ID   TPMT_FELCA              Reviewed;         245 AA.
AC   Q6EIC1; Q6EIC2;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, 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   Felis catus (Cat) (Felis silvestris catus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX   NCBI_TaxID=9685;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND VARIANTS SER-7; ILE-8;
RP   ASN-15; LEU-113 AND VAL-233.
RX   PubMed=14610243; DOI=10.1124/jpet.103.059055;
RA   Salavaggione O.E., Yang C., Kidd L.B., Thomae B.A., Pankratz V.S.,
RA   Trepanier L.A., Weinshilboum R.M.;
RT   "Cat red blood cell thiopurine S-methyltransferase: companion animal
RT   pharmacogenetics.";
RL   J. Pharmacol. Exp. Ther. 308:617-626(2004).
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; AY324659; AAP79318.1; -; mRNA.
DR   EMBL; AY324667; AAP79305.1; -; Genomic_DNA.
DR   EMBL; AY324660; AAP79305.1; JOINED; Genomic_DNA.
DR   EMBL; AY324661; AAP79305.1; JOINED; Genomic_DNA.
DR   EMBL; AY324662; AAP79305.1; JOINED; Genomic_DNA.
DR   EMBL; AY324664; AAP79305.1; JOINED; Genomic_DNA.
DR   EMBL; AY324666; AAP79305.1; JOINED; Genomic_DNA.
DR   EMBL; AY324665; AAP79305.1; JOINED; Genomic_DNA.
DR   EMBL; AY324663; AAP79305.1; JOINED; Genomic_DNA.
DR   RefSeq; NP_001009836.1; NM_001009836.1.
DR   AlphaFoldDB; Q6EIC1; -.
DR   SMR; Q6EIC1; -.
DR   STRING; 9685.ENSFCAP00000003933; -.
DR   GeneID; 493759; -.
DR   KEGG; fca:493759; -.
DR   CTD; 7172; -.
DR   InParanoid; Q6EIC1; -.
DR   Proteomes; UP000011712; 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_0000220099"
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"
FT   VARIANT         7
FT                   /note="L -> S"
FT                   /evidence="ECO:0000269|PubMed:14610243"
FT   VARIANT         8
FT                   /note="T -> I"
FT                   /evidence="ECO:0000269|PubMed:14610243"
FT   VARIANT         15
FT                   /note="D -> N (reduced activity)"
FT                   /evidence="ECO:0000269|PubMed:14610243"
FT   VARIANT         113
FT                   /note="M -> L"
FT                   /evidence="ECO:0000269|PubMed:14610243"
FT   VARIANT         233
FT                   /note="D -> V (reduced activity)"
FT                   /evidence="ECO:0000269|PubMed:14610243"
SQ   SEQUENCE   245 AA;  28321 MW;  56A82A18F02CE113 CRC64;
     MDDTSTLTDV KEYPDTEVQK NRVLTLEEWR EKWVDGKIGF HQEQGHQLLK KHLDTFLKGE
     NVLRVFFPLC GKAVEMKWFA DRGHCVVGVE ISELGIREFF TEQNLSYSEE PIMEIPGAKV
     FKSSSGNISL YCCNLFDLPR VNIGKFDRIW DRGALVAVNP GDRKCYTDIM LSLTRKGFRY
     LLAVLSYDPT KHPGPPFYVP DAEIKNLFGS TCNIHCLEKV DVFEERHKSW GIDYIVEKLY
     LLTEK