ID   THTPA_BOVIN             Reviewed;         219 AA.
AC   Q8MKF1; Q2KJ88;
DT   03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   16-JUN-2009, entry version 44.
DE   RecName: Full=Thiamine-triphosphatase;
DE            Short=ThTPase;
DE            EC=3.6.1.28;
GN   Name=THTPA;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION,
RP   SUBCELLULAR LOCATION, SUBUNIT, CHARACTERIZATION, AND MASS
RP   SPECTROMETRY.
RX   MEDLINE=21950722; PubMed=11827967; DOI=10.1074/jbc.M111241200;
RA   Lakaye B., Makarchikov A.F., Antunes A.F., Zorzi W., Coumans B.,
RA   De Pauw E., Wins P., Grisar T., Bettendorff L.;
RT   "Molecular characterization of a specific thiamine triphosphatase
RT   widely expressed in mammalian tissues.";
RL   J. Biol. Chem. 277:13771-13777(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Hydrolase highly specific for thiamine triphosphate
CC       (ThTP).
CC   -!- CATALYTIC ACTIVITY: Thiamine triphosphate + H(2)O = thiamine
CC       diphosphate + phosphate.
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- MASS SPECTROMETRY: Mass=23892; Method=Electrospray; Range=2-219;
CC       Source=PubMed:11827967;
CC   -!- SIMILARITY: Belongs to the ThTPase family.
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DR   EMBL; AF432863; AAM22404.1; -; mRNA.
DR   EMBL; BC105468; AAI05469.1; -; mRNA.
DR   IPI; IPI00714789; -.
DR   RefSeq; NP_776895.1; -.
DR   UniGene; Bt.8966; -.
DR   SMR; Q8MKF1; 2-217.
DR   Ensembl; ENSBTAG00000007097; Bos taurus.
DR   GeneID; 282090; -.
DR   KEGG; bta:282090; -.
DR   HOVERGEN; Q8MKF1; -.
DR   OMA; Q8MKF1; EVERKFV.
DR   BRENDA; 3.6.1.28; 251.
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.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Direct protein sequencing; Hydrolase.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    219       Thiamine-triphosphatase.
FT                                /FTId=PRO_0000221489.
FT   MOD_RES       2      2       N-acetylalanine.
SQ   SEQUENCE   219 AA;  23983 MW;  6E617AA2FDB7ACC3 CRC64;
     MAQGLIEVER KFVPGPSTEE RLQELGGTLE HRVTFRDSYY DTPELSLMRA DYWLRQREGS
     GWELKCPGAA GVSGPHTEYT ELTAEPSIVA QLCEVLGAEV PGAGGVAAVL GPLGLQLVAS
     FVTKRSAWKL VLSGADGEER LLRVDLDTAD FGYAVGEVEA LVHKEAEVPA ALEKIHHLSS
     LLGVLEQGRA PAKLIVYLQR FRPQDYQRLL EVYGSKEKP
//