Reviewed, UniProtKB/Swiss-Prot Q3BCQ8 (TPMT_RABIT)

Names and origin

Protein names

Recommended name:
    Thiopurine S-methyltransferase
    EC=2.1.1.67
Alternative name(s):
    Thiopurine methyltransferase

Gene names

Name:

TPMT

Organism

Oryctolagus cuniculus (Rabbit)

Taxonomic identifier

9986 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

Protein attributes

Sequence length	245 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level.

General annotation (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 structure	Monomer By similarity.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the methyltransferase superfamily. TPMT family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
PTM	Acetylation
Gene Ontology (GO)
Biological process	metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	thiopurine S-methyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 245	245	Thiopurine S-methyltransferase		PRO_0000220112
Sites
	Binding site	33	1	S-adenosyl-L-methionine By similarity
	Binding site	69	1	S-adenosyl-L-methionine; via carbonyl oxygen By similarity
	Binding site	90	1	S-adenosyl-L-methionine By similarity
	Binding site	152	1	S-adenosyl-L-methionine By similarity
Amino acid modifications
	Modified residue	58	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q3BCQ8-1 [UniParc]. Last modified November 22, 2005. Version 1. Checksum: C3973A3E662AD044	FASTA	245	28,283
	10 20 30 40 50 60 MDDARTLLDI KEYPDTEVQK NRVLTLEEWQ DKWVSHKIGF HQEQGHKLLK KHLDAFLKGE 70 80 90 100 110 120 SGLRVFFPLC GKAVEMKWFA DRGHSVVGVE ISELGIREFF SEQNLSYSEE PITEVPGAKV 130 140 150 160 170 180 FKSSAGNISL YCCSIFDLPR VNIGKFDRIW DRGALVAVNP SDRKRYAAVM LSLLRKGFQY 190 200 210 220 230 240 LLAVLSYDPT KHAGPPFYVP DAEIKMLFDT KCKIHCLEKV DAFEERHKSW GIDYIFEKLY LLTEK

References

[1]	"Thiopurine S-methyltransferase pharmacogenetics: variant allele functional and comparative genomics." Salavaggione O.E., Wang L., Wiepert M., Yee V.C., Weinshilboum R.M. Pharmacogenet. Genomics 15:801-815(2005) [PubMed: 16220112] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY827084 mRNA. Translation: AAX37648.1.
RefSeq	NP_001076153.1.
UniGene	Ocu.3344
3D structure databases
SMR	Q3BCQ8. Positions 14-245.
ModBase	Search...
Genome annotation databases
GeneID	100009411.
Organism-specific databases
CTD	100009411.
Phylogenomic databases
eggNOG	maNOG10315.
HOVERGEN	Q3BCQ8.
Enzyme and pathway databases
BRENDA	2.1.1.67. 255.
Family and domain databases
InterPro	IPR008854. Thiopurine_S-MeTrfase. IPR016822. Thiopurine_S-MeTrfase_sub. [Graphical view]
Pfam	PF05724. TPMT. 1 hit. [Graphical view]
PIRSF	PIRSF023956. Thiopurine_S-methyltransferase. 1 hit.
ProtoNet	Search...

Entry information

Entry name

TPMT_RABIT

Accession

Primary (citable) accession number: Q3BCQ8

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	November 22, 2005
Last modified:	January 19, 2010
This is version 27 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)