Q8JZL3 (THTPA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

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) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › 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. Ref.4
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the ThTPase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Magnesium Metal-binding
Molecular function	Hydrolase
PTM	Acetylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	dephosphorylation Inferred from electronic annotation. Source: Compara thiamine metabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleolus Inferred from electronic annotation. Source: Compara
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW 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

Sites

Metal binding

7

1

Magnesium

Metal binding

9

1

Magnesium

Metal binding

145

1

Magnesium

Metal binding

157

1

Magnesium

Metal binding

159

1

Magnesium

Binding site

11

1

Substrate

Binding site

55

1

Substrate

Binding site

57

1

Substrate

Binding site

65

1

Substrate

Binding site

125

1

Substrate

Binding site

193

1

Substrate

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 [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] [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.
+	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.

IPI

IPI00128570.

RefSeq

NP_694723.1. NM_153083.5.

UniGene

Mm.319204.

3D structure databases

PDBe
RCSB PDB
PDBj

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

ProteinModelPortal

Q8JZL3.

SMR

Q8JZL3. Positions 2-224.

ModBase

Search...

PTM databases

PhosphoSite

Q8JZL3.

Proteomic databases

PaxDb

Q8JZL3.

PRIDE

Q8JZL3.

Protocols and materials databases

DNASU

105663.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000050575; ENSMUSP00000056026; ENSMUSG00000045691.

GeneID

105663.

KEGG

mmu:105663.

UCSC

uc007tyb.2. mouse.

Organism-specific databases

CTD

79178.

MGI

MGI:2446078. Thtpa.

Phylogenomic databases

eggNOG

NOG42323.

GeneTree

ENSGT00390000005996.

HOGENOM

HOG000154571.

HOVERGEN

HBG057173.

InParanoid

Q8JZL3.

KO

K05307.

OMA

RDTYYDT.

OrthoDB

EOG4Z62PN.

Gene expression databases

Bgee

Q8JZL3.

CleanEx

MM_THTPA.

Genevestigator

Q8JZL3.

GermOnline

ENSMUSG00000045691. Mus musculus.

Family and domain databases

Gene3D

2.40.320.10. 1 hit.

InterPro

IPR023577. CYTH-like_domain.
IPR012177. ThTPase.
[Graphical view]

PANTHER

PTHR14586. PTHR14586. 1 hit.

Pfam

PF01928. CYTH. 1 hit.
[Graphical view]

PIRSF

PIRSF036561. ThTPase. 1 hit.

SUPFAM

SSF55154. mRNA_capping_enz_bsu. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

Q8JZL3.

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:	April 3, 2013
This is version 88 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program