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Protein

Diacylglycerol O-acyltransferase 1

Gene

dga1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates. Cells defective in triacylglycerol synthesis undergo apoptosis upon entry into the stationary phase. Generation of reactive oxygen species (ROS) is essential to lipoapoptosis. Also has monoacylglycerol acyltransferase (MGAT) activity, catalyzing the acyl-CoA-dependent esterification of monoacylglycerol to diacylglycerol (By similarity).By similarity1 Publication

Catalytic activityi

Acyl-CoA + 1,2-diacylglycerol = CoA + triacylglycerol.1 Publication
Acyl-CoA + 2-acylglycerol = CoA + diacylglycerol.1 Publication

Pathwayi: triacylglycerol biosynthesis

This protein is involved in the pathway triacylglycerol biosynthesis, which is part of Glycerolipid metabolism.
View all proteins of this organism that are known to be involved in the pathway triacylglycerol biosynthesis and in Glycerolipid metabolism.

GO - Molecular functioni

  • diacylglycerol O-acyltransferase activity Source: PomBase

GO - Biological processi

  • diacylglycerol metabolic process Source: PomBase
  • glycerol metabolic process Source: UniProtKB-KW
  • lipid storage Source: PomBase
  • triglyceride biosynthetic process Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Glycerol metabolism, Lipid biosynthesis, Lipid metabolism

Enzyme and pathway databases

ReactomeiR-SPO-1482883. Acyl chain remodeling of DAG and TAG.
R-SPO-2142753. Arachidonic acid metabolism.
R-SPO-535734. Fatty acid, triacylglycerol, and ketone body metabolism.
R-SPO-75109. Triglyceride Biosynthesis.
R-SPO-8848584. Wax biosynthesis.
UniPathwayiUPA00282.

Names & Taxonomyi

Protein namesi
Recommended name:
Diacylglycerol O-acyltransferase 1 (EC:2.3.1.20)
Alternative name(s):
Diglyceride acyltransferase
Gene namesi
Name:dga1
ORF Names:SPCC1235.15, SPCC548.01
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome III

Organism-specific databases

EuPathDBiFungiDB:SPCC1235.15.
PomBaseiSPCC1235.15. dga1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 4949CytoplasmicBy similarityAdd
BLAST
Transmembranei50 – 7021HelicalSequence analysisAdd
BLAST
Topological domaini71 – 11343LumenalBy similarityAdd
BLAST
Transmembranei114 – 13421HelicalSequence analysisAdd
BLAST
Topological domaini135 – 1417CytoplasmicBy similarity
Transmembranei142 – 16221HelicalSequence analysisAdd
BLAST
Topological domaini163 – 21654LumenalBy similarityAdd
BLAST
Transmembranei217 – 23721HelicalSequence analysisAdd
BLAST
Topological domaini238 – 345108CytoplasmicBy similarityAdd
BLAST

GO - Cellular componenti

  • cytoplasm Source: PomBase
  • endoplasmic reticulum Source: PomBase
  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB-KW
  • lipid particle Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Lipid droplet, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 345345Diacylglycerol O-acyltransferase 1PRO_0000176219Add
BLAST

Proteomic databases

MaxQBiO74850.

Interactioni

Protein-protein interaction databases

BioGridi857840. 12 interactions.
MINTiMINT-4681252.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

HOGENOMiHOG000179738.
InParanoidiO74850.
KOiK14457.
OMAiHEMVEEY.
OrthoDBiEOG7K3TW0.
PhylomeDBiO74850.

Family and domain databases

InterProiIPR007130. DAGAT.
[Graphical view]
PfamiPF03982. DAGAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O74850-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEETSIPGI IASTPPISKD SRRNVSHWLQ ALAVFLHSVS LTLTASWYTV
60 70 80 90 100
LWAFLPFWPF LIVYLIWLIY DDGFVTGKDR QKRWLRNAPP YRWFCHYFPI
110 120 130 140 150
RLHKTTELDS EKNYIFGYHP HGIISLGAFG GFASEGADFS KLFPGINVSV
160 170 180 190 200
LTLNSNFYVP VYRDYLMALN INSVSKKSCV SILSRKPGDS VLIVIGGAQE
210 220 230 240 250
SLLSRPGQNN LVLKKRFGFV KLAFLTGSSL VPCFAFGESD IFEQVDNNPR
260 270 280 290 300
TRIYKFQEIV KKIAGFTVPF FYGRGLLNKT FGLMPWRKPI NIVVGEPIDV
310 320 330 340
PKKSHPTNQE IYEVHEEYIR RLEGLWNKYK DVFLPNRISE LKLSA
Length:345
Mass (Da):39,486
Last modified:May 10, 2004 - v3
Checksum:i4360E92C3BA497AA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329672 Genomic DNA. Translation: CAE54965.2.
RefSeqiXP_001713160.1. XM_001713108.2.

Genome annotation databases

EnsemblFungiiSPCC1235.15.1; SPCC1235.15.1:pep; SPCC1235.15.
GeneIDi5802702.
KEGGispo:SPCC1235.15.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329672 Genomic DNA. Translation: CAE54965.2.
RefSeqiXP_001713160.1. XM_001713108.2.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi857840. 12 interactions.
MINTiMINT-4681252.

Proteomic databases

MaxQBiO74850.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPCC1235.15.1; SPCC1235.15.1:pep; SPCC1235.15.
GeneIDi5802702.
KEGGispo:SPCC1235.15.

Organism-specific databases

EuPathDBiFungiDB:SPCC1235.15.
PomBaseiSPCC1235.15. dga1.

Phylogenomic databases

HOGENOMiHOG000179738.
InParanoidiO74850.
KOiK14457.
OMAiHEMVEEY.
OrthoDBiEOG7K3TW0.
PhylomeDBiO74850.

Enzyme and pathway databases

UniPathwayiUPA00282.
ReactomeiR-SPO-1482883. Acyl chain remodeling of DAG and TAG.
R-SPO-2142753. Arachidonic acid metabolism.
R-SPO-535734. Fatty acid, triacylglycerol, and ketone body metabolism.
R-SPO-75109. Triglyceride Biosynthesis.
R-SPO-8848584. Wax biosynthesis.

Miscellaneous databases

PROiO74850.

Family and domain databases

InterProiIPR007130. DAGAT.
[Graphical view]
PfamiPF03982. DAGAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. "Schizosaccharomyces pombe cells deficient in triacylglycerols synthesis undergo apoptosis upon entry into the stationary phase."
    Zhang Q., Chieu H.K., Low C.P., Zhang S., Heng C.K., Yang H.
    J. Biol. Chem. 278:47145-47155(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
  3. "ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
    Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
    Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiDGAT2_SCHPO
AccessioniPrimary (citable) accession number: O74850
Secondary accession number(s): Q9P3V1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 13, 2002
Last sequence update: May 10, 2004
Last modified: June 8, 2016
This is version 106 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.