THTPA_RAT
ID THTPA_RAT Reviewed; 224 AA.
AC Q8CGV7;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Thiamine-triphosphatase;
DE Short=ThTPase;
DE EC=3.6.1.28;
GN Name=Thtpa;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 93-224.
RC STRAIN=Wistar;
RA Lakaye B.B., Coumans B.B., Makarchikov A.A., Grisar T.T., Bettendorff L.L.;
RT "Isolation and characterization of the rat ThTPase cDNA.";
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Hydrolase highly specific for thiamine triphosphate (ThTP).
CC {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ThTPase family. {ECO:0000305}.
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DR EMBL; BC081978; AAH81978.1; -; mRNA.
DR EMBL; AY065967; AAL41027.1; -; mRNA.
DR RefSeq; NP_001007683.1; NM_001007682.1.
DR AlphaFoldDB; Q8CGV7; -.
DR SMR; Q8CGV7; -.
DR STRING; 10116.ENSRNOP00000038507; -.
DR iPTMnet; Q8CGV7; -.
DR PhosphoSitePlus; Q8CGV7; -.
DR PaxDb; Q8CGV7; -.
DR GeneID; 305889; -.
DR KEGG; rno:305889; -.
DR UCSC; RGD:727917; rat.
DR CTD; 79178; -.
DR RGD; 727917; Thtpa.
DR VEuPathDB; HostDB:ENSRNOG00000018105; -.
DR eggNOG; ENOG502S5G9; Eukaryota.
DR HOGENOM; CLU_105907_0_0_1; -.
DR InParanoid; Q8CGV7; -.
DR OrthoDB; 1453157at2759; -.
DR PhylomeDB; Q8CGV7; -.
DR TreeFam; TF333398; -.
DR BRENDA; 3.6.1.28; 5301.
DR Reactome; R-RNO-196819; Vitamin B1 (thiamin) metabolism.
DR PRO; PR:Q8CGV7; -.
DR Proteomes; UP000002494; Chromosome 15.
DR Bgee; ENSRNOG00000018105; Expressed in cerebellum and 20 other tissues.
DR ExpressionAtlas; Q8CGV7; baseline and differential.
DR Genevisible; Q8CGV7; RN.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0050333; F:thiamin-triphosphatase activity; ISS:UniProtKB.
DR GO; GO:0016311; P:dephosphorylation; ISO:RGD.
DR GO; GO:0042357; P:thiamine diphosphate metabolic process; ISS: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 2: Evidence at transcript level;
KW 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_0000221493"
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 /evidence="ECO:0000250"
FT BINDING 9
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 11
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 55
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 57
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 65
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 125
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 159
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q8MKF1"
SQ SEQUENCE 224 AA; 24544 MW; 27013164E67F229B CRC64;
MAQGLIEVER KFTPGPDTEE RLQKLGATLE HRVTFRDTYY DTSELSLMLS DHWLRQREGS
GWEFKCPGVT GVSGPHNEYV EVTSESAIVT QLFELLGSGE QETAGVAAVL GRLKLQEVAS
FITTRSSWKL ALSGAHEEES LLTVDLDSTD FGYAVGEVEA VVHEKAEVPA ALEKIISVSS
MLGVPAQEKA PAKLLVYLQR FRPQDYQRLL EADSSGEATG DSVP
