CESA8_ARATH
ID CESA8_ARATH Reviewed; 985 AA.
AC Q8LPK5; Q9C5Z8; Q9SN37;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Cellulose synthase A catalytic subunit 8 [UDP-forming];
DE Short=AtCesA8;
DE EC=2.4.1.12;
DE AltName: Full=Protein IRREGULAR XYLEM 1;
DE Short=AtIRX1;
DE AltName: Full=Protein LEAF WILTING 2;
GN Name=CESA8; Synonyms=IRX1, LEW2; OrderedLocusNames=At4g18780;
GN ORFNames=F28A21.190;
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, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, INTERACTION WITH CESA7, AND MUTAGENESIS OF SER-679 AND ASP-683.
RX PubMed=11148295; DOI=10.2307/3871246;
RA Taylor N.G., Laurie S., Turner S.R.;
RT "Multiple cellulose synthase catalytic subunits are required for cellulose
RT synthesis in Arabidopsis.";
RL Plant Cell 12:2529-2539(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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, AND MUTAGENESIS OF SER-679 AND ASP-683.
RX PubMed=9165747; DOI=10.2307/3870425;
RA Turner S.R., Somerville C.R.;
RT "Collapsed xylem phenotype of Arabidopsis identifies mutants deficient in
RT cellulose deposition in the secondary cell wall.";
RL Plant Cell 9:689-701(1997).
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11178255; DOI=10.1186/gb-2000-1-4-reviews3001;
RA Richmond T.;
RT "Higher plant cellulose synthases.";
RL Genome Biol. 1:REVIEWS3001.1-REVIEWS3001.6(2000).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=12481071; DOI=10.1104/pp.102.010603;
RA Beeckman T., Przemeck G.K.H., Stamatiou G., Lau R., Terryn N., De Rycke R.,
RA Inze D., Berleth T.;
RT "Genetic complexity of cellulose synthase A gene function in Arabidopsis
RT embryogenesis.";
RL Plant Physiol. 130:1883-1893(2002).
RN [8]
RP SUBUNIT.
RX PubMed=12897249; DOI=10.1105/tpc.012815;
RA Gardiner J.C., Taylor N.G., Turner S.R.;
RT "Control of cellulose synthase complex localization in developing xylem.";
RL Plant Cell 15:1740-1748(2003).
RN [9]
RP TISSUE SPECIFICITY, AND INTERACTION WITH CESA4 AND CESA7.
RX PubMed=12538856; DOI=10.1073/pnas.0337628100;
RA Taylor N.G., Howells R.M., Huttly A.K., Vickers K., Turner S.R.;
RT "Interactions among three distinct CesA proteins essential for cellulose
RT synthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1450-1455(2003).
RN [10]
RP FUNCTION, AND MUTAGENESIS OF LEU-802.
RX PubMed=15998313; DOI=10.1111/j.1365-313x.2005.02452.x;
RA Chen Z., Hong X., Zhang H., Wang Y., Li X., Zhu J.-K., Gong Z.;
RT "Disruption of the cellulose synthase gene, AtCesA8/IRX1, enhances drought
RT and osmotic stress tolerance in Arabidopsis.";
RL Plant J. 43:273-283(2005).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17351116; DOI=10.1105/tpc.106.048058;
RA Hernandez-Blanco C., Feng D.X., Hu J., Sanchez-Vallet A., Deslandes L.,
RA Llorente F., Berrocal-Lobo M., Keller H., Barlet X., Sanchez-Rodriguez C.,
RA Anderson L.K., Somerville S., Marco Y., Molina A.;
RT "Impairment of cellulose synthases required for Arabidopsis secondary cell
RT wall formation enhances disease resistance.";
RL Plant Cell 19:890-903(2007).
RN [12]
RP INTERACTION WITH STL1 AND STL2, AND LACK OF INTERACTION WITH GOT1.
RX PubMed=27277162; DOI=10.1038/ncomms11656;
RA Zhang Y., Nikolovski N., Sorieul M., Vellosillo T., McFarlane H.E.,
RA Dupree R., Kesten C., Schneider R., Driemeier C., Lathe R., Lampugnani E.,
RA Yu X., Ivakov A., Doblin M.S., Mortimer J.C., Brown S.P., Persson S.,
RA Dupree P.;
RT "Golgi-localized STELLO proteins regulate the assembly and trafficking of
RT cellulose synthase complexes in Arabidopsis.";
RL Nat. Commun. 7:11656-11656(2016).
RN [13]
RP S-ACYLATION.
RX PubMed=27387950; DOI=10.1126/science.aaf4009;
RA Kumar M., Wightman R., Atanassov I., Gupta A., Hurst C.H., Hemsley P.A.,
RA Turner S.;
RT "S-acylation of the cellulose synthase complex is essential for its plasma
RT membrane localization.";
RL Science 353:166-169(2016).
CC -!- FUNCTION: Catalytic subunit of cellulose synthase terminal complexes
CC ('rosettes'), required for beta-1,4-glucan microfibril crystallization,
CC a major mechanism of the cell wall formation. Involved in the secondary
CC cell wall formation. Required for the xylem cell wall thickening.
CC {ECO:0000269|PubMed:11148295, ECO:0000269|PubMed:15998313,
CC ECO:0000269|PubMed:17351116, ECO:0000269|PubMed:9165747}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->4)-
CC beta-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:19929, Rhea:RHEA-
CC COMP:10033, Rhea:RHEA-COMP:10034, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:18246, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.12;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC -!- PATHWAY: Glycan metabolism; plant cellulose biosynthesis.
CC -!- SUBUNIT: Interacts with CESA4 and CESA7. Assembly with CESA4 and CESA7
CC is required for functional complex and localization in secondary cell
CC wall deposition sites. Interacts with STL1 and STL2, but not with GOT1
CC (PubMed:27277162). {ECO:0000269|PubMed:11148295,
CC ECO:0000269|PubMed:12538856, ECO:0000269|PubMed:12897249,
CC ECO:0000269|PubMed:27277162}.
CC -!- INTERACTION:
CC Q8LPK5; Q84JA6: CESA4; NbExp=4; IntAct=EBI-8579199, EBI-8579072;
CC Q8LPK5; Q9SWW6: CESA7; NbExp=7; IntAct=EBI-8579199, EBI-4477361;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Confined to secondary cell wall developing tissues
CC such as xylems and interfascicular regions. Expressed in young plants,
CC stems, flowers and inflorescences, but not in leaves.
CC {ECO:0000269|PubMed:11148295, ECO:0000269|PubMed:12481071,
CC ECO:0000269|PubMed:12538856}.
CC -!- DEVELOPMENTAL STAGE: Not found in embryos. Increasing amount as stems
CC mature. {ECO:0000269|PubMed:11148295}.
CC -!- PTM: S-acylated. {ECO:0000269|PubMed:27387950}.
CC -!- DISRUPTION PHENOTYPE: Enhanced resistance to the pathogens Ralstonia
CC solanacearum and Plectosphaerella cucumerina.
CC {ECO:0000269|PubMed:17351116}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. Plant
CC cellulose synthase subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB37463.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78880.1; 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; AF267742; AAK08700.1; -; mRNA.
DR EMBL; AL035526; CAB37463.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161549; CAB78880.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84089.1; -; Genomic_DNA.
DR EMBL; AY099636; AAM20487.1; -; mRNA.
DR PIR; T04870; T04870.
DR RefSeq; NP_567564.1; NM_117994.4.
DR AlphaFoldDB; Q8LPK5; -.
DR SMR; Q8LPK5; -.
DR BioGRID; 12905; 17.
DR IntAct; Q8LPK5; 11.
DR MINT; Q8LPK5; -.
DR STRING; 3702.AT4G18780.1; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR TCDB; 4.D.3.1.7; the glycan glucosyl transferase (opgh) family.
DR SwissPalm; Q8LPK5; -.
DR PaxDb; Q8LPK5; -.
DR PRIDE; Q8LPK5; -.
DR ProteomicsDB; 224475; -.
DR EnsemblPlants; AT4G18780.1; AT4G18780.1; AT4G18780.
DR GeneID; 827612; -.
DR Gramene; AT4G18780.1; AT4G18780.1; AT4G18780.
DR KEGG; ath:AT4G18780; -.
DR Araport; AT4G18780; -.
DR TAIR; locus:2124167; AT4G18780.
DR eggNOG; ENOG502QTVZ; Eukaryota.
DR HOGENOM; CLU_001418_0_2_1; -.
DR InParanoid; Q8LPK5; -.
DR OMA; RITPYRI; -.
DR OrthoDB; 679241at2759; -.
DR PhylomeDB; Q8LPK5; -.
DR BioCyc; MetaCyc:MON-2366; -.
DR BRENDA; 2.4.1.12; 399.
DR UniPathway; UPA00695; -.
DR PRO; PR:Q8LPK5; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8LPK5; baseline and differential.
DR Genevisible; Q8LPK5; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0016760; F:cellulose synthase (UDP-forming) activity; IMP:CACAO.
DR GO; GO:0016759; F:cellulose synthase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0030244; P:cellulose biosynthetic process; 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:0009833; P:plant-type primary cell wall biogenesis; IBA:GO_Central.
DR GO; GO:0009834; P:plant-type secondary cell wall biogenesis; IMP:TAIR.
DR GO; GO:0006970; P:response to osmotic stress; IMP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IMP:TAIR.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR005150; Cellulose_synth.
DR InterPro; IPR027934; CES_Znf_RING.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF03552; Cellulose_synt; 1.
DR Pfam; PF14569; zf-UDP; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell wall biogenesis/degradation; Cellulose biosynthesis;
KW Coiled coil; Glycoprotein; Glycosyltransferase; Lipoprotein; Membrane;
KW Metal-binding; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix; Zinc; Zinc-finger.
FT CHAIN 1..985
FT /note="Cellulose synthase A catalytic subunit 8 [UDP-
FT forming]"
FT /id="PRO_0000166374"
FT TOPO_DOM 1..179
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 201..208
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 230..767
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 768..788
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 789..793
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 794..814
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 815..829
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 830..850
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 851..879
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 880..900
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 901..911
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 912..932
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 933..941
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 942..962
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 963..985
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ZN_FING 9..55
FT /note="RING-type; degenerate"
FT REGION 69..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 358..385
FT /evidence="ECO:0000255"
FT COMPBIAS 144..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 304
FT /evidence="ECO:0000255"
FT ACT_SITE 683
FT /evidence="ECO:0000255"
FT BINDING 9
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 12
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 28
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 31
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 36
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 39
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 51
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 54
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 470
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 472
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT CARBOHYD 857
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 679
FT /note="S->L: In irx1-2; reduced levels of crystalline
FT cellulose in secondary cell wall."
FT /evidence="ECO:0000269|PubMed:11148295,
FT ECO:0000269|PubMed:9165747"
FT MUTAGEN 683
FT /note="D->N: In irx1-1; reduced levels of crystalline
FT cellulose in secondary cell wall."
FT /evidence="ECO:0000269|PubMed:11148295,
FT ECO:0000269|PubMed:9165747"
FT MUTAGEN 802
FT /note="L->F: In lew2-2; enhanced tolerance to drought, salt
FT and osmotic stresses. Higher accumulation of abscisic acid
FT (ABA), proline and soluble sugars."
FT /evidence="ECO:0000269|PubMed:15998313"
FT CONFLICT 18
FT /note="V -> A (in Ref. 1; AAK08700)"
FT /evidence="ECO:0000305"
FT CONFLICT 144..145
FT /note="HE -> QD (in Ref. 1; AAK08700)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="I -> V (in Ref. 1; AAK08700)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="T -> M (in Ref. 1; AAK08700)"
FT /evidence="ECO:0000305"
FT CONFLICT 583
FT /note="S -> A (in Ref. 1; AAK08700)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 985 AA; 111521 MW; D299F357625768E0 CRC64;
MMESRSPICN TCGEEIGVKS NGEFFVACHE CSFPICKACL EYEFKEGRRI CLRCGNPYDE
NVFDDVETKT SKTQSIVPTQ TNNTSQDSGI HARHISTVST IDSELNDEYG NPIWKNRVES
WKDKKDKKSK KKKKDPKATK AEQHEAQIPT QQHMEDTPPN TESGATDVLS VVIPIPRTKI
TSYRIVIIMR LIILALFFNY RITHPVDSAY GLWLTSVICE IWFAVSWVLD QFPKWSPINR
ETYIDRLSAR FEREGEQSQL AAVDFFVSTV DPLKEPPLIT ANTVLSILAL DYPVDKVSCY
VSDDGAAMLS FESLVETADF ARKWVPFCKK YSIEPRAPEF YFSLKIDYLR DKVQPSFVKE
RRAMKRDYEE FKIRMNALVA KAQKTPEEGW TMQDGTSWPG NNTRDHPGMI QVFLGYSGAR
DIEGNELPRL VYVSREKRPG YQHHKKAGAE NALVRVSAVL TNAPFILNLD CDHYVNNSKA
VREAMCFLMD PVVGQDVCFV QFPQRFDGID KSDRYANRNI VFFDVNMRGL DGIQGPVYVG
TGTVFRRQAL YGYSPPSKPR ILPQSSSSSC CCLTKKKQPQ DPSEIYKDAK REELDAAIFN
LGDLDNYDEY DRSMLISQTS FEKTFGLSTV FIESTLMENG GVPDSVNPST LIKEAIHVIS
CGYEEKTEWG KEIGWIYGSI TEDILTGFKM HCRGWRSIYC MPLRPAFKGS APINLSDRLH
QVLRWALGSV EIFLSRHCPL WYGCSGGRLK LLQRLAYINT IVYPFTSLPL VAYCTLPAIC
LLTGKFIIPT LSNLASMLFL GLFISIILTS VLELRWSGVS IEDLWRNEQF WVIGGVSAHL
FAVFQGFLKM LAGLDTNFTV TSKTADDLEF GELYIVKWTT LLIPPTSLLI INLVGVVAGF
SDALNKGYEA WGPLFGKVFF AFWVILHLYP FLKGLMGRQN RTPTIVILWS ILLASVFSLV
WVRINPFVSK TDTTSLSLNC LLIDC
