NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, CHARACTERIZATION, AND MASS SPECTROMETRY.
DOI=10.1074/jbc.M111241200; PubMed=11827967 [NCBI, ExPASy, EBI, Israel, Japan]
Lakaye B., Makarchikov A.F., Antunes A.F., Zorzi W., Coumans B., De Pauw E., Wins P., Grisar T., Bettendorff L.;
"Molecular characterization of a specific thiamine triphosphatase widely expressed in mammalian tissues.";
J. Biol. Chem. 277:13771-13777(2002).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Hereford;
TISSUE=Fetal liver;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.

Comments

FUNCTION: Hydrolase highly specific for thiamine triphosphate (ThTP).
CATALYTIC ACTIVITY: Thiamine triphosphate + H₂O = thiamine diphosphate + phosphate.
SUBUNIT: Monomer.
SUBCELLULAR LOCATION: Cytoplasm.
MASS SPECTROMETRY: Mass=23892; Method=Electrospray; Range=2-219; Source=PubMed:11827967;.
SIMILARITY: Belongs to the ThTPase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF432863; AAM22404.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC105468; AAI05469.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_776895.1; -.

UniGene

Bt.8966

3D structure databases

SMR

Q8MKF1; 2-217.

ModBase

Q8MKF1.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0004016;	Molecular function: adenylate cyclase activity (inferred from electronic annotation from InterPro).
GO:0050333;	Molecular function: thiamin-triphosphatase activity (inferred from sequence or structural similarity from UniProtKB).
GO:0006171;	Biological process: cAMP biosynthetic process (inferred from electronic annotation from InterPro).
GO:0006772;	Biological process: thiamin metabolic process (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR008172; Adenylate_cyclase.
IPR012177; ThTPase.
Graphical view of domain structure.

PANTHER

PTHR14586; ThTPase; 1.

Pfam

PF01928; CYTH; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF036561; ThTPase; 1.

ProtoNet

Q8MKF1.

Genome annotation databases

Ensembl

ENSBTAG00000007097; Bos taurus. [Contig view]

GeneID

282090; -.

KEGG

bta:282090; -.

Phylogenomic databases

HOVERGEN

Q8MKF1; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Acetylation; Cytoplasm; Direct protein sequencing; Hydrolase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 219`	`218`	`Thiamine-triphosphatase.`	`PRO_0000221489`
`MOD_RES`	`2 2`		`N-acetylalanine.`

Sequence information

Length: 219 AA [This is the length of the unprocessed precursor]

Molecular weight: 23983 Da [This is the MW of the unprocessed precursor]

CRC64: 6E617AA2FDB7ACC3 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAQGLIEVER KFVPGPSTEE RLQELGGTLE HRVTFRDSYY DTPELSLMRA DYWLRQREGS 

        70         80         90        100        110        120 
GWELKCPGAA GVSGPHTEYT ELTAEPSIVA QLCEVLGAEV PGAGGVAAVL GPLGLQLVAS 

       130        140        150        160        170        180 
FVTKRSAWKL VLSGADGEER LLRVDLDTAD FGYAVGEVEA LVHKEAEVPA ALEKIHHLSS 

       190        200        210 
LLGVLEQGRA PAKLIVYLQR FRPQDYQRLL EVYGSKEKP

Q8MKF1 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools