[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=Sprague-Dawley; Krynetski E.Y., Fessing M.Y., Evans W.E.; Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.

Comments

FUNCTION: Catalyzes the S-methylation of thiopurine drugs such as 6-mercaptopurine.
CATALYTIC ACTIVITY: S-adenosyl-L-methionine + a thiopurine = S-adenosyl-L-homocysteine + a thiopurine S-methylether.
SUBUNIT: Monomer (By similarity).
SUBCELLULAR LOCATION: Cytoplasm.
SIMILARITY: Belongs to the methyltransferase superfamily. TPMT family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF120100; AAD17293.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

XP_001058187.1; -.

UniGene

Rn.112598

3D structure databases

SMR

Q9Z0T0; 10-240.

ModBase

Q9Z0T0.

Organism-specific databases

RGD

620089; Tpmt.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from InterPro).
GO:0008119;	Molecular function: thiopurine S-methyltransferase activity (inferred from electronic annotation from InterPro).
GO:0008152;	Biological process: metabolic process (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR008854; Thiopurine_S-MeTrfase.
IPR016822; Thiopurine_S-MeTrfase_sub.
Graphical view of domain structure.

Pfam

PF05724; TPMT; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF023956; Thiopurine_S-methyltransferase; 1.

ProtoNet

Q9Z0T0.

Genome annotation databases

GeneID

681730; -.

KEGG

rno:681730; -.

Phylogenomic databases

HOVERGEN

Q9Z0T0; -.

Other

NextBio

721509; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cytoplasm; Methyltransferase; S-adenosyl-L-methionine; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 240`	`240`	`Thiopurine S-methyltransferase.`	`PRO_0000220113`
`BINDING`	`28 28`		`S-adenosyl-L-methionine (By similarity).`
`BINDING`	`64 64`		`S-adenosyl-L-methionine; via carbonyl oxygen (By similarity).`
`BINDING`	`85 85`		`S-adenosyl-L-methionine (By similarity).`
`BINDING`	`147 147`		`S-adenosyl-L-methionine (By similarity).`

Sequence information

Length: 240 AA [This is the length of the unprocessed precursor]

Molecular weight: 27692 Da [This is the MW of the unprocessed precursor]

CRC64: 04608B546BBDC1E3 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSLGIKEHPD AEVQKNRVLT LDDWQDKWVT RHIAFHQEQG HQLLKKHFDT FLKGQSGLRV 

        70         80         90        100        110        120 
FFPLCGKAIE MKWFADRGHT VVGVEISEIG IREFFAEQNL SYTEEPLTEI AGAKVFKSSS 

       130        140        150        160        170        180 
GNISLYCCSI FDLPRANIGK FDRIWDRGAL VAVNPGDRDR YADIILSLLR KGYHYLLVVL 

       190        200        210        220        230        240 
SYDPTKHTGP PFYVPDAELK KLFGTKCNMQ CLEEVDALEE RHKTWGVDYF FEKLYLLTEK

Q9Z0T0 in FASTA format

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View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools