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   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.
DR   Genevisible; P70695; MM.
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
//