GPT1_YEAST
ID GPT1_YEAST Reviewed; 759 AA.
AC P32784; D6VPY8; Q07062; Q96TV1;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 3.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Glycerol-3-phosphate O-acyltransferase 1;
DE Short=G-3-P acyltransferase 1;
DE Short=GPAT 1;
DE EC=2.3.1.15 {ECO:0000269|PubMed:11544256};
DE AltName: Full=Dihydroxyacetone phosphate acyltransferase 1;
DE Short=DHAP-AT 1;
DE EC=2.3.1.42 {ECO:0000269|PubMed:11544256};
DE AltName: Full=Glycerol-3-phosphate / dihydroxyacetone phosphate acyltransferase 1;
DE AltName: Full=Suppressor of choline-transport mutants 1 {ECO:0000303|PubMed:7608137};
GN Name=SCT1 {ECO:0000303|PubMed:7608137};
GN Synonyms=GAT2 {ECO:0000303|PubMed:11544256}; OrderedLocusNames=YBL011W;
GN ORFNames=YBL0309, YBL0315;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7608137; DOI=10.1093/jb/117.2.447;
RA Matsushita M., Nikawa J.;
RT "Isolation and characterization of a SCT1 gene which can suppress a
RT choline-transport mutant of Saccharomyces cerevisiae.";
RL J. Biochem. 117:447-451(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 204660 / DBY746;
RX PubMed=11544256; DOI=10.1074/jbc.m104749200;
RA Zheng Z., Zou J.;
RT "The initial step of the glycerolipid pathway: identification of glycerol-
RT 3-phosphate / dihydroxyacetone phosphate dual substrate acyltransferases in
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 276:41710-41716(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1332308; DOI=10.1002/yea.320080911;
RA Skala J., van Dyck L., Purnelle B., Goffeau A.;
RT "The sequence of an 8 kb segment on the left arm of chromosome II from
RT Saccharomyces cerevisiae identifies five new open reading frames of unknown
RT functions, two tRNA genes and two transposable elements.";
RL Yeast 8:777-785(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 609-759.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1441753; DOI=10.1002/yea.320080909;
RA Delaveau T., Jacq C., Perea J.;
RT "Sequence of a 12.7 kb segment of yeast chromosome II identifies a PDR-like
RT gene and several new open reading frames.";
RL Yeast 8:761-768(1992).
RN [7]
RP FUNCTION.
RX PubMed=12167660; DOI=10.1074/jbc.m207753200;
RA Zaremberg V., McMaster C.R.;
RT "Differential partitioning of lipids metabolized by separate yeast
RT glycerol-3-phosphate acyltransferases reveals that phospholipase D
RT generation of phosphatidic acid mediates sensitivity to choline-containing
RT lysolipids and drugs.";
RL J. Biol. Chem. 277:39035-39044(2002).
RN [8]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [9]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=19525420; DOI=10.1128/ec.00085-09;
RA Bratschi M.W., Burrowes D.P., Kulaga A., Cheung J.F., Alvarez A.L.,
RA Kearley J., Zaremberg V.;
RT "Glycerol-3-phosphate acyltransferases gat1p and gat2p are microsomal
RT phosphoproteins with differential contributions to polarized cell growth.";
RL Eukaryot. Cell 8:1184-1196(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [13]
RP FUNCTION.
RX PubMed=22323296; DOI=10.1091/mbc.e11-07-0624;
RA De Smet C.H., Vittone E., Scherer M., Houweling M., Liebisch G.,
RA Brouwers J.F., de Kroon A.I.;
RT "The yeast acyltransferase Sct1p regulates fatty acid desaturation by
RT competing with the desaturase Ole1p.";
RL Mol. Biol. Cell 23:1146-1156(2012).
RN [14]
RP TOPOLOGY.
RX PubMed=29073188; DOI=10.1371/journal.pone.0186840;
RA Debelyy M.O., Waridel P., Quadroni M., Schneiter R., Conzelmann A.;
RT "Chemical crosslinking and mass spectrometry to elucidate the topology of
RT integral membrane proteins.";
RL PLoS ONE 12:e0186840-e0186840(2017).
