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Protein

Phosphatidylethanolamine N-methyltransferase

Gene

Pemt

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes three sequential methylation reactions of phosphatidylethanolamine (PE) by AdoMet, thereby producing phosphatidylcholine (PC).

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

GO - Molecular functioni

  1. phosphatidylethanolamine N-methyltransferase activity Source: MGI
  2. phosphatidyl-N-dimethylethanolamine N-methyltransferase activity Source: UniProtKB-EC
  3. phosphatidyl-N-methylethanolamine N-methyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. phosphatidylcholine biosynthetic process Source: MGI
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

ReactomeiREACT_207335. Synthesis of PC.
UniPathwayiUPA00753.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylethanolamine N-methyltransferase (EC:2.1.1.17, EC:2.1.1.71)
Short name:
PEAMT
Short name:
PEMT
Alternative name(s):
PEMT2
Gene namesi
Name:Pemt
Synonyms:Pempt, Pemt2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:104535. Pemt.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 1211LumenalSequence AnalysisAdd
BLAST
Intramembranei13 – 3321HelicalSequence AnalysisAdd
BLAST
Topological domaini34 – 4512LumenalSequence AnalysisAdd
BLAST
Transmembranei46 – 6621HelicalSequence AnalysisAdd
BLAST
Topological domaini67 – 9024CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei91 – 11121HelicalSequence AnalysisAdd
BLAST
Topological domaini112 – 15746LumenalSequence AnalysisAdd
BLAST
Transmembranei158 – 17821HelicalSequence AnalysisAdd
BLAST
Topological domaini179 – 19921CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: MGI
  2. integral component of membrane Source: UniProtKB-KW
  3. mitochondrial envelope Source: MGI
  4. mitochondrial membrane Source: UniProtKB-SubCell
  5. mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 199198Phosphatidylethanolamine N-methyltransferasePRO_0000193921Add
BLAST

Proteomic databases

PaxDbiQ61907.
PRIDEiQ61907.

PTM databases

PhosphoSiteiQ61907.

Expressioni

Tissue specificityi

Liver.

Gene expression databases

CleanExiMM_PEMT.
ExpressionAtlasiQ61907. baseline and differential.
GenevestigatoriQ61907.

Interactioni

Protein-protein interaction databases

IntActiQ61907. 2 interactions.
MINTiMINT-8409735.
STRINGi10090.ENSMUSP00000099754.

Structurei

3D structure databases

ProteinModelPortaliQ61907.
ModBaseiSearch...
MobiDBiSearch...

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

eggNOGiNOG261676.
GeneTreeiENSGT00390000007041.
HOVERGENiHBG000990.
InParanoidiQ61907.
KOiK00551.
OMAiTSTWALG.
OrthoDBiEOG7TQV20.
TreeFamiTF300198.

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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q61907-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSWLLGYMDP TEPSFVAAVI TIVFNPLFWN VVARWEQRTR KLSRAFGSPH
60 70 80 90 100
LACYSLGICI LLLNILRSHC FTQAMMSQPK MEGLDNHTTY FLGLAFLGWG
110 120 130 140 150
FVFVLSSFYA LGFTGTFLGD YFGILKESRV TTFPFSVLDN PMYWGSTANY
160 170 180 190
LGWALMHASP TGLLLTVLVA IVYVVALLYE EPFTAEIYRQ KATRLHKRS
Length:199
Mass (Da):22,579
Last modified:October 16, 2013 - v4
Checksum:i0F96C1CC3B483DC6
GO
Isoform 2 (identifier: Q61907-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MEENTSPTTALISSSVAGHDCCGGFGNIDFRQADLFVM

Show »
Length:236
Mass (Da):26,453
Checksum:i8D321A6CA1C51849
GO

Sequence cautioni

The sequence AAQ01190.1 differs from that shown. Reason: Frameshift at position 195. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti168 – 1681L → V in AAA67686. (PubMed:8978486)Curated
Sequence conflicti173 – 1731Y → N in AAA67686. (PubMed:8978486)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MEENTSPTTALISSSVAGHD CCGGFGNIDFRQADLFVM in isoform 2. 1 PublicationVSP_053224

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U25051
, U25046, U25047, U25048, U25049, U25050 Genomic DNA. Translation: AAA67686.1.
AY334571 mRNA. Translation: AAQ01190.1. Frameshift.
AK133744 mRNA. Translation: BAE21818.1.
AL603710 Genomic DNA. No translation available.
AL645526 Genomic DNA. No translation available.
BC026796 mRNA. Translation: AAH26796.1.
CCDSiCCDS24782.1. [Q61907-1]
RefSeqiNP_001276940.1. NM_001290011.1. [Q61907-2]
NP_001276941.1. NM_001290012.1. [Q61907-1]
NP_001276942.1. NM_001290013.1. [Q61907-1]
NP_001276943.1. NM_001290014.1.
NP_032845.2. NM_008819.3. [Q61907-1]
UniGeneiMm.2731.
Mm.452195.

