ID   HNMT_CAVPO              Reviewed;         292 AA.
AC   Q9EST2;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, 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   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=Hartley; TISSUE=Brain;
RX   PubMed=11243563; DOI=10.1254/jjp.85.105;
RA   Kitanaka J., Kitanaka N., Tsujimura T., Kakihana M., Terada N.,
RA   Takemura M.;
RT   "Guinea pig histamine N-methyltransferase: cDNA cloning and mRNA
RT   distribution.";
RL   Jpn. J. Pharmacol. 85:105-108(2001).
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   -!- TISSUE SPECIFICITY: Expressed in jejunum, brain > lung, spleen, stomach
CC       > liver, kidney. {ECO:0000269|PubMed:11243563}.
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; AB032693; BAB13758.1; -; mRNA.
DR   RefSeq; NP_001166431.1; NM_001172960.2.
DR   AlphaFoldDB; Q9EST2; -.
DR   SMR; Q9EST2; -.
DR   STRING; 10141.ENSCPOP00000002230; -.
DR   BindingDB; Q9EST2; -.
DR   ChEMBL; CHEMBL4485; -.
DR   Ensembl; ENSCPOT00000002482.3; ENSCPOP00000002230.2; ENSCPOG00000002449.4.
DR   GeneID; 100135537; -.
DR   KEGG; cpoc:100135537; -.
DR   CTD; 3176; -.
DR   VEuPathDB; HostDB:ENSCPOG00000002449; -.
DR   eggNOG; ENOG502QQJ1; Eukaryota.
DR   GeneTree; ENSGT00390000002862; -.
DR   HOGENOM; CLU_058117_1_0_1; -.
DR   InParanoid; Q9EST2; -.
DR   OMA; LPQNDLC; -.
DR   OrthoDB; 5388438at2759; -.
DR   TreeFam; TF331080; -.
DR   PRO; PR:Q9EST2; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   Bgee; ENSCPOG00000002449; Expressed in hypothalamus and 12 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_0000084020"
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;  33712 MW;  1D7F79D84C11BF40 CRC64;
     MASSMRSLFS DHGRYFEAFR RFLNNSTEYQ CMREFMDKQL PGIIARIGGS KSEIKVLSIG
     GGAGEMDLHI LSKVKAQYPG VHIINEVVEP SAEQITKYKE LVAKTSNLEN IKFAWHKETS
     SEYQNRVMEQ KEIQKWDFIH MIQMLYYVDD IPATLKFFHS LLATNAKILI ILVSGKSGWL
     KFWKKYRSRL PQNDLCQYVT SFDIIQMLDS LGIKYQCYDL LSTMDITDCF IDGNENGELL
     WDFLTETCNF LTTAPPDLRA EIMKDLQGPE FIVRKEGKIL FDNSLSFITI EA
//