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Q01984 (HNMT_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histamine N-methyltransferase

Short name=HMT
EC=2.1.1.8
Gene names
Name:Hnmt
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length295 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Inactivates histamine by N-methylation. Plays an important role in degrading histamine and in regulating the airway response to histamine.

Catalytic activity

S-adenosyl-L-methionine + histamine = S-adenosyl-L-homocysteine + N(tau)-methylhistamine.

Subunit structure

Monomer.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the class I-like SAM-binding methyltransferase superfamily. HNMT family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 295295Histamine N-methyltransferase
PRO_0000084024

Sites

Binding site281Substrate By similarity
Binding site601S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site891S-adenosyl-L-methionine By similarity
Binding site941S-adenosyl-L-methionine By similarity
Binding site1201S-adenosyl-L-methionine; via amide nitrogen By similarity
Binding site1431S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site2841Substrate By similarity

Amino acid modifications

Modified residue21Blocked amino end (Ala)

Sequences

Sequence LengthMass (Da)Tools
Q01984 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: A54539BA3AE1032E

FASTA29533,942
        10         20         30         40         50         60 
MASFMRSLFS DHSRYVESFR RFLNNSTEHQ CMQEFMDKKL PGIIARIGET KAEIKILSIG 

        70         80         90        100        110        120 
GGAGEIDLQI LSKVQAQYPG ICINNEVVEP NAEQIVKYKE LVAKTSNMEN IKFAWHKETS 

       130        140        150        160        170        180 
SEYQKRVVEE DEEPPKWDFI HMIQMLYYVK DIPATLKFFH GLLAANAKIL IILVSGTSGW 

       190        200        210        220        230        240 
EKLWKKYGFR LPRDDLCQYV TSSDLAQILD DLGIKYECYD LLSTMDITDC FIDGNENGDL 

       250        260        270        280        290 
LWDFLTETCN FIKTAPLDLK EEIMKDLQEP EFSVKKEGKV LFNNNLSFIV VEANV 

« Hide

References

« Hide 'large scale' references
[1]"Histamine N-methyltransferase from rat kidney. Cloning, nucleotide sequence, and expression in Escherichia coli cells."
Takemura M., Tanaka T., Taguchi Y., Imamura I., Mizuguchi H., Kuroda M., Fukui H., Yamatodani A., Wada H.
J. Biol. Chem. 267:15687-15691(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Tissue: Kidney.
[2]"Genomic structure of the rat and mouse histamine N-methyltransferase gene."
Kitanaka N., Kitanaka J., Oue T., Tada Y., Tanaka T., Takemura M.
Jpn. J. Pharmacol. 88:85-92(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Sprague-Dawley.
Tissue: Liver.
[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].
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D10693 mRNA. Translation: BAA01535.1.
AB007834 Genomic DNA. Translation: BAB84319.1.
BC087635 mRNA. Translation: AAH87635.1.
PIRA42851.
RefSeqNP_112306.1. NM_031044.3.
UniGeneRn.13145.

3D structure databases

ProteinModelPortalQ01984.
SMRQ01984. Positions 5-293.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000007471.

Chemistry

BindingDBQ01984.
ChEMBLCHEMBL3241.

Proteomic databases

PaxDbQ01984.
PRIDEQ01984.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000007471; ENSRNOP00000007471; ENSRNOG00000005223.
GeneID81676.
KEGGrno:81676.
UCSCRGD:71049. rat.

Organism-specific databases

CTD3176.
RGD71049. Hnmt.

Phylogenomic databases

eggNOGNOG39680.
GeneTreeENSGT00390000002862.
HOGENOMHOG000231790.
HOVERGENHBG051914.
InParanoidQ01984.
KOK00546.
OMAMDISDCF.
OrthoDBEOG7Z69CQ.
TreeFamTF331080.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-14646.

Gene expression databases

GenevestigatorQ01984.

Family and domain databases

InterProIPR016673. Histamine_N-methyltransferase.
[Graphical view]
PANTHERPTHR32330:SF0. PTHR32330:SF0. 1 hit.
PIRSFPIRSF016616. HHMT. 1 hit.
PROSITEPS51597. SAM_HNMT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio615280.
PROQ01984.

Entry information

Entry nameHNMT_RAT
AccessionPrimary (citable) accession number: Q01984
Secondary accession number(s): Q59JM9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 90 of the entry and version 3 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