Phosphatidylethanolamine N-methyltransferase - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P05374 (CHO2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 106. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Phosphatidylethanolamine N-methyltransferase
Short name=PEAMT
EC=2.1.1.17

Alternative name(s):
Choline-requiring protein 2

Gene names

Name:	CHO2
Synonyms:	PEM1
Ordered Locus Names:	YGR157W
ORF Names:	G6673

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	869 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the first step in the conversion of phosphatidylethanolamine to phosphatidylcholine during the methylation pathway of phosphatidylcholine biosynthesis. Preferentially converts di-C16:1 substrates. Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.14
Catalytic activity	S-adenosyl-L-methionine + phosphatidylethanolamine = S-adenosyl-L-homocysteine + phosphatidyl-N-methylethanolamine.
Pathway	Phospholipid metabolism; phosphatidylcholine biosynthesis.
Subcellular location	Membrane; Multi-pass membrane protein.
Induction	Repressed by myo-inositol and choline. Ref.11 Ref.12
Miscellaneous	Present with 1810 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the CHO2 family.
Biophysicochemical properties	Kinetic parameters: K_M=60 µM for S-adenosyl-L-methionine Ref.10 pH dependence: Optimum pH is 9.9.

Ontologies

Keywords
Biological process	Lipid biosynthesis Lipid metabolism Phospholipid biosynthesis Phospholipid metabolism
Cellular component	Membrane
Domain	Transmembrane Transmembrane helix
Ligand	S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	phosphatidylcholine biosynthetic process Inferred from direct assay Ref.1 Ref.8. Source: SGD
Cellular_component	endoplasmic reticulum Inferred from direct assay PubMed 14562095. Source: SGD integral to membrane Inferred from sequence model PubMed 12192589 Ref.1. Source: SGD
Molecular_function	phosphatidylethanolamine N-methyltransferase activity Inferred from direct assay Ref.1 Ref.8. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct
AGP1	P25376	1	EBI-2049142,EBI-2357
CHO1	P08456	1	EBI-2049142,EBI-14055
ELO1	P39540	1	EBI-2049142,EBI-2049096
ERG11	P10614	1	EBI-2049142,EBI-5127
OST1	P41543	1	EBI-2049142,EBI-12651
PMP2	P40975	1	EBI-2049142,EBI-2043041
RTN1	Q04947	1	EBI-2049142,EBI-38020
SAC1	P32368	1	EBI-2049142,EBI-16210
SPF1	P39986	1	EBI-2049142,EBI-3128
YHR080C	P38800	1	EBI-2049142,EBI-24597

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 869

869

Phosphatidylethanolamine N-methyltransferase

PRO_0000058304

Regions

Topological domain

1 – 55

Extracellular Potential

Transmembrane

56 – 76

Helical; Potential

Topological domain

77 – 86

Cytoplasmic Potential

Transmembrane

87 – 107

Helical; Potential

Topological domain

108 – 187

Extracellular Potential

Transmembrane

188 – 208

Helical; Potential

Topological domain

209 – 212

Cytoplasmic Potential

Transmembrane

213 – 233

Helical; Potential

Topological domain

234 – 258

Extracellular Potential

Transmembrane

259 – 279

Helical; Potential

Topological domain

280 – 291

Cytoplasmic Potential

Transmembrane

292 – 310

Helical; Potential

Topological domain

311 – 362

Extracellular Potential

Transmembrane

363 – 383

Helical; Potential

Topological domain

384 – 389

Cytoplasmic Potential

Transmembrane

390 – 410

Helical; Potential

Topological domain

411 – 439

Extracellular Potential

Transmembrane

440 – 460

Helical; Potential

Topological domain

461 – 463

Cytoplasmic Potential

Transmembrane

464 – 484

Helical; Potential

Topological domain

485 – 534

Extracellular Potential

Transmembrane

535 – 555

Helical; Potential

Topological domain

556 – 869

314

Cytoplasmic Potential

Amino acid modifications

Modified residue

582

Phosphoserine Ref.16

Sequences

Sequence

Length

Mass (Da)

Tools

P05374 [UniParc].

