THTPA_MOUSE
ID THTPA_MOUSE Reviewed; 224 AA.
AC Q8JZL3; Q3V1G2; Q8C3P9;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Thiamine-triphosphatase;
DE Short=ThTPase;
DE EC=3.6.1.28;
GN Name=Thtpa;
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].
RC STRAIN=C57BL/6J;
RA Lakaye B., Coumans B., Makarchikov A., Grisar T., Bettendorff L.;
RT "Cloning and expression of mouse thiamine triphosphatase cDNA.";
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Skin;
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].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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, Heart, Kidney, Liver, and Lung;
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 STRUCTURE BY NMR OF 2-223, SUBUNIT, MAGNESIUM-BINDING SITES,
RP SUBSTRATE-BINDING SITES, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=18276586; DOI=10.1074/jbc.m709675200;
RA Song J., Bettendorff L., Tonelli M., Markley J.L.;
RT "Structural basis for the catalytic mechanism of mammalian 25-kDa thiamine
RT triphosphatase.";
RL J. Biol. Chem. 283:10939-10948(2008).
CC -!- FUNCTION: Hydrolase highly specific for thiamine triphosphate (ThTP).
CC {ECO:0000269|PubMed:18276586}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + thiamine triphosphate = H(+) + phosphate + thiamine
CC diphosphate; Xref=Rhea:RHEA:11744, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58937,
CC ChEBI:CHEBI:58938; EC=3.6.1.28;
CC Evidence={ECO:0000269|PubMed:18276586};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:18276586};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:18276586};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.5-9.5. {ECO:0000269|PubMed:18276586};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:18276586}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ThTPase family. {ECO:0000305}.
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DR EMBL; AF432864; AAM22405.1; -; mRNA.
DR EMBL; AK132479; BAE21189.1; -; mRNA.
DR EMBL; BC025562; AAH25562.1; -; mRNA.
DR CCDS; CCDS27108.1; -.
DR RefSeq; NP_694723.1; NM_153083.5.
DR PDB; 2JMU; NMR; -; A=2-224.
DR PDB; 5A64; X-ray; 2.10 A; A/B=1-224.
DR PDB; 5A65; X-ray; 1.98 A; A/B=3-215.
DR PDBsum; 2JMU; -.
DR PDBsum; 5A64; -.
DR PDBsum; 5A65; -.
DR AlphaFoldDB; Q8JZL3; -.
DR BMRB; Q8JZL3; -.
DR SMR; Q8JZL3; -.
DR STRING; 10090.ENSMUSP00000056026; -.
DR PhosphoSitePlus; Q8JZL3; -.
DR EPD; Q8JZL3; -.
DR MaxQB; Q8JZL3; -.
DR PaxDb; Q8JZL3; -.
DR PeptideAtlas; Q8JZL3; -.
DR PRIDE; Q8JZL3; -.
DR ProteomicsDB; 259186; -.
DR Antibodypedia; 55506; 217 antibodies from 23 providers.
DR DNASU; 105663; -.
DR Ensembl; ENSMUST00000050575; ENSMUSP00000056026; ENSMUSG00000045691.
DR GeneID; 105663; -.
DR KEGG; mmu:105663; -.
DR UCSC; uc007tyb.2; mouse.
DR CTD; 79178; -.
DR MGI; MGI:2446078; Thtpa.
DR VEuPathDB; HostDB:ENSMUSG00000045691; -.
DR eggNOG; ENOG502S5G9; Eukaryota.
DR GeneTree; ENSGT00390000005996; -.
DR HOGENOM; CLU_105907_0_0_1; -.
DR InParanoid; Q8JZL3; -.
DR OMA; LMRADHW; -.
DR OrthoDB; 1453157at2759; -.
DR PhylomeDB; Q8JZL3; -.
DR TreeFam; TF333398; -.
DR BRENDA; 3.6.1.28; 3474.
DR Reactome; R-MMU-196819; Vitamin B1 (thiamin) metabolism.
