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Protein

Fructose-1,6-bisphosphatase isozyme 2

Gene

Fbp2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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.

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: gluconeogenesis

This protein is involved in the pathway gluconeogenesis, which is part of Carbohydrate biosynthesis.
View all proteins of this organism that are known to be involved in the pathway gluconeogenesis and in Carbohydrate biosynthesis.

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

GO - Biological processi

  • dephosphorylation Source: GOC
  • gluconeogenesis Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Gluconeogenesis

Keywords - Ligandi

Calcium, Magnesium, Metal-binding

Enzyme and pathway databases

ReactomeiR-RNO-70263. Gluconeogenesis.
SABIO-RKQ9Z1N1.
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
Gene namesi
Name:Fbp2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 17

Organism-specific databases

RGDi620930. Fbp2.

Subcellular locationi

  • Cell junction
  • Cytoplasm
  • Nucleus
  • CytoplasmmyofibrilsarcomereZ line

  • 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.

GO - Cellular componenti

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_0000200507Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei216 – 2161PhosphotyrosineCombined sources
Modified residuei219 – 2191PhosphotyrosineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9Z1N1.
PRIDEiQ9Z1N1.

PTM databases

iPTMnetiQ9Z1N1.

Expressioni

Gene expression databases

GenevisibleiQ9Z1N1. RN.

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

STRINGi10116.ENSRNOP00000023865.

Structurei

3D structure databases

ProteinModelPortaliQ9Z1N1.
SMRiQ9Z1N1. Positions 7-337.
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

eggNOGiKOG1458. Eukaryota.
COG0158. LUCA.
GeneTreeiENSGT00390000015513.
HOGENOMiHOG000191265.
HOVERGENiHBG005627.
InParanoidiQ9Z1N1.
KOiK03841.
OMAiIHERCSV.
OrthoDBiEOG7GJ6D9.
PhylomeDBiQ9Z1N1.
TreeFamiTF314824.

Family and domain databases

HAMAPiMF_01855. FBPase_class1.
InterProiIPR000146. FBPase_class-1.
IPR033391. FBPase_N.
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.

Q9Z1N1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTDRSPFETD MLTLTRYVME KGRQAKGTGE LTQLLNSMLT AIKAISSAVR
60 70 80 90 100
KAGLANLYGI AGSVNVTGDE VKKLDVLSNS LVINMLQSSY STCVLVSEEN
110 120 130 140 150
KEAVITAKER RGKYVVCFDP LDGSSNIDCL ASIGTIFAIY RKTTEDEPSE
160 170 180 190 200
KDALQPGRNI VAAGYALYGS ATLVALSTGQ GVDLFMLDPA LGEFVLVEKD
210 220 230 240 250
IRIKKKGKIF SLNEGYAKYF DAATAEYVQK KKFPEDGSAP YGARYVGSMV
260 270 280 290 300
ADVHRTLVYG GIFMYPANQK SPNGKLRLLY ECNPVAYIIE QAGGMATTGT
310 320 330
QPVLDVKPES IHQRVPLILG SPEDVQEYLS CVQRNQAGR
Length:339
Mass (Da):36,887
Last modified:May 1, 1999 - v1
Checksum:i13096E40E96095D8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ005046 mRNA. Translation: CAA06313.1.
RefSeqiNP_446168.1. NM_053716.1.
UniGeneiRn.15319.

Genome annotation databases

EnsembliENSRNOT00000023865; ENSRNOP00000023865; ENSRNOG00000017637.
GeneIDi114508.
KEGGirno:114508.
UCSCiRGD:620930. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ005046 mRNA. Translation: CAA06313.1.
RefSeqiNP_446168.1. NM_053716.1.
UniGeneiRn.15319.

3D structure databases

ProteinModelPortaliQ9Z1N1.
SMRiQ9Z1N1. Positions 7-337.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000023865.

PTM databases

iPTMnetiQ9Z1N1.

Proteomic databases

PaxDbiQ9Z1N1.
PRIDEiQ9Z1N1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000023865; ENSRNOP00000023865; ENSRNOG00000017637.
GeneIDi114508.
KEGGirno:114508.
UCSCiRGD:620930. rat.

Organism-specific databases

CTDi8789.
RGDi620930. Fbp2.

Phylogenomic databases

eggNOGiKOG1458. Eukaryota.
COG0158. LUCA.
GeneTreeiENSGT00390000015513.
HOGENOMiHOG000191265.
HOVERGENiHBG005627.
InParanoidiQ9Z1N1.
KOiK03841.
OMAiIHERCSV.
OrthoDBiEOG7GJ6D9.
PhylomeDBiQ9Z1N1.
TreeFamiTF314824.

Enzyme and pathway databases

UniPathwayiUPA00138.
ReactomeiR-RNO-70263. Gluconeogenesis.
SABIO-RKQ9Z1N1.

Miscellaneous databases

NextBioi618609.
PROiQ9Z1N1.

Gene expression databases

GenevisibleiQ9Z1N1. RN.

Family and domain databases

HAMAPiMF_01855. FBPase_class1.
InterProiIPR000146. FBPase_class-1.
IPR033391. FBPase_N.
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. "Cloning and expression of rat muscle fructose-1,6-bisphosphatase cDNA."
    Al-Robaiy S., Eschrich K.
    Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Skeletal muscle.
  2. "Changes in subcellular localization of fructose 1,6-bisphosphatase during differentiation of isolated muscle satellite cells."
    Gizak A., Wrobel E., Moraczewski J., Dzugaj A.
    FEBS Lett. 580:4042-4046(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  3. "Regulation of subcellular localization of muscle FBPase in cardiomyocytes. The decisive role of calcium ions."
    Majkowski M., Wypych D., Pomorski P., Dzugaj A.
    Acta Biochim. Pol. 57:597-605(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  4. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-216 AND TYR-219, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiF16P2_RAT
AccessioniPrimary (citable) accession number: Q9Z1N1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2005
Last sequence update: May 1, 1999
Last modified: May 11, 2016
This is version 106 of the entry and version 1 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.