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   16-JUN-2009, entry version 56.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6;
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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Hydrolase highly specific for thiamine triphosphate
CC       (ThTP) (By similarity).
CC   -!- CATALYTIC ACTIVITY: Thiamine triphosphate + H(2)O = thiamine
CC       diphosphate + phosphate.
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the ThTPase family.
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DR   EMBL; AF432864; AAM22405.1; -; mRNA.
DR   EMBL; AK132479; BAE21189.1; -; mRNA.
DR   EMBL; BC025562; AAH25562.1; -; mRNA.
DR   IPI; IPI00128570; -.
DR   RefSeq; NP_694723.1; -.
DR   UniGene; Mm.319204; -.
DR   PDB; 2JMU; NMR; -; A=2-223.
DR   PDBsum; 2JMU; -.
DR   PhosphoSite; Q8JZL3; -.
DR   PRIDE; Q8JZL3; -.
DR   Ensembl; ENSMUSG00000045691; Mus musculus.
DR   GeneID; 105663; -.
DR   KEGG; mmu:105663; -.
DR   MGI; MGI:2446078; Thtpa.
DR   HOGENOM; Q8JZL3; -.
DR   HOVERGEN; Q8JZL3; -.
DR   OMA; Q8JZL3; EVERKFV.
DR   BRENDA; 3.6.1.28; 244.
DR   NextBio; 357818; -.
DR   Bgee; Q8JZL3; -.
DR   CleanEx; MM_THTPA; -.
DR   GermOnline; ENSMUSG00000045691; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004016; F:adenylate cyclase activity; IEA:InterPro.
DR   GO; GO:0050333; F:thiamin-triphosphatase activity; ISS:UniProtKB.
DR   GO; GO:0006171; P:cAMP biosynthetic process; IEA:InterPro.
DR   GO; GO:0006772; P:thiamin metabolic process; IEA:InterPro.
DR   InterPro; IPR008172; Adenylate_cyclase.
DR   InterPro; IPR012177; ThTPase.
DR   PANTHER; PTHR14586; ThTPase; 1.
DR   Pfam; PF01928; CYTH; 1.
DR   PIRSF; PIRSF036561; ThTPase; 1.
DR   ProDom; PD009560; CyaB; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; Hydrolase.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    224       Thiamine-triphosphatase.
FT                                /FTId=PRO_0000221492.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   STRAND        3     14
FT   HELIX        18     25
FT   STRAND       28     41
FT   HELIX        46     49
FT   STRAND       53     57
FT   TURN         58     60
FT   STRAND       61     66
FT   STRAND       80     82
FT   HELIX        85     96
FT   HELIX       106    113
FT   STRAND      116    131
FT   STRAND      141    149
FT   TURN        150    152
FT   STRAND      153    163
FT   HELIX       165    167
FT   HELIX       168    182
FT   STRAND      183    185
FT   HELIX       193    201
FT   HELIX       203    212
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
//