F16P2_BOVIN
ID F16P2_BOVIN Reviewed; 339 AA.
AC Q2KJJ9;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 111.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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 {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 -!- SIMILARITY: Belongs to the FBPase class 1 family. {ECO:0000305}.
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DR EMBL; BC102390; AAI02391.1; -; mRNA.
DR RefSeq; NP_001039629.1; NM_001046164.2.
DR AlphaFoldDB; Q2KJJ9; -.
DR SMR; Q2KJJ9; -.
DR STRING; 9913.ENSBTAP00000026056; -.
DR PaxDb; Q2KJJ9; -.
DR PeptideAtlas; Q2KJJ9; -.
DR Ensembl; ENSBTAT00000026056; ENSBTAP00000026056; ENSBTAG00000019554.
DR GeneID; 514066; -.
DR KEGG; bta:514066; -.
DR CTD; 8789; -.
DR VEuPathDB; HostDB:ENSBTAG00000019554; -.
DR VGNC; VGNC:28888; FBP2.
DR eggNOG; KOG1458; Eukaryota.
DR GeneTree; ENSGT00390000015513; -.
DR HOGENOM; CLU_039977_1_0_1; -.
DR InParanoid; Q2KJJ9; -.
DR OMA; HEKSECY; -.
DR OrthoDB; 1381522at2759; -.
DR TreeFam; TF314824; -.
DR SABIO-RK; Q2KJJ9; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000009136; Chromosome 8.
DR Bgee; ENSBTAG00000019554; Expressed in biceps femoris and 84 other tissues.
DR ExpressionAtlas; Q2KJJ9; 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; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
DR GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
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; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Calcium; Carbohydrate metabolism; Cell junction; Cytoplasm;
KW 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_0000247323"
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"
SQ SEQUENCE 339 AA; 36767 MW; DB3FE9856DDC5FB2 CRC64;
MGDRSPFETD MLTLTRYVME KGRQAKGTGE LTQLLNSMLT AIKAISSAVR KAGLANLYGI
AGSVNVTGDE VKKLDVLSNA LVINMLQSSY STCVLVSEEN KEAIITSKEK RGKYVVCFDP
LDGSSNIDCL ASIGTIFAIY RKTSEDEPSE KDALQPGRNI VAAGYALYGS ATLVALSTGQ
GVDLFMLDPA LGEFVLVEKD VKIKKKGKIY SLNEGYAKYF DAATTEYVQK KKFPEDGSAP
YGARYVGSMV ADVHRTLVYG GIFLYPANQK SPKGKLRLLY ECNPVAYIIE QAGGLATTGT
QPVLDVKPEA IHQRVPLILG SPEDVQEYLT CVQKNQAGR
