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   03-AUG-2022, entry version 72.
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; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; 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 functional
RT   and comparative genomics.";
RL   Pharmacogenet. Genomics 15:801-815(2005).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-adenosyl-L-methionine + a thiopurine = S-adenosyl-L-
CC         homocysteine + a thiopurine S-methylether.; EC=2.1.1.67;
CC         Evidence={ECO:0000250|UniProtKB:P51580};
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P51580}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. TPMT family. {ECO:0000305}.
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DR   EMBL; AY827084; AAX37648.1; -; mRNA.
DR   RefSeq; NP_001076153.1; NM_001082684.1.
DR   AlphaFoldDB; Q3BCQ8; -.
DR   SMR; Q3BCQ8; -.
DR   STRING; 9986.ENSOCUP00000003340; -.
DR   PRIDE; Q3BCQ8; -.
DR   GeneID; 100009411; -.
DR   KEGG; ocu:100009411; -.
DR   CTD; 7172; -.
DR   eggNOG; ENOG502QSF5; Eukaryota.
DR   InParanoid; Q3BCQ8; -.
DR   OrthoDB; 1590477at2759; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008119; F:thiopurine S-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   HAMAP; MF_00812; Thiopur_methtran; 1.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR025835; Thiopurine_S-MeTrfase.
DR   InterPro; IPR008854; TPMT.
DR   Pfam; PF05724; TPMT; 1.
DR   PIRSF; PIRSF023956; Thiopurine_S-methyltransferase; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51585; SAM_MT_TPMT; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Methyltransferase; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..245
FT                   /note="Thiopurine S-methyltransferase"
FT                   /id="PRO_0000220112"
FT   BINDING         29..40
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         40
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         69
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         90
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         134..135
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         152
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         58
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P51580"
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