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Glycerol-3-phosphate O-acyltransferase 1 (G-3-P acyltransferase 1) (EC 2.3.1.15) (Dihydroxyacetone phosphate acyltransferase 1) (DHAP-AT 1) (EC 2.3.1.42) (Glycerol-3-phosphate / dihydroxyacetone phosphate acyltransferase 1) (Suppressor of choline-transport mutants 1)

 GPT1_YEAST              Reviewed;         759 AA.
P32784; D6VPY8; Q07062; Q96TV1;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
31-AUG-2004, sequence version 3.
23-MAY-2018, entry version 152.
RecName: Full=Glycerol-3-phosphate O-acyltransferase 1;
Short=G-3-P acyltransferase 1;
EC=2.3.1.15;
AltName: Full=Dihydroxyacetone phosphate acyltransferase 1;
Short=DHAP-AT 1;
EC=2.3.1.42;
AltName: Full=Glycerol-3-phosphate / dihydroxyacetone phosphate acyltransferase 1;
AltName: Full=Suppressor of choline-transport mutants 1;
Name=SCT1; Synonyms=GAT2, GPT1; OrderedLocusNames=YBL011W;
ORFNames=YBL0309, YBL0315;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7608137; DOI=10.1093/jb/117.2.447;
Matsushita M., Nikawa J.;
"Isolation and characterization of a SCT1 gene which can suppress a
choline-transport mutant of Saccharomyces cerevisiae.";
J. Biochem. 117:447-451(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
STRAIN=ATCC 204660 / DBY746;
PubMed=11544256; DOI=10.1074/jbc.M104749200;
Zheng Z., Zou J.;
"The initial step of the glycerolipid pathway: identification of
glycerol-3-phosphate / dihydroxyacetone phosphate dual substrate
acyltransferases in Saccharomyces cerevisiae.";
J. Biol. Chem. 276:41710-41716(2001).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=1332308; DOI=10.1002/yea.320080911;
Skala J., van Dyck L., Purnelle B., Goffeau A.;
"The sequence of an 8 kb segment on the left arm of chromosome II from
Saccharomyces cerevisiae identifies five new open reading frames of
unknown functions, two tRNA genes and two transposable elements.";
Yeast 8:777-785(1992).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=7813418;
Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J.,
Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C.,
Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M.,
Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L.,
Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J.,
Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T.,
Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A.,
Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B.,
Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I.,
Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M.,
Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A.,
van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I.,
Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H.,
Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.;
"Complete DNA sequence of yeast chromosome II.";
EMBO J. 13:5795-5809(1994).
[5]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 609-759.
STRAIN=ATCC 204508 / S288c;
PubMed=1441753; DOI=10.1002/yea.320080909;
Delaveau T., Jacq C., Perea J.;
"Sequence of a 12.7 kb segment of yeast chromosome II identifies a
PDR-like gene and several new open reading frames.";
Yeast 8:761-768(1992).
[7]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[8]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
-!- FUNCTION: G-3-P/dihydroxyacetone phosphate dual substrate-specific
sn-1 acyltransferase. {ECO:0000269|PubMed:11544256}.
-!- CATALYTIC ACTIVITY: Acyl-CoA + sn-glycerol 3-phosphate = CoA + 1-
acyl-sn-glycerol 3-phosphate.
-!- CATALYTIC ACTIVITY: Acyl-CoA + glycerone phosphate = CoA +
acylglycerone phosphate.
-!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis;
CDP-diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:14562095}; Multi-pass membrane protein
{ECO:0000269|PubMed:14562095}.
-!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity
and may constitute the binding site for the phosphate moiety of
the glycerol-3-phosphate. {ECO:0000250}.
-!- MISCELLANEOUS: Present with 1050 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the GPAT/DAPAT family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; D38256; BAA07409.1; -; Genomic_DNA.
EMBL; AJ314608; CAC85390.1; -; Genomic_DNA.
EMBL; Z35773; CAA84831.1; -; Genomic_DNA.
EMBL; S47695; AAB23987.1; -; Genomic_DNA.
EMBL; BK006936; DAA07108.1; -; Genomic_DNA.
PIR; S25330; S25330.
RefSeq; NP_009542.1; NM_001178251.1.
ProteinModelPortal; P32784; -.
BioGrid; 32688; 194.
IntAct; P32784; 2.
MINT; P32784; -.
STRING; 4932.YBL011W; -.
SwissLipids; SLP:000000048; -.
iPTMnet; P32784; -.
MaxQB; P32784; -.
PaxDb; P32784; -.
PRIDE; P32784; -.
EnsemblFungi; YBL011W; YBL011W; YBL011W.
GeneID; 852271; -.
KEGG; sce:YBL011W; -.
EuPathDB; FungiDB:YBL011W; -.
SGD; S000000107; SCT1.
GeneTree; ENSGT00530000067105; -.
HOGENOM; HOG000191288; -.
InParanoid; P32784; -.
KO; K13507; -.
OMA; CFFREIR; -.
OrthoDB; EOG092C0TE2; -.
BioCyc; MetaCyc:MONOMER3O-4105; -.
BioCyc; YEAST:MONOMER3O-4105; -.
BRENDA; 2.3.1.15; 984.
SABIO-RK; P32784; -.
UniPathway; UPA00557; UER00612.
PRO; PR:P32784; -.
Proteomes; UP000002311; Chromosome II.
GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
GO; GO:0004366; F:glycerol-3-phosphate O-acyltransferase activity; IDA:SGD.
GO; GO:0016287; F:glycerone-phosphate O-acyltransferase activity; IDA:SGD.
GO; GO:0102420; F:sn-1-glycerol-3-phosphate C16:0-DCA-CoA acyl transferase activity; IEA:UniProtKB-EC.
GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0008654; P:phospholipid biosynthetic process; IMP:SGD.
InterPro; IPR002123; Plipid/glycerol_acylTrfase.
Pfam; PF01553; Acyltransferase; 1.
SMART; SM00563; PlsC; 1.
1: Evidence at protein level;
Acyltransferase; Complete proteome; Endoplasmic reticulum;
Lipid biosynthesis; Lipid metabolism; Membrane;
Phospholipid biosynthesis; Phospholipid metabolism;
Reference proteome; Transferase; Transmembrane; Transmembrane helix.
CHAIN 1 759 Glycerol-3-phosphate O-acyltransferase 1.
/FTId=PRO_0000195257.
TRANSMEM 49 66 Helical. {ECO:0000255}.
TRANSMEM 123 139 Helical. {ECO:0000255}.
TRANSMEM 260 276 Helical. {ECO:0000255}.
TRANSMEM 440 463 Helical. {ECO:0000255}.
TRANSMEM 494 516 Helical. {ECO:0000255}.
TRANSMEM 524 545 Helical. {ECO:0000255}.
MOTIF 414 419 HXXXXD motif.
COMPBIAS 736 753 Poly-Glu.
CONFLICT 10 10 F -> S (in Ref. 1; BAA07409 and 2;
CAC85390). {ECO:0000305}.
CONFLICT 30 38 Missing (in Ref. 2; CAC85390).
{ECO:0000305}.
CONFLICT 88 88 A -> R (in Ref. 1; BAA07409).
{ECO:0000305}.
CONFLICT 125 125 P -> A (in Ref. 1; BAA07409).
{ECO:0000305}.
CONFLICT 278 278 K -> R (in Ref. 2; CAC85390).
{ECO:0000305}.
CONFLICT 324 324 P -> S (in Ref. 2; CAC85390).
{ECO:0000305}.
CONFLICT 574 574 D -> N (in Ref. 2; CAC85390).
{ECO:0000305}.
CONFLICT 730 730 G -> S (in Ref. 1; BAA07409).
{ECO:0000305}.
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


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