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Protein

Phosphatidylethanolamine N-methyltransferase

Gene

CHO2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the first step in the conversion of phosphatidylethanolamine to phosphatidylcholine during the methylation pathway of phosphatidylcholine biosynthesis. Preferentially converts di-C16:1 substrates.7 Publications

Catalytic activityi

S-adenosyl-L-methionine + phosphatidylethanolamine = S-adenosyl-L-homocysteine + phosphatidyl-N-methylethanolamine.

Kineticsi

  1. KM=60 µM for S-adenosyl-L-methionine1 Publication

    pH dependencei

    Optimum pH is 9.9.1 Publication

    Pathway: phosphatidylcholine biosynthesis

    This protein is involved in the pathway phosphatidylcholine biosynthesis, which is part of Phospholipid metabolism.
    View all proteins of this organism that are known to be involved in the pathway phosphatidylcholine biosynthesis and in Phospholipid metabolism.

    GO - Molecular functioni

    • phosphatidylethanolamine N-methyltransferase activity Source: SGD

    GO - Biological processi

    • phosphatidylcholine biosynthetic process Source: SGD
    Complete GO annotation...

    Keywords - Molecular functioni

    Methyltransferase, Transferase

    Keywords - Biological processi

    Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

    Keywords - Ligandi

    S-adenosyl-L-methionine

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-16680.
    YEAST:YGR157W-MONOMER.
    UniPathwayiUPA00753.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphatidylethanolamine N-methyltransferase (EC:2.1.1.17)
    Short name:
    PEAMT
    Alternative name(s):
    Choline-requiring protein 2
    Gene namesi
    Name:CHO2
    Synonyms:PEM1
    Ordered Locus Names:YGR157W
    ORF Names:G6673
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311 Componenti: Chromosome VII

    Organism-specific databases

    CYGDiYGR157w.
    EuPathDBiFungiDB:YGR157W.
    SGDiS000003389. CHO2.

    Subcellular locationi

    Topology

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini2 – 5554ExtracellularSequence AnalysisAdd
    BLAST
    Transmembranei56 – 7621HelicalSequence AnalysisAdd
    BLAST
    Topological domaini77 – 8610CytoplasmicSequence Analysis
    Transmembranei87 – 10721HelicalSequence AnalysisAdd
    BLAST
    Topological domaini108 – 18780ExtracellularSequence AnalysisAdd
    BLAST
    Transmembranei188 – 20821HelicalSequence AnalysisAdd
    BLAST
    Topological domaini209 – 2124CytoplasmicSequence Analysis
    Transmembranei213 – 23321HelicalSequence AnalysisAdd
    BLAST
    Topological domaini234 – 25825ExtracellularSequence AnalysisAdd
    BLAST
    Transmembranei259 – 27921HelicalSequence AnalysisAdd
    BLAST
    Topological domaini280 – 29112CytoplasmicSequence AnalysisAdd
    BLAST
    Transmembranei292 – 31019HelicalSequence AnalysisAdd
    BLAST
    Topological domaini311 – 36252ExtracellularSequence AnalysisAdd
    BLAST
    Transmembranei363 – 38321HelicalSequence AnalysisAdd
    BLAST
    Topological domaini384 – 3896CytoplasmicSequence Analysis
    Transmembranei390 – 41021HelicalSequence AnalysisAdd
    BLAST
    Topological domaini411 – 43929ExtracellularSequence AnalysisAdd
    BLAST
    Transmembranei440 – 46021HelicalSequence AnalysisAdd
    BLAST
    Topological domaini461 – 4633CytoplasmicSequence Analysis
    Transmembranei464 – 48421HelicalSequence AnalysisAdd
    BLAST
    Topological domaini485 – 53450ExtracellularSequence AnalysisAdd
    BLAST
    Transmembranei535 – 55521HelicalSequence AnalysisAdd
    BLAST
    Topological domaini556 – 869314CytoplasmicSequence AnalysisAdd
    BLAST

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 869868Phosphatidylethanolamine N-methyltransferasePRO_0000058304Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP05374.
    PaxDbiP05374.
    PeptideAtlasiP05374.

    Expressioni

    Inductioni

    Repressed by myo-inositol and choline.2 Publications

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AGP1P253761EBI-2049142,EBI-2357
    CHO1P084561EBI-2049142,EBI-14055
    ELO1P395401EBI-2049142,EBI-2049096
    ERG11P106141EBI-2049142,EBI-5127
    OST1P415431EBI-2049142,EBI-12651
    PMP2P409751EBI-2049142,EBI-2043041
    RTN1Q049471EBI-2049142,EBI-38020
    SAC1P323681EBI-2049142,EBI-16210
    SPF1P399861EBI-2049142,EBI-3128
    YHR080CP388001EBI-2049142,EBI-24597

    Protein-protein interaction databases

    BioGridi33405. 355 interactions.
    DIPiDIP-8037N.
    IntActiP05374. 2 interactions.
    MINTiMINT-1358409.
    STRINGi4932.YGR157W.

    Structurei

    3D structure databases

    ProteinModelPortaliP05374.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG68139.
    InParanoidiP05374.
    KOiK16369.
    OMAiEAWRQWK.
    OrthoDBiEOG73Z333.

