F16P2_HUMAN
ID F16P2_HUMAN Reviewed; 339 AA.
AC O00757; Q17R39; Q6FI53;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 2.
DT 03-AUG-2022, entry version 181.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT LEU-86.
RC TISSUE=Skeletal muscle;
RX PubMed=9678974; DOI=10.1016/s0378-1119(98)00181-4;
RA Tillman H., Eschrich K.;
RT "Isolation and characterization of an allelic cDNA for human muscle
RT fructose-1,6-bisphosphatase.";
RL Gene 212:295-304(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-86.
RC 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 [5]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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 [6]
RP ACTIVITY REGULATION, COFACTOR, MUTAGENESIS OF LYS-21; THR-178 AND GLN-180,
RP AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=16213487; DOI=10.1016/j.febslet.2005.09.021;
RA Rakus D., Maciaszczyk E., Wawrzycka D., Ulaszewski S., Eschrich K.,
RA Dzugaj A.;
RT "The origin of the high sensitivity of muscle fructose 1,6-bisphosphatase
RT towards AMP.";
RL FEBS Lett. 579:5577-5581(2005).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND MUTAGENESIS OF GLU-70.
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 [8]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, INTERACTION WITH ALDOA,
RP AND MUTAGENESIS OF 1-MET--ASP-10.
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).
RN [9]
RP SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL, AND MUTAGENESIS OF
RP 204-LYS--LYS-208.
RX PubMed=19626708; DOI=10.1002/prot.22506;
RA Gizak A., Maciaszczyk-Dziubinska E., Jurowicz M., Rakus D.;
RT "Muscle FBPase is targeted to nucleus by its 203KKKGK207 sequence.";
RL Proteins 77:262-267(2009).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 2-339 OF MUTANT GLN-70 IN COMPLEX
RP WITH FRUCTOSE-6-PHOSPHATE AND AMP, AND SUBUNIT.
RX PubMed=22120740; DOI=10.1107/s090744491104385x;
RA Zarzycki M., Kolodziejczyk R., Maciaszczyk-Dziubinska E., Wysocki R.,
RA Jaskolski M., Dzugaj A.;
RT "Structure of E69Q mutant of human muscle fructose-1,6-bisphosphatase.";
RL Acta Crystallogr. D 67:1028-1034(2011).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 2-339 OF WILD-TYPE AND MUTANT
RP ARG-33 IN COMPLEXES WITH FRUCTOSE-6-PHOSPHATE; PHOSPHATE ION; AMP; ZINC ION
RP AND MAGNESIUM IONS, COFACTOR, AND SUBUNIT.
RX PubMed=24086250; DOI=10.1371/journal.pone.0071242;
RA Shi R., Chen Z.Y., Zhu D.W., Li C., Shan Y., Xu G., Lin S.X.;
RT "Crystal structures of human muscle fructose-1,6-bisphosphatase: novel
RT quaternary states, enhanced AMP affinity, and allosteric signal
RT transmission pathway.";
RL PLoS ONE 8:E71242-E71242(2013).
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: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:17350621, ECO:0000269|PubMed:18214967};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:16213487, ECO:0000269|PubMed:24086250};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000269|PubMed:16213487,
CC ECO:0000269|PubMed:24086250};
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:16213487,
CC ECO:0000269|PubMed:17350621, ECO:0000269|PubMed:18214967}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.3 uM for fructose 1,6-bisphosphate {ECO:0000269|PubMed:16213487,
CC ECO:0000269|PubMed:17350621};
CC KM=2.6 uM for fructose 1,6-bisphosphate {ECO:0000269|PubMed:16213487,
CC ECO:0000269|PubMed:17350621};
CC Note=The kinetic constants are determined for the recombinant enzyme
CC expressed in E.coli.;
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:18214967, ECO:0000269|PubMed:22120740,
CC ECO:0000269|PubMed:24086250}.
CC -!- INTERACTION:
CC O00757; P09467: FBP1; NbExp=16; IntAct=EBI-719781, EBI-712740;
CC O00757; O00757: FBP2; NbExp=5; IntAct=EBI-719781, EBI-719781;
CC O00757; P04792: HSPB1; NbExp=3; IntAct=EBI-719781, EBI-352682;
CC O00757; O60333-2: KIF1B; NbExp=3; IntAct=EBI-719781, EBI-10975473;
CC O00757; O60260-5: PRKN; NbExp=3; IntAct=EBI-719781, EBI-21251460;
CC O00757; P60891: PRPS1; NbExp=3; IntAct=EBI-719781, EBI-749195;
CC -!- SUBCELLULAR LOCATION: Cell junction {ECO:0000250}. Cytoplasm. Nucleus.
