Reviewed,
UniProtKB/Swiss-Prot P70695 (F16P2_MOUSE)
Last modified
January 19, 2010.
Version 80.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Fructose-1,6-bisphosphatase isozyme 2 Short name=FBPase 2 EC=3.1.3.11 Alternative name(s): D-fructose-1,6-bisphosphate 1-phosphohydrolase 2 RAE-30 | ||
| Gene names |
| ||
| Organism | Mus musculus (Mouse) | ||
| Taxonomic identifier | 10090 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus |
Protein attributes
| Sequence length | 339 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Function | May be involved in early differentiation. |
| Catalytic activity | D-fructose 1,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate. |
| Cofactor | Binds 3 magnesium ions per subunit By similarity. |
| Enzyme regulation | Subject to complex allosteric regulation. The enzyme can assume an active R-state, or an inactive T-state. Intermediate conformations may exist. AMP acts as allosteric inhibitor. Fructose-2,6-biphosphate acts as competitive inhibitor By similarity. |
| Pathway | |
| Subunit structure | Homotetramer By similarity. |
| Tissue specificity | Placenta and adult intestine. |
| Induction | By retinoic acid. |
| Sequence similarities | Belongs to the FBPase class 1 family. |
| Sequence caution | The sequence BAA07678.1 differs from that shown. Reason: Frameshift at position 321. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Carbohydrate metabolism Gluconeogenesis |
| Ligand | Magnesium Metal-binding |
| Molecular function | Hydrolase |
| PTM | Phosphoprotein |
| Technical term | Allosteric enzyme |
| Gene Ontology (GO) | |
| Biological process | gluconeogenesis Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | fructose 1,6-bisphosphate 1-phosphatase activity Inferred from electronic annotation. Source: EC magnesium ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 339 | 339 | Fructose-1,6-bisphosphatase isozyme 2 | PRO_0000200505 | |||||
Regions | |||||||||
| Nucleotide binding | 18 – 22 | 5 | AMP By similarity | ||||||
| Nucleotide binding | 28 – 32 | 5 | AMP By similarity | ||||||
| Nucleotide binding | 113 – 114 | 2 | AMP By similarity | ||||||
| Region | 122 – 125 | 4 | Substrate binding By similarity | ||||||
| Region | 213 – 216 | 4 | Substrate binding By similarity | ||||||
| Region | 244 – 249 | 6 | Substrate binding By similarity | ||||||
| Region | 275 – 277 | 3 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Metal binding | 69 | 1 | Magnesium 1 By similarity | ||||||
| Metal binding | 98 | 1 | Magnesium 1 By similarity | ||||||
| Metal binding | 98 | 1 | Magnesium 2 By similarity | ||||||
| Metal binding | 119 | 1 | Magnesium 2 By similarity | ||||||
| Metal binding | 119 | 1 | Magnesium 3 By similarity | ||||||
| Metal binding | 121 | 1 | Magnesium 2; via carbonyl oxygen By similarity | ||||||
| Metal binding | 122 | 1 | Magnesium 3 By similarity | ||||||
| Metal binding | 281 | 1 | Magnesium 3 By similarity | ||||||
| Binding site | 141 | 1 | AMP By similarity | ||||||
| Binding site | 265 | 1 | Substrate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 216 | 1 | Phosphotyrosine By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 171 | 1 | A → R in BAA07678. Ref.1 | ||||||
| Sequence conflict | 239 | 1 | E → A in AAH12720. Ref.3 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "One of the retinoic acid-inducible cDNA clones in mouse embryonal carcinoma F9 cells encodes a novel isoenzyme of fructose 1,6-bisphosphatase." Nomura M., Takihara Y., Yasunaga T., Shimada K. FEBS Lett. 348:201-205(1994) [PubMed: 8034042] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: BALB/c. |
| [2] | "Structure and chromosomal localization of the human and mouse muscle fructose-1,6-bisphosphatase genes." Tillmann H., Stein S., Liehr T., Eschrich K. Gene 247:241-253(2000) [PubMed: 10773464] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. Tissue: Skeletal muscle. |
| [3] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Colon. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | D42083 mRNA. Translation: BAA07678.1. Frameshift. AJ132692 mRNA. Translation: CAB65243.1. AJ243020 Genomic DNA. Translation: CAB90667.1. AJ243021 Genomic DNA. Translation: CAB90668.1. AJ243022 Genomic DNA. Translation: CAB90669.1. AJ243023 Genomic DNA. Translation: CAB90670.1. AJ243024 Genomic DNA. Translation: CAB90671.1. AJ243025 Genomic DNA. Translation: CAB90672.1. AJ243026 Genomic DNA. Translation: CAB90673.1. AJ243027 Genomic DNA. Translation: CAB90674.1. AJ243028 Genomic DNA. Translation: CAB90675.1. AJ245381 Genomic DNA. Translation: CAB65260.1. AJ245382 Genomic DNA. Translation: CAB65261.1. AJ245383 Genomic DNA. Translation: CAB65262.1. BC012720 mRNA. Translation: AAH12720.1. |
| IPI | IPI00111954. |
| PIR | S46245. |
| RefSeq | NP_032020.2. |
| UniGene | Mm.391871 |
3D structure databases | |
| SMR | P70695. Positions 7-337. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P70695. |
PTM databases | |
| PhosphoSite | P70695. |
Proteomic databases | |
| PRIDE | P70695. |
Genome annotation databases | |
| Ensembl | ENSMUST00000021907; ENSMUSP00000021907; ENSMUSG00000021456; Mus musculus. [Genome view] |
| GeneID | 14120. |
| KEGG | mmu:14120. |
| UCSC | uc007qxf.1. mouse. |
Organism-specific databases | |
| CTD | 14120. |
| MGI | MGI:95491. Fbp2. |
Phylogenomic databases | |
| eggNOG | roNOG08567. |
| HOVERGEN | P70695. |
| InParanoid | P70695. |
| OMA | ITAKEKR. |
| OrthoDB | EOG9Z3905. |
| PhylomeDB | P70695. |
Enzyme and pathway databases | |
| BRENDA | 3.1.3.11. 244. |
Gene expression databases | |
| ArrayExpress | P70695. |
| Bgee | P70695. |
| CleanEx | MM_FBP2. |
| Genevestigator | P70695. |
| GermOnline | ENSMUSG00000021456. Mus musculus. |
Family and domain databases | |
| InterPro | IPR000146. Fructose_bisphosphatase. IPR020548. Fructose_bisphosphatase_AS. [Graphical view] |
| PANTHER | PTHR11556. In_FB_phphtase. 1 hit. |
| Pfam | PF00316. FBPase. 1 hit. [Graphical view] |
| PRINTS | PR00115. F16BPHPHTASE. |
| PROSITE | PS00124. FBPASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 285188. |
| SOURCE | Search... |
Entry information
| Entry name | F16P2_MOUSE | ||||||||
| Accession | Primary (citable) accession number: P70695 Secondary accession number(s): Q91X26 Q9QXD7 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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