U89C1_ARATH
ID U89C1_ARATH Reviewed; 435 AA.
AC Q9LNE6; Q0WWJ0; Q8LGD9;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Flavonol 7-O-rhamnosyltransferase {ECO:0000305};
DE EC=2.4.1.- {ECO:0000269|PubMed:17314094, ECO:0000269|PubMed:23549747, ECO:0000269|PubMed:30893500};
DE AltName: Full=UDP-glycosyltransferase 89C1 {ECO:0000305};
DE AltName: Full=UDP-rhamnose: flavonol 7-O-rhamnosyltransferase {ECO:0000305};
GN Name=UGT89C1 {ECO:0000303|PubMed:17314094};
GN OrderedLocusNames=At1g06000 {ECO:0000312|Araport:AT1G06000};
GN ORFNames=T21E18.5 {ECO:0000312|EMBL:AAF80123.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP GENE FAMILY.
RX PubMed=11042215; DOI=10.1074/jbc.m007447200;
RA Li Y., Baldauf S., Lim E.K., Bowles D.J.;
RT "Phylogenetic analysis of the UDP-glycosyltransferase multigene family of
RT Arabidopsis thaliana.";
RL J. Biol. Chem. 276:4338-4343(2001).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=17314094; DOI=10.1074/jbc.m611498200;
RA Yonekura-Sakakibara K., Tohge T., Niida R., Saito K.;
RT "Identification of a flavonol 7-O-rhamnosyltransferase gene determining
RT flavonoid pattern in Arabidopsis by transcriptome coexpression analysis and
RT reverse genetics.";
RL J. Biol. Chem. 282:14932-14941(2007).
RN [8]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=23549747; DOI=10.1007/s00253-013-4844-7;
RA Kim H.J., Kim B.G., Ahn J.H.;
RT "Regioselective synthesis of flavonoid bisglycosides using Escherichia coli
RT harboring two glycosyltransferases.";
RL Appl. Microbiol. Biotechnol. 97:5275-5282(2013).
RN [9]
RP REVIEW, AND NOMENCLATURE.
RX PubMed=23473981; DOI=10.1016/j.plaphy.2013.02.001;
RA Saito K., Yonekura-Sakakibara K., Nakabayashi R., Higashi Y., Yamazaki M.,
RA Tohge T., Fernie A.R.;
RT "The flavonoid biosynthetic pathway in Arabidopsis: Structural and genetic
RT diversity.";
RL Plant Physiol. Biochem. 72:21-34(2013).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24251900; DOI=10.1111/nph.12558;
RA Yin R., Han K., Heller W., Albert A., Dobrev P.I., Zazimalova E.,
RA Schaeffner A.R.;
RT "Kaempferol 3-O-rhamnoside-7-O-rhamnoside is an endogenous flavonol
RT inhibitor of polar auxin transport in Arabidopsis shoots.";
RL New Phytol. 201:466-475(2014).
RN [11]
RP FUNCTION.
RX PubMed=26513760; DOI=10.1016/j.carres.2015.09.010;
RA Parajuli P., Pandey R.P., Trang N.T.H., Oh T.J., Sohng J.K.;
RT "Expanded acceptor substrates flexibility study of flavonol 7-O-
RT rhamnosyltransferase, AtUGT89C1 from Arabidopsis thaliana.";
RL Carbohydr. Res. 418:13-19(2015).
RN [12]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=26742840; DOI=10.1074/jbc.m115.701565;
RA Kuhn B.M., Errafi S., Bucher R., Dobrev P., Geisler M., Bigler L.,
RA Zazimalova E., Ringli C.;
RT "7-Rhamnosylated flavonols modulate homeostasis of the plant hormone auxin
RT and affect plant development.";
RL J. Biol. Chem. 291:5385-5395(2016).
RN [13]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF GLN-18; HIS-21; LEU-88; SER-124; PRO-147; ILE-148; SER-163;
RP TRP-335; GLY-336; GLN-354; ASP-356 AND HIS-357.
RX PubMed=30893500; DOI=10.1111/tpj.14321;
RA Zong G., Fei S., Liu X., Li J., Gao Y., Yang X., Wang X., Shen Y.;
RT "Crystal structures of rhamnosyltransferase UGT89C1 from Arabidopsis
RT thaliana reveal the molecular basis of sugar donor specificity for UDP-
RT beta-l-rhamnose and rhamnosylation mechanism.";
RL Plant J. 99:257-269(2019).
CC -!- FUNCTION: Flavonol 7-O-rhamnosyltransferase that catalyzes the transfer
CC of rhamnose from UDP-rhamnose to the 7-OH position of 3-O-glycosylated
CC flavonols, such as kaempferol 3-O-rhamnoside, kaempferol 3-O-glucoside,
CC quercetin 3-O-glucoside, quercetin 3-O-galactoside, quercetin 3-O-
CC rhamnoside and isorhamnetin 3-O-glucoside (PubMed:17314094,
CC PubMed:23549747, PubMed:24251900, PubMed:30893500). Is able to
CC glycosylate the flavonols quercetin and kaempferol to yield quercetin
CC 7-O-rhamnoside and kaempferol 7-O-rhamnoside (PubMed:17314094,
CC PubMed:26513760, PubMed:30893500). Shows a strict specificity for UDP-
CC rhamnose as sugar donor (PubMed:17314094, PubMed:30893500). Does not
CC act on 3-O-glycosylated anthocyanins (PubMed:17314094). The
CC accumulation of kaempferol 3-O-rhamnoside-7-O-rhamnoside inhibits
CC basipetal auxin transport, which influences auxin distribution and
CC plant organ development (PubMed:24251900, PubMed:26742840).
CC {ECO:0000269|PubMed:17314094, ECO:0000269|PubMed:23549747,
CC ECO:0000269|PubMed:24251900, ECO:0000269|PubMed:26513760,
CC ECO:0000269|PubMed:26742840, ECO:0000269|PubMed:30893500}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=quercitrin + UDP-beta-L-rhamnose = H(+) + quercetin 3,7-bis-O-
CC alpha-L-rhamnoside + UDP; Xref=Rhea:RHEA:61184, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58192, ChEBI:CHEBI:58223, ChEBI:CHEBI:83836,
CC ChEBI:CHEBI:144435; Evidence={ECO:0000269|PubMed:17314094,
CC ECO:0000269|PubMed:23549747, ECO:0000269|PubMed:30893500};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61185;
CC Evidence={ECO:0000269|PubMed:17314094, ECO:0000269|PubMed:23549747,
CC ECO:0000269|PubMed:30893500};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=quercetin 3-O-beta-D-glucoside + UDP-beta-L-rhamnose = H(+) +
CC quercetin 3-O-beta-D-glucoside-7-O-alpha-L-rhamnoside + UDP;
CC Xref=Rhea:RHEA:61188, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:83836, ChEBI:CHEBI:144436, ChEBI:CHEBI:144437;
CC Evidence={ECO:0000269|PubMed:17314094, ECO:0000269|PubMed:23549747,
CC ECO:0000269|PubMed:30893500};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61189;
CC Evidence={ECO:0000269|PubMed:17314094, ECO:0000269|PubMed:23549747,
CC ECO:0000269|PubMed:30893500};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.4 uM for quercetin {ECO:0000269|PubMed:30893500};
CC KM=14.1 uM for kaempferol {ECO:0000269|PubMed:30893500};
CC KM=546.9 uM for UDP-rhamnose {ECO:0000269|PubMed:30893500};
CC -!- PATHWAY: Flavonoid metabolism. {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in floral buds (PubMed:17314094).
CC Expressed in stems, leaves and flowers (PubMed:17314094). Expressed at
CC low levels in roots and siliques (PubMed:17314094). Expressed on the
CC adaxial side of cotyledons and emerging leaves, in trichomes, root
CC columella cells, and the late elongation/early differentiation zone of
CC roots (PubMed:26742840). {ECO:0000269|PubMed:17314094,
CC ECO:0000269|PubMed:26742840}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants do not accumulate 7-O-rhamnosylated
CC flavonols (PubMed:17314094, PubMed:24251900, PubMed:26742840).
CC Increased concentrations of auxin precursors and auxin metabolites
CC (PubMed:26742840). {ECO:0000269|PubMed:17314094,
CC ECO:0000269|PubMed:24251900, ECO:0000269|PubMed:26742840}.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AC024174; AAF80123.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27928.1; -; Genomic_DNA.
DR EMBL; AY093133; AAM13132.1; -; mRNA.
DR EMBL; BT006579; AAP31923.1; -; mRNA.
DR EMBL; AK226360; BAE98508.1; -; mRNA.
DR EMBL; AY084325; AAM60911.1; -; mRNA.
DR PIR; A86195; A86195.
DR RefSeq; NP_563756.1; NM_100480.3.
DR PDB; 6IJ7; X-ray; 2.70 A; A/B=1-435.
DR PDB; 6IJ9; X-ray; 3.00 A; A/B/C/D=1-435.
DR PDB; 6IJA; X-ray; 3.21 A; A/B/C/D=1-435.
DR PDB; 6IJD; X-ray; 3.21 A; A/B=1-435.
DR PDBsum; 6IJ7; -.
DR PDBsum; 6IJ9; -.
DR PDBsum; 6IJA; -.
DR PDBsum; 6IJD; -.
DR AlphaFoldDB; Q9LNE6; -.
DR SMR; Q9LNE6; -.
DR BioGRID; 22351; 1.
DR STRING; 3702.AT1G06000.1; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR PaxDb; Q9LNE6; -.
DR PRIDE; Q9LNE6; -.
DR ProteomicsDB; 242594; -.
DR DNASU; 837109; -.
DR EnsemblPlants; AT1G06000.1; AT1G06000.1; AT1G06000.
DR GeneID; 837109; -.
DR Gramene; AT1G06000.1; AT1G06000.1; AT1G06000.
DR KEGG; ath:AT1G06000; -.
DR Araport; AT1G06000; -.
DR TAIR; locus:2198791; AT1G06000.
DR eggNOG; KOG1192; Eukaryota.
DR HOGENOM; CLU_001724_2_2_1; -.
DR InParanoid; Q9LNE6; -.
DR OMA; FFCCWAN; -.
DR OrthoDB; 508327at2759; -.
DR PhylomeDB; Q9LNE6; -.
DR BioCyc; ARA:AT1G06000-MON; -.
DR BioCyc; MetaCyc:MON-17875; -.
DR BRENDA; 2.4.1.81; 399.
DR PRO; PR:Q9LNE6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LNE6; differential.
DR Genevisible; Q9LNE6; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR GO; GO:0103077; F:quercetin 3-glucoside 7-O-rhamnosyltransferase activity; IEA:RHEA.
DR GO; GO:0103078; F:quercetin 3-rhamnoside 7-O-rhamnosyltransferase activity; IEA:RHEA.
DR GO; GO:0008194; F:UDP-glycosyltransferase activity; IDA:TAIR.
DR GO; GO:0051555; P:flavonol biosynthetic process; IDA:TAIR.
DR CDD; cd03784; GT1_Gtf-like; 1.
DR InterPro; IPR002213; UDP_glucos_trans.
DR Pfam; PF00201; UDPGT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glycosyltransferase; Reference proteome; Transferase.
FT CHAIN 1..435
FT /note="Flavonol 7-O-rhamnosyltransferase"
FT /id="PRO_0000409138"
FT BINDING 18
FT /ligand="UDP-beta-L-rhamnose"
FT /ligand_id="ChEBI:CHEBI:83836"
FT /evidence="ECO:0000269|PubMed:30893500"
FT BINDING 21
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:30893500"
FT BINDING 147..148
FT /ligand="UDP-beta-L-rhamnose"
FT /ligand_id="ChEBI:CHEBI:83836"
FT /evidence="ECO:0000269|PubMed:30893500"
FT BINDING 250
FT /ligand="UDP-beta-L-rhamnose"
FT /ligand_id="ChEBI:CHEBI:83836"
FT /evidence="ECO:0000269|PubMed:30893500"
FT BINDING 314..317
FT /ligand="UDP-beta-L-rhamnose"
FT /ligand_id="ChEBI:CHEBI:83836"
FT /evidence="ECO:0000269|PubMed:30893500"
FT BINDING 332..340
FT /ligand="UDP-beta-L-rhamnose"
FT /ligand_id="ChEBI:CHEBI:83836"
FT /evidence="ECO:0000269|PubMed:30893500"
FT BINDING 356..357
FT /ligand="UDP-beta-L-rhamnose"
FT /ligand_id="ChEBI:CHEBI:83836"
FT /evidence="ECO:0000269|PubMed:30893500"
FT MUTAGEN 18
FT /note="Q->G: Slight decrease in catalytic activity."
FT /evidence="ECO:0000269|PubMed:30893500"
FT MUTAGEN 21
FT /note="H->A: Almost complete loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:30893500"
FT MUTAGEN 21
FT /note="H->N: Reduces catalytic activity 5.4-fold."
FT /evidence="ECO:0000269|PubMed:30893500"
FT MUTAGEN 88
FT /note="L->A,G,S: Reduces catalytic activity 1.6-fold."
FT /evidence="ECO:0000269|PubMed:30893500"
FT MUTAGEN 124
FT /note="S->A: No effect on catalytic activity."
FT /evidence="ECO:0000269|PubMed:30893500"
FT MUTAGEN 124
FT /note="S->D: Slight decrease in catalytic activity."
FT /evidence="ECO:0000269|PubMed:30893500"
FT MUTAGEN 147
FT /note="P->A: Slight decrease in catalytic activity."
FT /evidence="ECO:0000269|PubMed:30893500"
FT MUTAGEN 147
FT /note="P->T: Complete loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:30893500"
FT MUTAGEN 148
FT /note="I->A,S: Reduces catalytic activity 4.3-fold."
FT MUTAGEN 163
FT /note="S->A: Slight decrease in catalytic activity."
FT /evidence="ECO:0000269|PubMed:30893500"
FT MUTAGEN 335
FT /note="W->A: Reduces catalytic activity 6.5-fold."
FT /evidence="ECO:0000269|PubMed:30893500"
FT MUTAGEN 336
FT /note="G->N: Slight decrease in catalytic activity."
FT /evidence="ECO:0000269|PubMed:30893500"
FT MUTAGEN 354
FT /note="Q->A: Reduces catalytic activity 2.2-fold."
FT MUTAGEN 356
FT /note="D->A: Complete loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:30893500"
FT MUTAGEN 357
FT /note="H->A,Q: No effect on catalytic activity."
FT /evidence="ECO:0000269|PubMed:30893500"
FT CONFLICT 97
FT /note="A -> D (in Ref. 4; BAE98508)"
FT /evidence="ECO:0000305"
FT CONFLICT 270
FT /note="S -> G (in Ref. 5; AAM60911)"
FT /evidence="ECO:0000305"
FT STRAND 10..14
FT /evidence="ECO:0007829|PDB:6IJ7"
FT HELIX 19..34
FT /evidence="ECO:0007829|PDB:6IJ7"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:6IJ7"
FT HELIX 45..51
FT /evidence="ECO:0007829|PDB:6IJ7"
FT HELIX 52..57
FT /evidence="ECO:0007829|PDB:6IJ7"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:6IJ7"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:6IJ7"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:6IJ7"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:6IJ7"
FT HELIX 91..99
FT /evidence="ECO:0007829|PDB:6IJ7"
FT HELIX 102..111
FT /evidence="ECO:0007829|PDB:6IJ7"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:6IJ7"
FT STRAND 119..124
FT /evidence="ECO:0007829|PDB:6IJ7"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:6IJ7"
FT HELIX 128..138
FT /evidence="ECO:0007829|PDB:6IJ7"
FT STRAND 141..148
FT /evidence="ECO:0007829|PDB:6IJ7"
FT HELIX 150..157
FT /evidence="ECO:0007829|PDB:6IJ7"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:6IJ7"
FT HELIX 166..174
FT /evidence="ECO:0007829|PDB:6IJ7"
FT STRAND 175..182
FT /evidence="ECO:0007829|PDB:6IJ7"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:6IJ7"
FT HELIX 188..197
FT /evidence="ECO:0007829|PDB:6IJ7"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:6IJ7"
FT HELIX 227..236
FT /evidence="ECO:0007829|PDB:6IJ7"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:6IJ7"
FT STRAND 243..247
FT /evidence="ECO:0007829|PDB:6IJ7"
FT TURN 249..251
FT /evidence="ECO:0007829|PDB:6IJ9"
FT HELIX 256..269
FT /evidence="ECO:0007829|PDB:6IJ7"
FT STRAND 272..277
FT /evidence="ECO:0007829|PDB:6IJ7"
FT TURN 301..304
FT /evidence="ECO:0007829|PDB:6IJ7"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:6IJA"
FT STRAND 308..313
FT /evidence="ECO:0007829|PDB:6IJ7"
FT HELIX 317..321
FT /evidence="ECO:0007829|PDB:6IJ7"
FT STRAND 326..331
FT /evidence="ECO:0007829|PDB:6IJ7"
FT HELIX 335..344
FT /evidence="ECO:0007829|PDB:6IJ7"
FT STRAND 347..350
FT /evidence="ECO:0007829|PDB:6IJ7"
FT HELIX 355..364
FT /evidence="ECO:0007829|PDB:6IJ7"
FT TURN 365..368
FT /evidence="ECO:0007829|PDB:6IJ7"
FT STRAND 371..373
FT /evidence="ECO:0007829|PDB:6IJ7"
FT HELIX 384..392
FT /evidence="ECO:0007829|PDB:6IJ7"
FT TURN 393..395
FT /evidence="ECO:0007829|PDB:6IJ7"
FT HELIX 400..416
FT /evidence="ECO:0007829|PDB:6IJ7"
FT STRAND 417..420
FT /evidence="ECO:0007829|PDB:6IJ9"
FT HELIX 421..433
FT /evidence="ECO:0007829|PDB:6IJ7"
SQ SEQUENCE 435 AA; 48122 MW; 52718C8CDD0F448C CRC64;
MTTTTTKKPH VLVIPFPQSG HMVPHLDLTH QILLRGATVT VLVTPKNSSY LDALRSLHSP
EHFKTLILPF PSHPCIPSGV ESLQQLPLEA IVHMFDALSR LHDPLVDFLS RQPPSDLPDA
ILGSSFLSPW INKVADAFSI KSISFLPINA HSISVMWAQE DRSFFNDLET ATTESYGLVI
NSFYDLEPEF VETVKTRFLN HHRIWTVGPL LPFKAGVDRG GQSSIPPAKV SAWLDSCPED
NSVVYVGFGS QIRLTAEQTA ALAAALEKSS VRFIWAVRDA AKKVNSSDNS VEEDVIPAGF
EERVKEKGLV IRGWAPQTMI LEHRAVGSYL THLGWGSVLE GMVGGVMLLA WPMQADHFFN
TTLIVDKLRA AVRVGENRDS VPDSDKLARI LAESAREDLP ERVTLMKLRE KAMEAIKEGG
SSYKNLDELV AEMCL
