GPAT3_RAT
ID GPAT3_RAT Reviewed; 457 AA.
AC Q4V8J4;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Glycerol-3-phosphate acyltransferase 3 {ECO:0000312|RGD:1565703};
DE Short=GPAT-3;
DE EC=2.3.1.15 {ECO:0000250|UniProtKB:Q53EU6};
DE AltName: Full=1-acyl-sn-glycerol-3-phosphate O-acyltransferase 10 {ECO:0000250|UniProtKB:Q53EU6};
DE Short=AGPAT 10 {ECO:0000250|UniProtKB:Q53EU6};
DE AltName: Full=1-acyl-sn-glycerol-3-phosphate O-acyltransferase 9;
DE Short=1-AGP acyltransferase 9;
DE Short=1-AGPAT 9;
DE EC=2.3.1.51 {ECO:0000250|UniProtKB:Q53EU6};
DE AltName: Full=Lysophosphatidic acid acyltransferase theta;
DE Short=LPAAT-theta;
GN Name=Gpat3 {ECO:0000312|RGD:1565703}; Synonyms=Agpat9;
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 [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, AND IDENTIFICATION BY
RP 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: Converts glycerol-3-phosphate to 1-acyl-sn-glycerol-3-
CC phosphate (lysophosphatidic acid or LPA) by incorporating an acyl
CC moiety at the sn-1 position of the glycerol backbone. Also converts LPA
CC into 1,2-diacyl-sn-glycerol-3-phosphate (phosphatidic acid or PA) by
CC incorporating an acyl moiety at the sn-2 position of the glycerol
CC backbone. Protects cells against lipotoxicity.
CC {ECO:0000250|UniProtKB:Q53EU6}.
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:Q53EU6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15326;
CC Evidence={ECO:0000250|UniProtKB:Q53EU6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-
CC sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:19709,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:58608; EC=2.3.1.51;
CC Evidence={ECO:0000250|UniProtKB:Q53EU6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19710;
CC Evidence={ECO:0000250|UniProtKB:Q53EU6};
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:Q53EU6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35728;
CC Evidence={ECO:0000250|UniProtKB:Q53EU6};
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:Q53EU6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35724;
CC Evidence={ECO:0000250|UniProtKB:Q53EU6};
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:Q53EU6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37200;
CC Evidence={ECO:0000250|UniProtKB:Q53EU6};
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:Q53EU6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37204;
CC Evidence={ECO:0000250|UniProtKB:Q53EU6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-tetradecanoyl-sn-glycerol 3-
CC phosphate = 1-tetradecanoyl-2-(9Z)-octadecenoyl-sn-glycero-3-
CC phosphate + CoA; Xref=Rhea:RHEA:37187, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:72683, ChEBI:CHEBI:74586;
CC Evidence={ECO:0000250|UniProtKB:Q53EU6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37188;
CC Evidence={ECO:0000250|UniProtKB:Q53EU6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-phosphate
CC = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:33187, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:57518, ChEBI:CHEBI:64839;
CC Evidence={ECO:0000250|UniProtKB:Q53EU6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33188;
CC Evidence={ECO:0000250|UniProtKB:Q53EU6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphate = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37131, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:74544, ChEBI:CHEBI:74546;
CC Evidence={ECO:0000250|UniProtKB:Q53EU6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37132;
CC Evidence={ECO:0000250|UniProtKB:Q53EU6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-(6Z,9Z,12Z-octadecatrienoyl)-sn-
CC glycero-3-phosphate = (6Z,9Z,12Z)-octadecatrienoyl-2-(9Z)-
CC octadecenoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37179,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:74581,
CC ChEBI:CHEBI:74582; Evidence={ECO:0000250|UniProtKB:Q53EU6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37180;
CC Evidence={ECO:0000250|UniProtKB:Q53EU6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z,12Z,15Z)-octadecatrienoyl-sn-
CC glycero-3-phosphate = 1-(9Z,12Z,15Z)-octadecatrienoyl-2-(9Z)-
CC octadecenoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37139,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:74549,
CC ChEBI:CHEBI:74550; Evidence={ECO:0000250|UniProtKB:Q53EU6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37140;
CC Evidence={ECO:0000250|UniProtKB:Q53EU6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + tetradecanoyl-CoA
CC = 1-(9Z)-octadecenoyl-2-tetradecanoyl-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37171, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385,
CC ChEBI:CHEBI:74544, ChEBI:CHEBI:74579;
CC Evidence={ECO:0000250|UniProtKB:Q53EU6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37172;
CC Evidence={ECO:0000250|UniProtKB:Q53EU6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + hexadecanoyl-CoA
CC = 1-(9Z)-octadecenoyl-2-hexadecanoyl-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37143, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:74544, ChEBI:CHEBI:74551;
CC Evidence={ECO:0000250|UniProtKB:Q53EU6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37144;
CC Evidence={ECO:0000250|UniProtKB:Q53EU6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + octadecanoyl-CoA
CC = 1-(9Z-octadecenoyl)-2-octadecanoyl-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37147, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394,
CC ChEBI:CHEBI:74544, ChEBI:CHEBI:74552;
CC Evidence={ECO:0000250|UniProtKB:Q53EU6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37148;
CC Evidence={ECO:0000250|UniProtKB:Q53EU6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-
CC 3-phosphate = 1-(9Z)-octadecenoyl-2-(9Z,12Z)-octadecadienoyl-sn-
CC glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37159, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57383, ChEBI:CHEBI:74544, ChEBI:CHEBI:74563;
CC Evidence={ECO:0000250|UniProtKB:Q53EU6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37160;
CC Evidence={ECO:0000250|UniProtKB:Q53EU6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-
CC glycero-3-phosphate = 1-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-2-(9Z)-
CC octadecenoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37455,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:74938,
CC ChEBI:CHEBI:74941; Evidence={ECO:0000250|UniProtKB:Q53EU6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37456;
CC Evidence={ECO:0000250|UniProtKB:Q53EU6};
CC -!- PATHWAY: Glycerolipid metabolism; triacylglycerol biosynthesis.
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q53EU6}; Multi-pass membrane protein
CC {ECO:0000255}.
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|UniProtKB:Q9D517}.
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000305}.
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DR EMBL; BC097362; AAH97362.1; -; mRNA.
DR RefSeq; NP_001020841.1; NM_001025670.1.
DR RefSeq; XP_008768241.1; XM_008770019.2.
DR RefSeq; XP_008768242.1; XM_008770020.2.
DR RefSeq; XP_008768243.1; XM_008770021.2.
DR AlphaFoldDB; Q4V8J4; -.
DR STRING; 10116.ENSRNOP00000002936; -.
DR iPTMnet; Q4V8J4; -.
DR PhosphoSitePlus; Q4V8J4; -.
DR jPOST; Q4V8J4; -.
DR PaxDb; Q4V8J4; -.
DR PRIDE; Q4V8J4; -.
DR Ensembl; ENSRNOT00000002936; ENSRNOP00000002936; ENSRNOG00000002159.
DR GeneID; 305166; -.
DR KEGG; rno:305166; -.
DR CTD; 84803; -.
DR RGD; 1565703; Gpat3.
DR eggNOG; KOG2898; Eukaryota.
DR GeneTree; ENSGT01030000234574; -.
DR HOGENOM; CLU_031080_0_1_1; -.
DR InParanoid; Q4V8J4; -.
DR OMA; YMRILVK; -.
DR OrthoDB; 526132at2759; -.
DR PhylomeDB; Q4V8J4; -.
DR TreeFam; TF315039; -.
DR BRENDA; 2.3.1.15; 5301.
DR Reactome; R-RNO-1483166; Synthesis of PA.
DR UniPathway; UPA00282; -.
DR UniPathway; UPA00557; UER00612.
DR PRO; PR:Q4V8J4; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000002159; Expressed in duodenum and 19 other tissues.
DR Genevisible; Q4V8J4; RN.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; ISS:UniProtKB.
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:0006072; P:glycerol-3-phosphate metabolic process; ISO:RGD.
DR GO; GO:0008654; P:phospholipid biosynthetic process; ISO:RGD.
DR GO; GO:0032006; P:regulation of TOR signaling; ISO:RGD.
DR GO; GO:0019432; P:triglyceride biosynthetic process; ISS:UniProtKB.
DR CDD; cd07991; LPLAT_LPCAT1-like; 1.
DR InterPro; IPR045252; LPCAT1-like.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR Pfam; PF01553; Acyltransferase; 1.
DR SMART; SM00563; PlsC; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Endoplasmic reticulum; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Phospholipid biosynthesis;
KW Phospholipid metabolism; Phosphoprotein; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..457
FT /note="Glycerol-3-phosphate acyltransferase 3"
FT /id="PRO_0000291572"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 429..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 229..234
FT /note="HXXXXD motif"
FT /evidence="ECO:0000250|UniProtKB:Q9D517"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q53EU6"
SQ SEQUENCE 457 AA; 51012 MW; BC8A63BF240137A9 CRC64;
MEGTDLVVKL LSTWLTLVGS LILLPSAFGL SLGISEIYMK ILVKTLEWAT LRIEKGAPKE
SVLKSPASMG IIQRDESPME KGLSGLRGRD FELSDVFYFS KKGLEAIVED EVTQRFSSEE
LVSWNLLTRT NVNFHYISPK LTIVWVLGVL VRYCFLLPLR VTLAFIGISL LIIGTTLVGQ
LPDSSLKNWL SELVHLTCCR ICVRSLSGTI HYHNKQYRPQ KGGICVANHT SPIDVLILAT
DGCYAMVGQV HGGLMGIIQR AMVKACPHVW FERSEIKDRH LVTKRLKEHI ADKKKLPILI
FPEGTCINNT SVMMFKKGSF EIGGTIYPVA IKYNPQFGDA FWNSSKYNLV SYLLRIMTSW
AIVCDVWYMP PMTREEGEDA VQFANRVKSA IAVQGGLTEL PWDGGLKRAK VKDTFKEEQQ
KTYSKMIVGN GSPSLALDSS TVDNHGSPEP AFRSESL
