F16P2_RAT
ID F16P2_RAT Reviewed; 339 AA.
AC Q9Z1N1;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 132.
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;
GN Name=Fbp2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skeletal muscle;
RA Al-Robaiy S., Eschrich K.;
RT "Cloning and expression of rat muscle fructose-1,6-bisphosphatase cDNA.";
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=16814784; DOI=10.1016/j.febslet.2006.06.042;
RA Gizak A., Wrobel E., Moraczewski J., Dzugaj A.;
RT "Changes in subcellular localization of fructose 1,6-bisphosphatase during
RT differentiation of isolated muscle satellite cells.";
RL FEBS Lett. 580:4042-4046(2006).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=21046014; DOI=10.18388/abp.2010_2450;
RA Majkowski M., Wypych D., Pomorski P., Dzugaj A.;
RT "Regulation of subcellular localization of muscle FBPase in cardiomyocytes.
RT The decisive role of calcium ions.";
RL Acta Biochim. Pol. 57:597-605(2010).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-216 AND TYR-219, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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.
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 allosteric inhibitor.
CC Fructose 2,6-bisphosphate acts as competitive inhibitor. Strongly
CC 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. Cytoplasm. Nucleus. Cytoplasm,
CC myofibril, sarcomere, Z line. Note=In neonatal cardiomyocytes,
CC distributed throughout the cytosol, accumulating in the intercalated
CC disks which occur at the Z line of cardiomyocytes and connect adjacent
CC cells, and also located in the nucleus; dissociates from the Z line
CC following an increase in cytosolic Ca(2+) concentration. In muscle
CC precursor cells, localizes predominantly to the nucleus and to a lesser
CC extent to the cytoplasm at the proliferative phase, while mainly
CC localizing to the cytoplasm at the differentiation phase. Colocalizes
CC with ALDOA and alpha-actinin on both sides of the Z line of skeletal
CC muscle; dissociates rapidly from the Z line following an increase in
CC cytosolic Ca(2+) concentration.
CC -!- SIMILARITY: Belongs to the FBPase class 1 family. {ECO:0000305}.
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DR EMBL; AJ005046; CAA06313.1; -; mRNA.
DR RefSeq; NP_446168.1; NM_053716.1.
DR AlphaFoldDB; Q9Z1N1; -.
DR SMR; Q9Z1N1; -.
DR STRING; 10116.ENSRNOP00000023865; -.
DR iPTMnet; Q9Z1N1; -.
DR PhosphoSitePlus; Q9Z1N1; -.
DR jPOST; Q9Z1N1; -.
DR PaxDb; Q9Z1N1; -.
DR PRIDE; Q9Z1N1; -.
DR Ensembl; ENSRNOT00000023865; ENSRNOP00000023865; ENSRNOG00000017637.
DR GeneID; 114508; -.
DR KEGG; rno:114508; -.
DR UCSC; RGD:620930; rat.
DR CTD; 8789; -.
DR RGD; 620930; Fbp2.
DR eggNOG; KOG1458; Eukaryota.
DR GeneTree; ENSGT00390000015513; -.
DR HOGENOM; CLU_039977_1_0_1; -.
DR InParanoid; Q9Z1N1; -.
DR OMA; HEKSECY; -.
DR OrthoDB; 1381522at2759; -.
DR PhylomeDB; Q9Z1N1; -.
DR TreeFam; TF314824; -.
DR Reactome; R-RNO-70263; Gluconeogenesis.
DR SABIO-RK; Q9Z1N1; -.
DR UniPathway; UPA00138; -.
DR PRO; PR:Q9Z1N1; -.
DR Proteomes; UP000002494; Chromosome 17.
DR Bgee; ENSRNOG00000017637; Expressed in duodenum and 16 other tissues.
DR Genevisible; Q9Z1N1; RN.
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; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
DR GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
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; IDA:RGD.
DR GO; GO:0005986; P:sucrose biosynthetic process; IBA:GO_Central.
DR CDD; cd00354; FBPase; 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; PTHR11556; 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 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_0000200507"
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:0007744|PubMed:22673903"
FT MOD_RES 219
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 339 AA; 36887 MW; 13096E40E96095D8 CRC64;
MTDRSPFETD MLTLTRYVME KGRQAKGTGE LTQLLNSMLT AIKAISSAVR KAGLANLYGI
AGSVNVTGDE VKKLDVLSNS LVINMLQSSY STCVLVSEEN KEAVITAKER RGKYVVCFDP
LDGSSNIDCL ASIGTIFAIY RKTTEDEPSE KDALQPGRNI VAAGYALYGS ATLVALSTGQ
GVDLFMLDPA LGEFVLVEKD IRIKKKGKIF SLNEGYAKYF DAATAEYVQK KKFPEDGSAP
YGARYVGSMV ADVHRTLVYG GIFMYPANQK SPNGKLRLLY ECNPVAYIIE QAGGMATTGT
QPVLDVKPES IHQRVPLILG SPEDVQEYLS CVQRNQAGR
