DGAT2_SCHPO
ID DGAT2_SCHPO Reviewed; 345 AA.
AC O74850; Q9P3V1;
DT 13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 3.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Diacylglycerol O-acyltransferase 1;
DE EC=2.3.1.20;
DE AltName: Full=Diglyceride acyltransferase;
DE AltName: Full=Triacylglycerol synthase;
DE Short=TAG synthase;
GN Name=dga1; ORFNames=SPCC1235.15, SPCC548.01;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=12963726; DOI=10.1074/jbc.m306998200;
RA Zhang Q., Chieu H.K., Low C.P., Zhang S., Heng C.K., Yang H.;
RT "Schizosaccharomyces pombe cells deficient in triacylglycerols synthesis
RT undergo apoptosis upon entry into the stationary phase.";
RL J. Biol. Chem. 278:47145-47155(2003).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26990381; DOI=10.1111/tra.12394;
RA Meyers A., Del Rio Z.P., Beaver R.A., Morris R.M., Weiskittel T.M.,
RA Alshibli A.K., Mannik J., Morrell-Falvey J., Dalhaimer P.;
RT "Lipid droplets form from distinct regions of the cell in the fission yeast
RT Schizosaccharomyces pombe.";
RL Traffic 17:657-669(2016).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28011631; DOI=10.1242/bio.022384;
RA Yang H.J., Osakada H., Kojidani T., Haraguchi T., Hiraoka Y.;
RT "Lipid droplet dynamics during Schizosaccharomyces pombe sporulation and
RT their role in spore survival.";
RL Biol. Open 6:217-222(2017).
CC -!- FUNCTION: Catalyzes the terminal and only committed step in
CC triacylglycerol (TAG) synthesis by using diacylglycerol (DAG) and fatty
CC acyl-CoA as substrates. Required for storage lipid synthesis
CC (PubMed:12963726, PubMed:26990381). Major DAG esterifying enzyme in
CC stationary phase when TAG production is particularly active
CC (PubMed:12963726). Involved in lipid particle synthesis from the
CC endoplasmic reticulum, promoting localized TAG production at discrete
CC ER subdomains (PubMed:26990381, PubMed:28011631).
CC {ECO:0000269|PubMed:12963726, ECO:0000269|PubMed:26990381,
CC ECO:0000269|PubMed:28011631}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol
CC + CoA; Xref=Rhea:RHEA:10868, ChEBI:CHEBI:17815, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:58342, ChEBI:CHEBI:64615; EC=2.3.1.20;
CC Evidence={ECO:0000269|PubMed:12963726};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2-acylglycerol + an acyl-CoA = a 1,2-diacyl-sn-glycerol +
CC CoA; Xref=Rhea:RHEA:32947, ChEBI:CHEBI:17389, ChEBI:CHEBI:17815,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:58342;
CC Evidence={ECO:0000269|PubMed:12963726};
CC -!- PATHWAY: Glycerolipid metabolism; triacylglycerol biosynthesis.
CC {ECO:0000305|PubMed:12963726}.
CC -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000250|UniProtKB:Q08650}.
CC Endoplasmic reticulum membrane {ECO:0000269|PubMed:12963726,
CC ECO:0000269|PubMed:16823372}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Localizes to sites of lipid droplet biogenesis in
CC the endoplasmic reticulum. {ECO:0000250|UniProtKB:Q08650}.
CC -!- DISRUPTION PHENOTYPE: Has reduced whole-cell and lipid droplet (LD) TAG
CC levels. Cells lacking both TAG synthase genes (plh1 and dga1) have no
CC LDs and exhibit defects in spore germination and in spore wall
CC integrity. {ECO:0000269|PubMed:26990381, ECO:0000269|PubMed:28011631}.
CC -!- SIMILARITY: Belongs to the diacylglycerol acyltransferase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329672; CAE54965.2; -; Genomic_DNA.
DR RefSeq; XP_001713160.1; XM_001713108.2.
DR AlphaFoldDB; O74850; -.
DR BioGRID; 857840; 17.
DR STRING; 4896.SPCC1235.15.1; -.
DR MaxQB; O74850; -.
DR PaxDb; O74850; -.
DR PRIDE; O74850; -.
DR EnsemblFungi; SPCC1235.15.1; SPCC1235.15.1:pep; SPCC1235.15.
DR PomBase; SPCC1235.15; dga1.
DR VEuPathDB; FungiDB:SPCC1235.15; -.
DR eggNOG; KOG0831; Eukaryota.
DR HOGENOM; CLU_023995_4_0_1; -.
DR InParanoid; O74850; -.
DR OMA; PFYRDYI; -.
DR PhylomeDB; O74850; -.
DR Reactome; R-SPO-1482883; Acyl chain remodeling of DAG and TAG.
DR Reactome; R-SPO-2142753; Arachidonic acid metabolism.
DR Reactome; R-SPO-75109; Triglyceride biosynthesis.
DR Reactome; R-SPO-9640463; Wax biosynthesis.
DR UniPathway; UPA00282; -.
DR PRO; PR:O74850; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0032541; C:cortical endoplasmic reticulum; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005811; C:lipid droplet; IDA:PomBase.
DR GO; GO:0097038; C:perinuclear endoplasmic reticulum; IDA:PomBase.
DR GO; GO:0003846; F:2-acylglycerol O-acyltransferase activity; IEA:RHEA.
DR GO; GO:0004144; F:diacylglycerol O-acyltransferase activity; IMP:PomBase.
DR GO; GO:0046339; P:diacylglycerol metabolic process; IC:PomBase.
DR GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0140042; P:lipid droplet formation; IMP:PomBase.
DR GO; GO:0006629; P:lipid metabolic process; IBA:GO_Central.
DR GO; GO:0019915; P:lipid storage; EXP:PomBase.
DR GO; GO:0019432; P:triglyceride biosynthetic process; IMP:PomBase.
DR InterPro; IPR007130; DAGAT.
DR Pfam; PF03982; DAGAT; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Endoplasmic reticulum; Glycerol metabolism;
KW Lipid biosynthesis; Lipid droplet; Lipid metabolism; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..345
FT /note="Diacylglycerol O-acyltransferase 1"
FT /id="PRO_0000176219"
FT TOPO_DOM 1..49
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 71..113
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 135..141
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 163..216
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 238..345
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 345 AA; 39486 MW; 4360E92C3BA497AA CRC64;
MSEETSIPGI IASTPPISKD SRRNVSHWLQ ALAVFLHSVS LTLTASWYTV LWAFLPFWPF
LIVYLIWLIY DDGFVTGKDR QKRWLRNAPP YRWFCHYFPI RLHKTTELDS EKNYIFGYHP
HGIISLGAFG GFASEGADFS KLFPGINVSV LTLNSNFYVP VYRDYLMALN INSVSKKSCV
SILSRKPGDS VLIVIGGAQE SLLSRPGQNN LVLKKRFGFV KLAFLTGSSL VPCFAFGESD
IFEQVDNNPR TRIYKFQEIV KKIAGFTVPF FYGRGLLNKT FGLMPWRKPI NIVVGEPIDV
PKKSHPTNQE IYEVHEEYIR RLEGLWNKYK DVFLPNRISE LKLSA
