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P40936

- INMT_MOUSE

UniProt

P40936 - INMT_MOUSE

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Protein
Indolethylamine N-methyltransferase
Gene
Inmt, Temt
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 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.1 Publication

Catalytic activityi

S-adenosyl-L-methionine + an amine = S-adenosyl-L-homocysteine + a methylated amine.1 Publication
S-adenosyl-L-methionine + dimethyl sulfide = S-adenosyl-L-homocysteine + trimethylsulfonium.1 Publication

Enzyme regulationi

Inhibited by the S-adenosyl-L-methionine analog sinefungin and by the product S-adenosyl-L-homocysteine.1 Publication

Kineticsi

  1. KM=0.4 µM for dimethyl selenide
  2. KM=1.0 µM for dimethyl sulfide
  3. KM=1.0 µM for S-adenosyl-L-methionine

pH dependencei

Optimum pH is 6.3.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei21 – 211S-adenosyl-L-methionine By similarity
Binding sitei26 – 261S-adenosyl-L-methionine By similarity
Binding sitei70 – 701S-adenosyl-L-methionine By similarity
Binding sitei86 – 861S-adenosyl-L-methionine By similarity
Binding sitei91 – 911S-adenosyl-L-methionine By similarity
Binding sitei164 – 1641S-adenosyl-L-methionine; via carbonyl oxygen By similarity

GO - Molecular functioni

  1. amine N-methyltransferase activity Source: UniProtKB
  2. thioether S-methyltransferase activity Source: MGI

GO - Biological processi

  1. amine metabolic process Source: UniProtKB
  2. methylation Source: UniProtKB
  3. response to toxic substance Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Detoxification

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BRENDAi2.1.1.96. 3474.

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
Short name:
TEMT
Gene namesi
Name:Inmt
Synonyms:Temt
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 6

Organism-specific databases

MGIiMGI:102963. Inmt.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytosol Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 264264Indolethylamine N-methyltransferase
PRO_0000159713Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei14 – 141N6-succinyllysine1 Publication
Modified residuei97 – 971N6-succinyllysine1 Publication

Proteomic databases

MaxQBiP40936.
PaxDbiP40936.
PRIDEiP40936.

PTM databases

PhosphoSiteiP40936.

Expressioni

Tissue specificityi

Detected in lung and liver (at protein level).1 Publication

Gene expression databases

BgeeiP40936.
CleanExiMM_INMT.
GenevestigatoriP40936.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

IntActiP40936. 3 interactions.
MINTiMINT-1869696.
STRINGi10090.ENSMUSP00000003569.

Structurei

3D structure databases

ProteinModelPortaliP40936.
SMRiP40936. Positions 6-262.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni64 – 652S-adenosyl-L-methionine binding By similarity
Regioni143 – 1442S-adenosyl-L-methionine binding By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG71857.
GeneTreeiENSGT00390000011708.
HOGENOMiHOG000013229.
HOVERGENiHBG000797.
InParanoidiP40936.
KOiK00562.
OMAiLEYSCET.
OrthoDBiEOG7673B9.
PhylomeDBiP40936.
TreeFamiTF313114.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR025817. Amine_MeTrfase.
IPR025820. NNMT/PNMT/TEMT_CS.
IPR000940. NNMT_TEMT_trans.
IPR029063. SAM-dependent_MTases-like.
[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.

P40936-1 [UniParc]FASTAAdd to Basket

« Hide

MEGKVYIGGE DYEKEFTPKD YLTTYYSFHS GPVAEQEIVK FSLQNLYQTF    50
STGGVGGDVL IDIGSGPTIY QLLSACEVFR EIIVTDYTPQ NLQELQKWLK 100
KEPGAYDWSS IVQHACELEG DRSRWQEKEA KLRRTVTRVL RCDVTKTPPL 150
GSAQVPLADC VLTFLAMECA CPDIDTYRAA LRRLAGLLKP GGHLVTLVTL 200
RFQHYMVGPK KFSGVYLEKE VVEKAIQDAG CQVLKCNCVS LSYSEAYCSH 250
DGLCFVVARK GPSA 264
Length:264
Mass (Da):29,460
Last modified:February 1, 1995 - v1
Checksum:i58AC5BA580AFB2EE
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti92 – 921L → M in BAB28594. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M88694 mRNA. Translation: AAA62365.1.
AK002281 mRNA. Translation: BAB21985.1.
AK013010 mRNA. Translation: BAB28594.1.
BC013518 mRNA. Translation: AAH13518.1.
CCDSiCCDS20163.1.
PIRiS52102.
RefSeqiNP_033375.1. NM_009349.3.
UniGeneiMm.299.

