ID   INMT_RABIT              Reviewed;         263 AA.
AC   O97972;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   16-JUN-2009, entry version 47.
DE   RecName: Full=Indolethylamine N-methyltransferase;
DE            Short=Indolamine N-methyltransferase;
DE            EC=2.1.1.49;
DE   AltName: Full=Aromatic alkylamine N-methyltransferase;
DE            Short=Arylamine N-methyltransferase;
DE            Short=Amine N-methyltransferase;
GN   Name=INMT;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
OC   Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 1-129,
RP   AND CHARACTERIZATION.
RC   TISSUE=Lung;
RX   MEDLINE=99069450; PubMed=9852119; DOI=10.1074/jbc.273.51.34502;
RA   Thompson M.A., Weinshilboum R.M.;
RT   "Rabbit lung indolethylamine N-methyltransferase. cDNA and gene
RT   cloning and characterization.";
RL   J. Biol. Chem. 273:34502-34510(1998).
RN   [2]
RP   CHARACTERIZATION.
RC   TISSUE=Lung;
RX   MEDLINE=82182968; PubMed=7074100; DOI=10.1021/bi00535a054;
RA   Irace G., Colonna G., Camardella M., Della Pietra G., Porta R.;
RT   "Purification and molecular properties of rabbit lung indolamine N-
RT   methyltransferase.";
RL   Biochemistry 21:1464-1470(1982).
CC   -!- FUNCTION: Catalyzes the N-methylation of tryptamine and
CC       structurally related compounds (Potential).
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + an amine = S-
CC       adenosyl-L-homocysteine + a methylated amine.
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Highly expressed in lung, also detected in
CC       liver and at very low levels in brain.
CC   -!- SIMILARITY: Belongs to the NNMT/PNMT/TEMT family.
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DR   EMBL; AF077828; AAC97492.1; -; Genomic_DNA.
DR   EMBL; AF077827; AAC97492.1; JOINED; Genomic_DNA.
DR   EMBL; AF077826; AAC97491.1; -; mRNA.
DR   RefSeq; NP_001075512.1; -.
DR   UniGene; Ocu.2318; -.
DR   HSSP; P11086; 1HNN.
DR   SMR; O97972; 5-261.
DR   GeneID; 100008695; -.
DR   HOVERGEN; O97972; -.
DR   BRENDA; 2.1.1.49; 255.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030748; F:amine N-methyltransferase activity; IEA:EC.
DR   InterPro; IPR000940; NNMT_TEMT_trans.
DR   PANTHER; PTHR10867; NNMT_TEMT_trans; 1.
DR   Pfam; PF01234; NNMT_PNMT_TEMT; 1.
DR   PIRSF; PIRSF000384; PNMTase; 1.
DR   PROSITE; PS01100; NNMT_PNMT_TEMT; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Methyltransferase;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN         1    263       Indolethylamine N-methyltransferase.
FT                                /FTId=PRO_0000159715.
FT   REGION       63     64       S-adenosyl-L-methionine binding (By
FT                                similarity).
FT   REGION      142    143       S-adenosyl-L-methionine binding (By
FT                                similarity).
FT   BINDING      20     20       S-adenosyl-L-methionine (By similarity).
FT   BINDING      25     25       S-adenosyl-L-methionine (By similarity).
FT   BINDING      69     69       S-adenosyl-L-methionine (By similarity).
FT   BINDING      85     85       S-adenosyl-L-methionine (By similarity).
FT   BINDING      90     90       S-adenosyl-L-methionine (By similarity).
FT   BINDING     163    163       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen (By similarity).
SQ   SEQUENCE   263 AA;  28955 MW;  42F368414BE8B459 CRC64;
     MEGGFTGGDE YQKHFLPRDY LNTYYSFQSG PSPEAEMLKF NLECLHKTFG PGGLQGDTLI
     DIGSGPTIYQ VLAACESFKD ITLSDFTDRN REELAKWLKK EPGAYDWTPA LKFACELEGN
     SGRWQEKAEK LRATVKRVLK CDANLSNPLT PVVLPPADCV LTLLAMECAC CSLDAYRAAL
     RNLASLLKPG GHLVTTVTLQ LSSYMVGERE FSCVALEKEE VEQAVLDAGF DIEQLLYSPQ
     SYSASTAPNR GVCFLVARKK PGS
//