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Q5RFR7 (INMT_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 47. 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
OrganismPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome]
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pongo

Protein attributes

Sequence length263 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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 By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the NNMT/PNMT/TEMT family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 263263Indolethylamine N-methyltransferase
PRO_0000159714

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

Sequences

Sequence LengthMass (Da)Tools
Q5RFR7 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 05387543210CB66B

FASTA26328,848
        10         20         30         40         50         60 
MEGGFTGGDE YQKHFLPRDY LATYYSFDGS PSPEAEMLKF NLECLHKTFG PGGLQGDTLI 

        70         80         90        100        110        120 
DIGSGPTIYQ VLAACESFQD ITLSDFTDRN REELEKWLKK EPGAYDWTPV VKFACELEGN 

       130        140        150        160        170        180 
SGQWEEKEEK LRATVKRVLK CDVHLGNPLA PAVLPPADCV LTLLAMECAC CSLDAYCAAL 

       190        200        210        220        230        240 
CNLASLLKPG GHLVTTVTLR LSSYMVGKRE FSCVALEKEE VEQAVLDAGF DIEQLLQSPQ 

       250        260 
SYSVTNAANN GVCFIVARKK PGP

« Hide

References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Liver.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CR857085 mRNA. Translation: CAH89390.1.
RefSeqNP_001124586.1. NM_001131114.1.
UniGenePab.12389.

3D structure databases

ProteinModelPortalQ5RFR7.
SMRQ5RFR7. Positions 5-261.
ModBaseSearch...

Proteomic databases

PRIDEQ5RFR7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSPPYT00000020590; ENSPPYP00000019808; ENSPPYG00000017671.
GeneID100171421.
KEGGpon:100171421.

Organism-specific databases

CTD11185.

Phylogenomic databases

GeneTreeENSGT00390000011708.
HOVERGENHBG000797.
InParanoidQ5RFR7.
KOK00562.
OMADRNREEL.
OrthoDBEOG49079M.

Family and domain databases

InterProIPR025817. Amine_MeTrfase.
IPR025820. NNMT/PNMT/TEMT_CS.
IPR000940. NNMT_TEMT_trans.
[Graphical view]
PANTHERPTHR10867. PTHR10867. 1 hit.
PfamPF01234. NNMT_PNMT_TEMT. 1 hit.
[Graphical view]
PIRSFPIRSF000384. PNMTase. 1 hit.
PROSITEPS01100. NNMT_PNMT_TEMT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameINMT_PONAB
AccessionPrimary (citable) accession number: Q5RFR7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: December 21, 2004
Last modified: May 1, 2013
This is version 47 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

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