Genome annotation databases

EnsembliENSMUST00000003569; ENSMUSP00000003569; ENSMUSG00000003477.
GeneIDi21743.
KEGGimmu:21743.
UCSCiuc009can.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M88694 mRNA. Translation: AAA62365.1 .
AK002281 mRNA. Translation: BAB21985.1 .
AK013010 mRNA. Translation: BAB28594.1 .
BC013518 mRNA. Translation: AAH13518.1 .
CCDSi CCDS20163.1.
PIRi S52102.
RefSeqi NP_033375.1. NM_009349.3.
UniGenei Mm.299.

3D structure databases

ProteinModelPortali P40936.
SMRi P40936. Positions 6-262.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P40936. 3 interactions.
MINTi MINT-1869696.
STRINGi 10090.ENSMUSP00000003569.

PTM databases

PhosphoSitei P40936.

Proteomic databases

MaxQBi P40936.
PaxDbi P40936.
PRIDEi P40936.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000003569 ; ENSMUSP00000003569 ; ENSMUSG00000003477 .
GeneIDi 21743.
KEGGi mmu:21743.
UCSCi uc009can.1. mouse.

Organism-specific databases

CTDi 11185.
MGIi MGI:102963. Inmt.

Phylogenomic databases

eggNOGi NOG71857.
GeneTreei ENSGT00390000011708.
HOGENOMi HOG000013229.
HOVERGENi HBG000797.
InParanoidi P40936.
KOi K00562.
OMAi LEYSCET.
OrthoDBi EOG7673B9.
PhylomeDBi P40936.
TreeFami TF313114.

Enzyme and pathway databases

BRENDAi 2.1.1.96. 3474.

Miscellaneous databases

NextBioi 301024.
PROi P40936.
SOURCEi Search...

Gene expression databases

Bgeei P40936.
CleanExi MM_INMT.
Genevestigatori P40936.

Family and domain databases

Gene3Di 3.40.50.150. 1 hit.
InterProi IPR025817. Amine_MeTrfase.
IPR025820. NNMT/PNMT/TEMT_CS.
IPR000940. NNMT_TEMT_trans.
IPR029063. SAM-dependent_MTases-like.
[Graphical view ]
PANTHERi PTHR10867. PTHR10867. 1 hit.
Pfami PF01234. NNMT_PNMT_TEMT. 1 hit.
[Graphical view ]
PIRSFi PIRSF000384. PNMTase. 1 hit.
SUPFAMi SSF53335. SSF53335. 1 hit.
PROSITEi PS01100. NNMT_PNMT_TEMT. 1 hit.
PS51681. SAM_MT_NNMT_PNMT_TEMT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and base sequence analysis of a cDNA encoding mouse lung thioether S-methyltransferase."
    Warner D.R., Mozier N.M., Pearson J.D., Hoffman J.L.
    Biochim. Biophys. Acta 1246:160-166(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Tissue: Lung.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryo and Kidney.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Kidney.
  4. "S-adenosyl-L-methionine:thioether S-methyltransferase, a new enzyme in sulfur and selenium metabolism."
    Mozier N.M., McConnell K.P., Hoffman J.L.
    J. Biol. Chem. 263:4527-4531(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, ENZYME REGULATION, TISSUE SPECIFICITY.
  5. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-14 AND LYS-97, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiINMT_MOUSE
AccessioniPrimary (citable) accession number: P40936
Secondary accession number(s): Q9CZ50
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: July 9, 2014
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Was originally (1 Publication) thought to be a thioether S-methyltransferase but appears to be the ortholog of human INMT.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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