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Protein

Indolethylamine N-methyltransferase

Gene

INMT

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei20S-adenosyl-L-methionineBy similarity1
Binding sitei25S-adenosyl-L-methionineBy similarity1
Binding sitei69S-adenosyl-L-methionineBy similarity1
Binding sitei85S-adenosyl-L-methionineBy similarity1
Binding sitei90S-adenosyl-L-methionineBy similarity1
Binding sitei163S-adenosyl-L-methionine; via carbonyl oxygenBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Detoxification

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

SABIO-RKO97972.

Names & Taxonomyi

Protein namesi
Recommended name:
Indolethylamine N-methyltransferase (EC:2.1.1.49, EC:2.1.1.96)
Short name:
Indolamine N-methyltransferase
Alternative name(s):
Aromatic alkylamine N-methyltransferase
Short name:
Amine N-methyltransferase
Short name:
Arylamine N-methyltransferase
Thioether S-methyltransferase
Gene namesi
Name:INMT
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
Proteomesi
  • UP000001811 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3227915.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001597151 – 263Indolethylamine N-methyltransferaseAdd BLAST263

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei13N6-succinyllysineBy similarity1
Modified residuei96N6-succinyllysineBy similarity1

Expressioni

Tissue specificityi

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

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000021686.

Chemistry databases

BindingDBiO97972.

Structurei

3D structure databases

ProteinModelPortaliO97972.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni63 – 64S-adenosyl-L-methionine bindingBy similarity2
Regioni142 – 143S-adenosyl-L-methionine bindingBy similarity2

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG410IFTZ. Eukaryota.
ENOG41128ZR. LUCA.
HOGENOMiHOG000013229.
HOVERGENiHBG000797.
InParanoidiO97972.
KOiK00562.
TreeFamiTF313114.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR025820. NNMT/PNMT/TEMT_CS.
IPR000940. NNMT_TEMT_trans.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR10867. PTHR10867. 1 hit.
PfamiPF01234. NNMT_PNMT_TEMT. 1 hit.
[Graphical view]
PIRSFiPIRSF000384. PNMTase. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS01100. NNMT_PNMT_TEMT. 1 hit.
PS51681. SAM_MT_NNMT_PNMT_TEMT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O97972-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEGGFTGGDE YQKHFLPRDY LNTYYSFQSG PSPEAEMLKF NLECLHKTFG
60 70 80 90 100
PGGLQGDTLI DIGSGPTIYQ VLAACESFKD ITLSDFTDRN REELAKWLKK
110 120 130 140 150
EPGAYDWTPA LKFACELEGN SGRWQEKAEK LRATVKRVLK CDANLSNPLT
160 170 180 190 200
PVVLPPADCV LTLLAMECAC CSLDAYRAAL RNLASLLKPG GHLVTTVTLQ
210 220 230 240 250
LSSYMVGERE FSCVALEKEE VEQAVLDAGF DIEQLLYSPQ SYSASTAPNR
260
GVCFLVARKK PGS
Length:263
Mass (Da):28,955
Last modified:May 1, 1999 - v1
Checksum:i42F368414BE8B459
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF077828, AF077827 Genomic DNA. Translation: AAC97492.1.
AF077826 mRNA. Translation: AAC97491.1.
RefSeqiNP_001075512.1. NM_001082043.1.
UniGeneiOcu.2318.

Genome annotation databases

GeneIDi100008695.
KEGGiocu:100008695.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF077828, AF077827 Genomic DNA. Translation: AAC97492.1.
AF077826 mRNA. Translation: AAC97491.1.
RefSeqiNP_001075512.1. NM_001082043.1.
UniGeneiOcu.2318.

3D structure databases

ProteinModelPortaliO97972.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000021686.

Chemistry databases

BindingDBiO97972.
ChEMBLiCHEMBL3227915.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100008695.
KEGGiocu:100008695.

Organism-specific databases

CTDi11185.

Phylogenomic databases

eggNOGiENOG410IFTZ. Eukaryota.
ENOG41128ZR. LUCA.
HOGENOMiHOG000013229.
HOVERGENiHBG000797.
InParanoidiO97972.
KOiK00562.
TreeFamiTF313114.

Enzyme and pathway databases

SABIO-RKO97972.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR025820. NNMT/PNMT/TEMT_CS.
IPR000940. NNMT_TEMT_trans.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR10867. PTHR10867. 1 hit.
PfamiPF01234. NNMT_PNMT_TEMT. 1 hit.
[Graphical view]
PIRSFiPIRSF000384. PNMTase. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS01100. NNMT_PNMT_TEMT. 1 hit.
PS51681. SAM_MT_NNMT_PNMT_TEMT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiINMT_RABIT
AccessioniPrimary (citable) accession number: O97972
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: May 1, 1999
Last modified: October 5, 2016
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.