ID   TPMT_HORSE              Reviewed;         245 AA.
AC   Q3BCR6;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   16-JUN-2009, entry version 25.
DE   RecName: Full=Thiopurine S-methyltransferase;
DE            EC=2.1.1.67;
DE   AltName: Full=Thiopurine methyltransferase;
GN   Name=TPMT;
OS   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=16220112; DOI=10.1097/01.fpc.0000174788.69991.6b;
RA   Salavaggione O.E., Wang L., Wiepert M., Yee V.C., Weinshilboum R.M.;
RT   "Thiopurine S-methyltransferase pharmacogenetics: variant allele
RT   functional and comparative genomics.";
RL   Pharmacogenet. Genomics 15:801-815(2005).
CC   -!- FUNCTION: Catalyzes the S-methylation of thiopurine drugs such as
CC       6-mercaptopurine.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + a thiopurine = S-
CC       adenosyl-L-homocysteine + a thiopurine S-methylether.
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. TPMT
CC       family.
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DR   EMBL; AY827076; AAX37640.1; -; mRNA.
DR   RefSeq; NP_001075374.1; -.
DR   UniGene; Eca.3077; -.
DR   SMR; Q3BCR6; 17-245.
DR   Ensembl; ENSECAG00000013653; Equus caballus.
DR   GeneID; 100034066; -.
DR   KEGG; ecb:100034066; -.
DR   HOVERGEN; Q3BCR6; -.
DR   BRENDA; 2.1.1.67; 1464.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008119; F:thiopurine S-methyltransferase activity; IEA:EC.
DR   GO; GO:0008152; P:metabolic process; IEA:InterPro.
DR   InterPro; IPR008854; Thiopurine_S-MeTrfase.
DR   InterPro; IPR016822; Thiopurine_S-MeTrfase_sub.
DR   Pfam; PF05724; TPMT; 1.
DR   PIRSF; PIRSF023956; Thiopurine_S-methyltransferase; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Methyltransferase; Phosphoprotein; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN         1    245       Thiopurine S-methyltransferase.
FT                                /FTId=PRO_0000220101.
FT   BINDING      33     33       S-adenosyl-L-methionine (By similarity).
FT   BINDING      69     69       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen (By similarity).
FT   BINDING      90     90       S-adenosyl-L-methionine (By similarity).
FT   BINDING     152    152       S-adenosyl-L-methionine (By similarity).
FT   MOD_RES      14     14       Phosphoserine (By similarity).
SQ   SEQUENCE   245 AA;  28118 MW;  7CBB27DD98CB97B7 CRC64;
     MDGTRTVLDI KEYSDSEVQK NRVLTLEEWQ GKWVTGKTIF HQEQGHQLLK KHLDAFLKGE
     SGLKVFFPLC GKAVEMKWFA DRGHSVVGVE ISELGIREFF TEQNLSYSEE PIIEIPGAKV
     FKSSSGNISL YCCNIFDLPR TNIGKFDRIW DRGALVAVNP GDRKRYVDIM LSLTRKGFHY
     LLAVLSYDPT KHAGPPFFVS DAEVKRLFDS VCNIRCLEKV DALEERHKSW GIDYLVETLY
     LFTEK
//