CESA3_ARATH
ID CESA3_ARATH Reviewed; 1065 AA.
AC Q941L0; O48948; Q0WLU1; Q9FHK6;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Cellulose synthase A catalytic subunit 3 [UDP-forming];
DE Short=AtCesA3;
DE EC=2.4.1.12;
DE AltName: Full=Constitutive expression of VSP1 protein 1;
DE AltName: Full=Isoxaben-resistant protein 1;
DE Short=Ath-B;
DE AltName: Full=Protein ECTOPIC LIGNIN 1;
DE AltName: Full=Protein RADIALLY SWOLLEN 5;
DE Short=AtRSW5;
GN Name=CESA3; Synonyms=ATHB, CEV1, ELI1, IXR1, RSW5;
GN OrderedLocusNames=At5g05170; ORFNames=K2A11.4;
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. Columbia;
RX PubMed=9445479; DOI=10.1126/science.279.5351.717;
RA Arioli T., Peng L., Betzner A.S., Burn J., Wittke W., Herth W.,
RA Camilleri C., Hoefte H., Plazinski J., Birch R., Cork A., Glover J.,
RA Redmond J., Williamson R.E.;
RT "Molecular analysis of cellulose biosynthesis in Arabidopsis.";
RL Science 279:717-720(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10470850; DOI=10.1093/dnares/6.3.183;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT clones.";
RL DNA Res. 6:183-195(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 635-1065.
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 [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 FUNCTION, MUTAGENESIS OF GLY-617, AND DISRUPTION PHENOTYPE.
RX PubMed=11340179; DOI=10.2307/3871361;
RA Ellis C., Turner J.G.;
RT "The Arabidopsis mutant cev1 has constitutively active jasmonate and
RT ethylene signal pathways and enhanced resistance to pathogens.";
RL Plant Cell 13:1025-1033(2001).
RN [8]
RP TISSUE SPECIFICITY, AND MUTAGENESIS OF THR-942 AND GLY-998.
RX PubMed=11517344; DOI=10.1073/pnas.191361598;
RA Scheible W.-R., Eshed R., Richmond T., Delmer D., Somerville C.;
RT "Modifications of cellulose synthase confer resistance to isoxaben and
RT thiazolidinone herbicides in Arabidopsis Ixr1 mutants.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:10079-10084(2001).
RN [9]
RP MUTAGENESIS OF GLY-617.
RX PubMed=12437300; DOI=10.1094/mpmi.2002.15.10.1025;
RA Ellis C., Karafyllidis I., Turner J.G.;
RT "Constitutive activation of jasmonate signaling in an Arabidopsis mutant
RT correlates with enhanced resistance to Erysiphe cichoracearum, Pseudomonas
RT syringae, and Myzus persicae.";
RL Mol. Plant Microbe Interact. 15:1025-1030(2002).
RN [10]
RP FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF GLY-617.
RX PubMed=12119374; DOI=10.1105/tpc.002022;
RA Ellis C., Karafyllidis I., Wasternack C., Turner J.G.;
RT "The Arabidopsis mutant cev1 links cell wall signaling to jasmonate and
RT ethylene responses.";
RL Plant Cell 14:1557-1566(2002).
RN [11]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12068120; DOI=10.1104/pp.010931;
RA Burn J.E., Hocart C.H., Birch R.J., Cork A.C., Williamson R.E.;
RT "Functional analysis of the cellulose synthase genes CesA1, CesA2, and
RT CesA3 in Arabidopsis.";
RL Plant Physiol. 129:797-807(2002).
RN [12]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. La-0;
RX PubMed=14506206; DOI=10.1074/mcp.t300006-mcp200;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Large-scale analysis of in vivo phosphorylated membrane proteins by
RT immobilized metal ion affinity chromatography and mass spectrometry.";
RL Mol. Cell. Proteomics 2:1234-1243(2003).
RN [14]
RP FUNCTION, AND MUTAGENESIS OF SER-301.
RX PubMed=12713541; DOI=10.1046/j.1365-313x.2003.01729.x;
RA Cano-Delgado A., Penfield S., Smith C., Catley M., Bevan M.;
RT "Reduced cellulose synthesis invokes lignification and defense responses in
RT Arabidopsis thaliana.";
RL Plant J. 34:351-362(2003).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; SER-151 AND SER-216, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15308754; DOI=10.1105/tpc.104.023150;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Phosphoproteomics of the Arabidopsis plasma membrane and a new
RT phosphorylation site database.";
RL Plant Cell 16:2394-2405(2004).
RN [16]
RP MUTAGENESIS OF PRO-1056.
RX PubMed=16891551; DOI=10.1104/pp.106.084004;
RA Wang J., Howles P.A., Cork A.H., Birch R.J., Williamson R.E.;
RT "Chimeric proteins suggest that the catalytic and/or C-terminal domains
RT give CesA1 and CesA3 access to their specific sites in the cellulose
RT synthase of primary walls.";
RL Plant Physiol. 142:685-695(2006).
RN [17]
RP PHOSPHORYLATION AT SER-3; SER-151; SER-211 AND SER-216, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RX PubMed=17427041; DOI=10.1007/s11103-007-9142-2;
RA Taylor N.G.;
RT "Identification of cellulose synthase AtCesA7 (IRX3) in vivo
RT phosphorylation sites -- a potential role in regulating protein
RT degradation.";
RL Plant Mol. Biol. 64:161-171(2007).
RN [18]
RP FUNCTION, AND SUBUNIT.
RX PubMed=17878302; DOI=10.1073/pnas.0706592104;
RA Persson S., Paredez A., Carroll A., Palsdottir H., Doblin M.,
RA Poindexter P., Khitrov N., Auer M., Somerville C.R.;
RT "Genetic evidence for three unique components in primary cell-wall
RT cellulose synthase complexes in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:15566-15571(2007).
RN [19]
RP FUNCTION, AND INTERACTION WITH CESA1 AND CESA6.
RX PubMed=17878303; DOI=10.1073/pnas.0706569104;
RA Desprez T., Juraniec M., Crowell E.F., Jouy H., Pochylova Z., Parcy F.,
RA Hoefte H., Gonneau M., Vernhettes S.;
RT "Organization of cellulose synthase complexes involved in primary cell wall
RT synthesis in Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:15572-15577(2007).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151 AND SER-216, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [21]
RP INTERACTION WITH CSI1.
RC STRAIN=cv. Columbia;
RX PubMed=20616083; DOI=10.1073/pnas.1007092107;
RA Gu Y., Kaplinsky N., Bringmann M., Cobb A., Carroll A., Sampathkumar A.,
RA Baskin T.I., Persson S., Somerville C.R.;
RT "Identification of a cellulose synthase-associated protein required for
RT cellulose biosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:12866-12871(2010).
RN [22]
RP INTERACTION WITH CSI1 AND CSI3.
RX PubMed=24368796; DOI=10.1105/tpc.113.116715;
RA Lei L., Li S., Du J., Bashline L., Gu Y.;
RT "Cellulose synthase INTERACTIVE3 regulates cellulose biosynthesis in both a
RT microtubule-dependent and microtubule-independent manner in Arabidopsis.";
RL Plant Cell 25:4912-4923(2013).
RN [23]
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).
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 primary
CC cell wall formation, especially in roots. {ECO:0000269|PubMed:11340179,
CC ECO:0000269|PubMed:12068120, ECO:0000269|PubMed:12119374,
CC ECO:0000269|PubMed:12713541, ECO:0000269|PubMed:17878302,
CC ECO:0000269|PubMed:17878303}.
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 CESA1 and CESA6. Interacts with STL1 and STL2,
CC but not with GOT1 (PubMed:27277162). Binds to CSI1 and CSI3
CC (PubMed:20616083, PubMed:24368796). {ECO:0000269|PubMed:17878302,
CC ECO:0000269|PubMed:17878303, ECO:0000269|PubMed:20616083,
CC ECO:0000269|PubMed:24368796, ECO:0000269|PubMed:27277162}.
CC -!- INTERACTION:
CC Q941L0; Q94JQ6: CESA6; NbExp=2; IntAct=EBI-4448240, EBI-15659159;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in young plants, flowers and roots, and
CC to a lower extent in leaves and stems. Localized in all cells except
CC meristematic cells. Accumulates particularly in root caps, root hairs,
CC epidermal layer, midveins of leaves and anthers. Not present in old
CC tissues. {ECO:0000269|PubMed:11517344, ECO:0000269|PubMed:12068120,
CC ECO:0000269|PubMed:12119374, ECO:0000269|PubMed:12481071}.
CC -!- DEVELOPMENTAL STAGE: Mostly expressed in cotyledons during all steps of
CC embryogenesis, and decrease toward the bent-cotyledon stage.
CC {ECO:0000269|PubMed:12481071}.
CC -!- DISRUPTION PHENOTYPE: Mutants cev1 are dark green and contains more
CC jasmonates and ethylene, that leads to shorter and thickened hypocotyls
CC and roots, with prolific root hairs, and the accumulation of purple
CC anthocyanins. They exhibit constitutive and high expression in leaves
CC lamina of vegetative storage proteins (VSP1 and VSP2), basic chitinase
CC CHI-B and plant defensin PDF1.2. In addition, this mutation confers
CC resistance to powdery mildew pathogens such as E.cichoracearum,
CC E.orontii and O.lycopersicum, to the bacterial pathogen P.syringae pv
CC maculicola, and also to the green peach aphid M.persicae.
CC {ECO:0000269|PubMed:11340179}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. Plant
CC cellulose synthase subfamily. {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; AF027174; AAC39336.1; -; mRNA.
DR EMBL; AB018111; BAB09693.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90836.1; -; Genomic_DNA.
DR EMBL; AY045960; AAK76634.2; -; mRNA.
DR EMBL; BT002335; AAN86168.1; -; mRNA.
DR EMBL; AK230097; BAF01916.1; -; mRNA.
DR PIR; T52054; T52054.
DR RefSeq; NP_196136.1; NM_120599.4.
DR PDB; 7CK1; X-ray; 2.35 A; A/B=317-630, A/B=702-792.
DR PDB; 7CK2; X-ray; 2.05 A; A/B=317-630, A/B=702-792.
DR PDB; 7CK3; X-ray; 2.90 A; A/B=317-630, A/B=702-811.
DR PDBsum; 7CK1; -.
DR PDBsum; 7CK2; -.
DR PDBsum; 7CK3; -.
DR AlphaFoldDB; Q941L0; -.
DR SMR; Q941L0; -.
DR BioGRID; 15678; 48.
DR DIP; DIP-46437N; -.
DR IntAct; Q941L0; 38.
DR STRING; 3702.AT5G05170.1; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR TCDB; 4.D.3.1.4; the glycan glucosyl transferase (opgh) family.
DR iPTMnet; Q941L0; -.
DR SwissPalm; Q941L0; -.
DR PaxDb; Q941L0; -.
DR PRIDE; Q941L0; -.
DR ProteomicsDB; 220387; -.
DR EnsemblPlants; AT5G05170.1; AT5G05170.1; AT5G05170.
DR GeneID; 830399; -.
DR Gramene; AT5G05170.1; AT5G05170.1; AT5G05170.
DR KEGG; ath:AT5G05170; -.
DR Araport; AT5G05170; -.
DR TAIR; locus:2156789; AT5G05170.
DR eggNOG; ENOG502QSUQ; Eukaryota.
DR HOGENOM; CLU_001418_0_2_1; -.
DR InParanoid; Q941L0; -.
DR OMA; EIPRVYI; -.
DR OrthoDB; 679241at2759; -.
DR PhylomeDB; Q941L0; -.
DR BioCyc; MetaCyc:MON-2362; -.
DR BRENDA; 2.4.1.12; 399.
DR UniPathway; UPA00695; -.
DR PRO; PR:Q941L0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q941L0; baseline and differential.
DR Genevisible; Q941L0; AT.
DR GO; GO:0005768; C:endosome; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005802; C:trans-Golgi network; HDA:TAIR.
DR GO; GO:0016760; F:cellulose synthase (UDP-forming) activity; IEA:UniProtKB-EC.
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:0006952; P:defense response; TAS:TAIR.
DR GO; GO:0009833; P:plant-type primary cell wall biogenesis; IMP:TAIR.
DR GO; GO:0009834; P:plant-type secondary cell wall biogenesis; 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; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF03552; Cellulose_synt; 1.
DR Pfam; PF14569; zf-UDP; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cell wall biogenesis/degradation;
KW Cellulose biosynthesis; Coiled coil; Glycoprotein; Glycosyltransferase;
KW Membrane; Metal-binding; Phosphoprotein; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix; Zinc; Zinc-finger.
FT CHAIN 1..1065
FT /note="Cellulose synthase A catalytic subunit 3 [UDP-
FT forming]"
FT /id="PRO_0000166369"
FT TOPO_DOM 1..260
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 282..283
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 284..304
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 305..842
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 843..863
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 864..874
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 875..895
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 896..910
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 911..931
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 932..961
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 962..982
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 983..993
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 994..1014
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1015..1023
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1024..1044
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1045..1065
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ZN_FING 20..66
FT /note="RING-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 643..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 433..457
FT /evidence="ECO:0000255"
FT COMPBIAS 652..669
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 379
FT /evidence="ECO:0000255"
FT ACT_SITE 765
FT /evidence="ECO:0000255"
FT BINDING 20
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 23
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="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 42
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 47
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 50
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 545
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 547
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17427041,
FT ECO:0007744|PubMed:15308754"
FT MOD_RES 151
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17427041,
FT ECO:0007744|PubMed:14506206, ECO:0007744|PubMed:15308754,
FT ECO:0007744|PubMed:19376835"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17427041"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17427041,
FT ECO:0007744|PubMed:15308754, ECO:0007744|PubMed:19376835"
FT CARBOHYD 938
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 301
FT /note="S->F: In eli1-1; reduced cellulose synthesis and
FT aberrant deposition of lignin."
FT /evidence="ECO:0000269|PubMed:12713541"
FT MUTAGEN 522
FT /note="A->V: In eli1-2; reduced cellulose synthesis and
FT aberrant deposition of lignin."
FT MUTAGEN 617
FT /note="G->E: In cev1; reduced amount of crystalline
FT cellulose in roots."
FT /evidence="ECO:0000269|PubMed:11340179,
FT ECO:0000269|PubMed:12119374, ECO:0000269|PubMed:12437300"
FT MUTAGEN 942
FT /note="T->I: In ixr1-2; confers resistance to the
FT herbicides isoxaben and thiazolidinones."
FT /evidence="ECO:0000269|PubMed:11517344"
FT MUTAGEN 998
FT /note="G->D: In ixr1-1; confers resistance to the
FT herbicides isoxaben and thiazolidinones."
FT /evidence="ECO:0000269|PubMed:11517344"
FT MUTAGEN 1056
FT /note="P->S: In rsw5; reduction of cellulose synthesis, and
FT temperature sensitive."
FT /evidence="ECO:0000269|PubMed:16891551"
FT CONFLICT 377
FT /note="S -> F (in Ref. 1; AAC39336)"
FT /evidence="ECO:0000305"
FT CONFLICT 479
FT /note="R -> G (in Ref. 1; AAC39336)"
FT /evidence="ECO:0000305"
FT CONFLICT 858
FT /note="P -> L (in Ref. 1; AAC39336)"
FT /evidence="ECO:0000305"
FT STRAND 338..344
FT /evidence="ECO:0007829|PDB:7CK2"
FT TURN 347..349
FT /evidence="ECO:0007829|PDB:7CK2"
FT HELIX 352..363
FT /evidence="ECO:0007829|PDB:7CK2"
FT HELIX 369..371
FT /evidence="ECO:0007829|PDB:7CK2"
FT STRAND 372..378
FT /evidence="ECO:0007829|PDB:7CK2"
FT HELIX 383..406
FT /evidence="ECO:0007829|PDB:7CK2"
FT STRAND 409..412
FT /evidence="ECO:0007829|PDB:7CK3"
FT HELIX 413..416
FT /evidence="ECO:0007829|PDB:7CK2"
FT HELIX 423..425
FT /evidence="ECO:0007829|PDB:7CK3"
FT HELIX 431..457
FT /evidence="ECO:0007829|PDB:7CK2"
FT STRAND 470..472
FT /evidence="ECO:0007829|PDB:7CK2"
FT STRAND 484..490
FT /evidence="ECO:0007829|PDB:7CK2"
FT STRAND 504..509
FT /evidence="ECO:0007829|PDB:7CK2"
FT HELIX 520..535
FT /evidence="ECO:0007829|PDB:7CK2"
FT STRAND 539..544
FT /evidence="ECO:0007829|PDB:7CK2"
FT HELIX 555..563
FT /evidence="ECO:0007829|PDB:7CK2"
FT STRAND 596..600
FT /evidence="ECO:0007829|PDB:7CK2"
FT STRAND 605..610
FT /evidence="ECO:0007829|PDB:7CK2"
FT STRAND 612..614
FT /evidence="ECO:0007829|PDB:7CK2"
FT STRAND 618..621
FT /evidence="ECO:0007829|PDB:7CK2"
FT HELIX 622..626
FT /evidence="ECO:0007829|PDB:7CK2"
FT HELIX 711..716
FT /evidence="ECO:0007829|PDB:7CK2"
FT STRAND 719..722
FT /evidence="ECO:0007829|PDB:7CK3"
FT HELIX 730..739
FT /evidence="ECO:0007829|PDB:7CK2"
FT TURN 743..748
FT /evidence="ECO:0007829|PDB:7CK2"
FT TURN 751..753
FT /evidence="ECO:0007829|PDB:7CK2"
FT STRAND 754..757
FT /evidence="ECO:0007829|PDB:7CK2"
FT STRAND 761..763
FT /evidence="ECO:0007829|PDB:7CK2"
FT STRAND 767..772
FT /evidence="ECO:0007829|PDB:7CK2"
FT STRAND 774..782
FT /evidence="ECO:0007829|PDB:7CK2"
FT HELIX 797..807
FT /evidence="ECO:0007829|PDB:7CK3"
FT TURN 808..810
FT /evidence="ECO:0007829|PDB:7CK3"
SQ SEQUENCE 1065 AA; 119683 MW; 3AA4714CE3C4D581 CRC64;
MESEGETAGK PMKNIVPQTC QICSDNVGKT VDGDRFVACD ICSFPVCRPC YEYERKDGNQ
SCPQCKTRYK RLKGSPAIPG DKDEDGLADE GTVEFNYPQK EKISERMLGW HLTRGKGEEM
GEPQYDKEVS HNHLPRLTSR QDTSGEFSAA SPERLSVSST IAGGKRLPYS SDVNQSPNRR
IVDPVGLGNV AWKERVDGWK MKQEKNTGPV STQAASERGG VDIDASTDIL ADEALLNDEA
RQPLSRKVSI PSSRINPYRM VIMLRLVILC LFLHYRITNP VPNAFALWLV SVICEIWFAL
SWILDQFPKW FPVNRETYLD RLALRYDREG EPSQLAAVDI FVSTVDPLKE PPLVTANTVL
SILAVDYPVD KVSCYVSDDG AAMLSFESLA ETSEFARKWV PFCKKYSIEP RAPEWYFAAK
IDYLKDKVQT SFVKDRRAMK REYEEFKIRI NALVSKALKC PEEGWVMQDG TPWPGNNTRD
HPGMIQVFLG QNGGLDAEGN ELPRLVYVSR EKRPGFQHHK KAGAMNALVR VSAVLTNGPF
ILNLDCDHYI NNSKALREAM CFLMDPNLGK QVCYVQFPQR FDGIDKNDRY ANRNTVFFDI
NLRGLDGIQG PVYVGTGCVF NRTALYGYEP PIKVKHKKPS LLSKLCGGSR KKNSKAKKES
DKKKSGRHTD STVPVFNLDD IEEGVEGAGF DDEKALLMSQ MSLEKRFGQS AVFVASTLME
NGGVPPSATP ENLLKEAIHV ISCGYEDKSD WGMEIGWIYG SVTEDILTGF KMHARGWRSI
YCMPKLPAFK GSAPINLSDR LNQVLRWALG SVEILFSRHC PIWYGYNGRL KFLERFAYVN
TTIYPITSIP LLMYCTLPAV CLFTNQFIIP QISNIASIWF LSLFLSIFAT GILEMRWSGV
GIDEWWRNEQ FWVIGGVSAH LFAVFQGILK VLAGIDTNFT VTSKASDEDG DFAELYLFKW
TTLLIPPTTL LIVNLVGVVA GVSYAINSGY QSWGPLFGKL FFAFWVIVHL YPFLKGLMGR
QNRTPTIVVV WSVLLASIFS LLWVRIDPFT SRVTGPDILE CGINC
