ID   TPMT_RABIT              Reviewed;         245 AA.
AC   Q3BCQ8;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   16-JUN-2009, entry version 24.
DE   RecName: Full=Thiopurine S-methyltransferase;
DE            EC=2.1.1.67;
DE   AltName: Full=Thiopurine methyltransferase;
GN   Name=TPMT;
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 [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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AY827084; AAX37648.1; -; mRNA.
DR   RefSeq; NP_001076153.1; -.
DR   UniGene; Ocu.3344; -.
DR   SMR; Q3BCQ8; 17-245.
DR   GeneID; 100009411; -.
DR   HOVERGEN; Q3BCQ8; -.
DR   BRENDA; 2.1.1.67; 255.
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; S-adenosyl-L-methionine; Transferase.
FT   CHAIN         1    245       Thiopurine S-methyltransferase.
FT                                /FTId=PRO_0000220112.
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).
SQ   SEQUENCE   245 AA;  28283 MW;  C3973A3E662AD044 CRC64;
     MDDARTLLDI KEYPDTEVQK NRVLTLEEWQ DKWVSHKIGF HQEQGHKLLK KHLDAFLKGE
     SGLRVFFPLC GKAVEMKWFA DRGHSVVGVE ISELGIREFF SEQNLSYSEE PITEVPGAKV
     FKSSAGNISL YCCSIFDLPR VNIGKFDRIW DRGALVAVNP SDRKRYAAVM LSLLRKGFQY
     LLAVLSYDPT KHAGPPFYVP DAEIKMLFDT KCKIHCLEKV DAFEERHKSW GIDYIFEKLY
     LLTEK
//