Reviewed, UniProtKB/Swiss-Prot P36148 (GPT2_YEAST)

Names and origin

Protein names

Recommended name:
    Glycerol-3-phosphate O-acyltransferase 2
      Short name=G-3-P acyltransferase 2
    EC=2.3.1.15
Alternative name(s):
    Dihydroxyacetone phosphate acyltransferase 2
      Short name=DHAP-AT 2
    EC=2.3.1.42
    Glycerol-3-phosphate / dihydroxyacetone phosphate acyltransferase 2

Gene names

Name:	GPT2
Synonyms:	GAT1
Ordered Locus Names:	YKR067W

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	743 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.1
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.
Miscellaneous	Present with 3100 molecules/cell in log phase SD medium. Ref.3
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.1 Inferred from direct assay. Source: SGD
Cellular component	endoplasmic reticulum Inferred from direct assay. Source: SGD integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	glycerol-3-phosphate O-acyltransferase activity Ref.1 Inferred from direct assay. Source: SGD glycerone-phosphate O-acyltransferase activity Ref.1 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-26471,EBI-2357
ALG5	P40350	1	EBI-26471,EBI-2470
CHO1	P08456	1	EBI-26471,EBI-14055
GAP1	P19145	1	EBI-26471,EBI-7314
OST1	P41543	1	EBI-26471,EBI-12651
PMP2	P40975	1	EBI-26471,EBI-2043041
RER2	P35196	1	EBI-26471,EBI-14943
RTN1	Q04947	1	EBI-26471,EBI-38020
SPF1	P39986	1	EBI-26471,EBI-3128

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 743	743	Glycerol-3-phosphate O-acyltransferase 2		PRO_0000195258
Regions
	Topological domain	1 – 30	30	Cytoplasmic Potential
	Transmembrane	31 – 55	25	Potential
	Topological domain	56 – 68	13	Extracellular Potential
	Transmembrane	69 – 85	17	Potential
	Topological domain	86 – 501	416	Cytoplasmic Potential
	Transmembrane	502 – 524	23	Potential
	Topological domain	525 – 538	14	Extracellular Potential
	Transmembrane	539 – 555	17	Potential
	Topological domain	556 – 743	188	Cytoplasmic Potential
Amino acid modifications
	Modified residue	211	1	Phosphoserine Ref.8
	Modified residue	631	1	Phosphoserine Ref.8
	Modified residue	632	1	Phosphoserine Ref.8 Ref.7
	Modified residue	637	1	Phosphoserine Ref.7
	Modified residue	654	1	Phosphoserine Ref.6
	Modified residue	668	1	Phosphoserine Ref.8 Ref.6 Ref.4
	Modified residue	671	1	Phosphoserine Ref.8 Ref.6 Ref.4
	Modified residue	673	1	Phosphothreonine Ref.8
	Modified residue	688	1	Phosphoserine Ref.8 Ref.7
	Modified residue	692	1	Phosphothreonine Ref.8
	Modified residue	693	1	Phosphoserine Ref.8 Ref.7

Sequences

	Sequence		Length	Mass (Da)
	P36148-1 [UniParc]. Last modified June 1, 1994. Version 1. Checksum: 84B9946E56B82F15	FASTA	743	83,645
	10 20 30 40 50 60 MSAPAADHNA AKPIPHVPQA SRRYKNSYNG FVYNIHTWLY DVSVFLFNIL FTIFFREIKV 70 80 90 100 110 120 RGAYNVPEVG VPTILVCAPH ANQFIDPALV MSQTRLLKTS AGKSRSRMPC FVTAESSFKK 130 140 150 160 170 180 RFISFFGHAM GGIPVPRIQD NLKPVDENLE IYAPDLKNHP EIIKGRSKNP QTTPVNFTKR 190 200 210 220 230 240 FSAKSLLGLP DYLSNAQIKE IPDDETIILS SPFRTSKSKV VELLTNGTNF KYAEKIDNTE 250 260 270 280 290 300 TFQSVFDHLH TKGCVGIFPE GGSHDRPSLL PIKAGVAIMA LGAVAADPTM KVAVVPCGLH 310 320 330 340 350 360 YFHRNKFRSR AVLEYGEPIV VDGKYGEMYK DSPRETVSKL LKKITNSLFS VTENAPDYDT 370 380 390 400 410 420 LMVIQAARRL YQPVKVRLPL PAIVEINRRL LFGYSKFKDD PRIIHLKKLV YDYNRKLDSV 430 440 450 460 470 480 GLKDHQVMQL KTTKLEALRC FVTLIVRLIK FSVFAILSLP GSILFTPIFI ICRVYSEKKA 490 500 510 520 530 540 KEGLKKSLVK IKGTDLLATW KLIVALILAP ILYVTYSILL IILARKQHYC RIWVPSNNAF 550 560 570 580 590 600 IQFVYFYALL VFTTYSSLKT GEIGVDLFKS LRPLFVSIVY PGKKIEEIQT TRKNLSLELT 610 620 630 640 650 660 AVCNDLGPLV FPDYDKLATE IFSKRDGYDV SSDAESSISR MSVQSRSRSS SIHSIGSLAS 670 680 690 700 710 720 NALSRVNSRG SLTDIPIFSD AKQGQWKSEG ETSEDEDEFD EKNPAIVQTA RSSDLNKENS 730 740 RNTNISSKIA SLVRQKREHE KKE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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.
[2]	"Complete DNA sequence of yeast chromosome XI." Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C. , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W. Nature 369:371-378(1994) [PubMed: 8196765] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	"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].
[4]	"A proteomics approach to understanding protein ubiquitination." Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G., Roelofs J., Finley D., Gygi S.P. Nat. Biotechnol. 21:921-926(2003) [PubMed: 12872131] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-668 AND SER-671, MASS SPECTROMETRY.
[5]	"A global topology map of the Saccharomyces cerevisiae membrane proteome." Kim H., Melen K., Oesterberg M., von Heijne G. Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed: 16847258] [Abstract] Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
[6]	"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-654; SER-668 AND SER-671, MASS SPECTROMETRY.
[7]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-632; SER-637; SER-688 AND SER-693, MASS SPECTROMETRY.
[8]	"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-211; SER-631; SER-632; SER-668; SER-671; THR-673; SER-688; THR-692 AND SER-693, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AJ311354 Genomic DNA. Translation: CAC85303.1. Z28292 Genomic DNA. Translation: CAA82146.1.
PIR	S38143.
RefSeq	NP_012993.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:6620N.
IntAct	P36148. 63 interactions.
Proteomic databases
PeptideAtlas	P36148.
Genome annotation databases
Ensembl	YKR067W. Saccharomyces cerevisiae. [Contig view]
GeneID	853941.
GenomeReviews	Gene locus YKR067W in contig Y13137_GR.
KEGG	sce:YKR067W.
NMPDR	fig|4932.3.peg.3979.
Organism-specific databases
CYGD	YKR067w.
SGD	S000001775. GPT2.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	P36148.
OMA	P36148. GSHDRPS.
Enzyme and pathway databases
BRENDA	2.3.1.15. 250. 2.3.1.42. 250.
Gene expression databases
ArrayExpress	P36148.
GermOnline	YKR067W. 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	975330.

Entry information

Entry name

GPT2_YEAST

Accession

Primary (citable) accession number: P36148

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	June 16, 2009
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)