[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. PubMed=9699672 [NCBI, ExPASy, EBI, Israel, Japan] Pekarsky Y., Druck T., Cotticelli M.G., Ohta M., Shou J., Mendrola J., Montgomery J.C., Buchberg A.M., Siracusa L.D., Manenti G., Fong L.Y., Dragani T.A., Croce C.M., Huebner K.; "The murine Fhit locus: isolation, characterization, and expression in normal and tumor cells."; Cancer Res. 58:3401-3408(1998).
[2]	NUCLEOTIDE SEQUENCE. STRAIN=C57BL/10J; TISSUE=Muscle; Glover T.W., Hoge A., Miller D.E., Escara-Wilke J., Adam A.N., Dagenais S.L., Wilke C.M., Dierick H.A., Beer D.G.; Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=FVB/N; TISSUE=Mammary gland; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 36-150. STRAIN=C57BL/6J; TISSUE=Kidney; DOI=10.1073/pnas.2336256100; PubMed=14630947 [NCBI, ExPASy, EBI, Israel, Japan] Matsuyama A., Shiraishi T., Trapasso F., Kuroki T., Alder H., Mori M., Huebner K., Croce C.M.; "Fragile site orthologs FHIT/FRA3B and Fhit/Fra14A2: evolutionarily conserved but highly recombinogenic."; Proc. Natl. Acad. Sci. U.S.A. 100:14988-14993(2003).
[5]	TISSUE SPECIFICITY. DOI=10.1073/pnas.95.15.8744; PubMed=9671749 [NCBI, ExPASy, EBI, Israel, Japan] Pekarsky Y., Campiglio M., Siprashvili Z., Druck T., Sedkov Y., Tillib S., Draganescu A., Wermuth P., Rothman J.H., Huebner K., Buchberg A.M., Mazo A., Brenner C., Croce C.M.; "Nitrilase and Fhit homologs are encoded as fusion proteins in Drosophila melanogaster and Caenorhabditis elegans."; Proc. Natl. Acad. Sci. U.S.A. 95:8744-8749(1998).

Comments

FUNCTION: Cleaves A-5'-PPP-5'A to yield AMP and ADP.
CATALYTIC ACTIVITY: P¹-P³-bis(5'-adenosyl) triphosphate + H₂O = ADP + AMP.
COFACTOR: Divalent cations. Magnesium, but manganese and to a lesser extent calcium or cobalt can be substituted; but not zinc, cadmium or nickel (By similarity).
SUBUNIT: Homodimer (By similarity).
SUBCELLULAR LOCATION: Cytoplasm.
TISSUE SPECIFICITY: Expressed in heart, brain, lung and skeletal muscle. Particularly strong expression in liver, testis and kidney, where it is confined to the tubular epithelium.
SIMILARITY: Contains 1 HIT domain.

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

AF047702; AAC23967.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF047700; AAC23967.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF047701; AAC23967.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF047699; AAC24566.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF055573; AAC24117.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC012662; AAH12662.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY363103; AAR17701.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_034340.1; -.

UniGene

Mm.397619

3D structure databases

HSSP

P49789; 4FIT. [HSSP ENTRY / PDB]

SMR

O89106; 1-130, 2-131.

ModBase

O89106.

PTM databases

PhosphoSite

O89106; -.

Organism-specific databases

MGI

MGI:1277947; Fhit.

Gene expression databases

CleanEx

MM_FHIT; -.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from direct assay from UniProtKB).
GO:0047710;	Molecular function: bis(5'-adenosyl)-triphosphatase activity (inferred from direct assay from UniProtKB).
GO:0000287;	Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0030145;	Molecular function: manganese ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006260;	Biological process: DNA replication (inferred from direct assay from MGI).
GO:0009117;	Biological process: nucleotide metabolic process (traceable author statement from ProtInc).
QuickGo view.

Family and domain databases

InterPro

IPR011151; His_triad_motif.
IPR001310; HIT.
Graphical view of domain structure.

Gene3D

G3DSA:3.30.428.10; His_triad_motif; 1.

PANTHER

PTHR23089; HIT; 1.

Pfam

PF01230; HIT; 1.
Pfam graphical view of domain structure.

PROSITE

PS00892; HIT_1; 1.
PS51084; HIT_2; 1.
PROSITE graphical view of domain structure (profiles).

Proteomics databases

PRIDE

O89106; -.

Genome annotation databases

Ensembl

ENSMUSG00000060579; Mus musculus. [Contig view]

GeneID

14198; -.

KEGG

mmu:14198; -.

Phylogenomic databases

HOGENOM

O89106; -.

HOVERGEN

O89106; -.

Other

285422; -.

Fhit; Mus musculus.

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

Keywords

Cytoplasm; Hydrolase; Magnesium; Manganese; Phosphoprotein.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed (By similarity).`
`CHAIN`	`2 150`	`149`	`Bis(5'-adenosyl)-triphosphatase.`	`PRO_0000109790`
`DOMAIN`	`2 109`	`108`	`HIT.`
`REGION`	`82 99`	`18`	`Binding to substrate; phosphate linker (By similarity).`
`MOTIF`	`94 98`	`5`	`Histidine triad motif (By similarity).`
`ACT_SITE`	`96 96`		`Tele-AMP-histidine intermediate (By similarity).`
`BINDING`	`27 27`		`Substrate (By similarity).`
`MOD_RES`	`114 114`		`Phosphotyrosine; by SRC (By similarity).`
`MOD_RES`	`147 147`		`Phosphotyrosine (By similarity).`
`CONFLICT`	`135 135`		`K -> E (in Ref. 3; AAH12662).`

Sequence information

Length: 150 AA [This is the length of the unprocessed precursor]

Molecular weight: 17235 Da [This is the MW of the unprocessed precursor]

CRC64: 27CBC57C5A4A0E2B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSFRFGQHLI KPSVVFLKTE LSFALVNRKP VVPGHVLVCP LRPVERFRDL HPDEVADLFQ 

        70         80         90        100        110        120 
VTQRVGTVVE KHFQGTSITF SMQDGPEAGQ TVKHVHVHVL PRKAGDFPRN DNIYDELQKH 

       130        140        150 
DREEEDSPAF WRSEKEMAAE AEALRVYFQA

O89106 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