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Protein

Phosphatidyl-N-methylethanolamine N-methyltransferase

Gene

cho1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Catalyzes three sequential methylation reactions of phosphatidylethanolamine (PE) by AdoMet, thereby producing phosphatidylcholine (PC).PROSITE-ProRule annotation1 Publication

Catalytic activityi

S-adenosyl-L-methionine + phosphatidyl-N-methylethanolamine = S-adenosyl-L-homocysteine + phosphatidyl-N-dimethylethanolamine.PROSITE-ProRule annotation
S-adenosyl-L-methionine + phosphatidyl-N-dimethylethanolamine = S-adenosyl-L-homocysteine + phosphatidylcholine.PROSITE-ProRule annotation
S-adenosyl-L-methionine + phosphatidylethanolamine = S-adenosyl-L-homocysteine + phosphatidyl-N-methylethanolamine.PROSITE-ProRule annotation

Pathwayi: phosphatidylcholine biosynthesis

This protein is involved in the pathway phosphatidylcholine biosynthesis, which is part of Phospholipid metabolism.PROSITE-ProRule annotation
View 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

  • phosphatidylcholine biosynthetic process Source: PomBase
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

ReactomeiR-SPO-1483191. Synthesis of PC.
UniPathwayiUPA00753.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidyl-N-methylethanolamine N-methyltransferase (EC:2.1.1.17, EC:2.1.1.71)
Short name:
PLMT
Alternative name(s):
Unsaturated phospholipid methyltransferase
Gene namesi
Name:cho1
ORF Names:SPBC337.16
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC337.16.
PomBaseiSPBC337.16. cho1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei33 – 5321HelicalSequence analysisAdd
BLAST
Transmembranei73 – 9321HelicalSequence analysisAdd
BLAST
Transmembranei116 – 13621HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 221221Phosphatidyl-N-methylethanolamine N-methyltransferasePRO_0000193923Add
BLAST

Proteomic databases

MaxQBiO74827.

Interactioni

Protein-protein interaction databases

BioGridi277511. 95 interactions.
MINTiMINT-4681043.

Family & Domainsi

Sequence similaritiesi

Belongs to the class VI-like SAM-binding methyltransferase superfamily. PEMT/PEM2 methyltransferase family.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

HOGENOMiHOG000208789.
InParanoidiO74827.
KOiK00550.
OMAiTSTWALG.
OrthoDBiEOG71K6FR.
PhylomeDBiO74827.

Family and domain databases

InterProiIPR024960. PEMT/MFAP.
IPR007318. Phopholipid_MeTrfase.
[Graphical view]
PANTHERiPTHR15458. PTHR15458. 1 hit.
PfamiPF04191. PEMT. 1 hit.
[Graphical view]
PIRSFiPIRSF005444. PEMT. 1 hit.
PROSITEiPS51599. SAM_PEMT_PEM2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O74827-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLILYPKPT SYLYQPFIKA YFSLNMAIFE INNSFLICAV SIALNPLLWN
60 70 80 90 100
IAARSEYNHK TLTKLANGDS KKACYMLAAC IFVAGIVRDL IYQNALKQQP
110 120 130 140 150
TLGIFMNPLV QGIAKLIFCF GSVLVLSSMY KLGLVGTYLG DYFGFLLPER
160 170 180 190 200
VSGFPFNVND NPMYNGSTLC FLSTALRYGK VAGLLLTLEV FFVYRIALKF
210 220
EEPFTAKIYA ARDSKQAKKS E
Length:221
Mass (Da):24,767
Last modified:November 1, 1998 - v1
Checksum:i26CEEDF270FE9AD7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti160 – 1601D → DND (PubMed:9755189).Curated
Sequence conflicti202 – 22120Missing (PubMed:9755189).CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF004112 Genomic DNA. Translation: AAB61409.1.
CU329671 Genomic DNA. Translation: CAA21286.1.
PIRiT40269.
RefSeqiNP_595417.1. NM_001021324.2.

Genome annotation databases

EnsemblFungiiSPBC337.16.1; SPBC337.16.1:pep; SPBC337.16.
GeneIDi2540995.
KEGGispo:SPBC337.16.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF004112 Genomic DNA. Translation: AAB61409.1.
CU329671 Genomic DNA. Translation: CAA21286.1.
PIRiT40269.
RefSeqiNP_595417.1. NM_001021324.2.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi277511. 95 interactions.
MINTiMINT-4681043.

Proteomic databases

MaxQBiO74827.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC337.16.1; SPBC337.16.1:pep; SPBC337.16.
GeneIDi2540995.
KEGGispo:SPBC337.16.

Organism-specific databases

EuPathDBiFungiDB:SPBC337.16.
PomBaseiSPBC337.16. cho1.

Phylogenomic databases

HOGENOMiHOG000208789.
InParanoidiO74827.
KOiK00550.
OMAiTSTWALG.
OrthoDBiEOG71K6FR.
PhylomeDBiO74827.

Enzyme and pathway databases

UniPathwayiUPA00753.
ReactomeiR-SPO-1483191. Synthesis of PC.

Miscellaneous databases

NextBioi20802110.
PROiO74827.

Family and domain databases

InterProiIPR024960. PEMT/MFAP.
IPR007318. Phopholipid_MeTrfase.
[Graphical view]
PANTHERiPTHR15458. PTHR15458. 1 hit.
PfamiPF04191. PEMT. 1 hit.
[Graphical view]
PIRSFiPIRSF005444. PEMT. 1 hit.
PROSITEiPS51599. SAM_PEMT_PEM2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The Schizosaccharomyces pombe cho1+ gene encodes a phospholipid methyltransferase."
    Kanipes M.I., Hill J.E., Henry S.A.
    Genetics 150:553-562(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
  2. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.

Entry informationi

Entry nameiCHO1_SCHPO
AccessioniPrimary (citable) accession number: O74827
Secondary accession number(s): P87300
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: November 1, 1998
Last modified: May 11, 2016
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.