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UniProtKB - P05374 (CHO2_YEAST)
Protein
Phosphatidylethanolamine N-methyltransferase
Gene
CHO2
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Functioni
Catalyzes the first step of the methylation pathway of phosphatidylcholine biosynthesis, the SAM-dependent methylation of phosphatidylethanolamine (PE) to phosphatidylmonomethylethanolamine (PMME). Preferentially converts di-C16:1 substrates.
UniRule annotation8 PublicationsMiscellaneous
Present with 1810 molecules/cell in log phase SD medium.1 Publication
Catalytic activityi
- a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + S-adenosyl-L-methionine = 1,2-diacyl-sn-glycero-3-phospho-N-methylethanolamine + H+ + S-adenosyl-L-homocysteineUniRule annotation4 PublicationsEC:2.1.1.17UniRule annotation4 Publications
Kineticsi
- KM=60 µM for S-adenosyl-L-methionine1 Publication
- KM=110 µM for S-adenosyl-L-methionine1 Publication
- KM=57 µM for phosphatidylethanolamine (PE)1 Publication
pH dependencei
Optimum pH is 9.9.1 Publication
: phosphatidylcholine biosynthesis Pathwayi
This protein is involved in the pathway phosphatidylcholine biosynthesis, which is part of Phospholipid metabolism.UniRule annotation2 PublicationsView all proteins of this organism that are known to be involved in the pathway phosphatidylcholine biosynthesis and in Phospholipid metabolism.
GO - Molecular functioni
GO - Biological processi
- methylation Source: UniProtKB-KW
- phosphatidylcholine biosynthetic process Source: SGD
Keywordsi
Molecular function | Methyltransferase, Transferase |
Biological process | Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism |
Ligand | S-adenosyl-L-methionine |
Enzyme and pathway databases
UniPathwayi | UPA00753 |
Chemistry databases
SwissLipidsi | SLP:000000085 |
Names & Taxonomyi
Protein namesi | Recommended name: Phosphatidylethanolamine N-methyltransferase1 PublicationUniRule annotation (EC:2.1.1.17UniRule annotation4 Publications)Short name: PE methyltransferase1 PublicationUniRule annotation Short name: PEAMTUniRule annotation Short name: PEMT1 PublicationUniRule annotation Alternative name(s): Choline-requiring protein 21 Publication |
Gene namesi | Ordered Locus Names:YGR157WImported ORF Names:G6673 |
Organismi | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
Taxonomic identifieri | 559292 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › |
Proteomesi |
|
Organism-specific databases
SGDi | S000003389, CHO2 |
VEuPathDBi | FungiDB:YGR157W |
Subcellular locationi
Endoplasmic reticulum
- Endoplasmic reticulum membrane UniRule annotation1 Publication; Multi-pass membrane protein UniRule annotation
Endoplasmic reticulum
- endoplasmic reticulum Source: SGD
- endoplasmic reticulum membrane Source: UniProtKB-SubCell
Other locations
- cell periphery Source: SGD
- integral component of membrane Source: UniProtKB-KW
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 2 – 55 | LumenalUniRule annotation1 PublicationAdd BLAST | 54 | |
Transmembranei | 56 – 76 | HelicalUniRule annotationAdd BLAST | 21 | |
Topological domaini | 77 – 86 | CytoplasmicUniRule annotation1 Publication | 10 | |
Transmembranei | 87 – 107 | HelicalUniRule annotationAdd BLAST | 21 | |
Topological domaini | 108 – 187 | LumenalUniRule annotation1 PublicationAdd BLAST | 80 | |
Transmembranei | 188 – 208 | HelicalUniRule annotationAdd BLAST | 21 | |
Topological domaini | 209 – 212 | CytoplasmicUniRule annotation1 Publication | 4 | |
Transmembranei | 213 – 233 | HelicalUniRule annotationAdd BLAST | 21 | |
Topological domaini | 234 – 258 | LumenalUniRule annotation1 PublicationAdd BLAST | 25 | |
Transmembranei | 259 – 279 | HelicalUniRule annotationAdd BLAST | 21 | |
Topological domaini | 280 – 291 | CytoplasmicUniRule annotation1 PublicationAdd BLAST | 12 | |
Transmembranei | 292 – 310 | HelicalUniRule annotationAdd BLAST | 19 | |
Topological domaini | 311 – 362 | LumenalUniRule annotation1 PublicationAdd BLAST | 52 | |
Transmembranei | 363 – 383 | HelicalUniRule annotationAdd BLAST | 21 | |
Topological domaini | 384 – 389 | CytoplasmicUniRule annotation1 Publication | 6 | |
Transmembranei | 390 – 410 | HelicalUniRule annotationAdd BLAST | 21 | |