CC -!- FUNCTION: Dual substrate-specific glycerol-3-phosphate/dihydroxyacetone
CC phosphate sn-1 acyltransferase, catalyzing the first and committed
CC reaction in the de novo synthesis of glycerophospholipids and
CC triacylglycerols (TAGs). Prefers Gly-3-P over dihydroxyacetone
CC phosphate and has a marked preference for 16-carbon fatty acyl chains.
CC Transfers a fatty acid from fatty acyl-CoA to the sn-1 position of
CC glycerol-3-phosphate to produce lysophosphatidic acid (LysoPA). These
CC lipids not only are precursors of glycerolipids, but also are dynamic
CC components of signal transduction systems that control cell physiology
CC (PubMed:11544256). SCT1 is the primary supplier of diacylglycerols
CC (DAG), used mainly in TAG synthesis and phosphatidylcholine (PC)
CC synthesis through the CDP-choline pathway (PubMed:12167660). Regulates
CC fatty acid desaturation, that is, the ratio of unsaturated versus
CC saturated fatty acyl chains, by competing with the desaturase OLE1 for
CC the common substrate C16:0-CoA. Sequesters C16:0-CoA into lipids,
CC thereby shielding it from desaturation by OLE1 (PubMed:22323296).
CC {ECO:0000269|PubMed:11544256, ECO:0000269|PubMed:12167660,
CC ECO:0000269|PubMed:22323296}.
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:11544256};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acyl-CoA + dihydroxyacetone phosphate = a 1-acylglycerone
CC 3-phosphate + CoA; Xref=Rhea:RHEA:17657, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57534, ChEBI:CHEBI:57642, ChEBI:CHEBI:58342; EC=2.3.1.42;
CC Evidence={ECO:0000269|PubMed:11544256};
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:11544256};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35724;
CC Evidence={ECO:0000305|PubMed:11544256};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-hexadecenoyl-CoA + sn-glycerol 3-phosphate = 1-(9Z-
CC hexadecenoyl)-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:44188,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57597, ChEBI:CHEBI:61540,
CC ChEBI:CHEBI:74694; Evidence={ECO:0000269|PubMed:11544256};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44189;
CC Evidence={ECO:0000305|PubMed:11544256};
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:0000269|PubMed:11544256};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37196;
CC Evidence={ECO:0000305|PubMed:11544256};
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:0000269|PubMed:11544256};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37200;
CC Evidence={ECO:0000305|PubMed:11544256};
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 1/3. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:19525420}; Multi-pass
CC membrane protein {ECO:0000255}. Note=Localizes to both perinuclear and
CC cortical endoplasmic reticulum. {ECO:0000269|PubMed:19525420}.
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 -!- MISCELLANEOUS: Present with 1050 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the GPAT/DAPAT family. {ECO:0000305}.
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DR EMBL; D38256; BAA07409.1; -; Genomic_DNA.
DR EMBL; AJ314608; CAC85390.1; -; Genomic_DNA.
DR EMBL; Z35773; CAA84831.1; -; Genomic_DNA.
DR EMBL; S47695; AAB23987.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07108.1; -; Genomic_DNA.
DR PIR; S25330; S25330.
DR RefSeq; NP_009542.1; NM_001178251.1.
DR AlphaFoldDB; P32784; -.
DR BioGRID; 32688; 199.
DR IntAct; P32784; 2.
DR MINT; P32784; -.
DR STRING; 4932.YBL011W; -.
DR SwissLipids; SLP:000000048; -.
DR iPTMnet; P32784; -.
DR MaxQB; P32784; -.
DR PaxDb; P32784; -.
DR PRIDE; P32784; -.
DR EnsemblFungi; YBL011W_mRNA; YBL011W; YBL011W.
DR GeneID; 852271; -.
DR KEGG; sce:YBL011W; -.
DR SGD; S000000107; SCT1.
DR VEuPathDB; FungiDB:YBL011W; -.
DR eggNOG; ENOG502QQ2N; Eukaryota.
DR GeneTree; ENSGT00940000176524; -.
DR HOGENOM; CLU_007860_1_0_1; -.
DR InParanoid; P32784; -.
DR OMA; IMALGCM; -.
DR BioCyc; MetaCyc:MON3O-4105; -.
DR BioCyc; YEAST:MON3O-4105; -.
DR BRENDA; 2.3.1.15; 984.
