AKT1_ARATH
ID AKT1_ARATH Reviewed; 857 AA.
AC Q38998; B9DI19; Q0WTF6; Q38797; Q84MA7;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Potassium channel AKT1;
GN Name=AKT1; OrderedLocusNames=At2g26650; ORFNames=F18A8.2;
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].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=1585180; DOI=10.1126/science.1585180;
RA Sentenac H., Bonneaud N., Minet M., Lacroute F., Salmon J.-M., Gaymard F.,
RA Grignon C.;
RT "Cloning and expression in yeast of a plant potassium ion transport
RT system.";
RL Science 256:663-665(1992).
RN [2]
RP SEQUENCE REVISION.
RA Sentenac H.;
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=8555458; DOI=10.1007/bf00014968;
RA Basset M., Conejero G., Lepetit M., Fourcroy P., Sentenac H.;
RT "Organization and expression of the gene coding for the potassium transport
RT system AKT1 of Arabidopsis thaliana.";
RL Plant Mol. Biol. 29:947-958(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf {ECO:0000312|EMBL:BAH20386.1};
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 79-857.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 106-857.
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 [9]
RP TISSUE SPECIFICITY.
RX PubMed=8820606; DOI=10.1046/j.1365-313x.1996.09020195.x;
RA Lagarde D., Basset M., Lepetit M., Conejero G., Gaymard F., Astruc S.,
RA Grignon C.;
RT "Tissue-specific expression of Arabidopsis AKT1 gene is consistent with a
RT role in K+ nutrition.";
RL Plant J. 9:195-203(1996).
RN [10]
RP SUBUNIT.
RX PubMed=9218788; DOI=10.1093/emboj/16.12.3455;
RA Daram P., Urbach S., Gaymard F., Sentenac H., Cherel I.;
RT "Tetramerization of the AKT1 plant potassium channel involves its C-
RT terminal cytoplasmic domain.";
RL EMBO J. 16:3455-3463(1997).
RN [11]
RP FUNCTION.
RX PubMed=9572739; DOI=10.1126/science.280.5365.918;
RA Hirsch R.E., Lewis B.D., Spalding E.P., Sussman M.R.;
RT "A role for the AKT1 potassium channel in plant nutrition.";
RL Science 280:918-921(1998).
RN [12]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11500563; DOI=10.1104/pp.126.4.1646;
RA Maeser P., Thomine S., Schroeder J.I., Ward J.M., Hirschi K., Sze H.,
RA Talke I.N., Amtmann A., Maathuis F.J.M., Sanders D., Harper J.F.,
RA Tchieu J., Gribskov M., Persans M.W., Salt D.E., Kim S.A., Guerinot M.L.;
RT "Phylogenetic relationships within cation transporter families of
RT Arabidopsis.";
RL Plant Physiol. 126:1646-1667(2001).
RN [13]
RP FUNCTION, INTERACTION WITH AKT2 AND KAT3, AND INDUCTION.
RX PubMed=12678562; DOI=10.1023/a:1022597102282;
RA Pilot G., Gaymard F., Mouline K., Cherel I., Sentenac H.;
RT "Regulated expression of Arabidopsis shaker K(+) channel genes involved in
RT K(+) uptake and distribution in the plant.";
RL Plant Mol. Biol. 51:773-787(2003).
RN [14]
RP FUNCTION, INTERACTION WITH CIPK23, PHOSPHORYLATION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=16814720; DOI=10.1016/j.cell.2006.06.011;
RA Xu J., Li H.-D., Chen L.-Q., Wang Y., Liu L.-L., He L., Wu W.-H.;
RT "A protein kinase, interacting with two calcineurin B-like proteins,
RT regulates K+ transporter AKT1 in Arabidopsis.";
RL Cell 125:1347-1360(2006).
RN [15]
RP FUNCTION, INTERACTION WITH CIPK23, AND PHOSPHORYLATION.
RX PubMed=16895985; DOI=10.1073/pnas.0605129103;
RA Li L., Kim B.-G., Cheong Y.H., Pandey G.K., Luan S.;
RT "A Ca(2)+ signaling pathway regulates a K(+) channel for low-K response in
RT Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:12625-12630(2006).
RN [16]
RP FUNCTION, PHOSPHORYLATION, AND INTERACTION WITH AIP1; CIPK6; CIPK16 AND
RP CIPK23.
RX PubMed=17898163; DOI=10.1073/pnas.0707912104;
RA Lee S.-C., Lan W.-Z., Kim B.-G., Li L., Cheong Y.H., Pandey G.K., Lu G.,
RA Buchanan B.B., Luan S.;
RT "A protein phosphorylation/dephosphorylation network regulates a plant
RT potassium channel.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:15959-15964(2007).
RN [17]
RP FUNCTION.
RX PubMed=20413648; DOI=10.1104/pp.110.154369;
RA Pyo Y.J., Gierth M., Schroeder J.I., Cho M.H.;
RT "High-affinity K(+) transport in Arabidopsis: AtHAK5 and AKT1 are vital for
RT seedling establishment and postgermination growth under low-potassium
RT conditions.";
RL Plant Physiol. 153:863-875(2010).
RN [18]
RP INTERACTION WITH CBL10.
RX PubMed=23331977; DOI=10.1111/tpj.12123;
RA Ren X.L., Qi G.N., Feng H.Q., Zhao S., Zhao S.S., Wang Y., Wu W.H.;
RT "Calcineurin B-like protein CBL10 directly interacts with AKT1 and
RT modulates K+ homeostasis in Arabidopsis.";
RL Plant J. 74:258-266(2013).
RN [19]
RP CRYSTALLIZATION OF THE ANKYRIN-REPEAT DOMAIN.
RX PubMed=24699751; DOI=10.1107/s2053230x14005093;
RA Chaves-Sanjuan A., Sanchez-Barrena M.J., Gonzalez-Rubio J.M., Albert A.;
RT "Preliminary crystallographic analysis of the ankyrin-repeat domain of
RT Arabidopsis thaliana AKT1: identification of the domain boundaries for
RT protein crystallization.";
RL Acta Crystallogr. F Struct. Biol. Commun. 70:509-512(2014).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS) OF 518-702.
RA Chaves-Sanjuan A., Gonzalez-Rubio J.M., Sanchez-Barrena M.J., Albert A.;
RT "Structure of the Ankyrin Domain of Akt1.";
RL Submitted (JUL-2015) to the PDB data bank.
CC -!- FUNCTION: Highly selective inward-rectifying potassium channel that
CC mediate potassium uptake by plant roots in response to low K(+)
CC conditions, by a calcium-, CBL-, and CIPK-dependent pathway. Positively
CC regulated by phosphorylation by CIPK23. Negatively regulated by a
CC kinase-independent regulatory mechanism involving a competing direct
CC binding of CBL10. Involved in the stomatal regulation by monitoring the
CC turgor pressure in guard cells. Assuming opened or closed conformations
CC in response to the voltage difference across the membrane, the channel
CC is activated by hyperpolarization. May interact with the cytoskeleton
CC or with regulatory proteins (PubMed:12678562, PubMed:16814720,
CC PubMed:16895985, PubMed:17898163, PubMed:9572739). Is essential with
CC POT5/HAK5 for high-affinity potassium uptake in roots during seedling
CC establishment and postgermination growth under low potassium conditions
CC (PubMed:20413648). {ECO:0000269|PubMed:12678562,
CC ECO:0000269|PubMed:16814720, ECO:0000269|PubMed:16895985,
CC ECO:0000269|PubMed:17898163, ECO:0000269|PubMed:20413648,
CC ECO:0000269|PubMed:9572739}.
CC -!- SUBUNIT: The potassium channel is probably composed of a homo- or
CC heterotetrameric complex of pore-forming subunits. Possible
CC heteromultimer with AKT2 or KAT3. Part of a K(+)-channel calcium-
CC sensing kinase/phosphatase complex composed by a calcium sensor CBL
CC (CBL1, CBL2, CBL3 or CBL9), a kinase CIPK (CIPK6, CIPK16 or CIPK23), a
CC phosphatase PP2C (AIP1) and a K(+)-channel (AKT1). Interacts directly
CC with AIP1, CBL10, CIPK6, CIPK16 and CIPK23.
CC {ECO:0000269|PubMed:12678562, ECO:0000269|PubMed:16814720,
CC ECO:0000269|PubMed:16895985, ECO:0000269|PubMed:17898163,
CC ECO:0000269|PubMed:23331977, ECO:0000269|PubMed:9218788}.
