ID   TPMT_GORGO              Reviewed;         245 AA.
AC   Q3BCR3;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Thiopurine S-methyltransferase;
DE            EC=2.1.1.67;
DE   AltName: Full=Thiopurine methyltransferase;
GN   Name=TPMT;
OS   Gorilla gorilla gorilla (Western lowland gorilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Gorilla.
OX   NCBI_TaxID=9595;
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; AY827079; AAX37643.1; -; mRNA.
DR   RefSeq; XP_004043361.1; XM_004043313.2.
DR   RefSeq; XP_018884930.1; XM_019029385.1.
DR   AlphaFoldDB; Q3BCR3; -.
DR   BMRB; Q3BCR3; -.
DR   SMR; Q3BCR3; -.
DR   STRING; 9593.ENSGGOP00000015758; -.
DR   Ensembl; ENSGGOT00000016209; ENSGGOP00000015758; ENSGGOG00000016155.
DR   GeneID; 101127379; -.
DR   KEGG; ggo:101127379; -.
DR   CTD; 7172; -.
DR   eggNOG; ENOG502QSF5; Eukaryota.
DR   GeneTree; ENSGT00390000016823; -.
DR   HOGENOM; CLU_085515_2_0_1; -.
DR   InParanoid; Q3BCR3; -.
DR   OMA; LWCGDFF; -.
DR   OrthoDB; 1590477at2759; -.
DR   Proteomes; UP000001519; Chromosome 6.
DR   Bgee; ENSGGOG00000016155; Expressed in adult mammalian kidney and 6 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; Phosphoprotein;
KW   Reference proteome; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..245
FT                   /note="Thiopurine S-methyltransferase"
FT                   /id="PRO_0000220100"
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         14
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P51580"
FT   MOD_RES         58
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P51580"
SQ   SEQUENCE   245 AA;  28146 MW;  190E70BBF7B1D11B CRC64;
     MDGTRTSLDI EEYSDTEVQK NQVLTLEEWQ DKWVNGKTAF HQEQGHQLLK KHLDTFLKGK
     SGLRVFFPLC GKAVEMKWFA DRGHSVVGVE ISELGIQEFF TEQNLSYSEE PITEIPGTKV
     FKSSSGNISL YCCSIFDLPR TNIGKFDMIW DRGALVAINP GDRKCYADTM LSLLGKKFQY
     LLCVLSYDPT KHPGPPFYVP HAEIERLFGK ICNIRCLEKV DAFEERHKSW GIDCLFEKLY
     LLTEK