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Reviewed, UniProtKB/Swiss-Prot Q8MKF1 (THTPA_BOVIN)

Last modified June 16, 2009. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Thiamine-triphosphatase
      Short name=ThTPase
    EC=3.6.1.28
Gene names
Name: THTPA
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length219 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Hydrolase highly specific for thiamine triphosphate (ThTP). Ref.1

Catalytic activity

Thiamine triphosphate + H2O = thiamine diphosphate + phosphate.

Subunit structure

Monomer. Ref.1

Subcellular location

Cytoplasm. Ref.1

Sequence similarities

Belongs to the ThTPase family.

Mass spectrometry

Molecular mass is 23892 Da from positions 2 - 219. Determined by ESI. Ref.1

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionHydrolase
   PTMAcetylation
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processcAMP biosynthetic process

Inferred from electronic annotation. Source: InterPro

thiamin metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionadenylate cyclase activity

Inferred from electronic annotation. Source: InterPro

thiamin-triphosphatase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 219218Thiamine-triphosphatase
PRO_0000221489

Amino acid modifications

Modified residue21N-acetylalanine

Sequences

Sequence LengthMass (Da)Tools
Q8MKF1-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 6E617AA2FDB7ACC3

FASTA21923,983
        10         20         30         40         50         60 
MAQGLIEVER KFVPGPSTEE RLQELGGTLE HRVTFRDSYY DTPELSLMRA DYWLRQREGS 

        70         80         90        100        110        120 
GWELKCPGAA GVSGPHTEYT ELTAEPSIVA QLCEVLGAEV PGAGGVAAVL GPLGLQLVAS 

       130        140        150        160        170        180 
FVTKRSAWKL VLSGADGEER LLRVDLDTAD FGYAVGEVEA LVHKEAEVPA ALEKIHHLSS 

       190        200        210 
LLGVLEQGRA PAKLIVYLQR FRPQDYQRLL EVYGSKEKP 

« Hide

References

« Hide 'large scale' references
[1]"Molecular characterization of a specific thiamine triphosphatase widely expressed in mammalian tissues."
Lakaye B., Makarchikov A.F., Antunes A.F., Zorzi W., Coumans B., De Pauw E., Wins P., Grisar T., Bettendorff L.
J. Biol. Chem. 277:13771-13777(2002) [PubMed: 11827967] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, CHARACTERIZATION, MASS SPECTROMETRY.
[2]NIH - Mammalian Gene Collection (MGC) project
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Fetal liver.

Cross-references

Sequence databases

AF432863 mRNA. Translation: AAM22404.1.
BC105468 mRNA. Translation: AAI05469.1.
IPIIPI00714789.
RefSeqNP_776895.1.
UniGeneBt.8966

3D structure databases

SMRQ8MKF1. Positions 2-217.
ModBaseSearch...

Genome annotation databases

EnsemblENSBTAG00000007097. Bos taurus. [Contig view]
GeneID282090.
KEGGbta:282090.

Phylogenomic databases

HOVERGENQ8MKF1.
OMAQ8MKF1. EVERKFV.

Enzyme and pathway databases

BRENDA3.6.1.28. 251.

Family and domain databases

InterProIPR008172. Adenylate_cyclase.
IPR012177. ThTPase.
[Graphical view]
PANTHERPTHR14586. ThTPase. 1 hit.
PfamPF01928. CYTH. 1 hit.
[Graphical view]
PIRSFPIRSF036561. ThTPase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameTHTPA_BOVIN
AccessionPrimary (citable) accession number: Q8MKF1
Secondary accession number(s): Q2KJ88
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 44 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents