GPAT1_BOVIN
ID GPAT1_BOVIN Reviewed; 825 AA.
AC Q5GJ77;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 85.
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=GPAT1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RX PubMed=16276094; DOI=10.1159/000087517;
RA Roy R., Ordovas L., Taourit S., Zaragoza P., Eggen A., Rodellar C.;
RT "Genomic structure and an alternative transcript of bovine mitochondrial
RT glycerol-3-phosphate acyltransferase gene (GPAM).";
RL Cytogenet. Genome Res. 112:82-89(2006).
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 {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in adipose tissues and lung. Low
CC expression in liver. {ECO:0000269|PubMed:16276094}.
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; AY515690; AAS79429.1; -; mRNA.
DR EMBL; AY945228; AAY24765.1; -; Genomic_DNA.
DR EMBL; AY945226; AAY24765.1; JOINED; Genomic_DNA.
DR EMBL; AY945227; AAY24765.1; JOINED; Genomic_DNA.
DR RefSeq; NP_001012282.1; NM_001012282.1.
DR AlphaFoldDB; Q5GJ77; -.
DR STRING; 9913.ENSBTAP00000015811; -.
DR PaxDb; Q5GJ77; -.
DR PRIDE; Q5GJ77; -.
DR GeneID; 497202; -.
DR KEGG; bta:497202; -.
DR CTD; 57678; -.
DR eggNOG; KOG3729; Eukaryota.
DR InParanoid; Q5GJ77; -.
DR OrthoDB; 198209at2759; -.
DR UniPathway; UPA00557; UER00612.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0006654; P:phosphatidic acid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006655; P:phosphatidylglycerol biosynthetic process; ISS:UniProtKB.
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:0000255"
FT CHAIN ?..825
FT /note="Glycerol-3-phosphate acyltransferase 1,
FT mitochondrial"
FT /id="PRO_0000245029"
FT TOPO_DOM ?..470
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 471..493
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 494..573
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 574..592
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 593..825
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT REGION 435..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 230..235
FT /note="HXXXXD motif"
FT MOD_RES 380
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97564"
FT MOD_RES 685
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61586"
FT MOD_RES 692
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCL2"
FT MOD_RES 777
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q61586"
FT MOD_RES 781
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q61586"
SQ SEQUENCE 825 AA; 93144 MW; 01D294B9DE03CC04 CRC64;
MDESALTLGT IDVSYLPNSS EYSIGRCKHA TEEWGECGSR PTVFRSATLK WKESLMSRKR
PFVGRCCYSC TPQSWDKFFN PSIPSLGLRN VIYINETHTR HRGWLARRLS YVLFIQERDV
HKGMFATNVT ENVLNSSRVQ EAIAEVAGEL NPDGSAQQQS KAVNKVKKKA RKILQEMVAT
VSPAMIRLTG WVLLKLFNSF FWNIQIHKGQ LEMVKAATET NLPLIFLPVH RSHIDYLLLT
FILFCHNIKA PYIASGNNLN IPIFSTLIHK LGGFFIRRRL DETPDGRKDI LYRALLHGHI
VELLRQQQFL EIFLEGTRSR SGKISCARAG LLSVVVDTLS TNTIPDILII PGGISYDRII
EGHYNGEQLG KPKKNESLWS IARGVIRMLR KNYGCVKTDF AQPFSLKEYL ESQSQKPVSA
PLSLEQALLP AILPSRPSGA ADEGTDMSIN ESRNATDESR RRLIAHLAEH ILFTASKSCA
IMSTHIVACL LLYRHRQGIG LFTLVEDFFV MKEEVLARDF DLGFSGNSED VVMHAIQFLG
NCITITHTSK NDEFFITPST TIPSVFELNF YSNGVLHVFI MEAIIACSLY AVLKKRGPGG
PASPSLVSQE QLVHKAASLC YLLSNEGTIS LPCQTFYQIC HETVGRFIQY GILIVAEQDD
QEDISPGLAE QQWDKKLPEP LSWRSDEEDE DSDFGEEQRD CYLKVSQSKE HQQFITFLQR
LLGPLLEAYS SAAVFIHNFG GPVPEPEFLQ KLHKYLITRT ERRVAVYAES ATYCLVKNAV
KTFKDIGVFK ETKQKRVSGL ELSNTFLPQC NRQKLLEYIL SLVVL
