Reviewed, UniProtKB/Swiss-Prot Q8JZL3 (THTPA_MOUSE)

Names and origin

Protein names

Recommended name:
    Thiamine-triphosphatase
      Short name=ThTPase
    EC=3.6.1.28

Gene names

Name:

Thtpa

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 process Inferred 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 activity Inferred 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

1

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224

Helix Strand Turn

Details...

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

	Sequence		Length	Mass (Da)
	Q8JZL3-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: D33C844FDA8277D9	FASTA	224	24,264
	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

References

	« Hide 'large scale' referencesShow '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. , 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: 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

EMBLGenBankDDBJ

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

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2JMU	NMR	-	A	2-223	[»]

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

Integrated into UniProtKB/Swiss-Prot:	October 3, 2003
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 56 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)