ID FHIT_MOUSE Reviewed; 150 AA. AC O89106; Q6URW5; Q91VL1; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 16-JUN-2009, entry version 66. DE RecName: Full=Bis(5'-adenosyl)-triphosphatase; DE EC=3.6.1.29; DE AltName: Full=Diadenosine 5',5'''-P1,P3-triphosphate hydrolase; DE AltName: Full=Dinucleosidetriphosphatase; DE AltName: Full=AP3A hydrolase; DE Short=AP3Aase; DE AltName: Full=Fragile histidine triad protein; GN Name=Fhit; 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 [GENOMIC DNA / MRNA], SUBCELLULAR LOCATION, AND RP TISSUE SPECIFICITY. RX PubMed=9699672; RA Pekarsky Y., Druck T., Cotticelli M.G., Ohta M., Shou J., Mendrola J., RA Montgomery J.C., Buchberg A.M., Siracusa L.D., Manenti G., Fong L.Y., RA Dragani T.A., Croce C.M., Huebner K.; RT "The murine Fhit locus: isolation, characterization, and expression in RT normal and tumor cells."; RL Cancer Res. 58:3401-3408(1998). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/10J; TISSUE=Muscle; RA Glover T.W., Hoge A., Miller D.E., Escara-Wilke J., Adam A.N., RA Dagenais S.L., Wilke C.M., Dierick H.A., Beer D.G.; RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases. 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). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 36-150. RC STRAIN=C57BL/6J; TISSUE=Kidney; RX PubMed=14630947; DOI=10.1073/pnas.2336256100; RA Matsuyama A., Shiraishi T., Trapasso F., Kuroki T., Alder H., Mori M., RA Huebner K., Croce C.M.; RT "Fragile site orthologs FHIT/FRA3B and Fhit/Fra14A2: evolutionarily RT conserved but highly recombinogenic."; RL Proc. Natl. Acad. Sci. U.S.A. 100:14988-14993(2003). RN [5] RP TISSUE SPECIFICITY. RX MEDLINE=98337986; PubMed=9671749; DOI=10.1073/pnas.95.15.8744; RA Pekarsky Y., Campiglio M., Siprashvili Z., Druck T., Sedkov Y., RA Tillib S., Draganescu A., Wermuth P., Rothman J.H., Huebner K., RA Buchberg A.M., Mazo A., Brenner C., Croce C.M.; RT "Nitrilase and Fhit homologs are encoded as fusion proteins in RT Drosophila melanogaster and Caenorhabditis elegans."; RL Proc. Natl. Acad. Sci. U.S.A. 95:8744-8749(1998). CC -!- FUNCTION: Cleaves A-5'-PPP-5'A to yield AMP and ADP. CC -!- CATALYTIC ACTIVITY: P(1)-P(3)-bis(5'-adenosyl) triphosphate + CC H(2)O = ADP + AMP. CC -!- COFACTOR: Divalent cations. Magnesium, but manganese and to a CC lesser extent calcium or cobalt can be substituted; but not zinc, CC cadmium or nickel (By similarity). CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- TISSUE SPECIFICITY: Expressed in heart, brain, lung and skeletal CC muscle. Particularly strong expression in liver, testis and CC kidney, where it is confined to the tubular epithelium. CC -!- SIMILARITY: Contains 1 HIT domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF047702; AAC23967.1; -; Genomic_DNA. DR EMBL; AF047700; AAC23967.1; JOINED; Genomic_DNA. DR EMBL; AF047701; AAC23967.1; JOINED; Genomic_DNA. DR EMBL; AF047699; AAC24566.1; -; mRNA. DR EMBL; AF055573; AAC24117.1; -; mRNA. DR EMBL; BC012662; AAH12662.1; -; mRNA. DR EMBL; AY363103; AAR17701.1; -; Genomic_DNA. DR IPI; IPI00131502; -. DR RefSeq; NP_034340.1; -. DR UniGene; Mm.397619; -. DR UniGene; Mm.441926; -. DR HSSP; P49789; 4FIT. DR SMR; O89106; 1-130, 2-131. DR PhosphoSite; O89106; -. DR PRIDE; O89106; -. DR Ensembl; ENSMUSG00000060579; Mus musculus. DR GeneID; 14198; -. DR KEGG; mmu:14198; -. DR MGI; MGI:1277947; Fhit. DR HOGENOM; O89106; -. DR HOVERGEN; O89106; -. DR BRENDA; 3.6.1.29; 244. DR NextBio; 285422; -. DR Bgee; O89106; -. DR CleanEx; MM_FHIT; -. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0047710; F:bis(5'-adenosyl)-triphosphatase activity; IDA:UniProtKB. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-KW. DR GO; GO:0006260; P:DNA replication; IDA:MGI. DR GO; GO:0009117; P:nucleotide metabolic process; TAS:ProtInc. DR InterPro; IPR011151; His_triad_motif. DR InterPro; IPR019808; Histidine_triad_CS. DR InterPro; IPR001310; Histidine_triad_HIT. DR Gene3D; G3DSA:3.30.428.10; His_triad_motif; 1. DR PANTHER; PTHR23089; HIT; 1. DR Pfam; PF01230; HIT; 1. DR PROSITE; PS00892; HIT_1; 1. DR PROSITE; PS51084; HIT_2; 1. PE 2: Evidence at transcript level; KW Cytoplasm; Hydrolase; Magnesium; Manganese; Phosphoprotein. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 150 Bis(5'-adenosyl)-triphosphatase. FT /FTId=PRO_0000109790. FT DOMAIN 2 109 HIT. FT REGION 82 99 Binding to substrate; phosphate linker FT (By similarity). FT MOTIF 94 98 Histidine triad motif (By similarity). FT ACT_SITE 96 96 Tele-AMP-histidine intermediate (By FT similarity). FT BINDING 27 27 Substrate (By similarity). FT MOD_RES 114 114 Phosphotyrosine; by SRC (By similarity). FT MOD_RES 147 147 Phosphotyrosine (By similarity). FT CONFLICT 135 135 K -> E (in Ref. 3; AAH12662). SQ SEQUENCE 150 AA; 17235 MW; 27CBC57C5A4A0E2B CRC64; MSFRFGQHLI KPSVVFLKTE LSFALVNRKP VVPGHVLVCP LRPVERFRDL HPDEVADLFQ VTQRVGTVVE KHFQGTSITF SMQDGPEAGQ TVKHVHVHVL PRKAGDFPRN DNIYDELQKH DREEEDSPAF WRSEKEMAAE AEALRVYFQA //