrogates mitochondrial localization; when
FT                   associated with E-89, E-98, E-100, E-101, E-107, E-108 and
FT                   E-118."
FT                   /evidence="ECO:0000269|PubMed:36522428"
FT   MUTAGEN         107
FT                   /note="R->E: Abrogates mitochondrial localization; when
FT                   associated with E-89, E-98, E-100, E-101, E-102, E-108 and
FT                   E-118."
FT                   /evidence="ECO:0000269|PubMed:36522428"
FT   MUTAGEN         108
FT                   /note="R->E: Abrogates mitochondrial localization; when
FT                   associated with E-89, E-98, E-100, E-101, E-102, E-107 and
FT                   E-118."
FT                   /evidence="ECO:0000269|PubMed:36522428"
FT   MUTAGEN         118
FT                   /note="R->E: Abrogates mitochondrial localization; when
FT                   associated with E-89, E-98, E-100, E-101, E-102, E-107 and
FT                   E-108."
FT                   /evidence="ECO:0000269|PubMed:36522428"
FT   MUTAGEN         230
FT                   /note="H->A: Abolishes catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:36522428"
FT   MUTAGEN         233
FT                   /note="H->W: Abolishes catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:36522428"
FT   MUTAGEN         273
FT                   /note="G->L: Abolishes catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:36522428"
FT   MUTAGEN         278
FT                   /note="R->A: Abolishes catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:36522428"
FT   MUTAGEN         313
FT                   /note="F->A: Abolishes catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:36522428"
FT   MUTAGEN         318
FT                   /note="R->A: Abolishes catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:36522428"
FT   MUTAGEN         388
FT                   /note="M->W: Impairs catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:36522428"
FT   CONFLICT        204
FT                   /note="I -> F (in Ref. 1; CAD89932)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        652
FT                   /note="Q -> R (in Ref. 1; CAD89932)"
FT                   /evidence="ECO:0000305"
FT   STRAND          88..92
FT                   /evidence="ECO:0007829|PDB:8E4Y"
FT   TURN            96..98
FT                   /evidence="ECO:0007829|PDB:8E4Y"
FT   HELIX           104..108
FT                   /evidence="ECO:0007829|PDB:8E4Y"
FT   HELIX           110..115
FT                   /evidence="ECO:0007829|PDB:8E4Y"
FT   HELIX           129..134
FT                   /evidence="ECO:0007829|PDB:8E4Y"
FT   HELIX           137..150
FT                   /evidence="ECO:0007829|PDB:8E4Y"
FT   HELIX           163..175
FT                   /evidence="ECO:0007829|PDB:8E4Y"
FT   HELIX           183..200
FT                   /evidence="ECO:0007829|PDB:8E4Y"
FT   STRAND          204..207
FT                   /evidence="ECO:0007829|PDB:8E4Y"
FT   HELIX           208..219
FT                   /evidence="ECO:0007829|PDB:8E4Y"
FT   STRAND          220..222
FT                   /evidence="ECO:0007829|PDB:8E4Y"
FT   STRAND          224..228
FT                   /evidence="ECO:0007829|PDB:8E4Y"
FT   HELIX           235..244
FT                   /evidence="ECO:0007829|PDB:8E4Y"
FT   TURN            245..247
FT                   /evidence="ECO:0007829|PDB:8E4Y"
FT   HELIX           248..251
FT                   /evidence="ECO:0007829|PDB:8E4Y"
FT   STRAND          252..256
FT                   /evidence="ECO:0007829|PDB:8E4Y"
FT   HELIX           257..259
FT                   /evidence="ECO:0007829|PDB:8E4Y"
FT   HELIX           264..270
FT                   /evidence="ECO:0007829|PDB:8E4Y"
FT   STRAND          273..276
FT                   /evidence="ECO:0007829|PDB:8E4Y"
FT   HELIX           290..305
FT                   /evidence="ECO:0007829|PDB:8E4Y"
FT   STRAND          314..317
FT                   /evidence="ECO:0007829|PDB:8E4Y"
FT   STRAND          320..323
FT                   /evidence="ECO:0007829|PDB:8E4Y"
FT   HELIX           332..340
FT                   /evidence="ECO:0007829|PDB:8E4Y"
FT   STRAND          343..345
FT                   /evidence="ECO:0007829|PDB:8E4Y"
FT   STRAND          348..358
FT                   /evidence="ECO:0007829|PDB:8E4Y"
FT   HELIX           365..369
FT                   /evidence="ECO:0007829|PDB:8E4Y"
FT   HELIX           380..390
FT                   /evidence="ECO:0007829|PDB:8E4Y"
FT   STRAND          396..400
FT                   /evidence="ECO:0007829|PDB:8E4Y"
FT   HELIX           401..403
FT                   /evidence="ECO:0007829|PDB:8E4Y"
FT   HELIX           406..415
FT                   /evidence="ECO:0007829|PDB:8E4Y"
FT   HELIX           418..420
FT                   /evidence="ECO:0007829|PDB:8E4Y"
FT   HELIX           424..432
FT                   /evidence="ECO:0007829|PDB:8E4Y"
FT   HELIX           457..479
FT                   /evidence="ECO:0007829|PDB:8E4Y"
FT   HELIX           484..490
FT                   /evidence="ECO:0007829|PDB:8E4Y"
FT   HELIX           491..496
FT                   /evidence="ECO:0007829|PDB:8E4Y"
FT   HELIX           502..518
FT                   /evidence="ECO:0007829|PDB:8E4Y"
FT   HELIX           529..539
FT                   /evidence="ECO:0007829|PDB:8E4Y"
FT   TURN            540..543
FT                   /evidence="ECO:0007829|PDB:8E4Y"
FT   STRAND          544..548
FT                   /evidence="ECO:0007829|PDB:8E4Y"
FT   STRAND          554..559
FT                   /evidence="ECO:0007829|PDB:8E4Y"
FT   HELIX           563..573
FT                   /evidence="ECO:0007829|PDB:8E4Y"
FT   HELIX           574..576
FT                   /evidence="ECO:0007829|PDB:8E4Y"
FT   HELIX           577..594
FT                   /evidence="ECO:0007829|PDB:8E4Y"
FT   HELIX           612..625
FT                   /evidence="ECO:0007829|PDB:8E4Y"
FT   STRAND          626..630
FT                   /evidence="ECO:0007829|PDB:8E4Y"
FT   STRAND          635..637
FT                   /evidence="ECO:0007829|PDB:8E4Y"
FT   HELIX           639..653
FT                   /evidence="ECO:0007829|PDB:8E4Y"
FT   STRAND          655..658
FT                   /evidence="ECO:0007829|PDB:8E4Y"
FT   STRAND          705..708
FT                   /evidence="ECO:0007829|PDB:8E4Y"
FT   HELIX           712..724
FT                   /evidence="ECO:0007829|PDB:8E4Y"
FT   HELIX           726..738
FT                   /evidence="ECO:0007829|PDB:8E4Y"
FT   HELIX           739..741
FT                   /evidence="ECO:0007829|PDB:8E4Y"
FT   HELIX           748..765
FT                   /evidence="ECO:0007829|PDB:8E4Y"
FT   HELIX           771..774
FT                   /evidence="ECO:0007829|PDB:8E4Y"
FT   HELIX           777..789
FT                   /evidence="ECO:0007829|PDB:8E4Y"
FT   STRAND          791..796
FT                   /evidence="ECO:0007829|PDB:8E4Y"
FT   STRAND          798..805
FT                   /evidence="ECO:0007829|PDB:8E4Y"
FT   HELIX           812..823
FT                   /evidence="ECO:0007829|PDB:8E4Y"
SQ   SEQUENCE   828 AA;  93795 MW;  7AADD21BC8684693 CRC64;
     MDESALTLGT IDVSYLPHSS EYSVGRCKHT SEEWGECGFR PTIFRSATLK WKESLMSRKR
     PFVGRCCYSC TPQSWDKFFN PSIPSLGLRN VIYINETHTR HRGWLARRLS YVLFIQERDV
     HKGMFATNVT ENVLNSSRVQ EAIAEVAAEL NPDGSAQQQS KAVNKVKKKA KRILQEMVAT
     VSPAMIRLTG WVLLKLFNSF FWNIQIHKGQ LEMVKAATET NLPLLFLPVH RSHIDYLLLT
     FILFCHNIKA PYIASGNNLN IPIFSTLIHK LGGFFIRRRL DETPDGRKDV LYRALLHGHI
     VELLRQQQFL EIFLEGTRSR SGKTSCARAG LLSVVVDTLS TNVIPDILII PVGISYDRII
     EGHYNGEQLG KPKKNESLWS VARGVIRMLR KNYGCVRVDF AQPFSLKEYL ESQSQKPVSA
     LLSLEQALLP AILPSRPSDA ADEGRDTSIN ESRNATDESL RRRLIANLAE HILFTASKSC
     AIMSTHIVAC LLLYRHRQGI DLSTLVEDFF VMKEEVLARD FDLGFSGNSE DVVMHAIQLL
     GNCVTITHTS RNDEFFITPS TTVPSVFELN FYSNGVLHVF IMEAIIACSL YAVLNKRGLG
     GPTSTPPNLI SQEQLVRKAA SLCYLLSNEG TISLPCQTFY QVCHETVGKF IQYGILTVAE
     HDDQEDISPS LAEQQWDKKL PEPLSWRSDE EDEDSDFGEE QRDCYLKVSQ SKEHQQFITF
     LQRLLGPLLE AYSSAAIFVH NFSGPVPEPE YLQKLHKYLI TRTERNVAVY AESATYCLVK
     NAVKMFKDIG VFKETKQKRV SVLELSSTFL PQCNRQKLLE YILSFVVL
//