CC Cytoplasm, myofibril, sarcomere, Z line. Note=In neonatal
CC cardiomyocytes, distributed throughout the cytosol, accumulating in the
CC intercalated disks which occur at the Z line of cardiomyocytes and
CC connect adjacent cells, and also located in the nucleus; dissociates
CC from the Z line following an increase in cytosolic Ca(2+) concentration
CC (By similarity). In muscle precursor cells, localizes predominantly to
CC the nucleus and to a lesser extent to the cytoplasm at the
CC proliferative phase, while mainly localizing to the cytoplasm at the
CC differentiation phase (By similarity). 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 skeletal muscle (at protein level).
CC {ECO:0000269|PubMed:12507293}.
CC -!- MISCELLANEOUS: Specific for the alpha-anomer of the substrate
CC (PubMed:22120740). The Arg-33 mutant form has been shown to act on the
CC beta-anomer (PubMed:24086250). {ECO:0000305|PubMed:22120740,
CC ECO:0000305|PubMed:24086250}.
CC -!- SIMILARITY: Belongs to the FBPase class 1 family. {ECO:0000305}.
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DR EMBL; Y10812; CAA71772.1; -; mRNA.
DR EMBL; CR536483; CAG38722.1; -; mRNA.
DR EMBL; AL161728; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC113632; AAI13633.1; -; mRNA.
DR EMBL; BC117477; AAI17478.1; -; mRNA.
DR CCDS; CCDS6711.1; -.
DR RefSeq; NP_003828.2; NM_003837.3.
DR PDB; 3IFA; X-ray; 1.93 A; A/B/C/D=2-339.
DR PDB; 3IFC; X-ray; 1.97 A; A/B/C/D=2-339.
DR PDB; 4HE0; X-ray; 2.69 A; A=2-339.
DR PDB; 4HE1; X-ray; 2.23 A; A=2-339.
DR PDB; 4HE2; X-ray; 1.60 A; A=2-339.
DR PDB; 5ET5; X-ray; 1.67 A; A=2-339.
DR PDB; 5ET6; X-ray; 1.84 A; A/B/C/D=2-339.
DR PDB; 5ET7; X-ray; 2.99 A; A/B/C/D=2-339.
DR PDB; 5ET8; X-ray; 1.92 A; A=2-339.
DR PDB; 5K54; X-ray; 1.72 A; A=2-339.
DR PDB; 5K55; X-ray; 1.98 A; A=2-339.
DR PDB; 5K56; X-ray; 2.20 A; A=2-339.
DR PDB; 5L0A; X-ray; 2.30 A; A=2-339.
DR PDB; 5Q0C; X-ray; 2.40 A; A/B/C/D/E/F/G/H=1-339.
DR PDBsum; 3IFA; -.
DR PDBsum; 3IFC; -.
DR PDBsum; 4HE0; -.
DR PDBsum; 4HE1; -.
DR PDBsum; 4HE2; -.
DR PDBsum; 5ET5; -.
DR PDBsum; 5ET6; -.
DR PDBsum; 5ET7; -.
DR PDBsum; 5ET8; -.
DR PDBsum; 5K54; -.
DR PDBsum; 5K55; -.
DR PDBsum; 5K56; -.
DR PDBsum; 5L0A; -.
DR PDBsum; 5Q0C; -.
DR AlphaFoldDB; O00757; -.
DR SMR; O00757; -.
DR BioGRID; 114317; 25.
DR IntAct; O00757; 24.
DR MINT; O00757; -.
DR STRING; 9606.ENSP00000364486; -.
DR DEPOD; FBP2; -.
DR iPTMnet; O00757; -.
DR PhosphoSitePlus; O00757; -.
DR SwissPalm; O00757; -.
DR BioMuta; FBP2; -.
DR EPD; O00757; -.
DR jPOST; O00757; -.
DR MassIVE; O00757; -.
DR MaxQB; O00757; -.
DR PaxDb; O00757; -.
DR PeptideAtlas; O00757; -.
DR PRIDE; O00757; -.
DR ProteomicsDB; 48020; -.
DR Antibodypedia; 2920; 245 antibodies from 27 providers.
DR DNASU; 8789; -.
DR Ensembl; ENST00000375337.4; ENSP00000364486.3; ENSG00000130957.5.
DR GeneID; 8789; -.
DR KEGG; hsa:8789; -.
DR MANE-Select; ENST00000375337.4; ENSP00000364486.3; NM_003837.4; NP_003828.2.
DR UCSC; uc004auv.5; human.
DR CTD; 8789; -.
DR DisGeNET; 8789; -.
DR GeneCards; FBP2; -.
DR HGNC; HGNC:3607; FBP2.
