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Q8JZL3 (THTPA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Thiamine-triphosphatase

Short name=ThTPase
EC=3.6.1.28
Gene names
Name:Thtpa
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length224 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.4

Catalytic activity

Thiamine triphosphate + H2O = thiamine diphosphate + phosphate. Ref.4

Cofactor

Binds 1 Mg2+ ion per subunit. Ref.4

Subunit structure

Monomer. Ref.4

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the ThTPase family.

Contains 1 CYTH domain.

Biophysicochemical properties

pH dependence:

Optimum pH is 7.5-9.5. Ref.4

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 224223Thiamine-triphosphatase
PRO_0000221492

Regions

Domain5 – 201197CYTH

Sites

Metal binding71Magnesium
Metal binding91Magnesium
Metal binding1451Magnesium
Metal binding1571Magnesium
Metal binding1591Magnesium
Binding site111Substrate
Binding site551Substrate
Binding site571Substrate
Binding site651Substrate
Binding site1251Substrate
Binding site1571Substrate By similarity
Binding site1931Substrate

Amino acid modifications

Modified residue21N-acetylalanine By similarity

Secondary structure

................................. 224
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8JZL3 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: D33C844FDA8277D9

FASTA22424,264
        10         20         30         40         50         60 
MAQGLIEVER KFAPGPDTEE RLQELGATLE HRVTFRDTYY DTSELSLMLS DHWLRQREGS 

        70         80         90        100        110        120 
GWELKCPGVT GVSGPHNEYV EVTSEAAIVA QLFELLGSGE QKPAGVAAVL GSLKLQEVAS 

       130        140        150        160        170        180 
FITTRSSWKL ALSGAHGQEP QLTIDLDSAD FGYAVGEVEA MVHEKAEVPA ALEKIITVSS 

       190        200        210        220 
MLGVPAQEEA PAKLMVYLQR FRPLDYQRLL EAASSGEATG DSAS 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and expression of mouse thiamine triphosphatase cDNA."
Lakaye B., Coumans B., Makarchikov A., Grisar T., Bettendorff L.
Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Skin.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Mammary gland.
[4]"Structural basis for the catalytic mechanism of mammalian 25-kDa thiamine triphosphatase."
Song J., Bettendorff L., Tonelli M., Markley J.L.
J. Biol. Chem. 283:10939-10948(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 2-223, SUBUNIT, MAGNESIUM-BINDING SITES, SUBSTRATE-BINDING SITES, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF432864 mRNA. Translation: AAM22405.1.
AK132479 mRNA. Translation: BAE21189.1.
BC025562 mRNA. Translation: AAH25562.1.
CCDSCCDS27108.1.
RefSeqNP_694723.1. NM_153083.5.
UniGeneMm.319204.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2JMUNMR-A2-224[»]
ProteinModelPortalQ8JZL3.
SMRQ8JZL3. Positions 2-224.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ8JZL3. 1 interaction.
MINTMINT-4137740.

PTM databases

PhosphoSiteQ8JZL3.

Proteomic databases

MaxQBQ8JZL3.
PaxDbQ8JZL3.
PRIDEQ8JZL3.

Protocols and materials databases

DNASU105663.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000050575; ENSMUSP00000056026; ENSMUSG00000045691.
GeneID105663.
KEGGmmu:105663.
UCSCuc007tyb.2. mouse.

Organism-specific databases

CTD79178.
MGIMGI:2446078. Thtpa.

Phylogenomic databases

eggNOGNOG42323.
GeneTreeENSGT00390000005996.
HOGENOMHOG000154571.
HOVERGENHBG057173.
InParanoidQ8JZL3.
KOK05307.
OMARDTYYDT.
OrthoDBEOG7288SN.
PhylomeDBQ8JZL3.
TreeFamTF333398.

Gene expression databases

BgeeQ8JZL3.
CleanExMM_THTPA.
GenevestigatorQ8JZL3.

Family and domain databases

Gene3D2.40.320.10. 1 hit.
InterProIPR023577. CYTH-like_domain.
IPR012177. ThTPase.
[Graphical view]
PANTHERPTHR14586. PTHR14586. 1 hit.
PfamPF01928. CYTH. 1 hit.
[Graphical view]
PIRSFPIRSF036561. ThTPase. 1 hit.
SUPFAMSSF55154. SSF55154. 1 hit.
PROSITEPS51707. CYTH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ8JZL3.
NextBio357818.
PROQ8JZL3.
SOURCESearch...

Entry information

Entry nameTHTPA_MOUSE
AccessionPrimary (citable) accession number: Q8JZL3
Secondary accession number(s): Q3V1G2, Q8C3P9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 97 of the entry and version 3 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot