ID F261_RAT Reviewed; 471 AA. AC P07953; P16119; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 02-SEP-2026, entry version 225. DE RecName: Full=6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1 {ECO:0000305}; DE Short=6PF-2-K/Fru-2,6-P2ase 1; DE Short=PFK/FBPase 1; DE AltName: Full=6PF-2-K/Fru-2,6-P2ase liver isozyme; DE Includes: DE RecName: Full=6-phosphofructo-2-kinase; DE EC=2.7.1.105 {ECO:0000269|PubMed:2848802}; DE Includes: DE RecName: Full=Fructose-2,6-bisphosphatase; DE EC=3.1.3.46 {ECO:0000269|PubMed:2848802}; GN Name=Pfkfb1 {ECO:0000312|RGD:3307}; 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 (ISOFORM 1), AND PROTEIN SEQUENCE OF 16-29; 65-74; RP 90-105; 123-137; 189-195; 240-252; 259-266 AND 309-324 (ISOFORM 1). RC STRAIN=Wistar; TISSUE=Liver; RX PubMed=2856848; DOI=10.1016/0014-5793(87)80476-3; RA Darville M.I., Crepin K.M., Vandekerckhove J., van Damme J., Octave J.-N., RA Rider M.H., Marchand M.J., Hue L., Rousseau G.G.; RT "Complete nucleotide sequence coding for rat liver 6-phosphofructo-2- RT kinase/fructose-2,6-bisphosphatase derived from a cDNA clone."; RL FEBS Lett. 224:317-321(1987). RN [2] RP NUCLEOTIDE SEQUENCE (ISOFORM 1). RC STRAIN=Sprague-Dawley; RX PubMed=3032183; DOI=10.1016/0006-291x(87)90364-0; RA Colosa A.D., Lively M.O., El-Maghrabi M.R., Pilkis S.J.; RT "Isolation of a cDNA clone for rat liver 6-phosphofructo 2-kinase/fructose RT 2,6-bisphosphatase."; RL Biochem. Biophys. Res. Commun. 143:1092-1098(1987). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). RC STRAIN=Wistar; TISSUE=Liver; RX PubMed=2547611; DOI=10.1111/j.1432-1033.1989.tb14946.x; RA Crepin K.M., Darville M.I., Hue L., Rousseau G.G.; RT "Characterization of distinct mRNAs coding for putative isozymes of 6- RT phosphofructo-2-kinase/fructose-2,6-bisphosphatase."; RL Eur. J. Biochem. 183:433-440(1989). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY, AND FUNCTION. RC TISSUE=Liver; RX PubMed=2848802; DOI=10.1016/s0021-9258(18)37337-x; RA Colosia A.D., Marker A.J., Lange A.J., El-Maghrabi M.R., Granner D.K., RA Tauler A., Pilkis J., Pilkis S.J.; RT "Induction of rat liver 6-phosphofructo-2-kinase/fructose-2,6- RT bisphosphatase mRNA by refeeding and insulin."; RL J. Biol. Chem. 263:18669-18677(1988). RN [5] RP PROTEIN SEQUENCE (ISOFORM 1), AND ACETYLATION AT SER-2. RC TISSUE=Liver; RX PubMed=2826464; DOI=10.1016/s0021-9258(19)35431-6; RA Lively M.O., El-Maghrabi M.R., Pilkis J., D'Angelo G., Colosia A.D., RA Ciavola J.A., Fraser B.A., Pilkis S.J.; RT "Complete amino acid sequence of rat liver 6-phosphofructo-2- RT kinase/fructose-2,6-bisphosphatase."; RL J. Biol. Chem. 263:839-849(1988). RN [6] RP NUCLEOTIDE SEQUENCE (ISOFORM 2). RC STRAIN=Wistar; TISSUE=Liver; RX PubMed=2557826; DOI=10.1042/bj2640151; RA Crepin K.M., Darville M.I., Michel A., Hue L., Rousseau G.G.; RT "Cloning and expression in Escherichia coli of a rat hepatoma cell cDNA RT coding for 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase."; RL Biochem. J. 264:151-160(1989). RN [7] RP PROTEIN SEQUENCE OF 220-267. RC TISSUE=Liver; RX PubMed=3040762; DOI=10.1016/s0021-9258(18)45259-3; RA Pilkis S.J., Lively M.O., El-Maghrabi M.R.; RT "Active site sequence of hepatic fructose-2,6-bisphosphatase. Homology in RT primary structure with phosphoglycerate mutase."; RL J. Biol. Chem. 262:12672-12675(1987). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-32 (ISOFORM 1), AND PROTEIN SEQUENCE RP OF 2-10 (ISOFORM 2). RX PubMed=2549541; DOI=10.1073/pnas.86.17.6543; RA Darville M.I., Crepin K.M., Hue L., Rousseau G.G.; RT "5' flanking sequence and structure of a gene encoding rat 6-phosphofructo- RT 2-kinase/fructose-2,6-bisphosphatase."; RL Proc. Natl. Acad. Sci. U.S.A. 86:6543-6547(1989). RN [9] RP PROTEIN SEQUENCE OF 106-114, AND REGION. RX PubMed=2539378; DOI=10.1016/s0021-9258(18)83354-3; RA Kitamura K., Uyeda K., Hartman F.C., Kangawa K., Matsuo H.; RT "Catalytic site of rat liver and bovine heart fructose-6-phosphate,2- RT kinase:fructose-2,6-bisphosphatase. Identification of fructose 6-phosphate RT binding site."; RL J. Biol. Chem. 264:6344-6348(1989). RN [10] RP DOMAINS. RX PubMed=2557623; DOI=10.1073/pnas.86.24.9642; RA Bazan J.F., Fletterick R.J., Pilkis S.J.; RT "Evolution of a bifunctional enzyme: 6-phosphofructo-2-kinase/fructose-2,6- RT bisphosphatase."; RL Proc. Natl. Acad. Sci. U.S.A. 86:9642-9646(1989). RN [11] RP PHOSPHORYLATION AT SER-33, AND ACTIVITY REGULATION. RX PubMed=7549867; DOI=10.1002/pro.5560040601; RA Kurland I.J., Pilkis S.J.; RT "Covalent control of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase: RT insights into autoregulation of a bifunctional enzyme."; RL Protein Sci. 4:1023-1037(1995). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141, AND IDENTIFICATION BY RP 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). RN [13] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). RC TISSUE=Liver; RX PubMed=8634242; DOI=10.1021/bi9600613; RA Lee Y.-H., Ogata C., Pflugrath J.W., Levitt D.G., Sarma R., Banaszak L.J., RA Pilkis S.J.; RT "Crystal structure of the rat liver fructose-2,6-bisphosphatase based on RT selenomethionine multiwavelength anomalous dispersion phases."; RL Biochemistry 35:6010-6019(1996). RN [14] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 251-441 IN COMPLEX WITH FRUCTOSE RP 6-PHOSPHATE, AND ACTIVE SITE. RX PubMed=9253407; DOI=10.1038/nsb0897-615; RA Lee Y.-H., Olson T.W., Ogata C.M., Levitt D.G., Banaszak L.J., Lange A.J.; RT "Crystal structure of a trapped phosphoenzyme during a catalytic RT reaction."; RL Nat. Struct. Biol. 4:615-618(1997). RN [15] RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 252-440 IN COMPLEXES WITH RP SUBSTRATE ANALOG AND WITH GTP. RA Lee Y.-H., Olson T.W., McClard R.W., Witte J.F., McFarlan S.C., RA Banaszak L.J., Levitt D.G., Lange A.J.; RT "Reaction mechanism of fructose-2,6-bisphosphatase suggested by the crystal RT structures of a pseudo-Michaelis complex and metabolite complexes."; RL Submitted (APR-2000) to the PDB data bank. CC -!- FUNCTION: Synthesis and degradation of fructose 2,6-bisphosphate. CC {ECO:0000269|PubMed:2848802}. CC -!- CATALYTIC ACTIVITY: CC Reaction=beta-D-fructose 2,6-bisphosphate + H2O = beta-D-fructose 6- CC phosphate + phosphate; Xref=Rhea:RHEA:17289, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57634, ChEBI:CHEBI:58579; EC=3.1.3.46; CC Evidence={ECO:0000269|PubMed:2848802}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17290; CC Evidence={ECO:0000305|PubMed:2848802}; CC -!- CATALYTIC ACTIVITY: CC Reaction=beta-D-fructose 6-phosphate + ATP = beta-D-fructose 2,6- CC bisphosphate + ADP + H(+); Xref=Rhea:RHEA:15653, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:57634, ChEBI:CHEBI:58579, CC ChEBI:CHEBI:456216; EC=2.7.1.105; CC Evidence={ECO:0000269|PubMed:2848802}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15654; CC Evidence={ECO:0000305|PubMed:2848802}; CC -!- ACTIVITY REGULATION: Phosphorylation at Ser-33 inhibits the kinase and CC activates the bisphosphatase. {ECO:0000269|PubMed:7549867}. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:9253407}. CC -!- INTERACTION: CC P07953; P07953: Pfkfb1; NbExp=5; IntAct=EBI-709873, EBI-709873; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P07953-1; Sequence=Displayed; CC Name=2; CC IsoId=P07953-2; Sequence=VSP_004674; CC -!- TISSUE SPECIFICITY: Liver. CC -!- SIMILARITY: In the C-terminal section; belongs to the phosphoglycerate CC mutase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Y00702; CAA68694.1; -; mRNA. DR EMBL; X15579; CAA33606.1; -; mRNA. DR EMBL; X15580; CAA33607.1; -; mRNA. DR EMBL; M26215; AAA02888.2; -; Genomic_DNA. DR EMBL; M26216; AAA02889.1; -; Genomic_DNA. DR EMBL; J04197; AAA79008.1; -; mRNA. DR EMBL; M27886; AAA58780.1; -; Genomic_DNA. DR PIR; S11761; KIRTFB. DR RefSeq; NP_036753.4; NM_012621.5. [P07953-1] DR PDB; 1C7Z; X-ray; 2.60 A; A/B=252-441. DR PDB; 1C80; X-ray; 2.20 A; A/B=252-441. DR PDB; 1C81; X-ray; 2.50 A; A=252-441. DR PDB; 1FBT; X-ray; 2.00 A; A/B=252-441. DR PDB; 1TIP; X-ray; 2.20 A; A/B=252-441. DR AlphaFoldDB; P07953; -. DR BMRB; P07953; -. DR SMR; P07953; -. DR ComplexPortal; CPX-2040; 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 1 complex. DR FunCoup; P07953; 519. DR IntAct; P07953; 2. DR MINT; P07953; -. DR STRING; 10116.ENSRNOP00000035212; -. DR GlyGen; P07953; 1 site. DR iPTMnet; P07953; -. DR PhosphoSitePlus; P07953; -. DR jPOST; P07953; -. DR PaxDb; 10116-ENSRNOP00000035212; -. DR Ensembl; ENSRNOT00000174108.1; ENSRNOP00000105342.1; ENSRNOG00000000165.10. [P07953-1] DR Ensembl; ENSRNOT00055041095; ENSRNOP00055033424; ENSRNOG00055023911. [P07953-1] DR Ensembl; ENSRNOT00060039538; ENSRNOP00060032722; ENSRNOG00060022714. [P07953-1] DR Ensembl; ENSRNOT00065017947; ENSRNOP00065013691; ENSRNOG00065011071. [P07953-1] DR GeneID; 24638; -. DR KEGG; rno:24638; -. DR AGR; RGD:3307; -. DR CTD; 5207; -. DR RGD; 3307; Pfkfb1. DR eggNOG; KOG0234; Eukaryota. DR GeneTree; ENSGT00950000182835; -. DR HOGENOM; CLU_006383_1_1_1; -. DR InParanoid; P07953; -. DR OMA; RCMYAYF; -. DR OrthoDB; 267323at2759; -. DR PhylomeDB; P07953; -. DR BRENDA; 2.7.1.105; 5301. DR BRENDA; 3.1.3.46; 5301. DR Reactome; R-RNO-9634600; Regulation