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Glycerol-3-phosphate O-acyltransferase 2 (G-3-P acyltransferase 2) (EC 2.3.1.15) (Dihydroxyacetone phosphate acyltransferase 2) (DHAP-AT 2) (EC 2.3.1.42) (Glycerol-3-phosphate / dihydroxyacetone phosphate acyltransferase 2)

 GPT2_YEAST              Reviewed;         743 AA.
P36148; D6VXC8;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
01-JUN-1994, sequence version 1.
28-MAR-2018, entry version 152.
RecName: Full=Glycerol-3-phosphate O-acyltransferase 2;
Short=G-3-P acyltransferase 2;
EC=2.3.1.15;
AltName: Full=Dihydroxyacetone phosphate acyltransferase 2;
Short=DHAP-AT 2;
EC=2.3.1.42;
AltName: Full=Glycerol-3-phosphate / dihydroxyacetone phosphate acyltransferase 2;
Name=GPT2; Synonyms=GAT1; OrderedLocusNames=YKR067W;
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], 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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=8196765; DOI=10.1038/369371a0;
Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M.,
Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C.,
Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G.,
Zimmermann J., Haasemann M., Becker I., Mewes H.-W.;
"Complete DNA sequence of yeast chromosome XI.";
Nature 369:371-378(1994).
[3]
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).
[4]
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).
[5]
TOPOLOGY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 208353 / W303-1A;
PubMed=16847258; DOI=10.1073/pnas.0604075103;
Kim H., Melen K., Oesterberg M., von Heijne G.;
"A global topology map of the Saccharomyces cerevisiae membrane
proteome.";
Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-654; SER-668 AND
SER-671, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[7]
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).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-632; SER-637; SER-647;
SER-651; SER-654; SER-657; SER-664; SER-668; SER-671; THR-673;
SER-688; THR-692 AND SER-693, AND 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.
-!- INTERACTION:
P11484:SSB1; NbExp=3; IntAct=EBI-26471, EBI-8627;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
protein {ECO:0000305}.
-!- MISCELLANEOUS: Present with 3100 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; AJ311354; CAC85303.1; -; Genomic_DNA.
EMBL; Z28292; CAA82146.1; -; Genomic_DNA.
EMBL; BK006944; DAA09218.1; -; Genomic_DNA.
PIR; S38143; S38143.
RefSeq; NP_012993.3; NM_001179857.3.
ProteinModelPortal; P36148; -.
BioGrid; 34198; 158.
DIP; DIP-6620N; -.
IntAct; P36148; 44.
MINT; P36148; -.
STRING; 4932.YKR067W; -.
SwissLipids; SLP:000000047; -.
iPTMnet; P36148; -.
MaxQB; P36148; -.
PaxDb; P36148; -.
PRIDE; P36148; -.
EnsemblFungi; YKR067W; YKR067W; YKR067W.
GeneID; 853941; -.
KEGG; sce:YKR067W; -.
EuPathDB; FungiDB:YKR067W; -.
SGD; S000001775; GPT2.
GeneTree; ENSGT00530000067105; -.
HOGENOM; HOG000191288; -.
InParanoid; P36148; -.
KO; K13507; -.
OMA; GLHYFHR; -.
OrthoDB; EOG092C0TE2; -.
BioCyc; MetaCyc:MONOMER3O-4095; -.
BioCyc; YEAST:MONOMER3O-4095; -.
BRENDA; 2.3.1.15; 984.
SABIO-RK; P36148; -.
UniPathway; UPA00557; UER00612.
PRO; PR:P36148; -.
Proteomes; UP000002311; Chromosome XI.
GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
GO; GO:0005811; C:lipid droplet; IDA:SGD.
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; IDA:SGD.
InterPro; IPR002123; Plipid/glycerol_acylTrfase.
Pfam; PF01553; Acyltransferase; 1.
SMART; SM00563; PlsC; 1.
1: Evidence at protein level;
Acyltransferase; Complete proteome; Lipid biosynthesis;
Lipid metabolism; Membrane; Phospholipid biosynthesis;
Phospholipid metabolism; Phosphoprotein; Reference proteome;
Transferase; Transmembrane; Transmembrane helix.
CHAIN 1 743 Glycerol-3-phosphate O-acyltransferase 2.
/FTId=PRO_0000195258.
TOPO_DOM 1 30 Cytoplasmic. {ECO:0000255}.
TRANSMEM 31 55 Helical. {ECO:0000255}.
TOPO_DOM 56 68 Extracellular. {ECO:0000255}.
TRANSMEM 69 85 Helical. {ECO:0000255}.
TOPO_DOM 86 501 Cytoplasmic. {ECO:0000255}.
TRANSMEM 502 524 Helical. {ECO:0000255}.
TOPO_DOM 525 538 Extracellular. {ECO:0000255}.
TRANSMEM 539 555 Helical. {ECO:0000255}.
TOPO_DOM 556 743 Cytoplasmic. {ECO:0000255}.
MOD_RES 632 632 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 637 637 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 647 647 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 651 651 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 654 654 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:19779198}.
MOD_RES 657 657 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 664 664 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 668 668 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:19779198}.
MOD_RES 671 671 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:19779198}.
MOD_RES 673 673 Phosphothreonine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 688 688 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 692 692 Phosphothreonine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 693 693 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
SEQUENCE 743 AA; 83645 MW; 84B9946E56B82F15 CRC64;
MSAPAADHNA AKPIPHVPQA SRRYKNSYNG FVYNIHTWLY DVSVFLFNIL FTIFFREIKV
RGAYNVPEVG VPTILVCAPH ANQFIDPALV MSQTRLLKTS AGKSRSRMPC FVTAESSFKK
RFISFFGHAM GGIPVPRIQD NLKPVDENLE IYAPDLKNHP EIIKGRSKNP QTTPVNFTKR
FSAKSLLGLP DYLSNAQIKE IPDDETIILS SPFRTSKSKV VELLTNGTNF KYAEKIDNTE
TFQSVFDHLH TKGCVGIFPE GGSHDRPSLL PIKAGVAIMA LGAVAADPTM KVAVVPCGLH
YFHRNKFRSR AVLEYGEPIV VDGKYGEMYK DSPRETVSKL LKKITNSLFS VTENAPDYDT
LMVIQAARRL YQPVKVRLPL PAIVEINRRL LFGYSKFKDD PRIIHLKKLV YDYNRKLDSV
GLKDHQVMQL KTTKLEALRC FVTLIVRLIK FSVFAILSLP GSILFTPIFI ICRVYSEKKA
KEGLKKSLVK IKGTDLLATW KLIVALILAP ILYVTYSILL IILARKQHYC RIWVPSNNAF
IQFVYFYALL VFTTYSSLKT GEIGVDLFKS LRPLFVSIVY PGKKIEEIQT TRKNLSLELT
AVCNDLGPLV FPDYDKLATE IFSKRDGYDV SSDAESSISR MSVQSRSRSS SIHSIGSLAS
NALSRVNSRG SLTDIPIFSD AKQGQWKSEG ETSEDEDEFD EKNPAIVQTA RSSDLNKENS
RNTNISSKIA SLVRQKREHE KKE


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