DR SABIO-RK; P32784; -.
DR UniPathway; UPA00557; UER00612.
DR PRO; PR:P32784; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P32784; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004366; F:glycerol-3-phosphate O-acyltransferase activity; IDA:SGD.
DR GO; GO:0016287; F:glycerone-phosphate O-acyltransferase activity; IDA:SGD.
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:0008654; P:phospholipid biosynthetic process; IMP:SGD.
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; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..759
FT /note="Glycerol-3-phosphate O-acyltransferase 1"
FT /id="PRO_0000195257"
FT TOPO_DOM 1..48
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:29073188"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:29073188"
FT TOPO_DOM 70..434
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:29073188"
FT TRANSMEM 435..449
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:29073188"
FT TOPO_DOM 450
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:29073188"
FT TRANSMEM 451..465
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:29073188"
FT TOPO_DOM 466..493
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:29073188"
FT TRANSMEM 494..514
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:29073188"
FT TOPO_DOM 515..523
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:29073188"
FT TRANSMEM 524..544
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:29073188"
FT TOPO_DOM 545..759
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:29073188"
FT REGION 613..667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 684..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 729..759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 414..419
FT /note="HXXXXD motif"
FT COMPBIAS 632..658
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..704
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 735..759
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 10
FT /note="F -> S (in Ref. 1; BAA07409 and 2; CAC85390)"
FT /evidence="ECO:0000305"
FT CONFLICT 30..38
FT /note="Missing (in Ref. 2; CAC85390)"
FT /evidence="ECO:0000305"
FT CONFLICT 88
FT /note="A -> R (in Ref. 1; BAA07409)"
FT /evidence="ECO:0000305"
FT CONFLICT 125
FT /note="P -> A (in Ref. 1; BAA07409)"
FT /evidence="ECO:0000305"
FT CONFLICT 278
FT /note="K -> R (in Ref. 2; CAC85390)"
FT /evidence="ECO:0000305"
FT CONFLICT 324
FT /note="P -> S (in Ref. 2; CAC85390)"
FT /evidence="ECO:0000305"
FT CONFLICT 574
FT /note="D -> N (in Ref. 2; CAC85390)"
FT /evidence="ECO:0000305"
FT CONFLICT 730
FT /note="G -> S (in Ref. 1; BAA07409)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 759 AA; 85694 MW; CCB0D11E8ED7D728 CRC64;
MPAPKLTEKF ASSKSTQKTT NYSSIEAKSV KTSADQAYIY QEPSATKKIL YSIATWLLYN
IFHCFFREIR GRGSFKVPQQ GPVIFVAAPH ANQFVDPVIL MGEVKKSVNR RVSFLIAESS
LKQPPIGFLA SFFMAIGVVR PQDNLKPAEG TIRVDPTDYK RVIGHDTHFL TDCMPKGLIG
LPKSMGFGEI QSIESDTSLT LRKEFKMAKP EIKTALLTGT TYKYAAKVDQ SCVYHRVFEH
LAHNNCIGIF PEGGSHDRTN LLPLKAGVAI MALGCMDKHP DVNVKIVPCG MNYFHPHKFR
SRAVVEFGDP IEIPKELVAK YHNPETNRDA VKELLDTISK GLQSVTVTCS DYETLMVVQT
IRRLYMTQFS TKLPLPLIVE MNRRMVKGYE FYRNDPKIAD LTKDIMAYNA ALRHYNLPDH
LVEEAKVNFA KNLGLVFFRS IGLCILFSLA MPGIIMFSPV FILAKRISQE KARTALSKST
VKIKANDVIA TWKILIGMGF APLLYIFWSV LITYYLRHKP WNKIYVFSGS YISCVIVTYS
ALIVGDIGMD GFKSLRPLVL SLTSPKGLQK LQKDRRNLAE RIIEVVNNFG SELFPDFDSA
ALREEFDVID EEEEDRKTSE LNRRKMLRKQ KIKRQEKDSS SPIISQRDNH DAYEHHNQDS
DGVSLVNSDN SLSNIPLFSS TFHRKSESSL ASTSVAPSSS SEFEVENEIL EEKNGLASKI
AQAVLNKRIG ENTAREEEEE EEEEEEEEEE EEEGKEGDA
