Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Fructose-1,6-bisphosphatase isozyme 2

Gene

Fbp2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

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

Mg2+By similarityNote: Binds 3 Mg2+ 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
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Gluconeogenesis

Keywords - Ligandi

Calcium, Magnesium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_308431. Gluconeogenesis.
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 Componenti: 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. extracellular vesicular exosome Source: MGI
  3. nucleus Source: UniProtKB-SubCell
  4. Z disc Source: UniProtKB-SubCell
Complete GO annotation...

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

BgeeiP70695.
CleanExiMM_FBP2.
ExpressionAtlasiP70695. baseline and differential.
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.
OMAiIHERCSV.
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

        10         20         30         40         50
MTDRSPFETD MLTLTRYVME KGRQAKGTGE LTQLLNSMLT AIKAISSAVR
60 70 80 90 100
KAGLANLYGI SGSVNVTGDE VKKLDVLSNS LVINMLQSSY STCVLVSEEN
110 120 130 140 150
KEAVITAQER RGKYVVCFDP LDGSSNIDCL ASIGTIFAIY RKTTEDEPSE
160 170 180 190 200
KDALQPGRNI VAAGYALYGS ATLVALSTGQ GVDLFMLDPA LGEFVLVEKD
210 220 230 240 250
VRIKKKGKIF SLNEGYAKYF DAATAEYVQK KKFPEDGSEP YGARYVGSMV
260 270 280 290 300
ADVHRTLVYG GIFMYPANQK SPNGKLRLLY ECNPVAYIIE QAGGMATTGT
310 320 330
QPVLDVKPES IHQRVPLILG SPEDVQEYLS CVQRNQAGR
Length:339
Mass (Da):36,947
Last modified:September 26, 2005 - v2
Checksum:i442A3C5D09017415
GO

Sequence cautioni

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

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

IntActiP70695. 1 interaction.
MINTiMINT-4094831.

PTM databases

PhosphoSiteiP70695.

Proteomic databases

MaxQBiP70695.
PaxDbiP70695.
PRIDEiP70695.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi8789.
MGIiMGI:95491. Fbp2.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayiUPA00138.
ReactomeiREACT_308431. Gluconeogenesis.

Miscellaneous databases

NextBioi285188.
PROiP70695.
SOURCEiSearch...

Gene expression databases

BgeeiP70695.
CleanExiMM_FBP2.
ExpressionAtlasiP70695. baseline and differential.
GenevestigatoriP70695.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1993) [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(1999) [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(2003) [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(2000) [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: October 31, 1997
Last sequence update: September 26, 2005
Last modified: March 31, 2015
This is version 121 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.