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P70695

- F16P2_MOUSE

UniProt

P70695 - F16P2_MOUSE

Protein

Fructose-1,6-bisphosphatase isozyme 2

Gene

Fbp2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 2 (27 Sep 2005)
      Previous versions | rss
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    Functioni

    Catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate in the presence of divalent cations and probably participates in glycogen synthesis from carbohydrate precursors, such as lactate.1 Publication

    Catalytic activityi

    D-fructose 1,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate.

    Cofactori

    Binds 3 magnesium ions per subunit.By similarity

    Enzyme regulationi

    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-bisphosphate acts as competitive inhibitor. Strongly inhibited by Ca2+ By similarity.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei18 – 181AMP; via carbonyl oxygenBy similarity
    Sitei33 – 331Important for the conversion from active R-state to inactive T-state in the presence of AMPBy similarity
    Metal bindingi69 – 691Magnesium 1By similarity
    Metal bindingi98 – 981Magnesium 1By similarity
    Metal bindingi98 – 981Magnesium 2By similarity
    Metal bindingi119 – 1191Magnesium 2By similarity
    Metal bindingi119 – 1191Magnesium 3By similarity
    Metal bindingi121 – 1211Magnesium 2; via carbonyl oxygenBy similarity
    Metal bindingi122 – 1221Magnesium 3By similarity
    Binding sitei122 – 1221SubstrateBy similarity
    Binding sitei141 – 1411AMPBy similarity
    Binding sitei265 – 2651SubstrateBy similarity
    Binding sitei275 – 2751SubstrateBy similarity
    Metal bindingi281 – 2811Magnesium 3By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi28 – 325AMPBy similarity
    Nucleotide bindingi113 – 1142AMPBy similarity

    GO - Molecular functioni

    1. fructose 1,6-bisphosphate 1-phosphatase activity Source: UniProtKB-EC
    2. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. gluconeogenesis Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Gluconeogenesis

    Keywords - Ligandi

    Calcium, Magnesium, Metal-binding

    Enzyme and pathway databases

    UniPathwayiUPA00138.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fructose-1,6-bisphosphatase isozyme 2 (EC:3.1.3.11)
    Short name:
    FBPase 2
    Alternative name(s):
    D-fructose-1,6-bisphosphate 1-phosphohydrolase 2
    Muscle FBPase
    RAE-30
    Gene namesi
    Name:Fbp2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 13

    Organism-specific databases

    MGIiMGI:95491. Fbp2.

    Subcellular locationi

    Cell junction By similarity. Cytoplasm By similarity. Nucleus By similarity. CytoplasmmyofibrilsarcomereZ line By similarity
    Note: In neonatal cardiomyocytes, distributed throughout the cytosol, accumulating in the intercalated disks which occur at the Z line of cardiomyocytes and connect adjacent cells, and also located in the nucleus; dissociates from the Z line following an increase in cytosolic Ca2+ concentration. In muscle precursor cells, localizes predominantly to the nucleus and to a lesser extent to the cytoplasm at the proliferative phase, while mainly localizing to the cytoplasm at the differentiation phase. Colocalizes with ALDOA and alpha-actinin on both sides of the Z line of skeletal muscle; dissociates rapidly from the Z line following an increase in cytosolic Ca2+ concentration.By similarity

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB-SubCell
    3. Z disc Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 339339Fructose-1,6-bisphosphatase isozyme 2PRO_0000200505Add
    BLAST

    Proteomic databases

    MaxQBiP70695.
    PaxDbiP70695.
    PRIDEiP70695.

    PTM databases

    PhosphoSiteiP70695.

    Expressioni

    Tissue specificityi

    Expressed in muscle, intestine, brain and placenta and very weakly in liver.2 Publications

    Inductioni

    By retinoic acid.1 Publication

    Gene expression databases

    ArrayExpressiP70695.
    BgeeiP70695.
    CleanExiMM_FBP2.
    GenevestigatoriP70695.

    Interactioni

    Subunit structurei

    Homotetramer. Interacts with ALDOA; the interaction blocks inhibition by physiological concentrations of AMP and reduces inhibition by Ca2+. Interacts with alpha-actinin and F-actin By similarity.By similarity

    Protein-protein interaction databases

    IntActiP70695. 1 interaction.
    MINTiMINT-4094831.

    Structurei

    3D structure databases

    ProteinModelPortaliP70695.
    SMRiP70695. Positions 9-337.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni3 – 108Important for interaction with ALDOABy similarity
    Regioni213 – 2164Substrate bindingBy similarity
    Regioni245 – 2495Substrate bindingBy similarity

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi204 – 2085Nuclear localization signalBy similarity

    Sequence similaritiesi

    Belongs to the FBPase class 1 family.Curated

    Phylogenomic databases

    eggNOGiCOG0158.
    HOVERGENiHBG005627.
    InParanoidiP70695.
    KOiK03841.
    OMAiHPSINEY.
    OrthoDBiEOG7GJ6D9.
    PhylomeDBiP70695.
    TreeFamiTF314824.

