Q9R0M5 (TPK1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Thiamin pyrophosphokinase 1
Short name=mTPK1
EC=2.7.6.2

Alternative name(s):
Thiamine pyrophosphokinase 1

Gene names

Name:

Tpk1

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	243 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the phosphorylation of thiamine to thiamine pyrophosphate. Can also catalyze the phosphorylation of pyrithiamine to pyrithiamine pyrophosphate. Ref.1 Ref.5
Catalytic activity	ATP + thiamine = AMP + thiamine diphosphate.
Pathway	Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine diphosphate from thiamine: step 1/1.
Subunit structure	Homodimer. Ref.1 Ref.4
Tissue specificity	Detected in kidney and liver, and at lower levels in heart, brain and testis. Ref.1
Sequence similarities	Belongs to the thiamine pyrophosphokinase family.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	thiamine diphosphate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway thiamine metabolic process Inferred from direct assay Ref.1. Source: MGI
Cellular_component	cytoplasm Inferred from electronic annotation. Source: Compara
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW kinase activity Inferred from electronic annotation. Source: UniProtKB-KW thiamine diphosphokinase activity Inferred from direct assay Ref.1. Source: MGI
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9R0M5-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9R0M5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     119-167: Missing.

Isoform 3 (identifier: Q9R0M5-3)

The sequence of this isoform differs from the canonical sequence as follows:
     39-63: ALLRACADGGANHLYDLTEGERESF → VLGKKSQEVLAERRLIEPLGIQSSL
     64-243: Missing.

Note: May be due to intron retention. No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 243

243

Thiamin pyrophosphokinase 1

PRO_0000072648

Natural variations

Alternative sequence

39 – 63

25

ALLRA…ERESF → VLGKKSQEVLAERRLIEPLG IQSSL in isoform 3.

VSP_009595

Alternative sequence

64 – 243

180

Missing in isoform 3.

VSP_009596

Alternative sequence

119 – 167

49

Missing in isoform 2.

VSP_009597

Experimental info

Sequence conflict

20

1

C → W in BAC25948. Ref.2

Secondary structure

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243

Helix Strand Turn

Details...

Beta strand

3 – 5

3

Helix

9 – 11

3

Beta strand

12 – 14

3

Beta strand

19 – 23

5

Helix

32 – 38

7

Beta strand

40 – 45

6

Helix

48 – 54

7

Helix

60 – 62

3

Beta strand

66 – 70

5

Beta strand

72 – 75

4

Helix

77 – 85

9

Beta strand

89 – 92

4

Helix

100 – 114

15

Beta strand

120 – 125

6

Beta strand

128 – 130

3

Helix

132 – 144

13

Helix

145 – 147

3

Beta strand

153 – 157

5

Beta strand

160 – 165

6

Beta strand

167 – 173

7

Beta strand

179 – 186

8

Beta strand

192 – 202

11

Beta strand

205 – 210

6

Turn

211 – 213

3

Beta strand

216 – 219

4

Beta strand

223 – 233

11

Beta strand

235 – 241

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 946896D2493F44EA	FASTA	243	27,068
	10 20 30 40 50 60 MEHAFTPLEP LLPTGNLKYC LVVLNQPLDA RFRHLWKKAL LRACADGGAN HLYDLTEGER 70 80 90 100 110 120 ESFLPEFVSG DFDSIRPEVK EYYTKKGCDL ISTPDQDHTD FTKCLQVLQR KIEEKELQVD 130 140 150 160 170 180 VIVTLGGLGG RFDQIMASVN TLFQATHITP VPIIIIQKDS LIYLLQPGKH RLHVDTGMEG 190 200 210 220 230 240 SWCGLIPVGQ PCNQVTTTGL KWNLTNDVLG FGTLVSTSNT YDGSGLVTVE TDHPLLWTMA IKS
	Isoform 2 [UniParc]. Checksum: 58E61181F8A33A9B	FASTA	194	21,766
	10 20 30 40 50 60 MEHAFTPLEP LLPTGNLKYC LVVLNQPLDA RFRHLWKKAL LRACADGGAN HLYDLTEGER 70 80 90 100 110 120 ESFLPEFVSG DFDSIRPEVK EYYTKKGCDL ISTPDQDHTD FTKCLQVLQR KIEEKELQGK 130 140 150 160 170 180 HRLHVDTGME GSWCGLIPVG QPCNQVTTTG LKWNLTNDVL GFGTLVSTSN TYDGSGLVTV 190 ETDHPLLWTM AIKS
	Isoform 3 [UniParc]. Checksum: 1AEFBAE8B507EC14	FASTA	63	7,237
	10 20 30 40 50 60 MEHAFTPLEP LLPTGNLKYC LVVLNQPLDA RFRHLWKKVL GKKSQEVLAE RRLIEPLGIQ SSL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and expression of a mouse thiamin pyrophosphokinase cDNA." Nosaka K., Onozuka M., Nishino H., Nishimura H., Kawasaki Y., Ueyama H. J. Biol. Chem. 274:34129-34133(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBUNIT, TISSUE SPECIFICITY. Tissue: Embryo.
[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] (ISOFORMS 1; 2 AND 3). Strain: C57BL/6J. Tissue: Colon, Embryo, Embryonic liver and Hypothalamus.
[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] (ISOFORMS 1 AND 2). Tissue: Kidney.
[4]	"Crystal structure of thiamin pyrophosphokinase." Timm D.E., Liu J., Baker L.-J., Harris R.A. J. Mol. Biol. 310:195-204(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF ISOFORM 1 IN COMPLEX WITH THIAMINE, HOMODIMERIZATION.
[5]	"Pyrithiamine as a substrate for thiamine pyrophosphokinase." Liu J.Y., Timm D.E., Hurley T.D. J. Biol. Chem. 281:6601-6607(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF ISOFORM 2 IN COMPLEX WITH PYRITHIAMINE PYROPHOSPHATE AND AMP, FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB027568 mRNA. Translation: BAA87040.1.
AK028431 mRNA. Translation: BAC25948.1.
AK035044 mRNA. Translation: BAC28923.1.
AK039131 mRNA. Translation: BAC30248.1.
AK136486 mRNA. Translation: BAE23001.1.
BC015246 mRNA. Translation: AAH15246.1.
BC023354 mRNA. Translation: AAH23354.1.

IPI

IPI00313885.
IPI00408194.
IPI00468237.

RefSeq

NP_038889.1. NM_013861.3.

UniGene

Mm.320979.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1IG3	X-ray	1.90	A/B	1-243	[»]
2F17	X-ray	2.50	A/B	1-243	[»]

ProteinModelPortal

Q9R0M5.

SMR

Q9R0M5. Positions 1-243.

ModBase

Search...

Protein-protein interaction databases

STRING

10090.ENSMUSP00000065631.

PTM databases

PhosphoSite

Q9R0M5.

Proteomic databases

PaxDb

Q9R0M5.

PRIDE

Q9R0M5.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000067888; ENSMUSP00000065631; ENSMUSG00000029735.
ENSMUST00000114644; ENSMUSP00000110291; ENSMUSG00000029735.
ENSMUST00000150599; ENSMUSP00000121115; ENSMUSG00000029735.

GeneID

29807.

KEGG

mmu:29807.

UCSC

uc009bsq.1. mouse.
uc009bsr.1. mouse.

Organism-specific databases

CTD

27010.

MGI

MGI:1352500. Tpk1.

Phylogenomic databases

eggNOG

COG1564.

GeneTree

ENSGT00390000016016.

HOGENOM

HOG000180834.

HOVERGEN

HBG003568.

InParanoid

Q9R0M5.

KO

K00949.

OMA

KYCLVIL.

OrthoDB

EOG4DJJX5.

Enzyme and pathway databases

UniPathway

UPA00060; UER00597.

Gene expression databases

ArrayExpress

Q9R0M5.

Bgee

Q9R0M5.

CleanEx

MM_TPK1.

Genevestigator

Q9R0M5.

GermOnline

ENSMUSG00000029735. Mus musculus.

Family and domain databases

Gene3D

2.60.120.320. 1 hit.
3.40.50.10240. 1 hit.

InterPro

IPR006282. Thi_PPkinase.
IPR016966. Thiamin_pyrophosphokinase_euk.
IPR007373. Thiamin_PyroPKinase_B1-bd.
IPR007371. TPK_catalytic.
[Graphical view]

Pfam

PF04265. TPK_B1_binding. 1 hit.
PF04263. TPK_catalytic. 1 hit.
[Graphical view]

PIRSF

PIRSF031057. Thiamin_pyrophosphokinase. 1 hit.

SMART

SM00983. TPK_B1_binding. 1 hit.
[Graphical view]

SUPFAM

SSF63862. TPK_B1_bd. 1 hit.
SSF63999. TPK_catalytic. 1 hit.

TIGRFAMs

TIGR01378. thi_PPkinase. 1 hit.

ProtoNet

Search...

Other

DrugBank

DB00152. Thiamine.

EvolutionaryTrace

Q9R0M5.

NextBio

306944.

SOURCE

Search...

Entry information

Entry name

TPK1_MOUSE

Accession

Primary (citable) accession number: Q9R0M5
Secondary accession number(s): Q3UWB5 , Q8CAB5, Q8CEE8, Q8R1Q6

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2004
Last sequence update:	May 1, 2000
Last modified:	April 3, 2013
This is version 98 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program