HNMT_MOUSE
ID HNMT_MOUSE Reviewed; 295 AA.
AC Q91VF2; Q3TVH0;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Histamine N-methyltransferase;
DE Short=HMT;
DE EC=2.1.1.8 {ECO:0000269|PubMed:11475331};
GN Name=Hnmt; Synonyms=Hmt;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=11475331; DOI=10.1007/pl00000248;
RA Wang L., Yan L., McGuire C., Kozak C.A., Wang M., Kim U.J., Siciliano M.,
RA Weinshilboum R.M.;
RT "Mouse histamine N-methyltransferase: cDNA cloning, expression, gene
RT cloning and chromosomal localization.";
RL Inflamm. Res. 50:300-308(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=129/Sv, and ddY; 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 STRAIN=C57BL/6J; TISSUE=Cerebellum, and Liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary gland;
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).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, and
RC Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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:11475331}.
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:11475331};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.8 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:11475331};
CC KM=5.3 uM for histamine {ECO:0000269|PubMed:11475331};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P50135}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P50135}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. HNMT family. {ECO:0000255|PROSITE-ProRule:PRU00929}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF297037; AAL09305.1; -; mRNA.
DR EMBL; AF298150; AAL09306.1; -; Genomic_DNA.
DR EMBL; AF297039; AAL09306.1; JOINED; Genomic_DNA.
DR EMBL; AF297040; AAL09306.1; JOINED; Genomic_DNA.
DR EMBL; AF297041; AAL09306.1; JOINED; Genomic_DNA.
DR EMBL; AF297042; AAL09306.1; JOINED; Genomic_DNA.
DR EMBL; AF297043; AAL09306.1; JOINED; Genomic_DNA.
DR EMBL; AB070523; BAB84320.1; -; Genomic_DNA.
DR EMBL; AB070524; BAB84318.1; -; mRNA.
DR EMBL; AK050129; BAC34081.1; -; mRNA.
DR EMBL; AK160131; BAE35648.1; -; mRNA.
DR EMBL; BC033928; AAH33928.1; -; mRNA.
DR CCDS; CCDS15731.1; -.
DR RefSeq; NP_536710.1; NM_080462.2.
DR RefSeq; XP_006497734.1; XM_006497671.3.
DR AlphaFoldDB; Q91VF2; -.
DR SMR; Q91VF2; -.
DR STRING; 10090.ENSMUSP00000062747; -.
DR iPTMnet; Q91VF2; -.
DR PhosphoSitePlus; Q91VF2; -.
DR jPOST; Q91VF2; -.
DR MaxQB; Q91VF2; -.
DR PaxDb; Q91VF2; -.
DR PRIDE; Q91VF2; -.
DR ProteomicsDB; 269609; -.
DR Antibodypedia; 33593; 313 antibodies from 32 providers.
DR DNASU; 140483; -.
DR Ensembl; ENSMUST00000051416; ENSMUSP00000062747; ENSMUSG00000026986.
DR Ensembl; ENSMUST00000114497; ENSMUSP00000110141; ENSMUSG00000026986.
DR Ensembl; ENSMUST00000114498; ENSMUSP00000110142; ENSMUSG00000026986.
DR GeneID; 140483; -.
DR KEGG; mmu:140483; -.
DR UCSC; uc008iok.2; mouse.
DR CTD; 3176; -.
DR MGI; MGI:2153181; Hnmt.
DR VEuPathDB; HostDB:ENSMUSG00000026986; -.
DR eggNOG; ENOG502QQJ1; Eukaryota.
DR GeneTree; ENSGT00390000002862; -.
DR HOGENOM; CLU_058117_1_0_1; -.
DR InParanoid; Q91VF2; -.
DR OMA; FSDHSRY; -.
DR OrthoDB; 870728at2759; -.
DR PhylomeDB; Q91VF2; -.
DR TreeFam; TF331080; -.
DR BRENDA; 2.1.1.8; 3474.
DR BioGRID-ORCS; 140483; 3 hits in 72 CRISPR screens.
DR PRO; PR:Q91VF2; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q91VF2; protein.
DR Bgee; ENSMUSG00000026986; Expressed in parotid gland and 198 other tissues.
DR ExpressionAtlas; Q91VF2; baseline and differential.
DR Genevisible; Q91VF2; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0046539; F:histamine N-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0008170; F:N-methyltransferase activity; IDA:MGI.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0001695; P:histamine catabolic process; ISS:UniProtKB.
DR GO; GO:0001692; P:histamine metabolic process; ISO:MGI.
DR GO; GO:0006972; P:hyperosmotic response; IEA:Ensembl.
DR GO; GO:0032259; P:methylation; ISO:MGI.
DR GO; GO:0001505; P:regulation of neurotransmitter levels; TAS:MGI.
DR GO; GO:0014075; P:response to amine; IEA:Ensembl.
DR GO; GO:0042220; P:response to cocaine; IEA:Ensembl.
DR GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
DR GO; GO:0035902; P:response to immobilization stress; IEA:Ensembl.
DR GO; GO:0070555; P:response to interleukin-1; IEA:Ensembl.
DR GO; GO:0002347; P:response to tumor cell; IEA:Ensembl.
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; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..295
FT /note="Histamine N-methyltransferase"
FT /id="PRO_0000084022"
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"
SQ SEQUENCE 295 AA; 33665 MW; 04FA324ED14A51CA CRC64;
MASCMRSLFS DQGRYVESFR RFLNNSTEHQ CMQEFMDKKL PGIIARIGEA KAEIKILSVG
GGAGEVDLQI LSKVQAQYPG ICINNEVVEP SAEQIVKYKE LVAKTSNMEN IKFSWHKETS
SEYQKRMLEE EEEPPKWDFI HMIQMLYYVK DIPATLKFFH GLLAASAKIL IILVSGTSGW
EKLWKKYGSR LPRDDLCQYV TSSDLAQILD DLGIKYECYD LVSTMDITDC FIDGNENGDL
LWDFLTETCN FSKTAPLDLK AEIMKDLQEP EFSVKKEGKV LFNNNLSFIV VEANV
