O97972 (INMT_RABIT) Reviewed, UniProtKB/Swiss-Prot
Last modified
October 19, 2011.
Version 61.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames 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=Amine N-methyltransferase Short name=Arylamine N-methyltransferase | ||
| Gene names |
| ||
| Organism | Oryctolagus cuniculus (Rabbit) [Complete proteome] | ||
| Taxonomic identifier | 9986 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus |
Protein attributes
| Sequence length | 263 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
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. |
| Subcellular location | |
| Tissue specificity | Highly expressed in lung, also detected in liver and at very low levels in brain. |
| Sequence similarities | Belongs to the NNMT/PNMT/TEMT family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | S-adenosyl-L-methionine |
| Molecular function | Methyltransferase Transferase |
| Technical term | Complete proteome Direct protein sequencing |
| 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... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 263 | 263 | Indolethylamine N-methyltransferase | PRO_0000159715 | |||||
Regions | |||||||||
| Region | 63 – 64 | 2 | S-adenosyl-L-methionine binding By similarity | ||||||
| Region | 142 – 143 | 2 | S-adenosyl-L-methionine binding By similarity | ||||||
Sites | |||||||||
| Binding site | 20 | 1 | S-adenosyl-L-methionine By similarity | ||||||
| Binding site | 25 | 1 | S-adenosyl-L-methionine By similarity | ||||||
| Binding site | 69 | 1 | S-adenosyl-L-methionine By similarity | ||||||
| Binding site | 85 | 1 | S-adenosyl-L-methionine By similarity | ||||||
| Binding site | 90 | 1 | S-adenosyl-L-methionine By similarity | ||||||
| Binding site | 163 | 1 | S-adenosyl-L-methionine; via carbonyl oxygen By similarity | ||||||
Sequences
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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: 9852119] [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: 7074100] [Abstract] Cited for: CHARACTERIZATION. Tissue: Lung. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF077828, AF077827 Genomic DNA. Translation: AAC97492.1. AF077826 mRNA. Translation: AAC97491.1. |
| RefSeq | NP_001075512.1. NM_001082043.1. |
| UniGene | Ocu.2318. |
3D structure databases | |
| ProteinModelPortal | O97972. |
| SMR | O97972. Positions 5-261. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | O97972. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSOCUT00000024664; ENSOCUP00000021686; ENSOCUG00000024221. |
| GeneID | 100008695. |
Organism-specific databases | |
| CTD | 11185. |
Phylogenomic databases | |
| eggNOG | maNOG06009. |
| GeneTree | ENSGT00390000011708. |
| HOVERGEN | HBG000797. |
| OrthoDB | EOG49079M. |
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... |
Entry information
| Entry name | INMT_RABIT | ||||||||
| Accession | Primary (citable) accession number: O97972 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

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