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Protein

Glycerol-3-phosphate O-acyltransferase 1

Gene

SCT1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

G-3-P/dihydroxyacetone phosphate dual substrate-specific sn-1 acyltransferase.1 Publication

Catalytic activityi

Acyl-CoA + sn-glycerol 3-phosphate = CoA + 1-acyl-sn-glycerol 3-phosphate.
Acyl-CoA + glycerone phosphate = CoA + acylglycerone phosphate.

Pathwayi: CDP-diacylglycerol biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes CDP-diacylglycerol from sn-glycerol 3-phosphate.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Glycerol-3-phosphate O-acyltransferase 2 (GPT2), Glycerol-3-phosphate O-acyltransferase 1 (SCT1)
  2. Probable 1-acyl-sn-glycerol-3-phosphate acyltransferase (SLC1)
  3. Phosphatidate cytidylyltransferase (CDS1), Phosphatidate cytidylyltransferase, mitochondrial (TAM41)
This subpathway is part of the pathway CDP-diacylglycerol biosynthesis, which is itself part of Phospholipid metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes CDP-diacylglycerol from sn-glycerol 3-phosphate, the pathway CDP-diacylglycerol biosynthesis and in Phospholipid metabolism.

GO - Molecular functioni

  • glycerol-3-phosphate O-acyltransferase activity Source: SGD
  • glycerone-phosphate O-acyltransferase activity Source: SGD

GO - Biological processi

  • CDP-diacylglycerol biosynthetic process Source: UniProtKB-UniPathway
  • phospholipid biosynthetic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER3O-4105.
YEAST:MONOMER3O-4105.
BRENDAi2.3.1.15. 984.
SABIO-RKP32784.
UniPathwayiUPA00557; UER00612.

Chemistry

SwissLipidsiSLP:000000048.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycerol-3-phosphate O-acyltransferase 1 (EC:2.3.1.15)
Short name:
G-3-P acyltransferase 1
Alternative name(s):
Dihydroxyacetone phosphate acyltransferase 1 (EC:2.3.1.42)
Short name:
DHAP-AT 1
Glycerol-3-phosphate / dihydroxyacetone phosphate acyltransferase 1
Suppressor of choline-transport mutants 1
Gene namesi
Name:SCT1
Synonyms:GAT2, GPT1
Ordered Locus Names:YBL011W
ORF Names:YBL0309, YBL0315
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:YBL011W.
SGDiS000000107. SCT1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei49 – 6618HelicalSequence analysisAdd
BLAST
Transmembranei123 – 13917HelicalSequence analysisAdd
BLAST
Transmembranei260 – 27617HelicalSequence analysisAdd
BLAST
Transmembranei440 – 46324HelicalSequence analysisAdd
BLAST
Transmembranei494 – 51623HelicalSequence analysisAdd
BLAST
Transmembranei524 – 54522HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 759759Glycerol-3-phosphate O-acyltransferase 1PRO_0000195257Add
BLAST

Proteomic databases

MaxQBiP32784.
PeptideAtlasiP32784.

PTM databases

iPTMnetiP32784.

Interactioni

Protein-protein interaction databases

BioGridi32688. 82 interactions.
IntActiP32784. 1 interaction.
MINTiMINT-4475988.

Structurei

3D structure databases

ProteinModelPortaliP32784.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi414 – 4196HXXXXD motif

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi736 – 75318Poly-GluAdd
BLAST

Domaini

The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.By similarity

Sequence similaritiesi

Belongs to the GPAT/DAPAT family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00530000067105.
HOGENOMiHOG000191288.
InParanoidiP32784.
KOiK13507.
OMAiHEGHYCA.
OrthoDBiEOG75B8DT.

Family and domain databases

InterProiIPR002123. Plipid/glycerol_acylTrfase.
[Graphical view]
PfamiPF01553. Acyltransferase. 1 hit.
[Graphical view]
SMARTiSM00563. PlsC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P32784-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPAPKLTEKF ASSKSTQKTT NYSSIEAKSV KTSADQAYIY QEPSATKKIL
60 70 80 90 100
YSIATWLLYN IFHCFFREIR GRGSFKVPQQ GPVIFVAAPH ANQFVDPVIL
110 120 130 140 150
MGEVKKSVNR RVSFLIAESS LKQPPIGFLA SFFMAIGVVR PQDNLKPAEG
160 170 180 190 200
TIRVDPTDYK RVIGHDTHFL TDCMPKGLIG LPKSMGFGEI QSIESDTSLT
210 220 230 240 250
LRKEFKMAKP EIKTALLTGT TYKYAAKVDQ SCVYHRVFEH LAHNNCIGIF
260 270 280 290 300
PEGGSHDRTN LLPLKAGVAI MALGCMDKHP DVNVKIVPCG MNYFHPHKFR
310 320 330 340 350
SRAVVEFGDP IEIPKELVAK YHNPETNRDA VKELLDTISK GLQSVTVTCS
360 370 380 390 400
DYETLMVVQT IRRLYMTQFS TKLPLPLIVE MNRRMVKGYE FYRNDPKIAD
410 420 430 440 450
LTKDIMAYNA ALRHYNLPDH LVEEAKVNFA KNLGLVFFRS IGLCILFSLA
460 470 480 490 500
MPGIIMFSPV FILAKRISQE KARTALSKST VKIKANDVIA TWKILIGMGF
510 520 530 540 550
APLLYIFWSV LITYYLRHKP WNKIYVFSGS YISCVIVTYS ALIVGDIGMD
560 570 580 590 600
GFKSLRPLVL SLTSPKGLQK LQKDRRNLAE RIIEVVNNFG SELFPDFDSA
610 620 630 640 650
ALREEFDVID EEEEDRKTSE LNRRKMLRKQ KIKRQEKDSS SPIISQRDNH
660 670 680 690 700
DAYEHHNQDS DGVSLVNSDN SLSNIPLFSS TFHRKSESSL ASTSVAPSSS
710 720 730 740 750
SEFEVENEIL EEKNGLASKI AQAVLNKRIG ENTAREEEEE EEEEEEEEEE

EEEGKEGDA
Length:759
Mass (Da):85,694
Last modified:August 31, 2004 - v3
Checksum:iCCB0D11E8ED7D728
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti10 – 101F → S in BAA07409 (PubMed:7608137).Curated
Sequence conflicti10 – 101F → S in CAC85390 (PubMed:11544256).Curated
Sequence conflicti30 – 389Missing in CAC85390 (PubMed:11544256).Curated
Sequence conflicti88 – 881A → R in BAA07409 (PubMed:7608137).Curated
Sequence conflicti125 – 1251P → A in BAA07409 (PubMed:7608137).Curated
Sequence conflicti278 – 2781K → R in CAC85390 (PubMed:11544256).Curated
Sequence conflicti324 – 3241P → S in CAC85390 (PubMed:11544256).Curated
Sequence conflicti574 – 5741D → N in CAC85390 (PubMed:11544256).Curated
Sequence conflicti730 – 7301G → S in BAA07409 (PubMed:7608137).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D38256 Genomic DNA. Translation: BAA07409.1.
AJ314608 Genomic DNA. Translation: CAC85390.1.
Z35773 Genomic DNA. Translation: CAA84831.1.
S47695 Genomic DNA. Translation: AAB23987.1.
BK006936 Genomic DNA. Translation: DAA07108.1.
PIRiS25330.
RefSeqiNP_009542.1. NM_001178251.1.

Genome annotation databases

EnsemblFungiiYBL011W; YBL011W; YBL011W.
GeneIDi852271.
KEGGisce:YBL011W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D38256 Genomic DNA. Translation: BAA07409.1.
AJ314608 Genomic DNA. Translation: CAC85390.1.
Z35773 Genomic DNA. Translation: CAA84831.1.
S47695 Genomic DNA. Translation: AAB23987.1.
BK006936 Genomic DNA. Translation: DAA07108.1.
PIRiS25330.
RefSeqiNP_009542.1. NM_001178251.1.

3D structure databases

ProteinModelPortaliP32784.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32688. 82 interactions.
IntActiP32784. 1 interaction.
MINTiMINT-4475988.

Chemistry

SwissLipidsiSLP:000000048.

PTM databases

iPTMnetiP32784.

Proteomic databases

MaxQBiP32784.
PeptideAtlasiP32784.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYBL011W; YBL011W; YBL011W.
GeneIDi852271.
KEGGisce:YBL011W.

Organism-specific databases

EuPathDBiFungiDB:YBL011W.
SGDiS000000107. SCT1.

Phylogenomic databases

GeneTreeiENSGT00530000067105.
HOGENOMiHOG000191288.
InParanoidiP32784.
KOiK13507.
OMAiHEGHYCA.
OrthoDBiEOG75B8DT.

Enzyme and pathway databases

UniPathwayiUPA00557; UER00612.
BioCyciMetaCyc:MONOMER3O-4105.
YEAST:MONOMER3O-4105.
BRENDAi2.3.1.15. 984.
SABIO-RKP32784.

Miscellaneous databases

PROiP32784.

Family and domain databases

InterProiIPR002123. Plipid/glycerol_acylTrfase.
[Graphical view]
PfamiPF01553. Acyltransferase. 1 hit.
[Graphical view]
SMARTiSM00563. PlsC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of a SCT1 gene which can suppress a choline-transport mutant of Saccharomyces cerevisiae."
    Matsushita M., Nikawa J.
    J. Biochem. 117:447-451(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The initial step of the glycerolipid pathway: identification of glycerol-3-phosphate / dihydroxyacetone phosphate dual substrate acyltransferases in Saccharomyces cerevisiae."
    Zheng Z., Zou J.
    J. Biol. Chem. 276:41710-41716(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
    Strain: ATCC 204660 / DBY746.
  3. "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."
    Skala J., van Dyck L., Purnelle B., Goffeau A.
    Yeast 8:777-785(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. "Complete DNA sequence of yeast chromosome II."
    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.
    EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  6. "Sequence of a 12.7 kb segment of yeast chromosome II identifies a PDR-like gene and several new open reading frames."
    Delaveau T., Jacq C., Perea J.
    Yeast 8:761-768(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 609-759.
    Strain: ATCC 204508 / S288c.
  7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  9. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiGPT1_YEAST
AccessioniPrimary (citable) accession number: P32784
Secondary accession number(s): D6VPY8, Q07062, Q96TV1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: August 31, 2004
Last modified: June 8, 2016
This is version 135 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 1050 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome II
    Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

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.