    Family and domain databases

    InterProiIPR007318. Phopholipid_MeTrfase.
    IPR016219. Phosphatid-EA_MeTrfase_fun.
    [Graphical view]
    PfamiPF04191. PEMT. 2 hits.
    [Graphical view]
    PIRSFiPIRSF000383. PEAMT. 1 hit.
    PROSITEiPS51598. SAM_CHO2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P05374-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSSCKTTLSE MVGSVTKDRG TINVEARTRS SNVTFKPPVT HDMVRSLFDP
    60 70 80 90 100
    TLKKSLLEKC IALAIISNFF ICYWVFQRFG LQFTKYFFLV QYLFWRIAYN
    110 120 130 140 150
    LGIGLVLHYQ SHYETLTNCA KTHAIFSKIP QNKDANSNFS TNSNSFSEKF
    160 170 180 190 200
    WNFIRKFCQY EIRSKMPKEY DLFAYPEEIN VWLIFRQFVD LILMQDFVTY
    210 220 230 240 250
    IIYVYLSIPY SWVQIFNWRS LLGVILILFN IWVKLDAHRV VKDYAWYWGD
    260 270 280 290 300
    FFFLEESELI FDGVFNISPH PMYSIGYLGY YGLSLICNDY KVLLVSVFGH
    310 320 330 340 350
    YSQFLFLKYV ENPHIERTYG DGTDSDSQMN SRIDDLISKE NYDYSRPLIN
    360 370 380 390 400
    MGLSFNNFNK LRFTDYFTIG TVAALMLGTI MNARFINLNY LFITVFVTKL
    410 420 430 440 450
    VSWLFISTIL YKQSQSKWFT RLFLENGYTQ VYSYEQWQFI YNYYLVLTYT
    460 470 480 490 500
    LMIIHTGLQI WSNFSNINNS QLIFGLILVA LQTWCDKETR LAISDFGWFY
    510 520 530 540 550
    GDFFLSNYIS TRKLTSQGIY RYLNHPEAVL GVVGVWGTVL MTNFAVTNII
    560 570 580 590 600
    LAVLWTLTNF ILVKFIETPH VNKIYGKTKR VSGVGKTLLG LKPLRQVSDI
    610 620 630 640 650
    VNRIENIIIK SLVDESKNSN GGAELLPKNY QDNKEWNILI QEAMDSVATR
    660 670 680 690 700
    LSPYCELKIE NEQVETNFVL PTPVTLNWKM PIELYNGDDW IGLYKVIDTR
    710 720 730 740 750
    ADREKTRVGS GGHWSATSKD SYMNHGLRHK ESVTEIKATE KYVQGKVTFD
    760 770 780 790 800
    TSLLYFENGI YEFRYHSGNS HKVLLISTPF EISLPVLNTT TPELFEKDLT
    810 820 830 840 850
    EFLTKVNVLK DGKFRPLGNK FFGMDSLKQL IKNSIGVELS SEYMRRVNGD
    860
    AHVISHRAWD IKQTLDSLA
    Length:869
    Mass (Da):101,204
    Last modified:November 1, 1988 - v1
    Checksum:iA273F179B4E46A20
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M16987 Genomic DNA. Translation: AAA34850.1.
    X85807 Genomic DNA. Translation: CAA59814.1.
    Z72942 Genomic DNA. Translation: CAA97171.1.
    BK006941 Genomic DNA. Translation: DAA08248.1.
    PIRiA28443.
    RefSeqiNP_011673.1. NM_001181286.1.

    Genome annotation databases

    EnsemblFungiiYGR157W; YGR157W; YGR157W.
    GeneIDi853061.
    KEGGisce:YGR157W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M16987 Genomic DNA. Translation: AAA34850.1.
    X85807 Genomic DNA. Translation: CAA59814.1.
    Z72942 Genomic DNA. Translation: CAA97171.1.
    BK006941 Genomic DNA. Translation: DAA08248.1.
    PIRiA28443.
    RefSeqiNP_011673.1. NM_001181286.1.

    3D structure databases

    ProteinModelPortaliP05374.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi33405. 355 interactions.
    DIPiDIP-8037N.
    IntActiP05374. 2 interactions.
    MINTiMINT-1358409.
    STRINGi4932.YGR157W.

    Proteomic databases

    MaxQBiP05374.
    PaxDbiP05374.
    PeptideAtlasiP05374.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYGR157W; YGR157W; YGR157W.
    GeneIDi853061.
    KEGGisce:YGR157W.

    Organism-specific databases

    CYGDiYGR157w.
    EuPathDBiFungiDB:YGR157W.
    SGDiS000003389. CHO2.

    Phylogenomic databases

    eggNOGiNOG68139.
    InParanoidiP05374.
    KOiK16369.
    OMAiEAWRQWK.
    OrthoDBiEOG73Z333.

    Enzyme and pathway databases

    UniPathwayiUPA00753.
    BioCyciMetaCyc:MONOMER-16680.
    YEAST:YGR157W-MONOMER.

    Miscellaneous databases

    NextBioi972998.
    PROiP05374.

    Family and domain databases

    InterProiIPR007318. Phopholipid_MeTrfase.
    IPR016219. Phosphatid-EA_MeTrfase_fun.
    [Graphical view]
    PfamiPF04191. PEMT. 2 hits.
    [Graphical view]
    PIRSFiPIRSF000383. PEAMT. 1 hit.
    PROSITEiPS51598. SAM_CHO2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    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.
      , 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. 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. 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. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiCHO2_YEAST
    AccessioniPrimary (citable) accession number: P05374
    Secondary accession number(s): D6VUT7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1988
    Last sequence update: November 1, 1988
    Last modified: June 24, 2015
    This is version 121 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 1810 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome VII
      Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.