ID F16P2_MOUSE Reviewed; 339 AA.
AC P70695; Q91X26; Q9JK01; Q9JK02; Q9JK03; Q9JK04; Q9JK05; Q9JK06; Q9JK07;
AC Q9JK08; Q9JK09; Q9QXB4; Q9QXB5; Q9QXB6; Q9QXD7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 2.
DT 27-MAR-2024, entry version 171.
DE RecName: Full=Fructose-1,6-bisphosphatase isozyme 2;
DE Short=FBPase 2;
DE EC=3.1.3.11;
DE AltName: Full=D-fructose-1,6-bisphosphate 1-phosphohydrolase 2;
DE AltName: Full=Muscle FBPase;
DE AltName: Full=RAE-30;
GN Name=Fbp2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=BALB/cJ;
RX PubMed=8034042; DOI=10.1016/0014-5793(94)00608-3;
RA Nomura M., Takihara Y., Yasunaga T., Shimada K.;
RT "One of the retinoic acid-inducible cDNA clones in mouse embryonal
RT carcinoma F9 cells encodes a novel isoenzyme of fructose 1,6-
RT bisphosphatase.";
RL FEBS Lett. 348:201-205(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Skeletal muscle;
RX PubMed=10773464; DOI=10.1016/s0378-1119(00)00079-2;
RA Tillmann H., Stein S., Liehr T., Eschrich K.;
RT "Structure and chromosomal localization of the human and mouse muscle
RT fructose-1,6-bisphosphatase genes.";
RL Gene 247:241-253(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=11250076; DOI=10.1016/s0378-1119(01)00325-0;
RA Stein S., Liehr T., Eschrich K.;
RT "Characterization of the mouse liver fructose-1,6-bisphosphatase gene.";
RL Gene 264:215-224(2001).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Catalyzes the hydrolysis of fructose 1,6-bisphosphate to
CC fructose 6-phosphate in the presence of divalent cations and probably
CC participates in glycogen synthesis from carbohydrate precursors, such
CC as lactate. {ECO:0000269|PubMed:8034042}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-
CC phosphate + phosphate; Xref=Rhea:RHEA:11064, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:32966, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=3.1.3.11;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Subject to complex allosteric regulation. The
CC enzyme can assume an active R-state, or an inactive T-state.
CC Intermediate conformations may exist. AMP acts as an allosteric
CC inhibitor. Fructose 2,6-bisphosphate acts as a competitive inhibitor.
CC Strongly inhibited by Ca(2+) (By similarity). {ECO:0000250}.
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC -!- SUBUNIT: Homotetramer. Interacts with ALDOA; the interaction blocks
CC inhibition by physiological concentrations of AMP and reduces
CC inhibition by Ca(2+). Interacts with alpha-actinin and F-actin (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell junction {ECO:0000250}. Cytoplasm
CC {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, myofibril, sarcomere,
CC Z line {ECO:0000250}. Note=In neonatal cardiomyocytes, distributed
CC throughout the cytosol, accumulating in the intercalated disks which
CC occur at the Z line of cardiomyocytes and connect adjacent cells, and
CC also located in the nucleus; dissociates from the Z line following an
CC increase in cytosolic Ca(2+) concentration. In muscle precursor cells,
CC localizes predominantly to the nucleus and to a lesser extent to the
CC cytoplasm at the proliferative phase, while mainly localizing to the
CC cytoplasm at the differentiation phase. Colocalizes with ALDOA and
CC alpha-actinin on both sides of the Z line of skeletal muscle;
CC dissociates rapidly from the Z line following an increase in cytosolic
CC Ca(2+) concentration. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in muscle, intestine, brain and placenta
CC and very weakly in liver. {ECO:0000269|PubMed:11250076,
CC ECO:0000269|PubMed:8034042}.
CC -!- INDUCTION: By retinoic acid. {ECO:0000269|PubMed:8034042}.
CC -!- SIMILARITY: Belongs to the FBPase class 1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA07678.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D42083; BAA07678.1; ALT_FRAME; mRNA.
DR EMBL; AJ132692; CAB65243.1; -; mRNA.
DR EMBL; AJ243020; CAB90667.1; -; Genomic_DNA.
DR EMBL; AJ243021; CAB90668.1; -; Genomic_DNA.
DR EMBL; AJ243022; CAB90669.1; -; Genomic_DNA.
DR EMBL; AJ243023; CAB90670.1; -; Genomic_DNA.
DR EMBL; AJ243024; CAB90671.1; -; Genomic_DNA.
DR EMBL; AJ243025; CAB90672.1; -; Genomic_DNA.
DR EMBL; AJ243026; CAB90673.1; -; Genomic_DNA.
DR EMBL; AJ243027; CAB90674.1; -; Genomic_DNA.
DR EMBL; AJ243028; CAB90675.1; -; Genomic_DNA.
DR EMBL; AJ245381; CAB65260.1; -; Genomic_DNA.
DR EMBL; AJ245382; CAB65261.1; -; Genomic_DNA.
DR EMBL; AJ245383; CAB65262.1; -; Genomic_DNA.
DR EMBL; BC012720; AAH12720.1; -; mRNA.
DR CCDS; CCDS36698.1; -.
DR PIR; S46245; S46245.
DR RefSeq; NP_032020.2; NM_007994.3.
DR AlphaFoldDB; P70695; -.
DR SMR; P70695; -.
DR BioGRID; 199609; 2.
DR STRING; 10090.ENSMUSP00000021907; -.
DR iPTMnet; P70695; -.
DR PhosphoSitePlus; P70695; -.
DR jPOST; P70695; -.
DR PaxDb; 10090-ENSMUSP00000021907; -.
DR PeptideAtlas; P70695; -.
DR ProteomicsDB; 275717; -.
DR Antibodypedia; 2920; 274 antibodies from 27 providers.
DR DNASU; 14120; -.
DR Ensembl; ENSMUST00000021907.9; ENSMUSP00000021907.8; ENSMUSG00000021456.9.
DR GeneID; 14120; -.
DR KEGG; mmu:14120; -.
DR UCSC; uc007qxf.1; mouse.
DR AGR; MGI:95491; -.
DR CTD; 8789; -.
DR MGI; MGI:95491; Fbp2.
DR VEuPathDB; HostDB:ENSMUSG00000021456; -.
DR eggNOG; KOG1458; Eukaryota.
DR GeneTree; ENSGT00390000015513; -.
DR HOGENOM; CLU_039977_1_0_1; -.
DR InParanoid; P70695; -.
DR OMA; NSRFWEP; -.
DR OrthoDB; 292at2759; -.
DR PhylomeDB; P70695; -.
DR TreeFam; TF314824; -.
DR Reactome; R-MMU-70263; Gluconeogenesis.
DR UniPathway; UPA00138; -.
DR BioGRID-ORCS; 14120; 2 hits in 78 CRISPR screens.
DR ChiTaRS; Fbp2; mouse.
DR PRO; PR:P70695; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; P70695; Protein.
DR Bgee; ENSMUSG00000021456; Expressed in small intestine Peyer's patch and 131 other cell types or tissues.
DR ExpressionAtlas; P70695; baseline and differential.
DR Genevisible; P70695; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
DR GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006000; P:fructose metabolic process; IBA:GO_Central.
DR GO; GO:0006094; P:gluconeogenesis; ISO:MGI.
DR GO; GO:0005986; P:sucrose biosynthetic process; IBA:GO_Central.
DR CDD; cd00354; FBPase; 1.
DR Gene3D; 3.40.190.80; -; 1.
DR Gene3D; 3.30.540.10; Fructose-1,6-Bisphosphatase, subunit A, domain 1; 1.
DR HAMAP; MF_01855; FBPase_class1; 1.
DR InterPro; IPR044015; FBPase_C_dom.
DR InterPro; IPR000146; FBPase_class-1.
DR InterPro; IPR033391; FBPase_N.
DR InterPro; IPR028343; FBPtase.
DR InterPro; IPR020548; Fructose_bisphosphatase_AS.
DR PANTHER; PTHR11556:SF13; FRUCTOSE-1,6-BISPHOSPHATASE ISOZYME 2; 1.
DR PANTHER; PTHR11556; FRUCTOSE-1,6-BISPHOSPHATASE-RELATED; 1.
DR Pfam; PF00316; FBPase; 1.
DR Pfam; PF18913; FBPase_C; 1.
DR PIRSF; PIRSF500210; FBPtase; 1.
DR PIRSF; PIRSF000904; FBPtase_SBPase; 1.
DR PRINTS; PR00115; F16BPHPHTASE.
DR SUPFAM; SSF56655; Carbohydrate phosphatase; 1.
DR PROSITE; PS00124; FBPASE; 1.
PE 1: Evidence at protein level;
KW Allosteric enzyme; Calcium; Carbohydrate metabolism; Cell junction;
KW Cytoplasm; Gluconeogenesis; Hydrolase; Magnesium; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..339
FT /note="Fructose-1,6-bisphosphatase isozyme 2"
FT /id="PRO_0000200505"
FT REGION 3..10
FT /note="Important for interaction with ALDOA"
FT /evidence="ECO:0000250"
FT MOTIF 204..208
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT BINDING 18
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250"
FT BINDING 28..32
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250"
FT BINDING 69
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 98
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 98
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 113..114
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250"
FT BINDING 119
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 119
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 121
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 122
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 141
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250"
FT BINDING 213..216
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 245..249
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 265
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 275
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 281
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT SITE 33
FT /note="Important for the conversion from active R-state to
FT inactive T-state in the presence of AMP"
FT /evidence="ECO:0000250"
FT MOD_RES 216
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1N1"
FT MOD_RES 219
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1N1"
FT CONFLICT 171
FT /note="A -> R (in Ref. 1; BAA07678)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="E -> A (in Ref. 3; AAH12720)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 339 AA; 36947 MW; 442A3C5D09017415 CRC64;
MTDRSPFETD MLTLTRYVME KGRQAKGTGE LTQLLNSMLT AIKAISSAVR KAGLANLYGI
SGSVNVTGDE VKKLDVLSNS LVINMLQSSY STCVLVSEEN KEAVITAQER RGKYVVCFDP
LDGSSNIDCL ASIGTIFAIY RKTTEDEPSE KDALQPGRNI VAAGYALYGS ATLVALSTGQ
GVDLFMLDPA LGEFVLVEKD VRIKKKGKIF SLNEGYAKYF DAATAEYVQK KKFPEDGSEP
YGARYVGSMV ADVHRTLVYG GIFMYPANQK SPNGKLRLLY ECNPVAYIIE QAGGMATTGT
QPVLDVKPES IHQRVPLILG SPEDVQEYLS CVQRNQAGR
//
