ID   TPMT_BOVIN              Reviewed;         245 AA.
AC   Q17QQ2;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Thiopurine S-methyltransferase;
DE            EC=2.1.1.67;
DE   AltName: Full=Thiopurine methyltransferase;
GN   Name=TPMT;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Basal ganglia;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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 {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. TPMT family. {ECO:0000305}.
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DR   EMBL; BC118238; AAI18239.1; -; mRNA.
DR   RefSeq; NP_001068999.1; NM_001075531.1.
DR   RefSeq; XP_005223808.1; XM_005223751.3.
DR   RefSeq; XP_005223809.1; XM_005223752.3.
DR   RefSeq; XP_005223811.1; XM_005223754.3.
DR   AlphaFoldDB; Q17QQ2; -.
DR   SMR; Q17QQ2; -.
DR   STRING; 9913.ENSBTAP00000025698; -.
DR   PaxDb; Q17QQ2; -.
DR   PeptideAtlas; Q17QQ2; -.
DR   PRIDE; Q17QQ2; -.
DR   Ensembl; ENSBTAT00000025698; ENSBTAP00000025698; ENSBTAG00000019300.
DR   GeneID; 511644; -.
DR   KEGG; bta:511644; -.
DR   CTD; 7172; -.
DR   VEuPathDB; HostDB:ENSBTAG00000019300; -.
DR   VGNC; VGNC:36255; TPMT.
DR   eggNOG; ENOG502QSF5; Eukaryota.
DR   GeneTree; ENSGT00390000016823; -.
DR   HOGENOM; CLU_085515_2_0_1; -.
DR   InParanoid; Q17QQ2; -.
DR   OMA; LWCGDFF; -.
DR   OrthoDB; 1590477at2759; -.
DR   TreeFam; TF328951; -.
DR   Reactome; R-BTA-156581; Methylation.
DR   Reactome; R-BTA-9748787; Azathioprine ADME.
DR   Proteomes; UP000009136; Chromosome 23.
DR   Bgee; ENSBTAG00000019300; Expressed in ruminant reticulum and 105 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:1904047; F:S-adenosyl-L-methionine binding; IEA:Ensembl.
DR   GO; GO:0008119; F:thiopurine S-methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0006805; P:xenobiotic metabolic process; IEA:Ensembl.
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_0000278660"
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         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;  28335 MW;  C734333BEEC2828F CRC64;
     MGDSRALLDS EEYPNTEAQK DRVLTLEEWQ EKWVNHKTGF HQEQGHQLLK KYLDTFLKGE
     KALRVFFPLC GKAVEMKWFA DRGHSVVGVE ISELGIRDFF TEQNLSYSEE PIMEIPGAKI
     FKSSSGNISL YCCNLFDLPR ANIGKFDRIW DRGALVAVNP SDRKRYSDVM LSLTRPGFRY
     LLSVFSYDPT KHAGPPFYVT DGEVKKLFGS VCNIQCLEKV DVFEERHKSW GIDQIIERLY
     LFTEK