IPPK_ARATH
ID IPPK_ARATH Reviewed; 451 AA.
AC Q93YN9; Q9FMY6;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Inositol-pentakisphosphate 2-kinase;
DE EC=2.7.1.158;
DE AltName: Full=Inositol-1,3,4,5,6-pentakisphosphate 2-kinase;
DE AltName: Full=Ins(1,3,4,5,6)P5 2-kinase;
DE Short=AtIPK1;
DE Short=InsP5 2-kinase;
GN Name=IPK1; OrderedLocusNames=At5g42810; ORFNames=MJB21.19;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND ENZYME ACTIVITY.
RX PubMed=16107538; DOI=10.1073/pnas.0504172102;
RA Stevenson-Paulik J., Bastidas R.J., Chiou S.-T., Frye R.A., York J.D.;
RT "Generation of phytate-free seeds in Arabidopsis through disruption of
RT inositol polyphosphate kinases.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:12612-12617(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP FUNCTION, ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE
RP SPECIFICITY.
RX PubMed=16223361; DOI=10.1042/bj20051331;
RA Sweetman D., Johnson S., Caddick S.E.K., Hanke D.E., Brearley C.A.;
RT "Characterization of an Arabidopsis inositol 1,3,4,5,6-pentakisphosphate 2-
RT kinase (AtIPK1).";
RL Biochem. J. 394:95-103(2006).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH ADP; ATP ANALOG;
RP SUBSTRATE AND ZINC.
RX PubMed=20453199; DOI=10.1073/pnas.0912979107;
RA Gonzalez B., Banos-Sanz J.I., Villate M., Brearley C.A., Sanz-Aparicio J.;
RT "Inositol 1,3,4,5,6-pentakisphosphate 2-kinase is a distant IPK member with
RT a singular inositide binding site for axial 2-OH recognition.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:9608-9613(2010).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH ADP; SUBSTRATE AND
RP ZINC.
RX PubMed=22684075; DOI=10.1107/s1744309112017307;
RA Banos-Sanz J.I., Sanz-Aparicio J., Brearley C.A., Gonzalez B.;
RT "Expression, purification, crystallization and preliminary X-ray
RT diffraction analysis of the apo form of InsP5 2-K from Arabidopsis
RT thaliana.";
RL Acta Crystallogr. F 68:701-704(2012).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH ADP; ATP ANALOG;
RP SUBSTRATE AND ZINC.
RX PubMed=22745128; DOI=10.1074/jbc.m112.363671;
RA Banos-Sanz J.I., Sanz-Aparicio J., Whitfield H., Hamilton C.,
RA Brearley C.A., Gonzalez B.;
RT "Conformational changes in inositol 1,3,4,5,6-pentakisphosphate 2-kinase
RT upon substrate binding: role of N-terminal lobe and enantiomeric substrate
RT preference.";
RL J. Biol. Chem. 287:29237-29249(2012).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH ADP; SUBSTRATE AND
RP ZINC.
RX PubMed=22362712; DOI=10.1002/pro.2049;
RA Gosein V., Leung T.F., Krajden O., Miller G.J.;
RT "Inositol phosphate-induced stabilization of inositol 1,3,4,5,6-
RT pentakisphosphate 2-kinase and its role in substrate specificity.";
RL Protein Sci. 21:737-742(2012).
CC -!- FUNCTION: Phosphorylates Ins(1,3,4,5,6)P5 at position 2 to form
CC Ins(1,2,3,4,5,6)P6 (InsP6 or phytate). Phytate is a regulator of
CC intracellular signaling, a highly abundant animal antinutrient, and a
CC phosphate store in plant seeds. Also phosphorylates Ins(1,3,4,6)P4 and
CC Ins(1,4,5,6)P4 to produce Ins(1,2,3,4,6)P5 and Ins(1,2,4,5,6)P5.
CC {ECO:0000269|PubMed:16107538, ECO:0000269|PubMed:16223361}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 1,3,4,5,6-pentakisphosphate + ATP = 1D-myo-
CC inositol hexakisphosphate + ADP + H(+); Xref=Rhea:RHEA:20313,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57733,
CC ChEBI:CHEBI:58130, ChEBI:CHEBI:456216; EC=2.7.1.158;
CC Evidence={ECO:0000269|PubMed:16107538, ECO:0000269|PubMed:16223361};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:20453199, ECO:0000269|PubMed:22362712,
CC ECO:0000269|PubMed:22684075, ECO:0000269|PubMed:22745128};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:20453199,
CC ECO:0000269|PubMed:22362712, ECO:0000269|PubMed:22684075,
CC ECO:0000269|PubMed:22745128};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=38 uM for Ins(1,3,4,5,6)P5 (in the presence of 0.4 mM ATP)
CC {ECO:0000269|PubMed:16223361};
CC KM=176 uM for Ins(1,3,4,5,6)P5 (in the presence of 0.4 uM ATP)
CC {ECO:0000269|PubMed:16223361};
CC Vmax=22 nmol/min/mg enzyme (in the presence of 0.4 mM ATP)
CC {ECO:0000269|PubMed:16223361};
CC Vmax=1.5 nmol/min/mg enzyme (in the presence of 0.4 uM ATP)
CC {ECO:0000269|PubMed:16223361};
CC -!- TISSUE SPECIFICITY: Strongly expressed in leaves and cauline leaves.
CC Weakly expressed in siliques and flowers. In flower, it is expressed in
CC the major organs of developing flower buds. Strongly expressed in
CC sepals, petals, in the male and female organs of immature and mature
CC flower buds. Strongly expressed in the gynoecium and carpels which are
CC fused to form the gynoecium. Also expressed in the transmitting tissue
CC and ovules. {ECO:0000269|PubMed:16223361}.
CC -!- DOMAIN: The EXKPK motif is conserved in inositol-pentakisphosphate 2-
CC kinases of both family 1 and 2.
CC -!- BIOTECHNOLOGY: The gene coding for this protein might be inactivated to
CC commercially produce plants with phytate-free grain. Indeed, while the
CC role of phytate (InsP6) accumulation in seeds is unknown, it causes
CC nutritional and environmental problems, partly due to the inability of
CC monogastric animals to digest it.
CC -!- SIMILARITY: Belongs to the IPK1 type 2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB10637.1; Type=Erroneous gene model prediction; Evidence={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; DQ122931; AAZ99216.1; -; mRNA.
DR EMBL; AB007647; BAB10637.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED94867.1; -; Genomic_DNA.
DR EMBL; AY059898; AAL24380.1; -; mRNA.
DR EMBL; AY093362; AAM13361.1; -; mRNA.
DR RefSeq; NP_568613.1; NM_123646.4.
DR PDB; 2XAL; X-ray; 3.20 A; A/B=1-451.
DR PDB; 2XAM; X-ray; 2.20 A; A/B=1-451.
DR PDB; 2XAN; X-ray; 2.20 A; A/B=1-451.
DR PDB; 2XAO; X-ray; 2.90 A; A/B=1-451.
DR PDB; 2XAR; X-ray; 3.10 A; A/B=1-451.
DR PDB; 3UDS; X-ray; 3.10 A; A/B=1-451.
DR PDB; 3UDT; X-ray; 3.10 A; A/B=1-451.
DR PDB; 3UDZ; X-ray; 2.50 A; A/B=1-451.
DR PDB; 4AQK; X-ray; 2.40 A; A=1-451.
DR PDB; 4AXC; X-ray; 2.25 A; A=1-451.
DR PDB; 4AXD; X-ray; 2.05 A; A=1-451.
DR PDB; 4AXE; X-ray; 2.50 A; A=1-451.
DR PDB; 4AXF; X-ray; 2.93 A; A=1-451.
DR PDB; 4LV7; X-ray; 2.60 A; A/B=1-451.
DR PDB; 6FJK; X-ray; 2.02 A; A/B=1-451.
DR PDB; 6FL3; X-ray; 2.36 A; A/B=1-451.
DR PDB; 6FL8; X-ray; 2.10 A; A/B=1-451.
DR PDB; 6GFG; X-ray; 3.00 A; A/B=1-451.
DR PDB; 6GFH; X-ray; 2.65 A; A/B=1-451.
DR PDBsum; 2XAL; -.
DR PDBsum; 2XAM; -.
DR PDBsum; 2XAN; -.
DR PDBsum; 2XAO; -.
DR PDBsum; 2XAR; -.
DR PDBsum; 3UDS; -.
DR PDBsum; 3UDT; -.
DR PDBsum; 3UDZ; -.
DR PDBsum; 4AQK; -.
DR PDBsum; 4AXC; -.
DR PDBsum; 4AXD; -.
DR PDBsum; 4AXE; -.
DR PDBsum; 4AXF; -.
DR PDBsum; 4LV7; -.
DR PDBsum; 6FJK; -.
DR PDBsum; 6FL3; -.
DR PDBsum; 6FL8; -.
DR PDBsum; 6GFG; -.
DR PDBsum; 6GFH; -.
DR AlphaFoldDB; Q93YN9; -.
DR SMR; Q93YN9; -.
DR BioGRID; 19542; 1.
DR STRING; 3702.AT5G42810.1; -.
DR BindingDB; Q93YN9; -.
DR iPTMnet; Q93YN9; -.
DR PaxDb; Q93YN9; -.
DR PRIDE; Q93YN9; -.
DR ProteomicsDB; 247034; -.
DR DNASU; 834292; -.
DR EnsemblPlants; AT5G42810.1; AT5G42810.1; AT5G42810.
DR GeneID; 834292; -.
DR Gramene; AT5G42810.1; AT5G42810.1; AT5G42810.
DR KEGG; ath:AT5G42810; -.
DR Araport; AT5G42810; -.
DR TAIR; locus:2165437; AT5G42810.
DR eggNOG; KOG4749; Eukaryota.
DR HOGENOM; CLU_033188_1_0_1; -.
DR InParanoid; Q93YN9; -.
DR OMA; NCVHCGE; -.
DR OrthoDB; 1195478at2759; -.
DR PhylomeDB; Q93YN9; -.
DR BRENDA; 2.7.1.158; 399.
DR EvolutionaryTrace; Q93YN9; -.
DR PRO; PR:Q93YN9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q93YN9; baseline and differential.
DR Genevisible; Q93YN9; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0035299; F:inositol pentakisphosphate 2-kinase activity; IDA:TAIR.
DR GO; GO:0032942; F:inositol tetrakisphosphate 2-kinase activity; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030643; P:cellular phosphate ion homeostasis; IMP:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
DR GO; GO:0051607; P:defense response to virus; IMP:TAIR.
DR GO; GO:0032958; P:inositol phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0052746; P:inositol phosphorylation; IBA:GO_Central.
DR GO; GO:0048527; P:lateral root development; IMP:TAIR.
DR GO; GO:0010264; P:myo-inositol hexakisphosphate biosynthetic process; IMP:TAIR.
DR GO; GO:0055062; P:phosphate ion homeostasis; IMP:TAIR.
DR Gene3D; 3.30.200.110; -; 1.
DR InterPro; IPR009286; Ins_P5_2-kin.
DR InterPro; IPR043001; IP5_2-K_N_lobe.
DR PANTHER; PTHR14456; PTHR14456; 1.
DR Pfam; PF06090; Ins_P5_2-kin; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Kinase; Metal-binding;
KW Nucleotide-binding; Reference proteome; Transferase; Zinc.
FT CHAIN 1..451
FT /note="Inositol-pentakisphosphate 2-kinase"
FT /id="PRO_0000110534"
FT MOTIF 166..170
FT /note="EXKPK motif"
FT BINDING 19..22
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:20453199,
FT ECO:0000305|PubMed:22745128"
FT BINDING 40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:20453199,
FT ECO:0000305|PubMed:22745128"
FT BINDING 45
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:20453199,
FT ECO:0000305|PubMed:22362712, ECO:0000305|PubMed:22684075,
FT ECO:0000305|PubMed:22745128"
FT BINDING 130
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:20453199,
FT ECO:0000305|PubMed:22362712, ECO:0000305|PubMed:22684075,
FT ECO:0000305|PubMed:22745128"
FT BINDING 147..149
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:20453199,
FT ECO:0000305|PubMed:22745128"
FT BINDING 166..168
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:20453199,
FT ECO:0000305|PubMed:22745128"
FT BINDING 170
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:20453199,
FT ECO:0000305|PubMed:22362712, ECO:0000305|PubMed:22684075,
FT ECO:0000305|PubMed:22745128"
FT BINDING 200
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:20453199,
FT ECO:0000305|PubMed:22362712, ECO:0000305|PubMed:22684075,
FT ECO:0000305|PubMed:22745128"
FT BINDING 238
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:20453199,
FT ECO:0000305|PubMed:22362712, ECO:0000305|PubMed:22684075,
FT ECO:0000305|PubMed:22745128"
FT BINDING 241
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:22745128"
FT BINDING 320
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0007744|PDB:2XAL, ECO:0007744|PDB:2XAM,
FT ECO:0007744|PDB:2XAN, ECO:0007744|PDB:2XAO,
FT ECO:0007744|PDB:2XAR, ECO:0007744|PDB:3UDT,
FT ECO:0007744|PDB:3UDZ, ECO:0007744|PDB:4AQK,
FT ECO:0007744|PDB:4AXC, ECO:0007744|PDB:4AXD,
FT ECO:0007744|PDB:4AXE, ECO:0007744|PDB:4AXF,
FT ECO:0007744|PDB:4LV7"
FT BINDING 330
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0007744|PDB:2XAL, ECO:0007744|PDB:2XAM,
FT ECO:0007744|PDB:2XAN, ECO:0007744|PDB:2XAO,
FT ECO:0007744|PDB:2XAR, ECO:0007744|PDB:3UDT,
FT ECO:0007744|PDB:3UDZ, ECO:0007744|PDB:4AQK,
FT ECO:0007744|PDB:4AXC, ECO:0007744|PDB:4AXD,
FT ECO:0007744|PDB:4AXE, ECO:0007744|PDB:4AXF,
FT ECO:0007744|PDB:4LV7"
FT BINDING 333
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0007744|PDB:2XAL, ECO:0007744|PDB:2XAM,
FT ECO:0007744|PDB:2XAN, ECO:0007744|PDB:2XAO,
FT ECO:0007744|PDB:2XAR, ECO:0007744|PDB:3UDT,
FT ECO:0007744|PDB:4AQK, ECO:0007744|PDB:4AXC,
FT ECO:0007744|PDB:4AXD, ECO:0007744|PDB:4AXE,
FT ECO:0007744|PDB:4AXF, ECO:0007744|PDB:4LV7"
FT BINDING 346
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0007744|PDB:2XAL, ECO:0007744|PDB:2XAM,
FT ECO:0007744|PDB:2XAN, ECO:0007744|PDB:2XAO,
FT ECO:0007744|PDB:2XAR, ECO:0007744|PDB:3UDT,
FT ECO:0007744|PDB:3UDZ, ECO:0007744|PDB:4AQK,
FT ECO:0007744|PDB:4AXC, ECO:0007744|PDB:4AXD,
FT ECO:0007744|PDB:4AXE, ECO:0007744|PDB:4AXF,
FT ECO:0007744|PDB:4LV7"
FT BINDING 368
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:20453199,
FT ECO:0000305|PubMed:22362712, ECO:0000305|PubMed:22684075,
FT ECO:0000305|PubMed:22745128"
FT BINDING 407
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:20453199,
FT ECO:0000305|PubMed:22745128"
FT BINDING 411
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:20453199,
FT ECO:0000305|PubMed:22362712, ECO:0000305|PubMed:22684075,
FT ECO:0000305|PubMed:22745128"
FT BINDING 415
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:20453199,
FT ECO:0000305|PubMed:22362712, ECO:0000305|PubMed:22684075,
FT ECO:0000305|PubMed:22745128"
FT BINDING 419
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:20453199,
FT ECO:0000305|PubMed:22362712, ECO:0000305|PubMed:22684075,
FT ECO:0000305|PubMed:22745128"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT HELIX 7..12
FT /evidence="ECO:0007829|PDB:6FJK"
FT STRAND 13..18
FT /evidence="ECO:0007829|PDB:6FJK"
FT STRAND 20..27
FT /evidence="ECO:0007829|PDB:6FJK"
FT TURN 32..36
FT /evidence="ECO:0007829|PDB:6FJK"
FT STRAND 37..45
FT /evidence="ECO:0007829|PDB:6FJK"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:4AXD"
FT HELIX 63..68
FT /evidence="ECO:0007829|PDB:6FJK"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:6FJK"
FT HELIX 73..77
FT /evidence="ECO:0007829|PDB:6FJK"
FT HELIX 81..91
FT /evidence="ECO:0007829|PDB:6FJK"
FT HELIX 94..97
FT /evidence="ECO:0007829|PDB:6FJK"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:6FL8"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:6FJK"
FT HELIX 112..122
FT /evidence="ECO:0007829|PDB:6FJK"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:6FJK"
FT HELIX 128..133
FT /evidence="ECO:0007829|PDB:6FJK"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:6FJK"
FT STRAND 141..147
FT /evidence="ECO:0007829|PDB:6FJK"
FT STRAND 152..155
FT /evidence="ECO:0007829|PDB:4AXD"
FT STRAND 163..167
FT /evidence="ECO:0007829|PDB:6FJK"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:4AQK"
FT HELIX 182..188
FT /evidence="ECO:0007829|PDB:6FJK"
FT HELIX 192..202
FT /evidence="ECO:0007829|PDB:6FJK"
FT STRAND 205..208
FT /evidence="ECO:0007829|PDB:4AXD"
FT HELIX 214..217
FT /evidence="ECO:0007829|PDB:6FJK"
FT HELIX 222..234
FT /evidence="ECO:0007829|PDB:6FJK"
FT TURN 237..239
FT /evidence="ECO:0007829|PDB:4AXD"
FT STRAND 240..244
FT /evidence="ECO:0007829|PDB:6FJK"
FT STRAND 247..251
FT /evidence="ECO:0007829|PDB:6FJK"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:6FJK"
FT HELIX 262..271
FT /evidence="ECO:0007829|PDB:6FJK"
FT TURN 272..275
FT /evidence="ECO:0007829|PDB:2XAM"
FT TURN 280..282
FT /evidence="ECO:0007829|PDB:4AXD"
FT HELIX 283..298
FT /evidence="ECO:0007829|PDB:6FJK"
FT HELIX 300..308
FT /evidence="ECO:0007829|PDB:6FJK"
FT HELIX 315..325
FT /evidence="ECO:0007829|PDB:6FJK"
FT TURN 331..335
FT /evidence="ECO:0007829|PDB:4AXD"
FT HELIX 338..340
FT /evidence="ECO:0007829|PDB:4AXF"
FT HELIX 344..347
FT /evidence="ECO:0007829|PDB:6FJK"
FT HELIX 350..367
FT /evidence="ECO:0007829|PDB:6FJK"
FT STRAND 370..377
FT /evidence="ECO:0007829|PDB:6FJK"
FT STRAND 388..392
FT /evidence="ECO:0007829|PDB:6FJK"
FT TURN 393..396
FT /evidence="ECO:0007829|PDB:6FJK"
FT STRAND 397..406
FT /evidence="ECO:0007829|PDB:6FJK"
FT HELIX 415..435
FT /evidence="ECO:0007829|PDB:6FJK"
SQ SEQUENCE 451 AA; 50509 MW; C3172D638277D1B5 CRC64;
MEMILEEKDA SDWIYRGEGG ANLVLAYAGS SPLFVGKVIR IQKARRNDKA IKNANGVVSV
LTSDEQHLWR ENNELISSPN KEVLEQRYVK NVIIPLLGPK HVDAGVRVSV SKEFLECVDK
KVTKQRPLWR VNAANVDTSH DSALILNDHS LFSQGISSGG DCISVEIKPK CGFLPTSRFI
GKENMLKTSV SRFKMHQLLK LEYNEISEES EYDPLDLFSG SKESVLEAIK ALYSTPQNNF
RVFLNGSLIL GGSGESTGRT SPEIGYAFED ALKGFIQSED GHRTECFLQL VSDAVYGSGV
LDRLLEIQKL DKLDIEGAIH SYYDLINQPC PICKEGKPLE AELSLHALPL DESLKIVKEY
LIAATAKDCS IMISFQSRNA WDSEPSGDYV SLKPTNQTFD YKVHFIDLSL KPLKRMESYY
KLDKKIISFY NRKQKAENTA EQIGNSKPSH S