DR SABIO-RK; Q8JZL3; -.
DR BioGRID-ORCS; 105663; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Thtpa; mouse.
DR EvolutionaryTrace; Q8JZL3; -.
DR PRO; PR:Q8JZL3; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q8JZL3; protein.
DR Bgee; ENSMUSG00000045691; Expressed in ganglionic eminence and 74 other tissues.
DR Genevisible; Q8JZL3; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0050333; F:thiamin-triphosphatase activity; IDA:UniProtKB.
DR GO; GO:0016311; P:dephosphorylation; ISO:MGI.
DR GO; GO:0042357; P:thiamine diphosphate metabolic process; IDA:UniProtKB.
DR GO; GO:0006772; P:thiamine metabolic process; IEA:InterPro.
DR CDD; cd07758; ThTPase; 1.
DR InterPro; IPR033469; CYTH-like_dom_sf.
DR InterPro; IPR023577; CYTH_domain.
DR InterPro; IPR039582; THTPA.
DR InterPro; IPR012177; ThTPase_euk.
DR PANTHER; PTHR14586; PTHR14586; 1.
DR Pfam; PF01928; CYTH; 1.
DR PIRSF; PIRSF036561; ThTPase; 1.
DR SMART; SM01118; CYTH; 1.
DR SUPFAM; SSF55154; SSF55154; 1.
DR PROSITE; PS51707; CYTH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Hydrolase; Magnesium; Metal-binding;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q8MKF1"
FT CHAIN 2..224
FT /note="Thiamine-triphosphatase"
FT /id="PRO_0000221492"
FT DOMAIN 5..201
FT /note="CYTH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01044"
FT BINDING 7
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 9
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 11
FT /ligand="substrate"
FT BINDING 55
FT /ligand="substrate"
FT BINDING 57
FT /ligand="substrate"
FT BINDING 65
FT /ligand="substrate"
FT BINDING 125
FT /ligand="substrate"
FT BINDING 145
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 157
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 157
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 159
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 193
FT /ligand="substrate"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q8MKF1"
FT STRAND 6..12
FT /evidence="ECO:0007829|PDB:5A65"
FT HELIX 18..24
FT /evidence="ECO:0007829|PDB:5A65"
FT STRAND 28..41
FT /evidence="ECO:0007829|PDB:5A65"
FT HELIX 46..49
FT /evidence="ECO:0007829|PDB:5A65"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:5A65"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:5A65"
FT STRAND 61..67
FT /evidence="ECO:0007829|PDB:5A65"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:5A65"
FT HELIX 85..96
FT /evidence="ECO:0007829|PDB:5A65"
FT HELIX 106..109
FT /evidence="ECO:0007829|PDB:5A65"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:5A65"
FT STRAND 116..130
FT /evidence="ECO:0007829|PDB:5A65"
FT STRAND 142..149
FT /evidence="ECO:0007829|PDB:5A65"
FT TURN 150..152
FT /evidence="ECO:0007829|PDB:5A65"
FT STRAND 153..164
FT /evidence="ECO:0007829|PDB:5A65"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:5A65"
FT HELIX 168..182
FT /evidence="ECO:0007829|PDB:5A65"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:2JMU"
FT HELIX 193..201
FT /evidence="ECO:0007829|PDB:5A65"
FT HELIX 203..213
FT /evidence="ECO:0007829|PDB:5A65"
SQ SEQUENCE 224 AA; 24264 MW; D33C844FDA8277D9 CRC64;
MAQGLIEVER KFAPGPDTEE RLQELGATLE HRVTFRDTYY DTSELSLMLS DHWLRQREGS
GWELKCPGVT GVSGPHNEYV EVTSEAAIVA QLFELLGSGE QKPAGVAAVL GSLKLQEVAS
FITTRSSWKL ALSGAHGQEP QLTIDLDSAD FGYAVGEVEA MVHEKAEVPA ALEKIITVSS
MLGVPAQEEA PAKLMVYLQR FRPLDYQRLL EAASSGEATG DSAS