    Family and domain databases

    HAMAPiMF_01855. FBPase_class1.
    InterProiIPR000146. FBPase_class-1/SBPase.
    IPR028343. FBPtase.
    IPR020548. Fructose_bisphosphatase_AS.
    [Graphical view]
    PANTHERiPTHR11556. PTHR11556. 1 hit.
    PfamiPF00316. FBPase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF500210. FBPtase. 1 hit.
    PIRSF000904. FBPtase_SBPase. 1 hit.
    PRINTSiPR00115. F16BPHPHTASE.
    PROSITEiPS00124. FBPASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P70695-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTDRSPFETD MLTLTRYVME KGRQAKGTGE LTQLLNSMLT AIKAISSAVR    50
    KAGLANLYGI SGSVNVTGDE VKKLDVLSNS LVINMLQSSY STCVLVSEEN 100
    KEAVITAQER RGKYVVCFDP LDGSSNIDCL ASIGTIFAIY RKTTEDEPSE 150
    KDALQPGRNI VAAGYALYGS ATLVALSTGQ GVDLFMLDPA LGEFVLVEKD 200
    VRIKKKGKIF SLNEGYAKYF DAATAEYVQK KKFPEDGSEP YGARYVGSMV 250
    ADVHRTLVYG GIFMYPANQK SPNGKLRLLY ECNPVAYIIE QAGGMATTGT 300
    QPVLDVKPES IHQRVPLILG SPEDVQEYLS CVQRNQAGR 339
    Length:339
    Mass (Da):36,947
    Last modified:September 27, 2005 - v2
    Checksum:i442A3C5D09017415
    GO

    Sequence cautioni

    The sequence BAA07678.1 differs from that shown. Reason: Frameshift at position 321.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti171 – 1711A → R in BAA07678. (PubMed:8034042)Curated
    Sequence conflicti239 – 2391E → A in AAH12720. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS36698.1.
    PIRiS46245.
    RefSeqiNP_032020.2. NM_007994.3.
    UniGeneiMm.391871.

    Genome annotation databases

    EnsembliENSMUST00000021907; ENSMUSP00000021907; ENSMUSG00000021456.
    GeneIDi14120.
    KEGGimmu:14120.
    UCSCiuc007qxf.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS36698.1.
    PIRi S46245.
    RefSeqi NP_032020.2. NM_007994.3.
    UniGenei Mm.391871.

    3D structure databases

    ProteinModelPortali P70695.
    SMRi P70695. Positions 9-337.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P70695. 1 interaction.
    MINTi MINT-4094831.

    PTM databases

    PhosphoSitei P70695.

    Proteomic databases

    MaxQBi P70695.
    PaxDbi P70695.
    PRIDEi P70695.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000021907 ; ENSMUSP00000021907 ; ENSMUSG00000021456 .
    GeneIDi 14120.
    KEGGi mmu:14120.
    UCSCi uc007qxf.1. mouse.

    Organism-specific databases

    CTDi 8789.
    MGIi MGI:95491. Fbp2.

    Phylogenomic databases

    eggNOGi COG0158.
    HOVERGENi HBG005627.
    InParanoidi P70695.
    KOi K03841.
    OMAi HPSINEY.
    OrthoDBi EOG7GJ6D9.
    PhylomeDBi P70695.
    TreeFami TF314824.

    Enzyme and pathway databases

    UniPathwayi UPA00138 .

    Miscellaneous databases

    NextBioi 285188.
    PROi P70695.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P70695.
    Bgeei P70695.
    CleanExi MM_FBP2.
    Genevestigatori P70695.

    Family and domain databases

    HAMAPi MF_01855. FBPase_class1.
    InterProi IPR000146. FBPase_class-1/SBPase.
    IPR028343. FBPtase.
    IPR020548. Fructose_bisphosphatase_AS.
    [Graphical view ]
    PANTHERi PTHR11556. PTHR11556. 1 hit.
    Pfami PF00316. FBPase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF500210. FBPtase. 1 hit.
    PIRSF000904. FBPtase_SBPase. 1 hit.
    PRINTSi PR00115. F16BPHPHTASE.
    PROSITEi PS00124. FBPASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, INDUCTION.
      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] [Europe PMC] [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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: FVB/N.
      Tissue: Colon.
    4. "Characterization of the mouse liver fructose-1,6-bisphosphatase gene."
      Stein S., Liehr T., Eschrich K.
      Gene 264:215-224(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiF16P2_MOUSE
    AccessioniPrimary (citable) accession number: P70695
    Secondary accession number(s): Q91X26
    , Q9JK01, Q9JK02, Q9JK03, Q9JK04, Q9JK05, Q9JK06, Q9JK07, Q9JK08, Q9JK09, Q9QXB4, Q9QXB5, Q9QXB6, Q9QXD7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: September 27, 2005
    Last modified: October 1, 2014
    This is version 116 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Allosteric enzyme, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3