DR HPA; ENSG00000130957; Group enriched (skeletal muscle, tongue).
DR MIM; 603027; gene.
DR neXtProt; NX_O00757; -.
DR OpenTargets; ENSG00000130957; -.
DR PharmGKB; PA28019; -.
DR VEuPathDB; HostDB:ENSG00000130957; -.
DR eggNOG; KOG1458; Eukaryota.
DR GeneTree; ENSGT00390000015513; -.
DR HOGENOM; CLU_039977_1_0_1; -.
DR InParanoid; O00757; -.
DR OMA; HEKSECY; -.
DR OrthoDB; 1381522at2759; -.
DR PhylomeDB; O00757; -.
DR TreeFam; TF314824; -.
DR BioCyc; MetaCyc:HS05462-MON; -.
DR BRENDA; 3.1.3.11; 2681.
DR PathwayCommons; O00757; -.
DR Reactome; R-HSA-70263; Gluconeogenesis.
DR SABIO-RK; O00757; -.
DR SignaLink; O00757; -.
DR SIGNOR; O00757; -.
DR UniPathway; UPA00138; -.
DR BioGRID-ORCS; 8789; 23 hits in 1069 CRISPR screens.
DR EvolutionaryTrace; O00757; -.
DR GenomeRNAi; 8789; -.
DR Pharos; O00757; Tbio.
DR PRO; PR:O00757; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; O00757; protein.
DR Bgee; ENSG00000130957; Expressed in hindlimb stylopod muscle and 112 other tissues.
DR Genevisible; O00757; HS.
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; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
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; IPI:IntAct.
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 1: Evidence at protein level;
KW 3D-structure; Allosteric enzyme; Calcium; Carbohydrate metabolism;
KW Cell junction; Cytoplasm; Gluconeogenesis; Hydrolase; Magnesium;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..339
FT /note="Fructose-1,6-bisphosphatase isozyme 2"
FT /id="PRO_0000200504"
FT REGION 3..10
FT /note="Important for interaction with ALDOA"
FT /evidence="ECO:0000269|PubMed:18214967"
FT MOTIF 204..208
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:19626708"
FT BINDING 18
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:22120740"
FT BINDING 28..32
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:22120740"
FT BINDING 69
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT BINDING 98
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT BINDING 98
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT BINDING 113..114
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:22120740"
FT BINDING 119
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT BINDING 119
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT BINDING 121
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT BINDING 122
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT BINDING 122
FT /ligand="substrate"
FT BINDING 141
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:22120740"
FT BINDING 213..216
FT /ligand="substrate"
FT BINDING 245..249
FT /ligand="substrate"
FT BINDING 265
FT /ligand="substrate"
FT BINDING 275
FT /ligand="substrate"
FT BINDING 281
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT SITE 33
FT /note="Important for the conversion from active R-state to
FT inactive T-state in the presence of AMP"
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 VARIANT 86
FT /note="V -> L (in dbSNP:rs573212)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9678974"
FT /id="VAR_024448"
FT MUTAGEN 1..10
FT /note="Missing: Greatly reduces sensitivity to inhibition
FT by AMP and Ca(2+) and activation by Mg(2+). Decreases
FT binding to ALDOA."
FT /evidence="ECO:0000269|PubMed:18214967"
FT MUTAGEN 1..7
FT /note="Missing: Greatly reduces sensitivity to inhibition
FT by AMP and Ca(2+) and activation by Mg(2+). Decreases
FT binding to ALDOA."
FT MUTAGEN 1..6
FT /note="Missing: Reduces sensitivity to inhibition by AMP
FT and Ca(2+) and activation by Mg(2+). Decreases binding to
FT ALDOA."
FT MUTAGEN 1..5
FT /note="Missing: Reduces sensitivity to inhibition by AMP
FT and Ca(2+) and activation by Mg(2+). Decreases binding to
FT ALDOA."
FT MUTAGEN 1..4
FT /note="Missing: Slightly reduces sensitivity to inhibition
FT by AMP and Ca(2+) and activation by Mg(2+). Decreases
FT binding to ALDOA."
FT MUTAGEN 1..3
FT /note="Missing: No effect on kinetic properties but
FT decreases binding to ALDOA."
FT MUTAGEN 1..2
FT /note="Missing: No effect on kinetic properties and
FT interaction with ALDOA."
FT MUTAGEN 1
FT /note="Missing: No effect on kinetic properties and
FT interaction with ALDOA."
FT MUTAGEN 21
FT /note="K->E: Reduces sensitivity to AMP; when associated
FT with M-178 and C-180."
FT /evidence="ECO:0000269|PubMed:16213487"
FT MUTAGEN 33
FT /note="Q->R: Causes conformational change of N-terminal
FT residues and decreased sensitivity towards AMP with lack of
FT conversion to the inactive T-state in the presence of AMP."
FT MUTAGEN 70
FT /note="E->Q: Greatly reduces affinity towards Ca(2+) and
FT slightly reduces affinity towards Mg(2+)."
FT /evidence="ECO:0000269|PubMed:17350621"
FT MUTAGEN 178
FT /note="T->M: Reduces sensitivity to AMP; when associated
FT with E-21 and C-180."
FT /evidence="ECO:0000269|PubMed:16213487"
FT MUTAGEN 180
FT /note="Q->C: Reduces sensitivity to AMP; when associated
FT with E-21 and M-178."
FT /evidence="ECO:0000269|PubMed:16213487"
FT MUTAGEN 204..208
FT /note="KKKGK->AAAGA,EEEGE: Almost completely abolishes
FT nuclear localization."
FT /evidence="ECO:0000269|PubMed:19626708"
FT MUTAGEN 204
FT /note="K->E: Minor reduction in nuclear localization."
FT MUTAGEN 205
FT /note="K->E: Minor reduction in nuclear localization."
FT MUTAGEN 206
FT /note="K->E: Greatly reduces nuclear lozalization."
FT MUTAGEN 208
FT /note="K->E: Significantly reduces nuclear localization."
FT HELIX 14..24
FT /evidence="ECO:0007829|PDB:4HE2"
FT HELIX 30..50
FT /evidence="ECO:0007829|PDB:4HE2"
FT TURN 51..54
FT /evidence="ECO:0007829|PDB:4HE2"
FT TURN 58..61
FT /evidence="ECO:0007829|PDB:5ET6"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:4HE0"
FT HELIX 74..87
FT /evidence="ECO:0007829|PDB:4HE2"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:4HE2"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:4HE2"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:4HE2"
FT STRAND 111..122
FT /evidence="ECO:0007829|PDB:4HE2"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:4HE2"
FT TURN 127..130
FT /evidence="ECO:0007829|PDB:4HE2"
FT STRAND 133..141
FT /evidence="ECO:0007829|PDB:4HE2"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:5Q0C"
FT HELIX 150..153
FT /evidence="ECO:0007829|PDB:4HE2"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:4HE2"
FT STRAND 161..180
FT /evidence="ECO:0007829|PDB:4HE2"
FT STRAND 182..188
FT /evidence="ECO:0007829|PDB:4HE2"
FT TURN 189..192
FT /evidence="ECO:0007829|PDB:4HE2"
FT STRAND 193..201
FT /evidence="ECO:0007829|PDB:4HE2"
FT STRAND 208..211
FT /evidence="ECO:0007829|PDB:4HE2"
FT HELIX 214..219
FT /evidence="ECO:0007829|PDB:4HE2"
FT HELIX 222..232
FT /evidence="ECO:0007829|PDB:4HE2"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:4HE2"
FT HELIX 249..259
FT /evidence="ECO:0007829|PDB:4HE2"
FT STRAND 262..265
FT /evidence="ECO:0007829|PDB:4HE2"
FT STRAND 268..270
FT /evidence="ECO:0007829|PDB:5ET5"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:4HE2"
FT TURN 278..281
FT /evidence="ECO:0007829|PDB:4HE2"
FT HELIX 282..291
FT /evidence="ECO:0007829|PDB:4HE2"
FT STRAND 295..297
FT /evidence="ECO:0007829|PDB:4HE2"
FT STRAND 299..302
FT /evidence="ECO:0007829|PDB:4HE2"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:4HE2"
FT STRAND 317..321
FT /evidence="ECO:0007829|PDB:4HE2"
FT HELIX 322..335
FT /evidence="ECO:0007829|PDB:4HE2"
SQ SEQUENCE 339 AA; 36743 MW; 196B06D744710BC4 CRC64;
MTDRSPFETD MLTLTRYVME KGRQAKGTGE LTQLLNSMLT AIKAISSAVR KAGLAHLYGI
AGSVNVTGDE VKKLDVLSNS LVINMVQSSY STCVLVSEEN KDAIITAKEK RGKYVVCFDP
LDGSSNIDCL ASIGTIFAIY RKTSEDEPSE KDALQCGRNI VAAGYALYGS ATLVALSTGQ
GVDLFMLDPA LGEFVLVEKD VKIKKKGKIY SLNEGYAKYF DAATTEYVQK KKFPEDGSAP
YGARYVGSMV ADVHRTLVYG GIFLYPANQK SPKGKLRLLY ECNPVAYIIE QAGGLATTGT
QPVLDVKPEA IHQRVPLILG SPEDVQEYLT CVQKNQAGS
