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Q6EIC1 (TPMT_FELCA) Reviewed, UniProtKB/Swiss-Prot

Last modified October 19, 2011. Version 37. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Thiopurine S-methyltransferase

EC=2.1.1.67
Alternative name(s):
Thiopurine methyltransferase
Gene names
Name:TPMT
OrganismFelis catus (Cat) (Felis silvestris catus)
Taxonomic identifier9685 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraFeliformiaFelidaeFelinaeFelis

Protein attributes

Sequence length245 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes the S-methylation of thiopurine drugs such as 6-mercaptopurine By similarity.

Catalytic activity

S-adenosyl-L-methionine + a thiopurine = S-adenosyl-L-homocysteine + a thiopurine S-methylether.

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the methyltransferase superfamily. TPMT family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   LigandS-adenosyl-L-methionine
   Molecular functionMethyltransferase
Transferase
   PTMAcetylation
Gene Ontology (GO)
   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionthiopurine S-methyltransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 245245Thiopurine S-methyltransferase
PRO_0000220099

Sites

Binding site331S-adenosyl-L-methionine By similarity
Binding site691S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site901S-adenosyl-L-methionine By similarity
Binding site1521S-adenosyl-L-methionine By similarity

Amino acid modifications

Modified residue581N6-acetyllysine By similarity

Natural variations

Natural variant71L → S. Ref.1
Natural variant81T → I. Ref.1
Natural variant151D → N Reduced activity. Ref.1
Natural variant1131M → L. Ref.1
Natural variant2331D → V Reduced activity. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q6EIC1 [UniParc].

Last modified August 16, 2004. Version 1.
Checksum: 56A82A18F02CE113

FASTA24528,321
        10         20         30         40         50         60 
MDDTSTLTDV KEYPDTEVQK NRVLTLEEWR EKWVDGKIGF HQEQGHQLLK KHLDTFLKGE 

        70         80         90        100        110        120 
NVLRVFFPLC GKAVEMKWFA DRGHCVVGVE ISELGIREFF TEQNLSYSEE PIMEIPGAKV 

       130        140        150        160        170        180 
FKSSSGNISL YCCNLFDLPR VNIGKFDRIW DRGALVAVNP GDRKCYTDIM LSLTRKGFRY 

       190        200        210        220        230        240 
LLAVLSYDPT KHPGPPFYVP DAEIKNLFGS TCNIHCLEKV DVFEERHKSW GIDYIVEKLY 


LLTEK 

« Hide

References

[1]"Cat red blood cell thiopurine S-methyltransferase: companion animal pharmacogenetics."
Salavaggione O.E., Yang C., Kidd L.B., Thomae B.A., Pankratz V.S., Trepanier L.A., Weinshilboum R.M.
J. Pharmacol. Exp. Ther. 308:617-626(2004) [PubMed: 14610243] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], VARIANTS SER-7; ILE-8; ASN-15; LEU-113 AND VAL-233.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY324659 mRNA. Translation: AAP79318.1.
AY324667 expand/collapse EMBL AC list , AY324660, AY324661, AY324662, AY324664, AY324666, AY324665, AY324663 Genomic DNA. Translation: AAP79305.1.
RefSeqNP_001009836.1. NM_001009836.1.

3D structure databases

ProteinModelPortalQ6EIC1.
SMRQ6EIC1. Positions 17-245.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID493759.

Organism-specific databases

CTD7172.

Phylogenomic databases

eggNOGmaNOG10315.
HOVERGENHBG003037.

Family and domain databases

InterProIPR008854. Thiopurine_S-MeTrfase.
IPR016822. Thiopurine_S-MeTrfase_sub.
[Graphical view]
PANTHERPTHR10259. PTHR10259. 1 hit.
PfamPF05724. TPMT. 1 hit.
[Graphical view]
PIRSFPIRSF023956. Thiopurine_S-methyltransferase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameTPMT_FELCA
AccessionPrimary (citable) accession number: Q6EIC1
Secondary accession number(s): Q6EIC2
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: August 16, 2004
Last modified: October 19, 2011
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families