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P32784 (GPT1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Glycerol-3-phosphate O-acyltransferase 1

Short name=G-3-P acyltransferase 1
EC=2.3.1.15
Alternative name(s):
Dihydroxyacetone phosphate acyltransferase 1
Short name=DHAP-AT 1
EC=2.3.1.42
Glycerol-3-phosphate / dihydroxyacetone phosphate acyltransferase 1
Suppressor of choline-transport mutants 1
Gene names
Name:SCT1
Synonyms:GAT2, GPT1
Ordered Locus Names:YBL011W
ORF Names:YBL0309, YBL0315
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length759 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

G-3-P/dihydroxyacetone phosphate dual substrate-specific sn-1 acyltransferase. Ref.2

Catalytic activity

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

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; Multi-pass membrane protein Ref.7.

Domain

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.

Miscellaneous

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

Sequence similarities

Belongs to the GPAT/DAPAT family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 759759Glycerol-3-phosphate O-acyltransferase 1
PRO_0000195257

Regions

Transmembrane49 – 6618Helical; Potential
Transmembrane123 – 13917Helical; Potential
Transmembrane260 – 27617Helical; Potential
Transmembrane440 – 46324Helical; Potential
Transmembrane494 – 51623Helical; Potential
Transmembrane524 – 54522Helical; Potential
Motif414 – 4196HXXXXD motif
Compositional bias736 – 75318Poly-Glu

Amino acid modifications

Modified residue6411Phosphoserine Ref.9

Experimental info

Sequence conflict101F → S in BAA07409. Ref.1
Sequence conflict101F → S in CAC85390. Ref.2
Sequence conflict30 – 389Missing in CAC85390. Ref.2
Sequence conflict881A → R in BAA07409. Ref.1
Sequence conflict1251P → A in BAA07409. Ref.1
Sequence conflict2781K → R in CAC85390. Ref.2
Sequence conflict3241P → S in CAC85390. Ref.2
Sequence conflict5741D → N in CAC85390. Ref.2
Sequence conflict7301G → S in BAA07409. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P32784 [UniParc].

Last modified August 31, 2004. Version 3.
Checksum: CCB0D11E8ED7D728

FASTA75985,694
        10         20         30         40         50         60 
MPAPKLTEKF ASSKSTQKTT NYSSIEAKSV KTSADQAYIY QEPSATKKIL YSIATWLLYN 

        70         80         90        100        110        120 
IFHCFFREIR GRGSFKVPQQ GPVIFVAAPH ANQFVDPVIL MGEVKKSVNR RVSFLIAESS 

       130        140        150        160        170        180 
LKQPPIGFLA SFFMAIGVVR PQDNLKPAEG TIRVDPTDYK RVIGHDTHFL TDCMPKGLIG 

       190        200        210        220        230        240 
LPKSMGFGEI QSIESDTSLT LRKEFKMAKP EIKTALLTGT TYKYAAKVDQ SCVYHRVFEH 

       250        260        270        280        290        300 
LAHNNCIGIF PEGGSHDRTN LLPLKAGVAI MALGCMDKHP DVNVKIVPCG MNYFHPHKFR 

       310        320        330        340        350        360 
SRAVVEFGDP IEIPKELVAK YHNPETNRDA VKELLDTISK GLQSVTVTCS DYETLMVVQT 

       370        380        390        400        410        420 
IRRLYMTQFS TKLPLPLIVE MNRRMVKGYE FYRNDPKIAD LTKDIMAYNA ALRHYNLPDH 

       430        440        450        460        470        480 
LVEEAKVNFA KNLGLVFFRS IGLCILFSLA MPGIIMFSPV FILAKRISQE KARTALSKST 

       490        500        510        520        530        540 
VKIKANDVIA TWKILIGMGF APLLYIFWSV LITYYLRHKP WNKIYVFSGS YISCVIVTYS 

       550        560        570        580        590        600 
ALIVGDIGMD GFKSLRPLVL SLTSPKGLQK LQKDRRNLAE RIIEVVNNFG SELFPDFDSA 

       610        620        630        640        650        660 
ALREEFDVID EEEEDRKTSE LNRRKMLRKQ KIKRQEKDSS SPIISQRDNH DAYEHHNQDS 

       670        680        690        700        710        720 
DGVSLVNSDN SLSNIPLFSS TFHRKSESSL ASTSVAPSSS SEFEVENEIL EEKNGLASKI 

       730        740        750 
AQAVLNKRIG ENTAREEEEE EEEEEEEEEE EEEGKEGDA 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
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]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[8]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS25330.
RefSeqNP_009542.1. NM_001178251.1.

3D structure databases

ProteinModelPortalP32784.
ModBaseSearch...

Protein-protein interaction databases

IntActP32784. 1 interaction.
MINTMINT-4475988.
STRING4932.YBL011W.

Proteomic databases

PaxDbP32784.
PeptideAtlasP32784.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYBL011W; YBL011W; YBL011W.
GeneID852271.
KEGGsce:YBL011W.

Organism-specific databases

CYGDYBL011w.
SGDS000000107. SCT1.

Phylogenomic databases

eggNOGCOG0204.
GeneTreeENSGT00530000067105.
HOGENOMHOG000191288.
KOK13507.
OMAPCGMNYF.
OrthoDBEOG4W6S49.

Enzyme and pathway databases

BRENDA2.3.1.15. 984.
SABIO-RKP32784.
UniPathwayUPA00557; UER00612.

Gene expression databases

GenevestigatorP32784.
GermOnlineYBL011W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR002123. Plipid/glycerol_acylTrfase.
[Graphical view]
PfamPF01553. Acyltransferase. 1 hit.
[Graphical view]
SMARTSM00563. PlsC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio970881.

Entry information

Entry nameGPT1_YEAST
AccessionPrimary (citable) accession number: P32784
Secondary accession number(s): D6VPY8, Q07062, Q96TV1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: August 31, 2004
Last modified: May 1, 2013
This is version 110 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome II

Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families