TPMT_PONPY
ID TPMT_PONPY Reviewed; 245 AA.
AC Q5RBJ3; Q3BCQ9;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Thiopurine S-methyltransferase;
DE EC=2.1.1.67;
DE AltName: Full=Thiopurine methyltransferase;
GN Name=TPMT;
OS Pongo pygmaeus (Bornean orangutan).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9600;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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; AY827083; AAX37647.1; -; mRNA.
DR EMBL; CR858654; CAH90867.1; -; mRNA.
DR AlphaFoldDB; Q5RBJ3; -.
DR SMR; Q5RBJ3; -.
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; Phosphoprotein;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..245
FT /note="Thiopurine S-methyltransferase"
FT /id="PRO_0000220111"
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"
FT CONFLICT 112
FT /note="V -> I (in Ref. 1; AAX37647)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 245 AA; 28242 MW; 47D893B0E1E0A01C CRC64;
MDGIRTSLDI EEYSDTEVQK NQVLTLEEWQ DKWVNGNTAF HQEQGHRLLK KHLDTFLKGE
SGLRVFFPLC GKAVEMKWFA DRGHSVVGVE ISELGIREFF TEQNLSYSEE PVTEIPGTKI
FKSSSGNISL YCCSIFDLPR TNIGKFDMIW DRGALVAINP GDRKCYADTM LSLLGKKFQY
LLCVLSYDPT KHPGPPFYVP HAEIERLFGK ICNIHCLEKV DAFEERHKSW GIDYLFEKLY
LLTEK
