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UniProtKB/Swiss-Prot entry Q8JZL3


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name THTPA_MOUSE
Primary accession number Q8JZL3
Secondary accession numbers Q3V1G2 Q8C3P9
Integrated into Swiss-Prot on October 3, 2003
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    November 25, 2008 (Entry version 50)
Name and origin of the protein
Protein name Thiamine-triphosphatase
Synonyms ThTPase
EC 3.6.1.28
Gene name
Name: Thtpa
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6;
Lakaye B., Coumans B., Makarchikov A., Grisar T., Bettendorff L.;
"Cloning and expression of mouse thiamine triphosphatase cDNA.";
Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Skin;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N;
TISSUE=Mammary gland;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF432864; AAM22405.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK132479; BAE21189.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC025562; AAH25562.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_694723.1; -.
UniGene Mm.319204
3D structure databases
PDB
2JMU; NMR; -; A=2-224.[ExPASy / RCSB / EBI]
PDBsum 2JMU; -.
ModBase Q8JZL3.
PTM databases
PhosphoSite Q8JZL3; -.
Organism-specific databases
MGI MGI:2446078; Thtpa.
Gene expression databases
CleanEx MM_THTPA; -.
GermOnline ENSMUSG00000045691; Mus musculus.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0004016; Molecular function: adenylate cyclase activity (inferred from electronic annotation from InterPro).
GO:0050333; Molecular function: thiamin-triphosphatase activity (inferred from sequence or structural similarity from UniProtKB).
GO:0006171; Biological process: cAMP biosynthetic process (inferred from electronic annotation from InterPro).
GO:0006772; Biological process: thiamin metabolic process (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR008172; Adenylate_cyclase.
IPR012177; ThTPase.
Graphical view of domain structure.
PANTHER PTHR14586; ThTPase; 1.
Pfam PF01928; CYTH; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF036561; ThTPase; 1.
ProDom PD009560; CyaB; 1.
[Domain structure / List of seq. sharing at least 1 domain]
ProtoNet Q8JZL3.
Genome annotation databases
Ensembl ENSMUSG00000045691; Mus musculus. [Contig view]
GeneID 105663; -.
KEGG mmu:105663; -.
Phylogenomic databases
HOGENOM Q8JZL3; -.
HOVERGEN Q8JZL3; -.
Other
NextBio 357818; -.
SOURCE Thtpa; Mus musculus.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Cytoplasm; Hydrolase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   224  223     Thiamine-triphosphatase. PRO_0000221492
MOD_RES   2     2        N-acetylalanine (By similarity). 
STRAND   3    14  12      
HELIX   18    25  8      
STRAND   28    41  14      
HELIX   46    49  4      
STRAND   53    57  5      
TURN   58    60  3      
STRAND   61    66  6      
STRAND   80    82  3      
HELIX   85    96  12      
HELIX   106   113  8      
STRAND   116   131  16      
STRAND   141   149  9      
TURN   150   152  3      
STRAND   153   163  11      
HELIX   165   167  3      
HELIX   168   182  15      
STRAND   183   185  3      
HELIX   193   201  9      
HELIX   203   212  10      
Sequence information
Length: 224 AA [This is the length of the unprocessed precursor] Molecular weight: 24264 Da [This is the MW of the unprocessed precursor] CRC64: D33C844FDA8277D9 [This is a checksum on the sequence]
        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 

Q8JZL3 in FASTA format

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