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Protein

Fructose-1,6-bisphosphatase 1

Gene

Fbp1

Organism
Mus musculus (Mouse)
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, acting as a rate-limiting enzyme in gluconeogenesis. Plays a role in regulating glucose sensing and insulin secretion of pancreatic beta-cells. Appears to modulate glycerol gluconeogenesis in liver. Important regulator of appetite and adiposity; increased expression of the protein in liver after nutrient excess increases circulating satiety hormones and reduces appetite-stimulating neuropeptides and thus seems to provide a feedback mechanism to limit weight gain.3 Publications

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. AMP binding affects the turnover of bound substrate and not the affinity for substrate. Fructose 2,6-bisphosphate acts as competitive inhibitor. Fructose 2,6-bisphosphate and AMP have synergistic effects (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
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 sitei141 – 1411AMPBy similarity
Binding sitei265 – 2651SubstrateBy similarity
Metal bindingi281 – 2811Magnesium 3By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi18 – 225AMPBy similarity
Nucleotide bindingi28 – 325AMPBy similarity
Nucleotide bindingi113 – 1142AMPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Gluconeogenesis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

ReactomeiR-MMU-70263. Gluconeogenesis.
UniPathwayiUPA00138.

Names & Taxonomyi

Protein namesi
Recommended name:
Fructose-1,6-bisphosphatase 1 (EC:3.1.3.11)
Short name:
FBPase 1
Alternative name(s):
D-fructose-1,6-bisphosphate 1-phosphohydrolase 1
Fructose-1,6-bisphosphatase isozyme 3
Short name:
FBPase 3
Liver FBPase
Gene namesi
Name:Fbp1
Synonyms:Fbp, Fbp3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:95492. Fbp1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL5360.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 338337Fructose-1,6-bisphosphatase 1PRO_0000200499Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei151 – 1511N6-succinyllysineCombined sources
Modified residuei216 – 2161PhosphotyrosineCombined sources
Modified residuei245 – 2451PhosphotyrosineCombined sources
Modified residuei265 – 2651PhosphotyrosineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9QXD6.
MaxQBiQ9QXD6.
PaxDbiQ9QXD6.
PRIDEiQ9QXD6.

2D gel databases

REPRODUCTION-2DPAGEIPI00228630.
Q9QXD6.

PTM databases

iPTMnetiQ9QXD6.
PhosphoSiteiQ9QXD6.
SwissPalmiQ9QXD6.

Expressioni

Tissue specificityi

Detected in pancreatic beta-cell lines MIN6 and beta-TC and in liver (at protein level). Preferentially expressed in liver, with lower levels detected in pancreatic islets and intestine, and very low levels in blood, muscle, brain and spleen.4 Publications

Inductioni

Up-regulated in pancreas by obesity and dietary fat intake and in diabetic animals.1 Publication

Gene expression databases

BgeeiQ9QXD6.
CleanExiMM_FBP1.
ExpressionAtlasiQ9QXD6. baseline and differential.
GenevisibleiQ9QXD6. MM.

Interactioni

Subunit structurei

Homotetramer.By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi199610. 1 interaction.
IntActiQ9QXD6. 18 interactions.
MINTiMINT-1855171.
STRINGi10090.ENSMUSP00000090564.

Chemistry

BindingDBiQ9QXD6.

Structurei

3D structure databases

ProteinModelPortaliQ9QXD6.
SMRiQ9QXD6. Positions 13-335.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni122 – 1254Substrate bindingBy similarity
Regioni213 – 2164Substrate bindingBy similarity
Regioni244 – 2496Substrate bindingBy similarity
Regioni275 – 2773Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the FBPase class 1 family.Curated

Phylogenomic databases

eggNOGiKOG1458. Eukaryota.
COG0158. LUCA.
GeneTreeiENSGT00390000015513.
HOGENOMiHOG000191265.
HOVERGENiHBG005627.
InParanoidiQ9QXD6.
KOiK03841.
OMAiYRKNSTD.
OrthoDBiEOG7GJ6D9.
PhylomeDBiQ9QXD6.
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.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9QXD6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MANHAPFETD ISTLTRFVME QGRKAQGTGE LTQLLNSLCT AIKAISSAVR
60 70 80 90 100
QAGIAQLYGI AGSTNVTGDQ VKKLDILSND LVINMLKSSY ATCVLVSEEN
110 120 130 140 150
TNAIIIEPEK RGKYVVCFDP LDGSSNIDCL VSIGTIFGIY RKKSTDEPSE
160 170 180 190 200
KDALQPGRDL VAAGYALYGS ATMLVLAMDC GVNCFMLDPS IGEFIMVDRD
210 220 230 240 250
VKMKKKGNIY SLNEGYAKDF DPAINEYLQR KKFPPDGSAP YGARYVGSMV
260 270 280 290 300
ADIHRTLVYG GIFLYPANKK SPSGKLRLLY ECNPIAYVME KAGGLATTGD
310 320 330
KDILDIVPTE IHQKAPVVMG SSEDVQEFLE IYRKHKAK
Length:338
Mass (Da):36,912
Last modified:January 23, 2007 - v3
Checksum:i50AE999F0D517E4F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti198 – 1981D → E in CAA71946 (PubMed:9106734).Curated
Sequence conflicti201 – 2011V → G in CAA71946 (PubMed:9106734).Curated
Sequence conflicti221 – 2211D → N in CAA71946 (PubMed:9106734).Curated
Sequence conflicti225 – 2251N → L in CAA71946 (PubMed:9106734).Curated
Sequence conflicti228 – 2281L → H in CAA71946 (PubMed:9106734).Curated
Sequence conflicti231 – 2311K → Q in CAA71946 (PubMed:9106734).Curated
Sequence conflicti234 – 2352PP → HE in CAA71946 (PubMed:9106734).Curated
Sequence conflicti238 – 2381S → T in CAA71946 (PubMed:9106734).Curated
Sequence conflicti243 – 2431A → T in CAA71946 (PubMed:9106734).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ132693 mRNA. Translation: CAB65244.1.
AK002216 mRNA. Translation: BAB21941.1.
AK149527 mRNA. Translation: BAE28940.1.
BC011480 mRNA. Translation: AAH11480.1.
BC051392 mRNA. Translation: AAH51392.1.
Y11067 mRNA. Translation: CAA71946.1.
CCDSiCCDS26590.1.
RefSeqiNP_062268.1. NM_019395.3.
UniGeneiMm.423078.

Genome annotation databases

EnsembliENSMUST00000092888; ENSMUSP00000090564; ENSMUSG00000069805.
GeneIDi14121.
KEGGimmu:14121.
UCSCiuc007qxg.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ132693 mRNA. Translation: CAB65244.1.
AK002216 mRNA. Translation: BAB21941.1.
AK149527 mRNA. Translation: BAE28940.1.
BC011480 mRNA. Translation: AAH11480.1.
BC051392 mRNA. Translation: AAH51392.1.
Y11067 mRNA. Translation: CAA71946.1.
CCDSiCCDS26590.1.
RefSeqiNP_062268.1. NM_019395.3.
UniGeneiMm.423078.

3D structure databases

ProteinModelPortaliQ9QXD6.
SMRiQ9QXD6. Positions 13-335.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199610. 1 interaction.
IntActiQ9QXD6. 18 interactions.
MINTiMINT-1855171.
STRINGi10090.ENSMUSP00000090564.

Chemistry

BindingDBiQ9QXD6.
ChEMBLiCHEMBL5360.

PTM databases

iPTMnetiQ9QXD6.
PhosphoSiteiQ9QXD6.
SwissPalmiQ9QXD6.

2D gel databases

REPRODUCTION-2DPAGEIPI00228630.
Q9QXD6.

Proteomic databases

EPDiQ9QXD6.
MaxQBiQ9QXD6.
PaxDbiQ9QXD6.
PRIDEiQ9QXD6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000092888; ENSMUSP00000090564; ENSMUSG00000069805.
GeneIDi14121.
KEGGimmu:14121.
UCSCiuc007qxg.2. mouse.

Organism-specific databases

CTDi2203.
MGIiMGI:95492. Fbp1.

Phylogenomic databases

eggNOGiKOG1458. Eukaryota.
COG0158. LUCA.
GeneTreeiENSGT00390000015513.
HOGENOMiHOG000191265.
HOVERGENiHBG005627.
InParanoidiQ9QXD6.
KOiK03841.
OMAiYRKNSTD.
OrthoDBiEOG7GJ6D9.
PhylomeDBiQ9QXD6.
TreeFamiTF314824.

Enzyme and pathway databases

UniPathwayiUPA00138.
ReactomeiR-MMU-70263. Gluconeogenesis.

Miscellaneous databases

ChiTaRSiFbp1. mouse.
PROiQ9QXD6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9QXD6.
CleanExiMM_FBP1.
ExpressionAtlasiQ9QXD6. baseline and differential.
GenevisibleiQ9QXD6. MM.

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. "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: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Liver.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Kidney and Liver.
  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: Liver.
  4. "Various fructose-1,6-bisphosphatase mRNAs in mouse brain, liver, kidney and heart."
    Cloix J.F., Beaulieu E., Hevor T.K.
    NeuroReport 8:617-622(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 154-247.
    Strain: C57BL/6J.
  5. "Expression of human fructose-1,6-bisphosphatase in the liver of transgenic mice results in increased glycerol gluconeogenesis."
    Lamont B.J., Visinoni S., Fam B.C., Kebede M., Weinrich B., Papapostolou S., Massinet H., Proietto J., Favaloro J., Andrikopoulos S.
    Endocrinology 147:2764-2772(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-216, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  7. "Fructose-1,6-bisphosphatase overexpression in pancreatic beta-cells results in reduced insulin secretion: a new mechanism for fat-induced impairment of beta-cell function."
    Kebede M., Favaloro J., Gunton J.E., Laybutt D.R., Shaw M., Wong N., Fam B.C., Aston-Mourney K., Rantzau C., Zulli A., Proietto J., Andrikopoulos S.
    Diabetes 57:1887-1895(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, INDUCTION.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-216; TYR-245 AND TYR-265, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney, Liver and Testis.
  9. "Fructose-1,6-bisphosphatase regulates glucose-stimulated insulin secretion of mouse pancreatic beta-cells."
    Zhang Y., Xie Z., Zhou G., Zhang H., Lu J., Zhang W.J.
    Endocrinology 151:4688-4695(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  10. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-151, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiF16P1_MOUSE
AccessioniPrimary (citable) accession number: Q9QXD6
Secondary accession number(s): P97323, Q3UEH1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 137 of the entry and version 3 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

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.