of glycolysis by fructose 2,6-bisphosphate metabolism. DR SABIO-RK; P07953; -. DR EvolutionaryTrace; P07953; -. DR PRO; PR:P07953; -. DR Proteomes; UP000002494; Chromosome X. DR Bgee; ENSRNOG00000000165; Expressed in skeletal muscle tissue and 16 other cell types or tissues. DR ExpressionAtlas; P07953; baseline and differential. DR GO; GO:0043540; C:6-phosphofructo-2-kinase/fructose-2,6-biphosphatase complex; IDA:RGD. DR GO; GO:0005829; C:cytosol; IDA:MGI. DR GO; GO:0003873; F:6-phosphofructo-2-kinase activity; IDA:RGD. DR GO; GO:0005524; F:ATP binding; IDA:RGD. DR GO; GO:0004331; F:fructose-2,6-bisphosphate 2-phosphatase activity; IDA:MGI. DR GO; GO:0070095; F:fructose-6-phosphate binding; IDA:RGD. DR GO; GO:0042802; F:identical protein binding; IDA:RGD. DR GO; GO:0019900; F:kinase binding; IPI:RGD. DR GO; GO:0031100; P:animal organ regeneration; IEP:RGD. DR GO; GO:0046835; P:carbohydrate phosphorylation; IDA:RGD. DR GO; GO:0006003; P:fructose 2,6-bisphosphate metabolic process; ISS:UniProtKB. DR GO; GO:0006000; P:fructose metabolic process; IEA:InterPro. DR GO; GO:0006094; P:gluconeogenesis; NAS:ComplexPortal. DR GO; GO:0006007; P:glucose catabolic process; IMP:RGD. DR GO; GO:0006096; P:glycolytic process; NAS:ComplexPortal. DR GO; GO:0019249; P:lactate biosynthetic process; IMP:RGD. DR GO; GO:0045820; P:negative regulation of glycolytic process; ISO:RGD. DR GO; GO:1904539; P:negative regulation of glycolytic process through fructose-6-phosphate; ISO:RGD. DR GO; GO:1904540; P:positive regulation of glycolytic process through fructose-6-phosphate; IMP:FlyBase. DR GO; GO:1903301; P:positive regulation of hexokinase activity; IMP:RGD. DR GO; GO:0032024; P:positive regulation of insulin secretion; IMP:RGD. DR GO; GO:0042866; P:pyruvate biosynthetic process; IMP:RGD. DR GO; GO:0051591; P:response to cAMP; IEP:RGD. DR GO; GO:0033762; P:response to glucagon; IEP:RGD. DR GO; GO:0051384; P:response to glucocorticoid; IEP:RGD. DR GO; GO:0009749; P:response to glucose; IMP:RGD. DR GO; GO:0032868; P:response to insulin; IEP:RGD. DR GO; GO:0042594; P:response to starvation; IEP:RGD. DR CDD; cd07067; HP_PGM_like; 1. DR FunFam; 3.40.50.1240:FF:000001; 6-phosphofructo-2-kinase/fructose-2, 6-bisphosphatase 3 isoform 2; 1. DR FunFam; 3.40.50.300:FF:000047; 6-phosphofructo-2-kinase/fructose-2, 6-bisphosphatase 3 isoform 2; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1. DR InterPro; IPR003094; 6Pfruct_kin. DR InterPro; IPR013079; 6Phosfructo_kin. DR InterPro; IPR013078; His_Pase_superF_clade-1. DR InterPro; IPR029033; His_PPase_superfam. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR001345; PG/BPGM_mutase_AS. DR PANTHER; PTHR10606; 6-PHOSPHOFRUCTO-2-KINASE/FRUCTOSE-2,6-BISPHOSPHATASE; 1. DR PANTHER; PTHR10606:SF15; 6-PHOSPHOFRUCTO-2-KINASE_FRUCTOSE-2,6-BISPHOSPHATASE 1; 1. DR Pfam; PF01591; 6PF2K; 1. DR Pfam; PF00300; His_Phos_1; 1. DR PIRSF; PIRSF000709; 6PFK_2-Ptase; 1. DR PRINTS; PR00991; 6PFRUCTKNASE. DR SMART; SM00855; PGAM; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1. DR PROSITE; PS00175; PG_MUTASE; 1. DR PDBsum; 1C7Z; -. DR PDBsum; 1C80; -. DR PDBsum; 1C81; -. DR PDBsum; 1FBT; -. DR PDBsum; 1TIP; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; KW Direct protein sequencing; Hydrolase; Kinase; Multifunctional enzyme; KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:2826464" FT CHAIN 2..471 FT /note="6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase FT 1" FT /id="PRO_0000179962" FT REGION 2..250 FT /note="6-phosphofructo-2-kinase" FT REGION 251..471 FT /note="Fructose-2,6-bisphosphatase" FT ACT_SITE 131 FT /evidence="ECO:0000255" FT ACT_SITE 161 FT /evidence="ECO:0000255" FT ACT_SITE 259 FT /note="Tele-phosphohistidine intermediate" FT /evidence="ECO:0000269|PubMed:9253407" FT ACT_SITE 328 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000269|PubMed:9253407" FT BINDING 49..57 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:Q16875" FT BINDING 82 FT /ligand="beta-D-fructose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:57634" FT /evidence="ECO:0000250|UniProtKB:Q16875" FT BINDING 105 FT /ligand="beta-D-fructose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:57634" FT /evidence="ECO:0000250|UniProtKB:Q16875" FT BINDING 133 FT /ligand="beta-D-fructose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:57634" FT /evidence="ECO:0000250|UniProtKB:Q16875" FT BINDING 139 FT /ligand="beta-D-fructose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:57634" FT /evidence="ECO:0000250|UniProtKB:Q16875" FT BINDING 170..175 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:Q16875" FT BINDING 175 FT /ligand="beta-D-fructose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:57634" FT /evidence="ECO:0000250|UniProtKB:Q16875" FT BINDING 196 FT /ligand="beta-D-fructose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:57634" FT /evidence="ECO:0000250|UniProtKB:Q16875" FT BINDING 200 FT /ligand="beta-D-fructose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:57634" FT /evidence="ECO:0000250|UniProtKB:Q16875" FT BINDING 258 FT /ligand="beta-D-fructose 2,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58579" FT /evidence="ECO:0000250|UniProtKB:Q16875" FT BINDING 265 FT /ligand="beta-D-fructose 2,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58579" FT /evidence="ECO:0000250|UniProtKB:Q16875" FT BINDING 271 FT /ligand="beta-D-fructose 2,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58579" FT /evidence="ECO:0000269|PubMed:9253407" FT BINDING 308 FT /ligand="beta-D-fructose 2,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58579" FT /evidence="ECO:0000250|UniProtKB:Q16875" FT BINDING 339 FT /ligand="beta-D-fructose 2,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58579" FT /evidence="ECO:0000269|PubMed:9253407" FT BINDING 350..353 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|Ref.15" FT BINDING 353 FT /ligand="beta-D-fructose 2,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58579" FT /evidence="ECO:0000269|PubMed:9253407" FT BINDING 357 FT /ligand="beta-D-fructose 2,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58579" FT /evidence="ECO:0000269|PubMed:9253407" FT BINDING 368 FT /ligand="beta-D-fructose 2,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58579" FT /evidence="ECO:0000269|PubMed:9253407" FT BINDING 394..398 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|Ref.15" FT BINDING 394 FT /ligand="beta-D-fructose 2,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58579" FT /evidence="ECO:0000269|PubMed:9253407" FT BINDING 398 FT /ligand="beta-D-fructose 2,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58579" FT /evidence="ECO:0000269|PubMed:9253407" FT BINDING 430 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:Q16875" FT SITE 393 FT /note="Transition state stabilizer" FT /evidence="ECO:0000250|UniProtKB:P00950" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0000269|PubMed:2826464" FT MOD_RES 33 FT /note="Phosphoserine; by PKA" FT /evidence="ECO:0000269|PubMed:7549867" FT MOD_RES 141 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT VAR_SEQ 1..33 FT /note="MSREMGELTQTRLQKIWIPHSSSSSVLQRRRGS -> MEEKASKRTA (in FT isoform 2)" FT /evidence="ECO:0000303|PubMed:2547611" FT /id="VSP_004674" FT CONFLICT 135 FT /note="T -> Y (in Ref. 3, 4 and 5)" FT /evidence="ECO:0000305" FT CONFLICT 138 FT /note="E -> F (in Ref. 3)" FT /evidence="ECO:0000305" FT CONFLICT 257 FT /note="Missing (in Ref. 7; AA sequence)" FT /evidence="ECO:0000305" FT STRAND 253..258 FT /evidence="ECO:0007829|PDB:1FBT" FT HELIX 263..267 FT /evidence="ECO:0007829|PDB:1FBT" FT HELIX 278..292 FT /evidence="ECO:0007829|PDB:1FBT" FT STRAND 300..306 FT /evidence="ECO:0007829|PDB:1FBT" FT HELIX 307..314 FT /evidence="ECO:0007829|PDB:1FBT" FT TURN 315..317 FT /evidence="ECO:0007829|PDB:1C80" FT STRAND 321..323 FT /evidence="ECO:0007829|PDB:1FBT" FT HELIX 324..326 FT /evidence="ECO:0007829|PDB:1FBT" FT HELIX 328..330 FT /evidence="ECO:0007829|PDB:1FBT" FT HELIX 332..334 FT /evidence="ECO:0007829|PDB:1FBT" FT HELIX 339..345 FT /evidence="ECO:0007829|PDB:1FBT" FT HELIX 347..355 FT /evidence="ECO:0007829|PDB:1FBT" FT TURN 357..359 FT /evidence="ECO:0007829|PDB:1FBT" FT HELIX 368..374 FT /evidence="ECO:0007829|PDB:1FBT" FT HELIX 376..383 FT /evidence="ECO:0007829|PDB:1FBT" FT STRAND 386..392 FT /evidence="ECO:0007829|PDB:1FBT" FT HELIX 394..404 FT /evidence="ECO:0007829|PDB:1FBT" FT TURN 409..411 FT /evidence="ECO:0007829|PDB:1FBT" FT HELIX 412..414 FT /evidence="ECO:0007829|PDB:1FBT" FT STRAND 421..428 FT /evidence="ECO:0007829|PDB:1FBT" FT STRAND 431..438 FT /evidence="ECO:0007829|PDB:1FBT" SQ SEQUENCE 471 AA; 54763 MW; E307AF13945E0FCD CRC64; MSREMGELTQ TRLQKIWIPH SSSSSVLQRR RGSSIPQFTN SPTMVIMVGL PARGKTYIST KLTRYLNWIG TPTKVFNLGQ YRREAVSYRN YEFFRPDNTE AQLIRKQCAL AALKDVHKYL SREEGHVAVF DATNTTRERR SLILQFAKEH GYKVFFIESI CNDPEIIAEN IKQVKLGSPD YIDCDQEKVL EDFLKRIECY EINYQPLDEE LDSHLSYIKI FDVGTRYMVN RVQDHVQSRT AYYLMNIHVT PRSIYLCRHG ESELNLRGRI GGDSGLSARG KQYAYALANF IRSQGISSLK VWTSHMKRTI QTAEALGVPY EQWKALNEID AGVCEEMTYE EIQEHYPEEF ALRDQDKYRY RYPKGESYED LVQRLEPVIM ELERQENVLV ICHQAVMRCL LAYFLDKSSD ELPYLKCPLH TVLKLTPVAY GCRVESIYLN VEAVNTHRDK PENVDITREA EEALDTVPAH Y //