Topological domaini | 411 – 439 | LumenalUniRule annotation1 PublicationAdd BLAST | 29 | |
Transmembranei | 440 – 460 | HelicalUniRule annotationAdd BLAST | 21 | |
Topological domaini | 461 – 463 | CytoplasmicUniRule annotation1 Publication | 3 | |
Transmembranei | 464 – 484 | HelicalUniRule annotationAdd BLAST | 21 | |
Topological domaini | 485 – 534 | LumenalUniRule annotation1 PublicationAdd BLAST | 50 | |
Transmembranei | 535 – 555 | HelicalUniRule annotationAdd BLAST | 21 | |
Topological domaini | 556 – 869 | CytoplasmicUniRule annotation1 PublicationAdd BLAST | 314 |
Keywords - Cellular componenti
Endoplasmic reticulum, MembranePTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | RemovedCombined sources | |||
ChainiPRO_0000058304 | 2 – 869 | Phosphatidylethanolamine N-methyltransferaseAdd BLAST | 868 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 2 | N-acetylserineCombined sources | 1 |
Keywords - PTMi
AcetylationProteomic databases
MaxQBi | P05374 |
PaxDbi | P05374 |
PRIDEi | P05374 |
PTM databases
iPTMneti | P05374 |
Expressioni
Inductioni
Repressed by myo-inositol and choline.4 Publications
Interactioni
Protein-protein interaction databases
BioGRIDi | 33405, 714 interactors |
DIPi | DIP-8037N |
IntActi | P05374, 2 interactors |
MINTi | P05374 |
STRINGi | 4932.YGR157W |
Miscellaneous databases
RNActi | P05374, protein |
Structurei
3D structure databases
AlphaFoldDBi | P05374 |
ModBasei | Search... |
SWISS-MODEL-Workspacei | Submit a new modelling project... |
Family & Domainsi
Sequence similaritiesi
Belongs to the class VI-like SAM-binding methyltransferase superfamily. CHO2 family.UniRule annotation
Keywords - Domaini
Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | ENOG502QRGH, Eukaryota |
HOGENOMi | CLU_005987_0_1_1 |
InParanoidi | P05374 |
OMAi | LAWEQTE |
Family and domain databases
HAMAPi | MF_03217, PEMT, 1 hit |
InterProi | View protein in InterPro IPR007318, Phopholipid_MeTrfase IPR016219, Phosphatid-EA_MeTrfase_fun |
Pfami | View protein in Pfam PF04191, PEMT, 2 hits |
PIRSFi | PIRSF000383, PEAMT, 1 hit |
PROSITEi | View protein in PROSITE PS51598, SAM_CHO2, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P05374-1 [UniParc]FASTAAdd to basket
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
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 |
PIRi | A28443 |
RefSeqi | NP_011673.1, NM_001181286.1 |
Genome annotation databases
EnsemblFungii | YGR157W_mRNA; YGR157W; YGR157W |
GeneIDi | 853061 |
KEGGi | sce:YGR157W |
Similar proteinsi
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 |
PIRi | A28443 |
RefSeqi | NP_011673.1, NM_001181286.1 |
3D structure databases
AlphaFoldDBi | P05374 |
ModBasei | Search... |
SWISS-MODEL-Workspacei | Submit a new modelling project... |
Protein-protein interaction databases
BioGRIDi | 33405, 714 interactors |
DIPi | DIP-8037N |
IntActi | P05374, 2 interactors |
MINTi | P05374 |
STRINGi | 4932.YGR157W |
Chemistry databases
SwissLipidsi | SLP:000000085 |
PTM databases
iPTMneti | P05374 |
Proteomic databases
MaxQBi | P05374 |
PaxDbi | P05374 |
PRIDEi | P05374 |
Genome annotation databases
EnsemblFungii | YGR157W_mRNA; YGR157W; YGR157W |
GeneIDi | 853061 |
KEGGi | sce:YGR157W |
Organism-specific databases
SGDi | S000003389, CHO2 |
VEuPathDBi | FungiDB:YGR157W |
Phylogenomic databases
eggNOGi | ENOG502QRGH, Eukaryota |
HOGENOMi | CLU_005987_0_1_1 |
InParanoidi | P05374 |
OMAi | LAWEQTE |
Enzyme and pathway databases
UniPathwayi | UPA00753 |
Miscellaneous databases
PROi | PR:P05374 |
RNActi | P05374, protein |
Family and domain databases
HAMAPi | MF_03217, PEMT, 1 hit |
InterProi | View protein in InterPro IPR007318, Phopholipid_MeTrfase IPR016219, Phosphatid-EA_MeTrfase_fun |
Pfami | View protein in Pfam PF04191, PEMT, 2 hits |
PIRSFi | PIRSF000383, PEAMT, 1 hit |
PROSITEi | View protein in PROSITE PS51598, SAM_CHO2, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | CHO2_YEAST | |
Accessioni | P05374Primary (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: | May 25, 2022 | |
This is version 171 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Fungal Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- 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