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P05374 (CHO2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length869 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 class VI-like SAM-binding methyltransferase superfamily. CHO2 family.

Biophysicochemical properties

Kinetic parameters:

KM=60 µM for S-adenosyl-L-methionine Ref.10

pH dependence:

Optimum pH is 9.9.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.17
Chain2 – 869868Phosphatidylethanolamine N-methyltransferase
PRO_0000058304

Regions

Topological domain2 – 5554Extracellular Potential
Transmembrane56 – 7621Helical; Potential
Topological domain77 – 8610Cytoplasmic Potential
Transmembrane87 – 10721Helical; Potential
Topological domain108 – 18780Extracellular Potential
Transmembrane188 – 20821Helical; Potential
Topological domain209 – 2124Cytoplasmic Potential
Transmembrane213 – 23321Helical; Potential
Topological domain234 – 25825Extracellular Potential
Transmembrane259 – 27921Helical; Potential
Topological domain280 – 29112Cytoplasmic Potential
Transmembrane292 – 31019Helical; Potential
Topological domain311 – 36252Extracellular Potential
Transmembrane363 – 38321Helical; Potential
Topological domain384 – 3896Cytoplasmic Potential
Transmembrane390 – 41021Helical; Potential
Topological domain411 – 43929Extracellular Potential
Transmembrane440 – 46021Helical; Potential
Topological domain461 – 4633Cytoplasmic Potential
Transmembrane464 – 48421Helical; Potential
Topological domain485 – 53450Extracellular Potential
Transmembrane535 – 55521Helical; Potential
Topological domain556 – 869314Cytoplasmic Potential

Amino acid modifications

Modified residue21N-acetylserine Ref.17

Sequences

Sequence LengthMass (Da)Tools
P05374 [UniParc].

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

FASTA869101,204
        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' 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. expand/collapse author list , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
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]"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].
[17]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
+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.
PIRA28443.
RefSeqNP_011673.1. NM_001181286.1.

3D structure databases

ProteinModelPortalP05374.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33405. 353 interactions.
DIPDIP-8037N.
IntActP05374. 2 interactions.
MINTMINT-1358409.
STRING4932.YGR157W.

Proteomic databases

MaxQBP05374.
PaxDbP05374.
PeptideAtlasP05374.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYGR157W; YGR157W; YGR157W.
GeneID853061.
KEGGsce:YGR157W.

Organism-specific databases

CYGDYGR157w.
SGDS000003389. CHO2.

Phylogenomic databases

eggNOGNOG68139.
KOK16369.
OMAEAWRQWK.
OrthoDBEOG73Z333.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-16680.
YEAST:YGR157W-MONOMER.
UniPathwayUPA00753.

Gene expression databases

GenevestigatorP05374.

Family and domain databases

InterProIPR007318. Phopholipid_MeTrfase.
IPR016219. Phosphatid-EA_MeTrfase_fun.
[Graphical view]
PfamPF04191. PEMT. 2 hits.
[Graphical view]
PIRSFPIRSF000383. PEAMT. 1 hit.
PROSITEPS51598. SAM_CHO2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio972998.

Entry information

Entry nameCHO2_YEAST
AccessionPrimary (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 14, 2014
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome VII

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

Yeast

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

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways