F16P2_RABIT
ID F16P2_RABIT Reviewed; 339 AA.
AC Q9N0J6;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 97.
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 Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Muscle;
RX PubMed=12095679; DOI=10.1016/s0378-1119(02)00627-3;
RA Tillmann H., Bernhard D., Eschrich K.;
RT "Fructose-1,6-bisphosphatase genes in animals.";
RL Gene 291:57-66(2002).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND INTERACTION WITH
RP ALDOA.
RX PubMed=12860378; DOI=10.1016/s0014-5793(03)00661-6;
RA Rakus D., Pasek M., Krotkiewski H., Dzugaj A.;
RT "Muscle FBPase in a complex with muscle aldolase is insensitive to AMP
RT inhibition.";
RL FEBS Lett. 547:11-14(2003).
RN [3]
RP INTERACTION WITH ALPHA-ACTININ AND F-ACTIN.
RX PubMed=12507293; DOI=10.14670/hh-18.135;
RA Gizak A., Rakus D., Dzugaj A.;
RT "Immunohistochemical localization of human fructose-1,6-bisphosphatase in
RT subcellular structures of myocytes.";
RL Histol. Histopathol. 18:135-142(2003).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, INTERACTION WITH ALDOA
RP AND ALPHA-ACTININ, AND SUBCELLULAR LOCATION.
RX PubMed=15757649; DOI=10.1016/j.febslet.2005.01.071;
RA Mamczur P., Rakus D., Gizak A., Dus D., Dzugaj A.;
RT "The effect of calcium ions on subcellular localization of aldolase-FBPase
RT complex in skeletal muscle.";
RL FEBS Lett. 579:1607-1612(2005).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=17350621; DOI=10.1016/j.febslet.2007.02.051;
RA Zarzycki M., Maciaszczyk E., Dzugaj A.;
RT "Glu 69 is essential for the high sensitivity of muscle fructose-1,6-
RT bisphosphatase inhibition by calcium ions.";
RL FEBS Lett. 581:1347-1350(2007).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND INTERACTION WITH
RP ALDOA.
RX PubMed=18214967; DOI=10.1002/prot.21909;
RA Gizak A., Maciaszczyk E., Dzugaj A., Eschrich K., Rakus D.;
RT "Evolutionary conserved N-terminal region of human muscle fructose 1,6-
RT bisphosphatase regulates its activity and the interaction with aldolase.";
RL Proteins 72:209-216(2008).
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:12860378, ECO:0000269|PubMed:15757649,
CC ECO:0000269|PubMed:17350621, ECO:0000269|PubMed:18214967}.
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 Evidence={ECO:0000269|PubMed:12860378, ECO:0000269|PubMed:15757649,
CC ECO:0000269|PubMed:17350621, ECO:0000269|PubMed:18214967};
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+). {ECO:0000269|PubMed:12860378,
CC ECO:0000269|PubMed:15757649, ECO:0000269|PubMed:17350621,
CC ECO:0000269|PubMed:18214967}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.1 uM for fructose 1,6-bisphosphate
CC {ECO:0000269|PubMed:17350621};
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.
CC {ECO:0000269|PubMed:12507293, ECO:0000269|PubMed:12860378,
CC ECO:0000269|PubMed:15757649, ECO:0000269|PubMed:18214967}.
CC -!- SUBCELLULAR LOCATION: Cell junction {ECO:0000250}. Cytoplasm
CC {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, myofibril, sarcomere,
CC Z line {ECO:0000269|PubMed:15757649}. 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 (By
CC similarity). In muscle precursor cells, localizes predominantly to the
CC nucleus and to a lesser extent to the cytoplasm at the proliferative
CC phase, while mainly localizing to the cytoplasm at the differentiation
CC phase (By similarity). Colocalizes with ALDOA and alpha-actinin on both
CC sides of the Z line of skeletal muscle; dissociates rapidly from the Z
CC line following an increase in cytosolic Ca(2+) concentration.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FBPase class 1 family. {ECO:0000305}.
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DR EMBL; AJ272520; CAB76202.1; -; mRNA.
DR RefSeq; NP_001075597.1; NM_001082128.1.
DR AlphaFoldDB; Q9N0J6; -.
DR SMR; Q9N0J6; -.
DR GeneID; 100008853; -.
DR KEGG; ocu:100008853; -.
DR CTD; 8789; -.
DR InParanoid; Q9N0J6; -.
DR OrthoDB; 1381522at2759; -.
DR SABIO-RK; Q9N0J6; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
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_0000200506"
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; 36816 MW; C1D65B70F8763872 CRC64;
MTDRSPFETD MLTLTRYVME KGRQAKGTGE LTQLLNSMLT AIKAISSAVR KAGLAHLYGI
AGTVNVTGDE VKKLDVLSNA LVINMLQSSY STCVLVSEEN KEAIITAKER RGKYVVCFDP
LDGSSNIDCL ASIGTIFAIY RKTTEDEPSD KDALQPGRNI VAAGYALYGS ATLVALSTGQ
GVDLFMLDPA LGEFVLVEKD VKIKKKGKIF SLNEGYAKYF DAATTEYVQK KKFPEDGSAP
YGARYVGSMV ADVHRTLVYG GIFLYPANQK SPKGKLRLLY ECNPVAYIIE QAGGLATTGT
QPVLDVKPES IHQRVPLILG SPDDVQEYLA CVQKNQAGR