Genome annotation databases

EnsembliENSMUST00000000310; ENSMUSP00000000310; ENSMUSG00000000301. [Q61907-1]
ENSMUST00000102692; ENSMUSP00000099753; ENSMUSG00000000301. [Q61907-1]
ENSMUST00000102693; ENSMUSP00000099754; ENSMUSG00000000301. [Q61907-2]
GeneIDi18618.
KEGGimmu:18618.
UCSCiuc007jfi.1. mouse.
uc007jfj.1. mouse.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U25051
, U25046, U25047, U25048, U25049, U25050 Genomic DNA. Translation: AAA67686.1.
AY334571 mRNA. Translation: AAQ01190.1. Frameshift.
AK133744 mRNA. Translation: BAE21818.1.
AL603710 Genomic DNA. No translation available.
AL645526 Genomic DNA. No translation available.
BC026796 mRNA. Translation: AAH26796.1.
CCDSiCCDS24782.1. [Q61907-1]
RefSeqiNP_001276940.1. NM_001290011.1. [Q61907-2]
NP_001276941.1. NM_001290012.1. [Q61907-1]
NP_001276942.1. NM_001290013.1. [Q61907-1]
NP_001276943.1. NM_001290014.1.
NP_032845.2. NM_008819.3. [Q61907-1]
UniGeneiMm.2731.
Mm.452195.

3D structure databases

ProteinModelPortaliQ61907.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ61907. 2 interactions.
MINTiMINT-8409735.
STRINGi10090.ENSMUSP00000099754.

PTM databases

PhosphoSiteiQ61907.

Proteomic databases

PaxDbiQ61907.
PRIDEiQ61907.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000000310; ENSMUSP00000000310; ENSMUSG00000000301. [Q61907-1]
ENSMUST00000102692; ENSMUSP00000099753; ENSMUSG00000000301. [Q61907-1]
ENSMUST00000102693; ENSMUSP00000099754; ENSMUSG00000000301. [Q61907-2]
GeneIDi18618.
KEGGimmu:18618.
UCSCiuc007jfi.1. mouse.
uc007jfj.1. mouse.

Organism-specific databases

CTDi10400.
MGIiMGI:104535. Pemt.

Phylogenomic databases

eggNOGiNOG261676.
GeneTreeiENSGT00390000007041.
HOVERGENiHBG000990.
InParanoidiQ61907.
KOiK00551.
OMAiTSTWALG.
OrthoDBiEOG7TQV20.
TreeFamiTF300198.

Enzyme and pathway databases

UniPathwayiUPA00753.
ReactomeiREACT_207335. Synthesis of PC.

Miscellaneous databases

NextBioi294564.
PROiQ61907.
SOURCEiSearch...

Gene expression databases

CleanExiMM_PEMT.
ExpressionAtlasiQ61907. baseline and differential.
GenevestigatoriQ61907.

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. "Characterization of the murine phosphatidylethanolamine N-methyltransferase-2 gene."
    Walkey C.J., Cui Z., Agellon L.B., Vance D.E.
    J. Lipid Res. 37:2341-2350(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129/J.
    Tissue: Liver.
  2. "Cloning of Mus musculus phosphatidylethanolamine N-methyltransferase (Pemt)."
    Zhou G., Yu L., Zhao S.
    Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Liver.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: C57BL/6J.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: FVB/N.
    Tissue: Liver.
  6. "Disruption of the murine gene encoding phosphatidylethanolamine N-methyltransferase."
    Walkey C.J., Donohue L.R., Bronson R., Agellon L.B., Vance D.E.
    Proc. Natl. Acad. Sci. U.S.A. 94:12880-12885(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  7. "Biochemical and evolutionary significance of phospholipid methylation."
    Walkey C.J., Yu L., Agellon L.B., Vance D.E.
    J. Biol. Chem. 273:27043-27046(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.

Entry informationi

Entry nameiPEMT_MOUSE
AccessioniPrimary (citable) accession number: Q61907
Secondary accession number(s): Q3UZN8, Q7TNW6, Q8R0I1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: October 16, 2013
Last modified: January 7, 2015
This is version 104 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

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.