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O97972 (INMT_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Indolethylamine N-methyltransferase

Short name=Indolamine N-methyltransferase
EC=2.1.1.49
EC=2.1.1.96
Alternative name(s):
Aromatic alkylamine N-methyltransferase
Short name=Amine N-methyltransferase
Short name=Arylamine N-methyltransferase
Thioether S-methyltransferase
Gene names
Name:INMT
OrganismOryctolagus cuniculus (Rabbit) [Reference proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus

Protein attributes

Sequence length263 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the N-methylation of tryptamine and structurally related compounds By similarity. Functions as thioether S-methyltransferase and is active with a variety of thioethers and the corresponding selenium and tellurium compounds, including 3-methylthiopropionaldehyde, dimethyl selenide, dimethyl telluride, 2-methylthioethylamine, 2-methylthioethanol, methyl-n-propyl sulfide and diethyl sulfide. Plays an important role in the detoxification of selenium compounds By similarity.

Catalytic activity

S-adenosyl-L-methionine + an amine = S-adenosyl-L-homocysteine + a methylated amine.

S-adenosyl-L-methionine + dimethyl sulfide = S-adenosyl-L-homocysteine + trimethylsulfonium.

Subunit structure

Monomer.

Subcellular location

Cytoplasm.

Tissue specificity

Highly expressed in lung, also detected in liver and at very low levels in brain.

Sequence similarities

Belongs to the class I-like SAM-binding methyltransferase superfamily. NNMT/PNMT/TEMT family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 263263Indolethylamine N-methyltransferase
PRO_0000159715

Regions

Region63 – 642S-adenosyl-L-methionine binding By similarity
Region142 – 1432S-adenosyl-L-methionine binding By similarity

Sites

Binding site201S-adenosyl-L-methionine By similarity
Binding site251S-adenosyl-L-methionine By similarity
Binding site691S-adenosyl-L-methionine By similarity
Binding site851S-adenosyl-L-methionine By similarity
Binding site901S-adenosyl-L-methionine By similarity
Binding site1631S-adenosyl-L-methionine; via carbonyl oxygen By similarity

Amino acid modifications

Modified residue131N6-succinyllysine By similarity
Modified residue961N6-succinyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
O97972 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 42F368414BE8B459

FASTA26328,955
        10         20         30         40         50         60 
MEGGFTGGDE YQKHFLPRDY LNTYYSFQSG PSPEAEMLKF NLECLHKTFG PGGLQGDTLI 

        70         80         90        100        110        120 
DIGSGPTIYQ VLAACESFKD ITLSDFTDRN REELAKWLKK EPGAYDWTPA LKFACELEGN 

       130        140        150        160        170        180 
SGRWQEKAEK LRATVKRVLK CDANLSNPLT PVVLPPADCV LTLLAMECAC CSLDAYRAAL 

       190        200        210        220        230        240 
RNLASLLKPG GHLVTTVTLQ LSSYMVGERE FSCVALEKEE VEQAVLDAGF DIEQLLYSPQ 

       250        260 
SYSASTAPNR GVCFLVARKK PGS 

« Hide

References

[1]"Rabbit lung indolethylamine N-methyltransferase. cDNA and gene cloning and characterization."
Thompson M.A., Weinshilboum R.M.
J. Biol. Chem. 273:34502-34510(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 1-129, CHARACTERIZATION.
Tissue: Lung.
[2]"Purification and molecular properties of rabbit lung indolamine N-methyltransferase."
Irace G., Colonna G., Camardella M., Della Pietra G., Porta R.
Biochemistry 21:1464-1470(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
Tissue: Lung.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF077828, AF077827 Genomic DNA. Translation: AAC97492.1.
AF077826 mRNA. Translation: AAC97491.1.
RefSeqNP_001075512.1. NM_001082043.1.
UniGeneOcu.2318.

3D structure databases

ProteinModelPortalO97972.
SMRO97972. Positions 5-261.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9986.ENSOCUP00000021686.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100008695.

Organism-specific databases

CTD11185.

Phylogenomic databases

eggNOGNOG71857.
HOGENOMHOG000013229.
HOVERGENHBG000797.
OMAAMECACC.
OrthoDBEOG7673B9.
TreeFamTF313114.

Enzyme and pathway databases

SABIO-RKO97972.

Family and domain databases

Gene3D3.40.50.150. 1 hit.
InterProIPR025817. Amine_MeTrfase.
IPR025820. NNMT/PNMT/TEMT_CS.
IPR000940. NNMT_TEMT_trans.
IPR029063. SAM-dependent_MTases-like.
[Graphical view]
PANTHERPTHR10867. PTHR10867. 1 hit.
PfamPF01234. NNMT_PNMT_TEMT. 1 hit.
[Graphical view]
PIRSFPIRSF000384. PNMTase. 1 hit.
SUPFAMSSF53335. SSF53335. 1 hit.
PROSITEPS01100. NNMT_PNMT_TEMT. 1 hit.
PS51681. SAM_MT_NNMT_PNMT_TEMT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameINMT_RABIT
AccessionPrimary (citable) accession number: O97972
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: May 1, 1999
Last modified: June 11, 2014
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families