HNMT_RAT
ID HNMT_RAT Reviewed; 295 AA.
AC Q01984; Q59JM9;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Histamine N-methyltransferase;
DE Short=HMT;
DE EC=2.1.1.8 {ECO:0000269|PubMed:1639806};
GN Name=Hnmt;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC
RP ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Kidney;
RX PubMed=1639806; DOI=10.1016/s0021-9258(19)49590-2;
RA Takemura M., Tanaka T., Taguchi Y., Imamura I., Mizuguchi H., Kuroda M.,
RA Fukui H., Yamatodani A., Wada H.;
RT "Histamine N-methyltransferase from rat kidney. Cloning, nucleotide
RT sequence, and expression in Escherichia coli cells.";
RL J. Biol. Chem. 267:15687-15691(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=11855681; DOI=10.1254/jjp.88.85;
RA Kitanaka N., Kitanaka J., Oue T., Tada Y., Tanaka T., Takemura M.;
RT "Genomic structure of the rat and mouse histamine N-methyltransferase
RT gene.";
RL Jpn. J. Pharmacol. 88:85-92(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Inactivates histamine by N-methylation. Plays an important
CC role in degrading histamine and in regulating the airway response to
CC histamine. {ECO:0000269|PubMed:1639806}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=histamine + S-adenosyl-L-methionine = H(+) + N(tau)-
CC methylhistamine + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:19301,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:58432,
CC ChEBI:CHEBI:58600, ChEBI:CHEBI:59789; EC=2.1.1.8;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00929,
CC ECO:0000269|PubMed:1639806};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.1 uM for histamine (at pH 7.5) {ECO:0000269|PubMed:1639806};
CC KM=6.3 uM for AdoMet (at pH 7.5) {ECO:0000269|PubMed:1639806};
CC Vmax=1.6 umol/min/mg enzyme (at pH 8.5) {ECO:0000269|PubMed:1639806};
CC -!- SUBUNIT: Monomer. {ECO:0000305|PubMed:1639806}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:1639806}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. HNMT family. {ECO:0000255|PROSITE-ProRule:PRU00929}.
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DR EMBL; D10693; BAA01535.1; -; mRNA.
DR EMBL; AB007834; BAB84319.1; -; Genomic_DNA.
DR EMBL; BC087635; AAH87635.1; -; mRNA.
DR PIR; A42851; A42851.
DR RefSeq; NP_112306.1; NM_031044.3.
DR AlphaFoldDB; Q01984; -.
DR SMR; Q01984; -.
DR STRING; 10116.ENSRNOP00000007471; -.
DR BindingDB; Q01984; -.
DR ChEMBL; CHEMBL3241; -.
DR DrugCentral; Q01984; -.
DR iPTMnet; Q01984; -.
DR PhosphoSitePlus; Q01984; -.
DR PaxDb; Q01984; -.
DR Ensembl; ENSRNOT00000007471; ENSRNOP00000007471; ENSRNOG00000005223.
DR GeneID; 81676; -.
DR KEGG; rno:81676; -.
DR UCSC; RGD:71049; rat.
DR CTD; 3176; -.
DR RGD; 71049; Hnmt.
DR eggNOG; ENOG502QQJ1; Eukaryota.
DR GeneTree; ENSGT00390000002862; -.
DR HOGENOM; CLU_058117_1_0_1; -.
DR InParanoid; Q01984; -.
DR OMA; FSDHSRY; -.
DR OrthoDB; 870728at2759; -.
DR PhylomeDB; Q01984; -.
DR TreeFam; TF331080; -.
DR BioCyc; MetaCyc:MON-14646; -.
DR SABIO-RK; Q01984; -.
DR PRO; PR:Q01984; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000005223; Expressed in kidney and 11 other tissues.
DR Genevisible; Q01984; RN.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0046539; F:histamine N-methyltransferase activity; IDA:RGD.
DR GO; GO:0008170; F:N-methyltransferase activity; ISO:RGD.
DR GO; GO:0098603; F:selenol Se-methyltransferase activity; TAS:Reactome.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0001695; P:histamine catabolic process; ISS:UniProtKB.
DR GO; GO:0001692; P:histamine metabolic process; ISO:RGD.
DR GO; GO:0006972; P:hyperosmotic response; IEP:RGD.
DR GO; GO:0032259; P:methylation; ISO:RGD.
DR GO; GO:0014075; P:response to amine; IEP:RGD.
DR GO; GO:0042220; P:response to cocaine; IEP:RGD.
DR GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
DR GO; GO:0035902; P:response to immobilization stress; IEP:RGD.
DR GO; GO:0070555; P:response to interleukin-1; IEP:RGD.
DR GO; GO:0002347; P:response to tumor cell; IEP:RGD.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR016673; HHMT-like.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PIRSF; PIRSF016616; HHMT; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51597; SAM_HNMT; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Methyltransferase;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..295
FT /note="Histamine N-methyltransferase"
FT /id="PRO_0000084024"
FT BINDING 28
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00929"
FT BINDING 60
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00929"
FT BINDING 89
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00929"
FT BINDING 94
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00929"
FT BINDING 120
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00929"
FT BINDING 143
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00929"
FT BINDING 284
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00929"
FT MOD_RES 2
FT /note="Blocked amino end (Ala)"
SQ SEQUENCE 295 AA; 33942 MW; A54539BA3AE1032E CRC64;
MASFMRSLFS DHSRYVESFR RFLNNSTEHQ CMQEFMDKKL PGIIARIGET KAEIKILSIG
GGAGEIDLQI LSKVQAQYPG ICINNEVVEP NAEQIVKYKE LVAKTSNMEN IKFAWHKETS
SEYQKRVVEE DEEPPKWDFI HMIQMLYYVK DIPATLKFFH GLLAANAKIL IILVSGTSGW
EKLWKKYGFR LPRDDLCQYV TSSDLAQILD DLGIKYECYD LLSTMDITDC FIDGNENGDL
LWDFLTETCN FIKTAPLDLK EEIMKDLQEP EFSVKKEGKV LFNNNLSFIV VEANV
