Indolethylamine N-methyltransferase

Names and origin

Protein names

Recommended name:
    Indolethylamine N-methyltransferase
      Short name=Indolamine N-methyltransferase
    EC=2.1.1.49
Alternative name(s):
    Aromatic alkylamine N-methyltransferase
      Short name=Arylamine N-methyltransferase
      Short name=Amine N-methyltransferase

Gene names

Name:

INMT

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	263 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Catalyzes the N-methylation of tryptamine and structurally related compounds Potential.
Catalytic activity	S-adenosyl-L-methionine + an amine = S-adenosyl-L-homocysteine + a methylated amine.
Subunit structure	Monomer By similarity.
Subcellular location	Cytoplasm By similarity.
Tissue specificity	Widely expressed. The highest levels were in thyroid, adrenal gland, adult and fetal lung. Intermediate levels in heart, placenta, skeletal muscle, testis, small intestine, pancreas, stomach, spinal cord, lymph node and trachea. Very low levels in adult and fetal kidney and liver, in adult spleen, thymus, ovary, colon and bone marrow. Not expressed in peripheral blood leukocytes and brain.
Sequence similarities	Belongs to the NNMT/PNMT/TEMT family.
Biophysicochemical properties	Kinetic parameters: K_M=2.9 mM for tryptamine

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Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Ligand	S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	amine N-methyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 263

263

Indolethylamine N-methyltransferase

PRO_0000159712

Regions

Region

85 – 87

3

S-adenosyl-L-methionine binding

Region

142 – 143

2

S-adenosyl-L-methionine binding

Sites

Binding site

20

1

S-adenosyl-L-methionine

Binding site

25

1

S-adenosyl-L-methionine

Binding site

63

1

S-adenosyl-L-methionine; via carbonyl oxygen

Binding site

69

1

S-adenosyl-L-methionine

Binding site

90

1

S-adenosyl-L-methionine

Binding site

163

1

S-adenosyl-L-methionine; via carbonyl oxygen

Natural variations

Natural variant

28

1

D → N: dbSNP rs4723010. Ref.3

VAR_036991

Natural variant

205

1

M → V: dbSNP rs2302339. Ref.1

VAR_011616

Natural variant

219

1

E → G: dbSNP rs2302340. Ref.3 Ref.1

VAR_011617

Natural variant

246

1

N → S: dbSNP rs6970210.

VAR_036992

Natural variant

254

1

F → C: dbSNP rs4720015.

VAR_036993

Natural variant

258

1

R → H: dbSNP rs6970605.

VAR_036994

Secondary structure

1

.

263

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

O95050-1 [UniParc].

Last modified November 13, 2007. Version 3.
Checksum: 12B3AC66597E70A3
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FASTA

263

28,891

        10         20         30         40         50         60 
MKGGFTGGDE YQKHFLPRDY LATYYSFDGS PSPEAEMLKF NLECLHKTFG PGGLQGDTLI 

        70         80         90        100        110        120 
DIGSGPTIYQ VLAACDSFQD ITLSDFTDRN REELEKWLKK EPGAYDWTPA VKFACELEGN 

       130        140        150        160        170        180 
SGRWEEKEEK LRAAVKRVLK CDVHLGNPLA PAVLPLADCV LTLLAMECAC CSLDAYRAAL 

       190        200        210        220        230        240 
CNLASLLKPG GHLVTTVTLR LPSYMVGKRE FSCVALEKEE VEQAVLDAGF DIEQLLHSPQ 

       250        260 
SYSVTNAANN GVCFIVARKK PGP

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human indolethylamine N-methyltransferase: cDNA cloning and expression, gene cloning, and chromosomal localization." Thompson M.A., Moon E., Kim U.-J., Xu J., Siciliano M.J., Weinshilboum R.M. Genomics 61:285-297(1999) [PubMed: 10552930] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], VARIANTS VAL-205 AND GLY-219, BIOPHYSICOCHEMICAL PROPERTIES. Tissue: Placenta and Skeletal muscle.
[2]	"The DNA sequence of human chromosome 7." Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. Wilson R.K. Nature 424:157-164(2003) [PubMed: 12853948] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"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], VARIANTS ASN-28 AND GLY-219. Tissue: Lung and Spleen.
[4]	"Human-specific amino acid changes found in 103 protein-coding genes." Kitano T., Liu Y.-H., Ueda S., Saitou N. Mol. Biol. Evol. 21:936-944(2004) [PubMed: 15014171] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-12.
[5]	"The crystal structure of human indolethylamine N-methyltransferase in complex with SAH." Structural genomics consortium (SGC) Submitted (JUN-2005) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE.

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Cross-references

Sequence databases

AF128846 mRNA. Translation: AAF18304.1.
AF128847 mRNA. Translation: AAF18305.1.
AF128848 Genomic DNA. Translation: AAF18306.1.
AC006022 Genomic DNA. Translation: AAD04723.1.
BC033813 mRNA. Translation: AAH33813.1.
BC106902 mRNA. Translation: AAI06903.1.
BC106903 mRNA. Translation: AAI06904.1.
AB041362 Genomic DNA. Translation: BAA94451.1.

IPI

IPI00028239.

RefSeq

NP_006765.4.

UniGene

Hs.632629

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2A14	X-ray	1.70	A	1-263	[»]

ModBase

Search...

Genome annotation databases

Ensembl

ENSG00000011177. Homo sapiens. [Contig view]

GeneID

11185.

KEGG

hsa:11185.

UCSC

uc003tbs.1. human.

Organism-specific databases

GeneCards

GC07P030758.

HGNC

HGNC:6069. INMT.

MIM

604854. gene.

PharmGKB

PA403.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

O95050.

HOVERGEN

O95050.

OMA

O95050. KEPGAYD.

Enzyme and pathway databases

BioCyc

MetaCyc:ENSG00000011177-MON.

BRENDA

2.1.1.49. 247.

Gene expression databases

ArrayExpress

O95050.

Bgee

O95050.

CleanEx

HS_INMT.

GermOnline

ENSG00000011177. Homo sapiens.

Family and domain databases

InterPro

IPR000940. NNMT_TEMT_trans.
[Graphical view]

PANTHER

PTHR10867. NNMT_TEMT_trans. 1 hit.

Pfam

PF01234. NNMT_PNMT_TEMT. 1 hit.
[Graphical view]

PIRSF

PIRSF000384. PNMTase. 1 hit.

PROSITE

PS01100. NNMT_PNMT_TEMT. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

42567.

SOURCE

Search...

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Entry information

Entry name

INMT_HUMAN

Accession

Primary (citable) accession number: O95050
Secondary accession number(s): Q3KP49

Q9UHQ0

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	November 13, 2007
Last modified:	July 7, 2009
This is version 73 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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