ID TPMT_LYNRU Reviewed; 245 AA. AC Q3BCR9; DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 22-NOV-2005, sequence version 1. DT 08-APR-2008, entry version 17. DE Thiopurine S-methyltransferase (EC 2.1.1.67) (Thiopurine DE methyltransferase). GN Name=TPMT; OS Lynx rufus (Bobcat) (Felis rufus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; OC Felinae; Lynx. OX NCBI_TaxID=61384; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=16220112; 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 https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY819776; AAX37638.1; -; mRNA. DR SMR; Q3BCR9; 17-245. 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_0000220104. 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; 28333 MW; E233F17546F11D1C CRC64; MDDTSTLIDV KEYPDTEVQK NRVLTLEEWR EKWVDGKIGF HQEQGHQLLK KHLDTFLKGE NVLRVFFPLC GKAVEMKWFA DRGHCVVGVE ISELGIREFF TEQNLSYSEE PIMEIPGAKV FKSSSGNISL YCCNLFDLPR VNIGKFDRIW DRGALVAVNP GDRKCYTDIM LSLTRKGFRY LLAVLSYDPT KHPGPPFYVP DAEIKNLFGS TCNIHCLEKV DVFEERHKSW GIDYIVEKLY LLTEK //