Reviewed,
UniProtKB/Swiss-Prot Q8JZL3 (THTPA_MOUSE)
Last modified
June 16, 2009.
Version 56.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Thiamine-triphosphatase Short name=ThTPase EC=3.6.1.28 | ||
| Gene names |
| ||
| Organism | Mus musculus (Mouse) | ||
| Taxonomic identifier | 10090 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus |
Protein attributes
| Sequence length | 224 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Hydrolase highly specific for thiamine triphosphate (ThTP) By similarity. |
| Catalytic activity | Thiamine triphosphate + H2O = thiamine diphosphate + phosphate. |
| Subunit structure | Monomer By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | Belongs to the ThTPase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Molecular function | Hydrolase |
| PTM | Acetylation |
| Technical term | 3D-structure |
| Gene Ontology (GO) | |
| Biological process | cAMP biosynthetic process Inferred from electronic annotation. Source: InterPro thiamin metabolic processInferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | adenylate cyclase activity Inferred from electronic annotation. Source: InterPro thiamin-triphosphatase activityInferred from sequence or structural similarity. Source: UniProtKB |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||||||||||||||||||||||||||||||||||
| Chain | 2 – 224 | 223 | Thiamine-triphosphatase | PRO_0000221492 | |||||||||||||||||||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||||||||||||||||||||
| Modified residue | 2 | 1 | N-acetylalanine By similarity | ||||||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 3 – 14 | 12 | |||||||||||||||||||||||||||||||||||||||
| Helix | 18 – 25 | 8 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 28 – 41 | 14 | |||||||||||||||||||||||||||||||||||||||
| Helix | 46 – 49 | 4 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 53 – 57 | 5 | |||||||||||||||||||||||||||||||||||||||
| Turn | 58 – 60 | 3 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 61 – 66 | 6 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 80 – 82 | 3 | |||||||||||||||||||||||||||||||||||||||
| Helix | 85 – 96 | 12 | |||||||||||||||||||||||||||||||||||||||
| Helix | 106 – 113 | 8 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 116 – 131 | 16 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 141 – 149 | 9 | |||||||||||||||||||||||||||||||||||||||
| Turn | 150 – 152 | 3 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 153 – 163 | 11 | |||||||||||||||||||||||||||||||||||||||
| Helix | 165 – 167 | 3 | |||||||||||||||||||||||||||||||||||||||
| Helix | 168 – 182 | 15 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 183 – 185 | 3 | |||||||||||||||||||||||||||||||||||||||
| Helix | 193 – 201 | 9 | |||||||||||||||||||||||||||||||||||||||
| Helix | 203 – 212 | 10 | |||||||||||||||||||||||||||||||||||||||
Sequences
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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. Hayashizaki Y.Science 309:1559-1563(2005) [PubMed: 16141072] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Mammary gland. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| AF432864 mRNA. Translation: AAM22405.1. AK132479 mRNA. Translation: BAE21189.1. BC025562 mRNA. Translation: AAH25562.1. | |||||||||||||
| IPI | IPI00128570. | ||||||||||||
| RefSeq | NP_694723.1. | ||||||||||||
| UniGene | Mm.319204 | ||||||||||||
3D structure databases | |||||||||||||
| |||||||||||||
| ModBase | Search... | ||||||||||||
PTM databases | |||||||||||||
| PhosphoSite | Q8JZL3. | ||||||||||||
Proteomic databases | |||||||||||||
| PRIDE | Q8JZL3. | ||||||||||||
Genome annotation databases | |||||||||||||
| Ensembl | ENSMUSG00000045691. Mus musculus. [Contig view] | ||||||||||||
| GeneID | 105663. | ||||||||||||
| KEGG | mmu:105663. | ||||||||||||
Organism-specific databases | |||||||||||||
| MGI | MGI:2446078. Thtpa. | ||||||||||||
Phylogenomic databases | |||||||||||||
| HOGENOM | Q8JZL3. | ||||||||||||
| HOVERGEN | Q8JZL3. | ||||||||||||
| OMA | Q8JZL3. EVERKFV. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BRENDA | 3.6.1.28. 244. | ||||||||||||
Gene expression databases | |||||||||||||
| Bgee | Q8JZL3. | ||||||||||||
| CleanEx | MM_THTPA. | ||||||||||||
| GermOnline | ENSMUSG00000045691. Mus musculus. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR008172. Adenylate_cyclase. IPR012177. ThTPase. [Graphical view] | ||||||||||||
| PANTHER | PTHR14586. ThTPase. 1 hit. | ||||||||||||
| Pfam | PF01928. CYTH. 1 hit. [Graphical view] | ||||||||||||
| PIRSF | PIRSF036561. ThTPase. 1 hit. | ||||||||||||
| ProDom | PD009560. CyaB. 1 hit. [Graphical view] [Entries sharing at least one domain] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other Resources | |||||||||||||
| NextBio | 357818. | ||||||||||||
| SOURCE | Search... | ||||||||||||
Entry information
| Entry name | THTPA_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q8JZL3 Secondary accession number(s): Q3V1G2, Q8C3P9 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