CC -!- INTERACTION:
CC Q38998; Q38998: AKT1; NbExp=7; IntAct=EBI-974289, EBI-974289;
CC Q38998; Q38898: AKT2; NbExp=3; IntAct=EBI-974289, EBI-1552774;
CC Q38998; Q93VD3: CIPK23; NbExp=6; IntAct=EBI-974289, EBI-974277;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16814720};
CC Multi-pass membrane protein {ECO:0000269|PubMed:16814720}.
CC -!- TISSUE SPECIFICITY: Preferentially expressed in the peripheral cell
CC layers of root mature including root cortex and root hairs. Detected
CC also, at a lower level, in the mesophyll of the leaves and at
CC restricted sites corresponding to hydathodes and guard cells.
CC {ECO:0000269|PubMed:8555458, ECO:0000269|PubMed:8820606}.
CC -!- INDUCTION: In roots, strongly reduced after 2,4-dichlorophenoxyacetic
CC acid (2,4-D) treatment and weakly reduced after benzyladenine (BA)
CC treatment. In shoots, strongly reduced after abscisic acid (ABA)
CC treatment and induced after benzyladenine (BA) treatment.
CC {ECO:0000269|PubMed:12678562}.
CC -!- DOMAIN: The segment S4 is probably the voltage-sensor and is
CC characterized by a series of positively charged amino acids. The pore-
CC forming region H5 is enclosed by the transmembrane segments S5 and S6
CC in the Shaker-type (1P/6TM) and contains the GYGD signature motif which
CC seems to be involved in potassium selectivity.
CC -!- DOMAIN: The KHA domain (rich in hydrophobic and acidic residues)
CC present in the C-terminal part is likely to be important for
CC tetramerization.
CC -!- PTM: Phosphorylated by CIPK proteins CIPK6, CIPK16 and CIPK23. The
CC activation by phosphorylation is induced by low K(+) conditions and
CC stimulates K(+) uptake and relocation. Dephosphorylation by AIP1
CC repressed the transport activity. {ECO:0000269|PubMed:16814720,
CC ECO:0000269|PubMed:16895985, ECO:0000269|PubMed:17898163}.
CC -!- SIMILARITY: Belongs to the potassium channel family. Plant (TC 1.A.1.4)
CC subfamily. {ECO:0000305}.
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DR EMBL; X62907; CAA44693.1; -; mRNA.
DR EMBL; U06745; AAA96810.1; -; Genomic_DNA.
DR EMBL; AC003105; AAB95299.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07870.1; -; Genomic_DNA.
DR EMBL; AK317729; BAH20386.1; -; mRNA.
DR EMBL; AK227601; BAE99592.1; -; mRNA.
DR EMBL; BT006442; AAP21250.1; -; mRNA.
DR PIR; S23606; S23606.
DR PIR; S62694; S62694.
DR RefSeq; NP_001324538.1; NM_001336078.1.
DR RefSeq; NP_180233.1; NM_128222.6.
DR PDB; 5AAR; X-ray; 1.87 A; A=518-702.
DR PDB; 7T4X; EM; 2.80 A; A/B/C/D=1-857.
DR PDBsum; 5AAR; -.
DR PDBsum; 7T4X; -.
DR AlphaFoldDB; Q38998; -.
DR SMR; Q38998; -.
DR BioGRID; 2558; 17.
DR DIP; DIP-36762N; -.
DR IntAct; Q38998; 9.
DR STRING; 3702.AT2G26650.1; -.
DR TCDB; 1.A.1.4.1; the voltage-gated ion channel (vic) superfamily.
DR iPTMnet; Q38998; -.
DR PaxDb; Q38998; -.
DR PRIDE; Q38998; -.
DR ProteomicsDB; 244667; -.
DR EnsemblPlants; AT2G26650.1; AT2G26650.1; AT2G26650.
DR GeneID; 817206; -.
DR Gramene; AT2G26650.1; AT2G26650.1; AT2G26650.
DR KEGG; ath:AT2G26650; -.
DR Araport; AT2G26650; -.
DR TAIR; locus:2043839; AT2G26650.
DR eggNOG; KOG0498; Eukaryota.
DR HOGENOM; CLU_005746_8_3_1; -.
DR InParanoid; Q38998; -.
DR OrthoDB; 118742at2759; -.
DR PhylomeDB; Q38998; -.
DR BioCyc; ARA:AT2G26550-MON; -.
DR BioCyc; MetaCyc:MON-14552; -.
DR PRO; PR:Q38998; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q38998; baseline and differential.
DR Genevisible; Q38998; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005242; F:inward rectifier potassium channel activity; IDA:TAIR.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; IDA:TAIR.
DR GO; GO:0006813; P:potassium ion transport; IMP:TAIR.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0090333; P:regulation of stomatal closure; IMP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IMP:TAIR.
DR GO; GO:0048767; P:root hair elongation; IMP:TAIR.
DR CDD; cd00038; CAP_ED; 1.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 2.60.120.10; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR018490; cNMP-bd-like.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR003938; K_chnl_volt-dep_EAG/ELK/ERG.
DR InterPro; IPR045319; KAT/AKT.
DR InterPro; IPR021789; KHA_dom.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR PANTHER; PTHR45743; PTHR45743; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF11834; KHA; 1.
DR PRINTS; PR01415; ANKYRIN.
DR PRINTS; PR01463; EAGCHANLFMLY.
DR SMART; SM00248; ANK; 5.
DR SMART; SM00100; cNMP; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF51206; SSF51206; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 3.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
DR PROSITE; PS51490; KHA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ANK repeat; Cell membrane; Ion channel; Ion transport;
KW Membrane; Phosphoprotein; Potassium; Potassium channel;
KW Potassium transport; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..857
FT /note="Potassium channel AKT1"
FT /id="PRO_0000054121"
FT TOPO_DOM 1..61
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..82
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 83..90
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 91..111
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 112..134
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 135..155
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 156..158
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 180..193
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..214
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 215..241
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 242..261
FT /note="Pore-forming; Name=Segment H5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 262..265
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..286
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 287..857
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 515..546
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 550..579
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT REPEAT 583..612
FT /note="ANK 3"
FT /evidence="ECO:0000255"
FT REPEAT 614..643
FT /note="ANK 4"
FT /evidence="ECO:0000255"
FT REPEAT 647..676
FT /note="ANK 5"
FT /evidence="ECO:0000255"
FT REPEAT 680..709
FT /note="ANK 6"
FT /evidence="ECO:0000255"
FT DOMAIN 790..857
FT /note="KHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00823"
FT BINDING 372..493
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00060"
FT HELIX 5..14
FT /evidence="ECO:0007829|PDB:7T4X"
FT HELIX 55..81
FT /evidence="ECO:0007829|PDB:7T4X"
FT HELIX 89..106
FT /evidence="ECO:0007829|PDB:7T4X"
FT TURN 107..109
FT /evidence="ECO:0007829|PDB:7T4X"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:7T4X"
FT HELIX 124..133
FT /evidence="ECO:0007829|PDB:7T4X"
FT HELIX 136..141
FT /evidence="ECO:0007829|PDB:7T4X"
FT HELIX 146..151
FT /evidence="ECO:0007829|PDB:7T4X"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:7T4X"
FT HELIX 157..163
FT /evidence="ECO:0007829|PDB:7T4X"
FT HELIX 164..168
FT /evidence="ECO:0007829|PDB:7T4X"
FT HELIX 169..178
FT /evidence="ECO:0007829|PDB:7T4X"
FT HELIX 186..214
FT /evidence="ECO:0007829|PDB:7T4X"
FT TURN 223..227
FT /evidence="ECO:0007829|PDB:7T4X"
FT STRAND 231..234
FT /evidence="ECO:0007829|PDB:7T4X"
FT HELIX 236..251
FT /evidence="ECO:0007829|PDB:7T4X"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:7T4X"
FT HELIX 264..295
FT /evidence="ECO:0007829|PDB:7T4X"
FT HELIX 297..316
FT /evidence="ECO:0007829|PDB:7T4X"
FT HELIX 320..335
FT /evidence="ECO:0007829|PDB:7T4X"
FT TURN 336..339
FT /evidence="ECO:0007829|PDB:7T4X"
FT HELIX 340..347
FT /evidence="ECO:0007829|PDB:7T4X"
FT HELIX 352..367
FT /evidence="ECO:0007829|PDB:7T4X"
FT HELIX 371..373
FT /evidence="ECO:0007829|PDB:7T4X"
FT HELIX 378..387
FT /evidence="ECO:0007829|PDB:7T4X"
FT STRAND 389..393
FT /evidence="ECO:0007829|PDB:7T4X"
FT STRAND 398..400
FT /evidence="ECO:0007829|PDB:7T4X"
FT STRAND 408..415
FT /evidence="ECO:0007829|PDB:7T4X"
FT STRAND 417..420
FT /evidence="ECO:0007829|PDB:7T4X"
FT STRAND 431..433
FT /evidence="ECO:0007829|PDB:7T4X"
FT STRAND 437..440
FT /evidence="ECO:0007829|PDB:7T4X"
FT HELIX 441..446
FT /evidence="ECO:0007829|PDB:7T4X"
FT STRAND 451..466
FT /evidence="ECO:0007829|PDB:7T4X"
FT HELIX 467..475
FT /evidence="ECO:0007829|PDB:7T4X"
FT TURN 478..480
FT /evidence="ECO:0007829|PDB:7T4X"
FT HELIX 481..489
FT /evidence="ECO:0007829|PDB:7T4X"
FT TURN 490..492
FT /evidence="ECO:0007829|PDB:7T4X"
FT HELIX 522..527
FT /evidence="ECO:0007829|PDB:5AAR"
FT HELIX 531..539
FT /evidence="ECO:0007829|PDB:5AAR"
FT HELIX 554..561
FT /evidence="ECO:0007829|PDB:5AAR"
FT HELIX 564..572
FT /evidence="ECO:0007829|PDB:5AAR"
FT HELIX 587..593
FT /evidence="ECO:0007829|PDB:5AAR"
FT HELIX 597..605
FT /evidence="ECO:0007829|PDB:5AAR"
FT HELIX 610..612
FT /evidence="ECO:0007829|PDB:5AAR"
FT HELIX 615..624
FT /evidence="ECO:0007829|PDB:5AAR"
FT HELIX 628..636
FT /evidence="ECO:0007829|PDB:5AAR"
FT HELIX 651..657
FT /evidence="ECO:0007829|PDB:5AAR"
FT HELIX 661..669
FT /evidence="ECO:0007829|PDB:5AAR"
FT HELIX 684..690
FT /evidence="ECO:0007829|PDB:5AAR"
FT HELIX 694..701
FT /evidence="ECO:0007829|PDB:5AAR"
SQ SEQUENCE 857 AA; 96990 MW; 28E1622BA3505F4C CRC64;
MRGGALLCGQ VQDEIEQLSR ESSHFSLSTG ILPSLGARSN RRVKLRRFVV SPYDHKYRIW
EAFLVVLVVY TAWVSPFEFG FLRKPRPPLS ITDNIVNAFF AIDIIMTFFV GYLDKSTYLI
VDDRKQIAFK YLRSWFLLDL VSTIPSEAAM RISSQSYGLF NMLRLWRLRR VGALFARLEK
DRNFNYFWVR CAKLVCVTLF AVHCAACFYY LIAARNSNPA KTWIGANVAN FLEESLWMRY
VTSMYWSITT LTTVGYGDLH PVNTKEMIFD IFYMLFNLGL TAYLIGNMTN LVVHGTSRTR
NFRDTIQAAS NFAHRNHLPP RLQDQMLAHL CLKYRTDSEG LQQQETLDAL PKAIRSSISH
FLFYSLMDKV YLFRGVSNDL LFQLVSEMKA EYFPPKEDVI LQNEAPTDFY ILVNGTADLV
DVDTGTESIV REVKAGDIIG EIGVLCYRPQ LFTVRTKRLC QLLRMNRTTF LNIIQANVGD
GTIIMNNLLQ HLKEMNDPVM TNVLLEIENM LARGKMDLPL NLCFAAIRED DLLLHQLLKR
GLDPNESDNN GRTPLHIAAS KGTLNCVLLL LEYHADPNCR DAEGSVPLWE AMVEGHEKVV
KVLLEHGSTI DAGDVGHFAC TAAEQGNLKL LKEIVLHGGD VTRPRATGTS ALHTAVCEEN
IEMVKYLLEQ GADVNKQDMH GWTPRDLAEQ QGHEDIKALF REKLHERRVH IETSSSVPIL
KTGIRFLGRF TSEPNIRPAS REVSFRIRET RARRKTNNFD NSLFGILANQ SVPKNGLATV
DEGRTGNPVR VTISCAEKDD IAGKLVLLPG SFKELLELGS NKFGIVATKV MNKDNNAEID
DVDVIRDGDH LIFATDS