Last modified November 1, 1988. Version 1.
Checksum: A273F179B4E46A20
Show »

FASTA

869

101,204

        10         20         30         40         50         60 
MSSCKTTLSE MVGSVTKDRG TINVEARTRS SNVTFKPPVT HDMVRSLFDP TLKKSLLEKC 

        70         80         90        100        110        120 
IALAIISNFF ICYWVFQRFG LQFTKYFFLV QYLFWRIAYN LGIGLVLHYQ SHYETLTNCA 

       130        140        150        160        170        180 
KTHAIFSKIP QNKDANSNFS TNSNSFSEKF WNFIRKFCQY EIRSKMPKEY DLFAYPEEIN 

       190        200        210        220        230        240 
VWLIFRQFVD LILMQDFVTY IIYVYLSIPY SWVQIFNWRS LLGVILILFN IWVKLDAHRV 

       250        260        270        280        290        300 
VKDYAWYWGD FFFLEESELI FDGVFNISPH PMYSIGYLGY YGLSLICNDY KVLLVSVFGH 

       310        320        330        340        350        360 
YSQFLFLKYV ENPHIERTYG DGTDSDSQMN SRIDDLISKE NYDYSRPLIN MGLSFNNFNK 

       370        380        390        400        410        420 
LRFTDYFTIG TVAALMLGTI MNARFINLNY LFITVFVTKL VSWLFISTIL YKQSQSKWFT 

       430        440        450        460        470        480 
RLFLENGYTQ VYSYEQWQFI YNYYLVLTYT LMIIHTGLQI WSNFSNINNS QLIFGLILVA 

       490        500        510        520        530        540 
LQTWCDKETR LAISDFGWFY GDFFLSNYIS TRKLTSQGIY RYLNHPEAVL GVVGVWGTVL 

       550        560        570        580        590        600 
MTNFAVTNII LAVLWTLTNF ILVKFIETPH VNKIYGKTKR VSGVGKTLLG LKPLRQVSDI 

       610        620        630        640        650        660 
VNRIENIIIK SLVDESKNSN GGAELLPKNY QDNKEWNILI QEAMDSVATR LSPYCELKIE 

       670        680        690        700        710        720 
NEQVETNFVL PTPVTLNWKM PIELYNGDDW IGLYKVIDTR ADREKTRVGS GGHWSATSKD 

       730        740        750        760        770        780 
SYMNHGLRHK ESVTEIKATE KYVQGKVTFD TSLLYFENGI YEFRYHSGNS HKVLLISTPF 

       790        800        810        820        830        840 
EISLPVLNTT TPELFEKDLT EFLTKVNVLK DGKFRPLGNK FFGMDSLKQL IKNSIGVELS 

       850        860 
SEYMRRVNGD AHVISHRAWD IKQTLDSLA

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Yeast phosphatidylethanolamine methylation pathway. Cloning and characterization of two distinct methyltransferase genes." Kodaki T., Yamashita S. J. Biol. Chem. 262:15428-15435(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The sequence of a 27 kb segment on the right arm of chromosome VII from Saccharomyces cerevisiae reveals MOL1, NAT2, RPL30B, RSR1, CYS4, PEM1/CHO2, NSR1 genes and ten new open reading frames." Skala J., Nawrocki A., Goffeau A. Yeast 11:1421-1427(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII." Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. Kleine K. Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"Regulation of phosphatidylethanolamine methyltransferase level by myo-inositol in Saccaromyces cerevisiae." Yamashita S., Oshima A. Eur. J. Biochem. 104:611-616(1980) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[6]	"Regulation of the phosphatidylethanolamine methylation pathway in Saccharomyces cerevisiae." Yamashita S., Oshima A., Nikawa J., Hosaka K. Eur. J. Biochem. 128:589-595(1982) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[7]	"Expression of the Saccharomyces cerevisiae inositol-1-phosphate synthase (INO1) gene is regulated by factors that affect phospholipid synthesis." Hirsch J.P., Henry S.A. Mol. Cell. Biol. 6:3320-3328(1986) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[8]	"Saccharomyces cerevisiae cho2 mutants are deficient in phospholipid methylation and cross-pathway regulation of inositol synthesis." Summers E.F., Letts V.A., McGraw P., Henry S.A. Genetics 120:909-922(1988) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[9]	"Inositol regulates phosphatidylglycerolphosphate synthase expression in Saccharomyces cerevisiae." Greenberg M.L., Hubbell S., Lam C. Mol. Cell. Biol. 8:4773-4779(1988) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[10]	"Characterization of the methyltransferases in the yeast phosphatidylethanolamine methylation pathway by selective gene disruption." Kodaki T., Yamashita S. Eur. J. Biochem. 185:243-251(1989) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
[11]	"Regulation of phosphatidylethanolamine methyltransferase and phospholipid methyltransferase by phospholipid precursors in Saccharomyces cerevisiae." Gaynor P.M., Gill T., Toutenhoofd S., Summers E.F., McGraw P., Homann M.J., Henry S.A., Carman G.M. Biochim. Biophys. Acta 1090:326-332(1991) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION.
[12]	"Identification of the upstream activation sequences responsible for the expression and regulation of the PEM1 and PEM2 genes encoding the enzymes of the phosphatidylethanolamine methylation pathway in Saccharomyces cerevisiae." Kodaki T., Hosaka K., Nikawa J., Yamashita S. J. Biochem. 109:276-287(1991) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION.
[13]	"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].
[14]	"The yeast phospholipid N-methyltransferases catalyzing the synthesis of phosphatidylcholine preferentially convert di-C16:1 substrates both in vivo and in vitro." Boumann H.A., Chin P.T., Heck A.J., De Kruijff B., De Kroon A.I. J. Biol. Chem. 279:40314-40319(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[15]	"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] [Europe PMC] [Abstract] Cited for: TOPOLOGY [LARGE SCALE ANALYSIS]. Strain: ATCC 208353 / W303-1A.
[16]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-582, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M16987 Genomic DNA. Translation: AAA34850.1. X85807 Genomic DNA. Translation: CAA59814.1. Z72942 Genomic DNA. Translation: CAA97171.1. BK006941 Genomic DNA. Translation: DAA08248.1.
PIR	A28443.
RefSeq	NP_011673.1. NM_001181286.1.
3D structure databases
ProteinModelPortal	P05374.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-8037N.
IntAct	P05374. 1 interaction.
MINT	MINT-1358409.
STRING	4932.YGR157W.
Proteomic databases
PaxDb	P05374.
PeptideAtlas	P05374.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YGR157W; YGR157W; YGR157W.
GeneID	853061.
KEGG	sce:YGR157W.
Organism-specific databases
CYGD	YGR157w.
SGD	S000003389. CHO2.
Phylogenomic databases
eggNOG	NOG68139.
KO	K16369.
OMA	AHRVVKD.
OrthoDB	EOG4T4H3J.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-16680.
UniPathway	UPA00753.
Gene expression databases
Genevestigator	P05374.
GermOnline	YGR157W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR007318. Phopholipid_MeTrfase. IPR016219. Phosphatid-EA_MeTrfase_fun. [Graphical view]
Pfam	PF04191. PEMT. 2 hits. [Graphical view]
PIRSF	PIRSF000383. PEAMT. 1 hit.
ProtoNet	Search...
Other
NextBio	972998.

Entry information

Entry name

CHO2_YEAST

Accession

Primary (citable) accession number: P05374
Secondary accession number(s): D6VUT7

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	November 1, 1988
Last modified:	May 1, 2013
This is version 106 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome VII

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents