F261_RAT
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 03-AUG-2022, entry version 208.
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=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-
CC bisphosphate + 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}.
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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_012621.4. [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 PDBsum; 1C7Z; -.
DR PDBsum; 1C80; -.
DR PDBsum; 1C81; -.
DR PDBsum; 1FBT; -.
DR PDBsum; 1TIP; -.
DR AlphaFoldDB; P07953; -.
DR BMRB; P07953; -.
DR SMR; P07953; -.
DR ComplexPortal; CPX-2040; 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 1 complex.
DR IntAct; P07953; 2.
DR MINT; P07953; -.
DR STRING; 10116.ENSRNOP00000035212; -.
DR iPTMnet; P07953; -.
DR PhosphoSitePlus; P07953; -.
DR jPOST; P07953; -.
DR PaxDb; P07953; -.
DR Ensembl; ENSRNOT00000033656; ENSRNOP00000035212; ENSRNOG00000000165. [P07953-1]
DR GeneID; 24638; -.
DR KEGG; rno:24638; -.
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; SHRGAKF; -.
DR OrthoDB; 392001at2759; -.
DR PhylomeDB; P07953; -.
DR TreeFam; TF313541; -.
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 tissues.
DR ExpressionAtlas; P07953; baseline and differential.
DR Genevisible; P07953; RN.
DR GO; GO:0043540; C:6-phosphofructo-2-kinase/fructose-2,6-biphosphatase complex; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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:RGD.
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:0033133; P:positive regulation of glucokinase activity; 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: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 Gene3D; 3.40.50.1240; -; 1.
DR Gene3D; 3.40.50.300; -; 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; PTHR10606; 1.
DR Pfam; PF01591; 6PF2K; 1.
DR Pfam; PF00300; His_Phos_1; 1.
DR PRINTS; PR00991; 6PFRUCTKNASE.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF53254; SSF53254; 1.
DR PROSITE; PS00175; PG_MUTASE; 1.
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 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
