TPK1_MOUSE
ID TPK1_MOUSE Reviewed; 243 AA.
AC Q9R0M5; Q3UWB5; Q8CAB5; Q8CEE8; Q8R1Q6;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Thiamin pyrophosphokinase 1 {ECO:0000303|PubMed:10567383};
DE Short=mTPK1 {ECO:0000303|PubMed:10567383};
DE EC=2.7.6.2 {ECO:0000269|PubMed:10567383};
DE AltName: Full=Thiamine pyrophosphokinase 1;
GN Name=Tpk1 {ECO:0000303|PubMed:10567383, ECO:0000312|MGI:MGI:1352500};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBUNIT, TISSUE
RP SPECIFICITY, AND CATALYTIC ACTIVITY.
RC TISSUE=Embryo;
RX PubMed=10567383; DOI=10.1074/jbc.274.48.34129;
RA Nosaka K., Onozuka M., Nishino H., Nishimura H., Kawasaki Y., Ueyama H.;
RT "Molecular cloning and expression of a mouse thiamin pyrophosphokinase
RT cDNA.";
RL J. Biol. Chem. 274:34129-34133(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Colon, Embryo, Embryonic liver, and Hypothalamus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Lung, Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF ISOFORM 1 IN COMPLEX WITH
RP THIAMINE, AND HOMODIMERIZATION.
RX PubMed=11419946; DOI=10.1006/jmbi.2001.4727;
RA Timm D.E., Liu J., Baker L.-J., Harris R.A.;
RT "Crystal structure of thiamin pyrophosphokinase.";
RL J. Mol. Biol. 310:195-204(2001).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF ISOFORM 2 IN COMPLEX WITH
RP PYRITHIAMINE PYROPHOSPHATE AND AMP, AND FUNCTION.
RX PubMed=16365036; DOI=10.1074/jbc.m510951200;
RA Liu J.Y., Timm D.E., Hurley T.D.;
RT "Pyrithiamine as a substrate for thiamine pyrophosphokinase.";
RL J. Biol. Chem. 281:6601-6607(2006).
CC -!- FUNCTION: Catalyzes the phosphorylation of thiamine to thiamine
CC pyrophosphate. Can also catalyze the phosphorylation of pyrithiamine to
CC pyrithiamine pyrophosphate. {ECO:0000269|PubMed:10567383,
CC ECO:0000269|PubMed:16365036}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + thiamine = AMP + H(+) + thiamine diphosphate;
CC Xref=Rhea:RHEA:11576, ChEBI:CHEBI:15378, ChEBI:CHEBI:18385,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58937, ChEBI:CHEBI:456215; EC=2.7.6.2;
CC Evidence={ECO:0000269|PubMed:10567383};
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis;
CC thiamine diphosphate from thiamine: step 1/1.
CC {ECO:0000305|PubMed:10567383}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10567383,
CC ECO:0000269|PubMed:11419946, ECO:0000269|PubMed:16365036}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9R0M5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9R0M5-2; Sequence=VSP_009597;
CC Name=3;
CC IsoId=Q9R0M5-3; Sequence=VSP_009595, VSP_009596;
CC -!- TISSUE SPECIFICITY: Detected in kidney and liver, and at lower levels
CC in heart, brain and testis. {ECO:0000269|PubMed:10567383}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be due to intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the thiamine pyrophosphokinase family.
CC {ECO:0000305}.
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DR EMBL; AB027568; BAA87040.1; -; mRNA.
DR EMBL; AK028431; BAC25948.1; -; mRNA.
DR EMBL; AK035044; BAC28923.1; -; mRNA.
DR EMBL; AK039131; BAC30248.1; -; mRNA.
DR EMBL; AK136486; BAE23001.1; -; mRNA.
DR EMBL; BC015246; AAH15246.1; -; mRNA.
DR EMBL; BC023354; AAH23354.1; -; mRNA.
DR CCDS; CCDS39474.1; -. [Q9R0M5-1]
DR CCDS; CCDS80529.1; -. [Q9R0M5-2]
DR RefSeq; NP_001298040.1; NM_001311111.1. [Q9R0M5-2]
DR RefSeq; NP_038889.1; NM_013861.4. [Q9R0M5-1]
DR PDB; 1IG3; X-ray; 1.90 A; A/B=1-243.
DR PDB; 2F17; X-ray; 2.50 A; A/B=1-243.
DR PDBsum; 1IG3; -.
DR PDBsum; 2F17; -.
DR AlphaFoldDB; Q9R0M5; -.
DR SMR; Q9R0M5; -.
DR STRING; 10090.ENSMUSP00000065631; -.
DR PhosphoSitePlus; Q9R0M5; -.
DR EPD; Q9R0M5; -.
DR jPOST; Q9R0M5; -.
DR MaxQB; Q9R0M5; -.
DR PaxDb; Q9R0M5; -.
DR PeptideAtlas; Q9R0M5; -.
DR PRIDE; Q9R0M5; -.
DR ProteomicsDB; 297506; -. [Q9R0M5-1]
DR ProteomicsDB; 297507; -. [Q9R0M5-2]
DR ProteomicsDB; 297508; -. [Q9R0M5-3]
DR Antibodypedia; 18523; 182 antibodies from 24 providers.
DR DNASU; 29807; -.
DR Ensembl; ENSMUST00000067888; ENSMUSP00000065631; ENSMUSG00000029735. [Q9R0M5-1]
DR Ensembl; ENSMUST00000114644; ENSMUSP00000110291; ENSMUSG00000029735. [Q9R0M5-2]
DR GeneID; 29807; -.
DR KEGG; mmu:29807; -.
DR UCSC; uc009bsq.1; mouse. [Q9R0M5-1]
DR UCSC; uc009bsr.1; mouse. [Q9R0M5-2]
DR CTD; 27010; -.
DR MGI; MGI:1352500; Tpk1.
DR VEuPathDB; HostDB:ENSMUSG00000029735; -.
DR eggNOG; KOG3153; Eukaryota.
DR GeneTree; ENSGT00390000016016; -.
DR HOGENOM; CLU_044237_0_1_1; -.
DR InParanoid; Q9R0M5; -.
DR OMA; HHLYMMT; -.
DR OrthoDB; 1428589at2759; -.
DR PhylomeDB; Q9R0M5; -.
DR TreeFam; TF313224; -.
DR Reactome; R-MMU-196819; Vitamin B1 (thiamin) metabolism.
DR UniPathway; UPA00060; UER00597.
DR BioGRID-ORCS; 29807; 6 hits in 74 CRISPR screens.
DR ChiTaRS; Tpk1; mouse.
DR EvolutionaryTrace; Q9R0M5; -.
DR PRO; PR:Q9R0M5; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9R0M5; protein.
DR Bgee; ENSMUSG00000029735; Expressed in right kidney and 158 other tissues.
DR Genevisible; Q9R0M5; MM.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0030975; F:thiamine binding; IEA:InterPro.
DR GO; GO:0004788; F:thiamine diphosphokinase activity; IDA:MGI.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; ISO:MGI.
DR GO; GO:0006772; P:thiamine metabolic process; IDA:MGI.
DR CDD; cd07995; TPK; 1.
DR Gene3D; 3.40.50.10240; -; 1.
DR InterPro; IPR006282; Thi_PPkinase.
DR InterPro; IPR016966; Thiamin_pyrophosphokinase_euk.
DR InterPro; IPR007373; Thiamin_PyroPKinase_B1-bd.
DR InterPro; IPR036371; TPK_B1-bd_sf.
DR InterPro; IPR007371; TPK_catalytic.
DR InterPro; IPR036759; TPK_catalytic_sf.
DR Pfam; PF04265; TPK_B1_binding; 1.
DR Pfam; PF04263; TPK_catalytic; 1.
DR PIRSF; PIRSF031057; Thiamin_pyrophosphokinase; 1.
DR SMART; SM00983; TPK_B1_binding; 1.
DR SUPFAM; SSF63862; SSF63862; 1.
DR SUPFAM; SSF63999; SSF63999; 1.
DR TIGRFAMs; TIGR01378; thi_PPkinase; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Kinase;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..243
FT /note="Thiamin pyrophosphokinase 1"
FT /id="PRO_0000072648"
FT VAR_SEQ 39..63
FT /note="ALLRACADGGANHLYDLTEGERESF -> VLGKKSQEVLAERRLIEPLGIQS
FT SL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_009595"
FT VAR_SEQ 64..243
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_009596"
FT VAR_SEQ 119..167
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_009597"
FT CONFLICT 20
FT /note="C -> W (in Ref. 2; BAC25948)"
FT /evidence="ECO:0000305"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:1IG3"
FT HELIX 9..11
FT /evidence="ECO:0007829|PDB:1IG3"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:1IG3"
FT STRAND 19..23
FT /evidence="ECO:0007829|PDB:1IG3"
FT HELIX 32..38
FT /evidence="ECO:0007829|PDB:1IG3"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:1IG3"
FT HELIX 48..54
FT /evidence="ECO:0007829|PDB:1IG3"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:1IG3"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:1IG3"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:2F17"
FT HELIX 77..85
FT /evidence="ECO:0007829|PDB:1IG3"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:1IG3"
FT HELIX 100..114
FT /evidence="ECO:0007829|PDB:1IG3"
FT STRAND 120..125
FT /evidence="ECO:0007829|PDB:1IG3"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:1IG3"
FT HELIX 132..144
FT /evidence="ECO:0007829|PDB:1IG3"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:1IG3"
FT STRAND 153..157
FT /evidence="ECO:0007829|PDB:1IG3"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:1IG3"
FT STRAND 167..173
FT /evidence="ECO:0007829|PDB:1IG3"
FT STRAND 179..186
FT /evidence="ECO:0007829|PDB:1IG3"
FT STRAND 192..202
FT /evidence="ECO:0007829|PDB:1IG3"
FT STRAND 205..210
FT /evidence="ECO:0007829|PDB:1IG3"
FT TURN 211..213
FT /evidence="ECO:0007829|PDB:1IG3"
FT STRAND 216..219
FT /evidence="ECO:0007829|PDB:1IG3"
FT STRAND 223..233
FT /evidence="ECO:0007829|PDB:1IG3"
FT STRAND 235..241
FT /evidence="ECO:0007829|PDB:1IG3"
SQ SEQUENCE 243 AA; 27068 MW; 946896D2493F44EA CRC64;
MEHAFTPLEP LLPTGNLKYC LVVLNQPLDA RFRHLWKKAL LRACADGGAN HLYDLTEGER
ESFLPEFVSG DFDSIRPEVK EYYTKKGCDL ISTPDQDHTD FTKCLQVLQR KIEEKELQVD
VIVTLGGLGG RFDQIMASVN TLFQATHITP VPIIIIQKDS LIYLLQPGKH RLHVDTGMEG
SWCGLIPVGQ PCNQVTTTGL KWNLTNDVLG FGTLVSTSNT YDGSGLVTVE TDHPLLWTMA
IKS
