Reviewed, UniProtKB/Swiss-Prot Q9QXF8 (GNMT_MOUSE)

Names and origin

Protein names

Recommended name:
    Glycine N-methyltransferase
    EC=2.1.1.20

Gene names

Name:

Gnmt

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	293 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the methylation of glycine by using S-adenosylmethionine (AdoMet) to form N-methylglycine (sarcosine) with the concomitant production of S-adenosylhomocysteine (AdoHcy). Possible crucial role in the regulation of tissue concentration of AdoMet and of metabolism of methionine By similarity.
Catalytic activity	S-adenosyl-L-methionine + glycine = S-adenosyl-L-homocysteine + sarcosine.
Subunit structure	Homotetramer By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the glycine N-methyltransferase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Folate-binding S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	S-adenosylmethionine metabolic process Ref.6 Inferred from direct assay. Source: UniProtKB glycogen metabolic process Inferred from mutant phenotype. Source: MGI methionine metabolic process Inferred from mutant phenotype. Source: MGI one-carbon metabolic process Inferred from mutant phenotype. Source: MGI protein homotetramerization Ref.6 Inferred from physical interaction. Source: UniProtKB regulation of gluconeogenesis Inferred from mutant phenotype. Source: MGI
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	folic acid binding Inferred from electronic annotation. Source: UniProtKB-KW glycine N-methyltransferase activity Ref.6 Inferred from direct assay. Source: UniProtKB glycine binding Ref.6 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 293

292

Glycine N-methyltransferase

PRO_0000087525

Regions

Region

117 – 118

2

S-adenosyl-L-methionine binding By similarity

Sites

Binding site

22

1

S-adenosyl-L-methionine By similarity

Binding site

31

1

S-adenosyl-L-methionine By similarity

Binding site

34

1

Substrate By similarity

Binding site

41

1

S-adenosyl-L-methionine By similarity

Binding site

65

1

S-adenosyl-L-methionine; via carbonyl oxygen By similarity

Binding site

86

1

S-adenosyl-L-methionine By similarity

Binding site

137

1

S-adenosyl-L-methionine; via carbonyl oxygen By similarity

Binding site

139

1

Substrate By similarity

Binding site

176

1

Substrate By similarity

Binding site

221

1

Substrate By similarity

Amino acid modifications

Modified residue

2

1

N-acetylvaline By similarity

Modified residue

233

1

Phosphoserine Ref.5

Experimental info

Sequence conflict

157

1

A → E in AAH14283. Ref.4

Secondary structure

1

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293

Helix Strand Turn

Details...

Turn

21 – 24

4

Helix

26 – 35

10

Beta strand

39 – 41

3

Helix

43 – 55

13

Beta strand

60 – 65

6

Helix

70 – 77

8

Beta strand

81 – 87

7

Helix

89 – 101

13

Turn

102 – 104

3

Helix

106 – 109

4

Beta strand

112 – 115

4

Helix

118 – 120

3

Helix

122 – 124

3

Beta strand

131 – 136

6

Helix

141 – 143

3

Beta strand

148 – 151

4

Helix

152 – 162

11

Beta strand

165 – 176

12

Helix

178 – 184

7

Beta strand

193 – 195

3

Beta strand

201 – 210

10

Beta strand

213 – 224

12

Beta strand

236 – 243

8

Helix

248 – 257

10

Turn

258 – 261

4

Beta strand

263 – 273

11

Beta strand

283 – 291

9

Sequences

	Sequence		Length	Mass (Da)
	Q9QXF8-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 264F0ACB6BBF3CDA	FASTA	293	32,675
	10 20 30 40 50 60 MVDSVYRTRS LGVAAEGLPD QYADGEAARV WQLYIGDTRS RTAEYKAWLL GLLRQHGCHR 70 80 90 100 110 120 VLDVACGTGV DSIMLVEEGF SVMSVDASDK MLKYALKERW NRRKEPSFDN WVIEEANWLT 130 140 150 160 170 180 LDKDVLSGDG FDAVICLGNS FAHLPDCKGD QSEHRLALKN IASMVRPGGL LVIDHRNYDY 190 200 210 220 230 240 ILSTGCAPPG KNIYYKSDLT KDITTSVLTV NNKAHMVTLD YTVQVPGTGR DGSPGFSKFR 250 260 270 280 290 LSYYPHCLAS FTELVRAAFG GRCQHSVLGD FKPYKPGQAY VPCYFIHVLK KTD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Mouse glycine N-methyltransferase is sexually dimorphic and regulated by growth hormone." Aida K., Tawata M., Negishi M., Onaya T. Horm. Metab. Res. 29:646-649(1997) [PubMed: 9497905] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[2]	"Mouse glycine methyltransferase gene." Luka Z.A., Wagner C. Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 129/SvJ.
[3]	"Identification of the mouse GNMT and PEX6 genes." Chen Y.-M.A., Wang Y.-C., Liu S.-P., Lee C.-M., Tsai T.-F. Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 129/SvEv.
[4]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Liver.
[5]	"Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis." Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H. J. Proteome Res. 7:3957-3967(2008) [PubMed: 18630941] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-233, MASS SPECTROMETRY. Tissue: Liver.
[6]	"Glycine N-methyltransferases: a comparison of the crystal structures and kinetic properties of recombinant human, mouse and rat enzymes." Pakhomova S., Luka Z., Grohmann S., Wagner C., Newcomer M.E. Proteins 57:331-337(2004) [PubMed: 15340920] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 2-293, SUBUNIT, FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

D89664 mRNA. Translation: BAA88218.1.
AF325352 Genomic DNA. Translation: AAK00338.1.
AY054408 Genomic DNA. Translation: AAL06142.1.
BC014283 mRNA. Translation: AAH14283.1.

IPI

IPI00467066.

RefSeq

NP_034451.1.

UniGene

Mm.29395

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1R8X	X-ray	2.95	A/B	2-293	[»]
1R8Y	X-ray	3.00	A/B/C/D/E/F/G/H	2-293	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

Q9QXF8.

PTM databases

PhosphoSite

Q9QXF8.

Proteomic databases

PRIDE

Q9QXF8.

Genome annotation databases

Ensembl

ENSMUST00000002846; ENSMUSP00000002846; ENSMUSG00000002769; Mus musculus. [Genome view]

GeneID

14711.

KEGG

mmu:14711.

UCSC

uc008cue.1. mouse.

Organism-specific databases

CTD

14711.

MGI

MGI:1202304. Gnmt.

Phylogenomic databases

HOGENOM

Q9QXF8.

HOVERGEN

Q9QXF8.

OMA

KCQHSIL.

Enzyme and pathway databases

BRENDA

2.1.1.20. 244.

Gene expression databases

ArrayExpress

Q9QXF8.

Bgee

Q9QXF8.

CleanEx

MM_GNMT.

Genevestigator

Q9QXF8.

GermOnline

ENSMUSG00000002769. Mus musculus.

Family and domain databases

InterPro

IPR014369. Gly_N_MeTrfase.
IPR013217. Methyltransf_12.
[Graphical view]

Pfam

PF08242. Methyltransf_12. 1 hit.
[Graphical view]

PIRSF

PIRSF000385. Gly_N-mtase. 1 hit.

ProtoNet

Search...

Other Resources

NextBio

286711.

SOURCE

Search...

Entry information

Entry name

GNMT_MOUSE

Accession

Primary (citable) accession number: Q9QXF8
Secondary accession number(s): Q91WN7

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 23, 2004
Last sequence update:	January 23, 2007
Last modified:	November 3, 2009
This is version 67 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)