ID   HNMT_BOVIN              Reviewed;         292 AA.
AC   Q58DV7; Q29RR4;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   24-JAN-2024, entry version 112.
DE   RecName: Full=Histamine N-methyltransferase;
DE            Short=HMT;
DE            EC=2.1.1.8 {ECO:0000250|UniProtKB:P50135};
GN   Name=HNMT;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Hypothalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:P50135}.
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:0000250|UniProtKB:P50135, ECO:0000255|PROSITE-
CC         ProRule:PRU00929};
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}.
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DR   EMBL; BT021490; AAX46337.1; -; mRNA.
DR   EMBL; BC114060; AAI14061.1; -; mRNA.
DR   RefSeq; NP_001030511.1; NM_001035434.1.
DR   RefSeq; XP_010800392.1; XM_010802090.2.
DR   AlphaFoldDB; Q58DV7; -.
DR   SMR; Q58DV7; -.
DR   STRING; 9913.ENSBTAP00000019196; -.
DR   PaxDb; 9913-ENSBTAP00000019196; -.
DR   Ensembl; ENSBTAT00000019196.6; ENSBTAP00000019196.5; ENSBTAG00000014432.6.
DR   GeneID; 613413; -.
DR   KEGG; bta:613413; -.
DR   CTD; 3176; -.
DR   VEuPathDB; HostDB:ENSBTAG00000014432; -.
DR   VGNC; VGNC:29893; HNMT.
DR   eggNOG; ENOG502QQJ1; Eukaryota.
DR   GeneTree; ENSGT00390000002862; -.
DR   HOGENOM; CLU_058117_1_0_1; -.
DR   InParanoid; Q58DV7; -.
DR   OMA; LPQNDLC; -.
DR   OrthoDB; 5388438at2759; -.
DR   TreeFam; TF331080; -.
DR   Proteomes; UP000009136; Chromosome 2.
DR   Bgee; ENSBTAG00000014432; Expressed in monocyte and 98 other cell types or tissues.
DR   GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0046539; F:histamine N-methyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0001695; P:histamine catabolic process; ISS:UniProtKB.
DR   GO; GO:0032259; P:methylation; ISS:UniProtKB.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR016673; HHMT-like.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF13489; Methyltransf_23; 1.
DR   PIRSF; PIRSF016616; HHMT; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51597; SAM_HNMT; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..292
FT                   /note="Histamine N-methyltransferase"
FT                   /id="PRO_0000084019"
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         142
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00929"
FT   BINDING         283
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00929"
SQ   SEQUENCE   292 AA;  33646 MW;  F86A32390137EECC CRC64;
     MASSMRSLFT DHSRYVESFR RFLSNSTEHQ CMQEFMDKKL PGIIARIGDI KSEIKILSIG
     GGAGEIDLQI LSKVQAQYPG VHIINEVVEP SAEQITKYKE LVAKTSNLEN IKFAWHKETS
     SEYQNRMMEK KELQRWDFIH MIQMLYYVKD IPATLKFFHS LLATNAKILI IIVSGASSWQ
     KLWEKYGSRL PRNDLCQYVT SSDLTQMLDK LGIKYEYYDL LSTMDISDCF IDGNENGDLL
     WDFLTETCNF NTTAPPDLKA EIMKDLQKPE FSIKKEGKVL FNNSLSFIVV EA
//