Reviewed, UniProtKB/Swiss-Prot P32784 (GPT1_YEAST)

Names and origin

Protein names

Recommended 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

Gene names

Name:	GPT1
Synonyms:	GAT2, SCT1
Ordered Locus Names:	YBL011W
ORF Names:	YBL0315, YBL0309

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	759 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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	Membrane; Multi-pass membrane protein Probable.
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. Ref.6
Sequence similarities	Belongs to the GPAT/DAPAT family.

Ontologies

Keywords
Biological process	Phospholipid biosynthesis
Cellular component	Membrane
Domain	Transmembrane
Molecular function	Acyltransferase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	phospholipid biosynthetic process Ref.2 Inferred from genetic interaction. Source: SGD
Cellular component	endoplasmic reticulum Inferred from direct assay. Source: SGD integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell microsome Inferred from direct assay. Source: SGD
Molecular function	glycerol-3-phosphate O-acyltransferase activity Ref.2 Inferred from direct assay. Source: SGD glycerone-phosphate O-acyltransferase activity Ref.2 Inferred from direct assay. Source: SGD protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
AGP1	P25376	1	EBI-2086016,EBI-2357
PMP2	P40975	1	EBI-2086016,EBI-2043041
RER2	P35196	1	EBI-2086016,EBI-14943

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 759	759	Glycerol-3-phosphate O-acyltransferase 1		PRO_0000195257
Regions
	Transmembrane	49 – 66	18	Potential
	Transmembrane	123 – 139	17	Potential
	Transmembrane	260 – 276	17	Potential
	Transmembrane	440 – 463	24	Potential
	Transmembrane	494 – 516	23	Potential
	Transmembrane	524 – 545	22	Potential
	Motif	414 – 419	6	HXXXXD motif
	Compositional bias	736 – 753	18	Poly-Glu
Amino acid modifications
	Modified residue	641	1	Phosphoserine Ref.7
Experimental info
	Sequence conflict	10	1	F → S Ref.1
	Sequence conflict	10	1	F → S Ref.2
	Sequence conflict	30 – 38	9	Missing in CAC85390. Ref.2
	Sequence conflict	88	1	A → R in BAA07409. Ref.1
	Sequence conflict	125	1	P → A in BAA07409. Ref.1
	Sequence conflict	278	1	K → R in CAC85390. Ref.2
	Sequence conflict	324	1	P → S in CAC85390. Ref.2
	Sequence conflict	574	1	D → N in CAC85390. Ref.2
	Sequence conflict	730	1	G → S in BAA07409. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P32784-1 [UniParc]. Last modified August 31, 2004. Version 3. Checksum: CCB0D11E8ED7D728	FASTA	759	85,694
	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

References

	« Hide 'large scale' referencesShow '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: 7608137] [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: 11544256] [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: 1332308] [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: 7813418] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	"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: 1441753] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 609-759. Strain: ATCC 204508 / S288c.
[6]	"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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]	"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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D38256 Genomic DNA. Translation: BAA07409.1. AJ314608 Genomic DNA. Translation: CAC85390.1. Z35773 Genomic DNA. Translation: CAA84831.1. S47695 Genomic DNA. Translation: AAB23987.1.
PIR	S25330.
RefSeq	NP_009542.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	P32784. 4 interactions.
STRING	P32784.
Proteomic databases
PeptideAtlas	P32784.
Genome annotation databases
Ensembl	YBL011W; YBL011W; YBL011W; Saccharomyces cerevisiae. [Genome view]
GeneID	852271.
GenomeReviews	Gene locus YBL011W in contig Y13134_GR.
KEGG	sce:YBL011W.
NMPDR	fig|4932.3.peg.235.
Organism-specific databases
CYGD	YBL011w.
SGD	S000000107. SCT1.
Phylogenomic databases
HOGENOM	P32784.
OMA	PCGMNYF.
Enzyme and pathway databases
BRENDA	2.3.1.15. 250. 2.3.1.42. 250.
Gene expression databases
ArrayExpress	P32784.
Genevestigator	P32784.
GermOnline	YBL011W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR002123. Acyltransferase. [Graphical view]
Pfam	PF01553. Acyltransferase. 1 hit. [Graphical view]
SMART	SM00563. PlsC. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	970881.

Entry information

Entry name

GPT1_YEAST

Accession

Primary (citable) accession number: P32784
Secondary accession number(s): Q07062, Q96TV1

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	August 31, 2004
Last modified:	November 3, 2009
This is version 76 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)