KAT1_ARATH
ID KAT1_ARATH Reviewed; 677 AA.
AC Q39128; Q42426;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Potassium channel KAT1;
GN Name=KAT1; OrderedLocusNames=At5g46240; ORFNames=MPL12.2;
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].
RX PubMed=1570292; DOI=10.1073/pnas.89.9.3736;
RA Anderson J.A., Huprikar S.S., Kochian L.V., Lucas W.J., Gaber R.F.;
RT "Functional expression of a probable Arabidopsis thaliana potassium channel
RT in Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:3736-3740(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. RLD;
RX PubMed=7480337; DOI=10.1104/pp.109.2.371;
RA Nakamura R.L., McKendree W.L. Jr., Hirsch R.E., Sedbrook J.C., Gaber R.F.,
RA Sussman M.R.;
RT "Expression of an Arabidopsis potassium channel gene in guard cells.";
RL Plant Physiol. 109:371-374(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=8798465; DOI=10.1074/jbc.271.37.22863;
RA Gaymard F., Cerrutti M., Horeau C., Lemaillet G., Urbach S., Ravallec M.,
RA Devauchelle G., Sentenac H., Thibaud J.-B.;
RT "The baculovirus/insect cell system as an alternative to Xenopus oocytes.
RT First characterization of the AKT1 K+ channel from Arabidopsis thaliana.";
RL J. Biol. Chem. 271:22863-22870(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
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 FUNCTION.
RX PubMed=8966547; DOI=10.1126/science.8966547;
RA Schachtman D.P., Schroeder J.I., Lucas W.J., Anderson J.A., Gaber R.F.;
RT "Expression of an inward-rectifying potassium channel by the Arabidopsis
RT KAT1 cDNA.";
RL Science 258:1654-1658(1992).
RN [7]
RP PORE SELECTIVITY, AND MUTAGENESIS OF THR-256.
RX PubMed=7592636; DOI=10.1074/jbc.270.41.24276;
RA Uozumi N., Gassmann W., Cao Y., Schroeder J.I.;
RT "Identification of strong modifications in cation selectivity in an
RT Arabidopsis inward rectifying potassium channel by mutant selection in
RT yeast.";
RL J. Biol. Chem. 270:24276-24281(1995).
RN [8]
RP PORE SELECTIVITY, AND MUTAGENESIS OF LEU-251; THR-256; THR-259; THR-260 AND
RP 259-THR-THR-260.
RX PubMed=8755614; DOI=10.1073/pnas.93.15.8123;
RA Becker D., Dreyer I., Hoth S., Reid J.D., Busch H., Lehnen M., Palme K.,
RA Hedrich R.;
RT "Changes in voltage activation, Cs+ sensitivity, and ion permeability in H5
RT mutants of the plant K+ channel KAT1.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:8123-8128(1996).
RN [9]
RP PORE SELECTIVITY, AND MUTAGENESIS OF TYR-263 AND GLY-264.
RX PubMed=8995396; DOI=10.1074/jbc.272.2.1011;
RA Nakamura R.L., Anderson J.A., Gaber R.F.;
RT "Determination of key structural requirements of a K+ channel pore.";
RL J. Biol. Chem. 272:1011-1018(1997).
RN [10]
RP PORE SELECTIVITY, AND MUTAGENESIS OF HIS-267 AND GLU-269.
RX PubMed=9368418; DOI=10.2307/3870529;
RA Ichida A.M., Pei Z.-M., Baizabal-Aguirre V.M., Turner K.J., Schroeder J.I.;
RT "Expression of a Cs(+)-resistant guard cell K+ channel confers Cs(+)-
RT resistant, light-induced stomatal opening in transgenic Arabidopsis.";
RL Plant Cell 9:1843-1857(1997).
RN [11]
RP PORE SELECTIVITY, AND MUTAGENESIS OF THR-256 AND HIS-267.
RX PubMed=9688573; DOI=10.1016/s0014-5793(98)00694-2;
RA Dreyer I., Becker D., Bregante M., Gambale F., Lehnen M., Palme K.,
RA Hedrich R.;
RT "Single mutations strongly alter the K(+)-selective pore of the K(in)
RT channel KAT1.";
RL FEBS Lett. 430:370-376(1998).
RN [12]
RP VOLTAGE-DEPENDENT GATING, AND MUTAGENESIS OF ARG-176.
RX PubMed=9635749; DOI=10.1016/s0006-3495(98)78002-6;
RA Marten I., Hoshi T.;
RT "The N-terminus of the K channel KAT1 controls its voltage-dependent gating
RT by altering the membrane electric field.";
RL Biophys. J. 74:2953-2962(1998).
RN [13]
RP VOLTAGE-DEPENDENT GATING, AND MUTAGENESIS OF ARG-176 AND ARG-177.
RX PubMed=9834140; DOI=10.1085/jgp.112.6.679;
RA Zei P.C., Aldrich R.W.;
RT "Voltage-dependent gating of single wild-type and S4 mutant KAT1 inward
RT rectifier potassium channels.";
RL J. Gen. Physiol. 112:679-713(1998).
RN [14]
RP INTERACTION WITH AKT2, AND MUTAGENESIS OF THR-256 AND GLY-262.
RX PubMed=9916143; DOI=10.1007/s002329900476;
RA Baizabal-Aguirre V.M., Clemens S., Uozumi N., Schroeder J.I.;
RT "Suppression of inward-rectifying K+ channels KAT1 and AKT2 by dominant
RT negative point mutations in the KAT1 alpha-subunit.";
RL J. Membr. Biol. 167:119-125(1999).
RN [15]
RP PROTON SENSITIVITY, AND MUTAGENESIS OF ASP-265.
RX PubMed=10206968; DOI=10.1074/jbc.274.17.11599;
RA Hoth S., Hedrich R.;
RT "Distinct molecular bases for pH sensitivity of the guard cell K+ channels
RT KST1 and KAT1.";
RL J. Biol. Chem. 274:11599-11603(1999).
RN [16]
RP INTERACTION WITH KAT2.
RX PubMed=11042178; DOI=10.1074/jbc.m007303200;
RA Pilot G., Lacombe B., Gaymard F., Cherel I., Boucherez J., Thibaud J.-B.,
RA Sentenac H.;
RT "Guard cell inward K+ channel activity in Arabidopsis involves expression
RT of the twin channel subunits KAT1 and KAT2.";
RL J. Biol. Chem. 276:3215-3221(2001).
RN [17]
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 [18]
RP INTERACTION WITH SLAC1 AND SLAH3.
RX PubMed=27002025; DOI=10.1105/tpc.16.01050;
RA Zhang A., Ren H.M., Tan Y.Q., Qi G.N., Yao F.Y., Wu G.L., Yang L.W.,
RA Hussain J., Sun S.J., Wang Y.F.;
RT "S-type anion channels SLAC1 and SLAH3 function as essential negative
RT regulators of inward K+ channels and stomatal opening in Arabidopsis.";
RL Plant Cell 28:949-955(2016).
CC -!- FUNCTION: Highly selective inward-rectifying potassium channel. This
CC voltage-gated channel could mediate long-term potassium influx into
CC guard cells leading to stomatal opening. Assuming opened or closed
CC conformations in response to the voltage difference across the
CC membrane, the channel is activated by hyperpolarization. The channel
CC activity is enhanced upon external acidification. Also permeable to
CC ammonium ions. Blocked by tetraethylammonium and barium ions.
CC {ECO:0000269|PubMed:8966547}.
CC -!- SUBUNIT: The potassium channel is probably composed of a homo- or
CC heterotetrameric complex of pore-forming subunits. May interact with
CC AKT2 and KAT2 (Probable). Interacts with SLAC1 and SLAH3
CC (PubMed:27002025). {ECO:0000269|PubMed:27002025, ECO:0000305}.
CC -!- INTERACTION:
CC Q39128; Q38898: AKT2; NbExp=4; IntAct=EBI-1552490, EBI-1552774;
CC Q39128; Q39128: KAT1; NbExp=6; IntAct=EBI-1552490, EBI-1552490;
CC Q39128; Q38849: KAT2; NbExp=3; IntAct=EBI-1552490, EBI-2117720;
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in guard cells, and in roots.
CC {ECO:0000269|PubMed:7480337}.
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 -!- SIMILARITY: Belongs to the potassium channel family. Plant (TC 1.A.1.4)
CC subfamily. {ECO:0000305}.
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DR EMBL; M86990; AAA32824.1; -; mRNA.
DR EMBL; U25088; AAC49113.1; -; Genomic_DNA.
DR EMBL; X93022; CAA63601.1; -; mRNA.
DR EMBL; AB010698; BAB11079.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95356.1; -; Genomic_DNA.
DR PIR; S32816; S32816.
DR RefSeq; NP_199436.1; NM_123993.3.
DR PDB; 5NWI; X-ray; 2.35 A; P=673-677.
DR PDB; 5NWJ; X-ray; 2.07 A; P=671-677.
DR PDB; 5NWK; X-ray; 3.30 A; P/Q/R/S/T/U/V/W=673-677.
DR PDB; 6V1X; EM; 3.50 A; A/B/C/D=1-502.
DR PDB; 6V1Y; EM; 3.80 A; A/B/C/D/M/N/O/P=1-502.
DR PDB; 7CAL; EM; 3.20 A; A/B/C/D=1-677.
DR PDBsum; 5NWI; -.
DR PDBsum; 5NWJ; -.
DR PDBsum; 5NWK; -.
DR PDBsum; 6V1X; -.
DR PDBsum; 6V1Y; -.
DR PDBsum; 7CAL; -.
DR AlphaFoldDB; Q39128; -.
DR SMR; Q39128; -.
DR BioGRID; 19915; 17.
DR IntAct; Q39128; 8.
DR STRING; 3702.AT5G46240.1; -.
DR TCDB; 1.A.1.4.7; the voltage-gated ion channel (vic) superfamily.
DR iPTMnet; Q39128; -.
DR PaxDb; Q39128; -.
DR PRIDE; Q39128; -.
DR ProteomicsDB; 232242; -.
DR EnsemblPlants; AT5G46240.1; AT5G46240.1; AT5G46240.
DR GeneID; 834666; -.
DR Gramene; AT5G46240.1; AT5G46240.1; AT5G46240.
DR KEGG; ath:AT5G46240; -.
DR Araport; AT5G46240; -.
DR TAIR; locus:2170468; AT5G46240.
DR eggNOG; KOG0498; Eukaryota.
DR HOGENOM; CLU_005746_8_3_1; -.
DR InParanoid; Q39128; -.
DR OMA; YPNFKED; -.
DR OrthoDB; 247304at2759; -.
DR PhylomeDB; Q39128; -.
DR BioCyc; ARA:AT5G46240-MON; -.
DR BioCyc; MetaCyc:MON-14553; -.
DR PRO; PR:Q39128; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q39128; baseline and differential.
DR Genevisible; Q39128; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
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:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR CDD; cd00038; CAP_ED; 1.
DR Gene3D; 2.60.120.10; -; 1.
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; 2.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF11834; KHA; 1.
DR PRINTS; PR01463; EAGCHANLFMLY.
DR SMART; SM00100; cNMP; 1.
DR SUPFAM; SSF51206; SSF51206; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
DR PROSITE; PS51490; KHA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Ion channel; Ion transport; Membrane; Potassium;
KW Potassium channel; Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..677
FT /note="Potassium channel KAT1"
FT /id="PRO_0000054125"
FT TOPO_DOM 1..63
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 64..84
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 85..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..165
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..186
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 187..200
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 222..248
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 249..268
FT /note="Pore-forming; Name=Segment H5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 269..272
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 273..293
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 294..677
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 612..677
FT /note="KHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00823"
FT REGION 568..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 377..496
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT MUTAGEN 176
FT /note="R->S,L: Affects the voltage-dependent gating."
FT /evidence="ECO:0000269|PubMed:9635749,
FT ECO:0000269|PubMed:9834140"
FT MUTAGEN 177
FT /note="R->Q: Affects the voltage-dependent gating."
FT /evidence="ECO:0000269|PubMed:9834140"
FT MUTAGEN 251
FT /note="L->I,F: Enhances cesium sensitivity."
FT /evidence="ECO:0000269|PubMed:8755614"
FT MUTAGEN 256
FT /note="T->D,G,Q,E: Increases sensitivity to ammonium and
FT sodium."
FT /evidence="ECO:0000269|PubMed:7592636,
FT ECO:0000269|PubMed:8755614, ECO:0000269|PubMed:9688573,
FT ECO:0000269|PubMed:9916143"
FT MUTAGEN 256
FT /note="T->E: Increases rubidium uptake and both cesium and
FT calcium sensitivity; facilitated entry of calcium ions;
FT when associated with A-267."
FT /evidence="ECO:0000269|PubMed:7592636,
FT ECO:0000269|PubMed:8755614, ECO:0000269|PubMed:9688573,
FT ECO:0000269|PubMed:9916143"
FT MUTAGEN 256
FT /note="T->F,L,P,R,W: Abolishes channel activity."
FT /evidence="ECO:0000269|PubMed:7592636,
FT ECO:0000269|PubMed:8755614, ECO:0000269|PubMed:9688573,
FT ECO:0000269|PubMed:9916143"
FT MUTAGEN 256
FT /note="T->S: Increases calcium sensitivity; facilitated
FT entry of calcium ions; when associated with A-267."
FT /evidence="ECO:0000269|PubMed:7592636,
FT ECO:0000269|PubMed:8755614, ECO:0000269|PubMed:9688573,
FT ECO:0000269|PubMed:9916143"
FT MUTAGEN 259
FT /note="T->S: Increases rubidium uptake and cesium
FT sensitivity; additional increase of rubidium uptake; when
FT associated with S-260."
FT /evidence="ECO:0000269|PubMed:8755614"
FT MUTAGEN 260
FT /note="T->S: Increases rubidium uptake; additional increase
FT of rubidium uptake; when associated with S-259."
FT /evidence="ECO:0000269|PubMed:8755614"
FT MUTAGEN 262
FT /note="G->K: Abolishes channel activity."
FT /evidence="ECO:0000269|PubMed:9916143"
FT MUTAGEN 263
FT /note="Y->F: The only mutation at this site that do not
FT perturb the channel activity."
FT /evidence="ECO:0000269|PubMed:8995396"
FT MUTAGEN 264
FT /note="G->C,F,K,L,P,S,T: Abolishes channel activity."
FT /evidence="ECO:0000269|PubMed:8995396"
FT MUTAGEN 265
FT /note="D->N: Affects the pH-dependence."
FT /evidence="ECO:0000269|PubMed:10206968"
FT MUTAGEN 267
FT /note="H->A: Increases calcium sensitivity; facilitated
FT entry of calcium ions; when associated with S-256."
FT /evidence="ECO:0000269|PubMed:9368418,
FT ECO:0000269|PubMed:9688573"
FT MUTAGEN 267
FT /note="H->T: Resistance to the cesium inhibition of
FT stomatal opening; when associated with V-269."
FT /evidence="ECO:0000269|PubMed:9368418,
FT ECO:0000269|PubMed:9688573"
FT MUTAGEN 269
FT /note="E->V: Resistance to the cesium inhibition of
FT stomatal opening; when associated with T-267."
FT /evidence="ECO:0000269|PubMed:9368418"
FT CONFLICT 5
FT /note="W -> C (in Ref. 3; CAA63601)"
FT /evidence="ECO:0000305"
FT CONFLICT 330
FT /note="Q -> E (in Ref. 3; CAA63601)"
FT /evidence="ECO:0000305"
FT CONFLICT 573
FT /note="V -> E (in Ref. 3; CAA63601)"
FT /evidence="ECO:0000305"
FT CONFLICT 580
FT /note="T -> S (in Ref. 3; CAA63601)"
FT /evidence="ECO:0000305"
FT CONFLICT 629
FT /note="L -> V (in Ref. 3; CAA63601)"
FT /evidence="ECO:0000305"
FT CONFLICT 664
FT /note="D -> N (in Ref. 3; CAA63601)"
FT /evidence="ECO:0000305"
FT TURN 58..61
FT /evidence="ECO:0007829|PDB:7CAL"
FT HELIX 62..71
FT /evidence="ECO:0007829|PDB:7CAL"
FT TURN 72..75
FT /evidence="ECO:0007829|PDB:7CAL"
FT HELIX 76..82
FT /evidence="ECO:0007829|PDB:7CAL"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:7CAL"
FT HELIX 94..108
FT /evidence="ECO:0007829|PDB:7CAL"
FT TURN 117..119
FT /evidence="ECO:0007829|PDB:7CAL"
FT HELIX 126..136
FT /evidence="ECO:0007829|PDB:7CAL"
FT TURN 139..141
FT /evidence="ECO:0007829|PDB:7CAL"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:7CAL"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:7CAL"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:7CAL"
FT HELIX 162..165
FT /evidence="ECO:0007829|PDB:7CAL"
FT HELIX 167..175
FT /evidence="ECO:0007829|PDB:7CAL"
FT HELIX 176..185
FT /evidence="ECO:0007829|PDB:7CAL"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:6V1X"
FT HELIX 194..213
FT /evidence="ECO:0007829|PDB:7CAL"
FT TURN 215..217
FT /evidence="ECO:0007829|PDB:7CAL"
FT HELIX 218..221
FT /evidence="ECO:0007829|PDB:7CAL"
FT STRAND 224..227
FT /evidence="ECO:0007829|PDB:7CAL"
FT TURN 230..234
FT /evidence="ECO:0007829|PDB:7CAL"
FT HELIX 248..258
FT /evidence="ECO:0007829|PDB:7CAL"
FT STRAND 264..266
FT /evidence="ECO:0007829|PDB:7CAL"
FT HELIX 271..281
FT /evidence="ECO:0007829|PDB:7CAL"
FT HELIX 283..302
FT /evidence="ECO:0007829|PDB:7CAL"
FT HELIX 305..322
FT /evidence="ECO:0007829|PDB:7CAL"
FT HELIX 327..343
FT /evidence="ECO:0007829|PDB:7CAL"
FT STRAND 346..348
FT /evidence="ECO:0007829|PDB:7CAL"
FT TURN 349..353
FT /evidence="ECO:0007829|PDB:7CAL"
FT HELIX 360..366
FT /evidence="ECO:0007829|PDB:7CAL"
FT HELIX 369..372
FT /evidence="ECO:0007829|PDB:7CAL"
FT STRAND 373..375
FT /evidence="ECO:0007829|PDB:7CAL"
FT STRAND 378..380
FT /evidence="ECO:0007829|PDB:7CAL"
FT TURN 383..387
FT /evidence="ECO:0007829|PDB:7CAL"
FT STRAND 403..405
FT /evidence="ECO:0007829|PDB:7CAL"
FT STRAND 415..420
FT /evidence="ECO:0007829|PDB:6V1X"
FT STRAND 422..424
FT /evidence="ECO:0007829|PDB:7CAL"
FT STRAND 427..429
FT /evidence="ECO:0007829|PDB:7CAL"
FT STRAND 432..434
FT /evidence="ECO:0007829|PDB:7CAL"
FT TURN 447..450
FT /evidence="ECO:0007829|PDB:7CAL"
FT STRAND 457..460
FT /evidence="ECO:0007829|PDB:7CAL"
FT STRAND 469..473
FT /evidence="ECO:0007829|PDB:7CAL"
FT STRAND 476..479
FT /evidence="ECO:0007829|PDB:7CAL"
FT HELIX 483..490
FT /evidence="ECO:0007829|PDB:7CAL"
SQ SEQUENCE 677 AA; 78271 MW; 7F9C8285ED702338 CRC64;
MSISWTRNFF ERFCVEEYNI DTIKQSSFLS ADLLPSLGAR INQSTKLRKH IISPFNPRYR
AWEMWLVLLV IYSAWICPFQ FAFITYKKDA IFIIDNIVNG FFAIDIILTF FVAYLDSHSY
LLVDSPKKIA IRYLSTWFAF DVCSTAPFQP LSLLFNYNGS ELGFRILSML RLWRLRRVSS
LFARLEKDIR FNYFWIRCTK LISVTLFAIH CAGCFNYLIA DRYPNPRKTW IGAVYPNFKE
ASLWNRYVTA LYWSITTLTT TGYGDFHAEN PREMLFDIFF MMFNLGLTAY LIGNMTNLVV
HWTSRTRTFR DSVRAASEFA SRNQLPHDIQ DQMLSHICLK FKTEGLKQQE TLNNLPKAIR
SSIANYLFFP IVHNIYLFQG VSRNFLFQLV SDIDAEYFPP KEDIILQNEA PTDLYILVSG
AVDFTVYVDG HDQFQGKAVI GETFGEVGVL YYRPQPFTVR TTELSQILRI SRTSLMSAMH
AHADDGRVIM NNLFMKLRGQ QSIAIDDSNT SGHENRDFKS MGWEEWRDSR KDGYGLDVTN
PTSDTALMDA IHKEDTEMVK KILKEQKIER AKVERSSSET AGRSYANDSS KKDPYCSSSN
QIIKPCKREE KRVTIHMMSE SKNGKLILLP SSIEELLRLA SEKFGGCNFT KITNADNAEI
DDLDVIWDGD HLYFSSN
