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Cellulose synthase A catalytic subunit 3 [UDP-forming] (AtCesA3) (EC 2.4.1.12) (Constitutive expression of VSP1 protein 1) (Isoxaben-resistant protein 1) (Ath-B) (Protein ECTOPIC LIGNIN 1) (Protein RADIALLY SWOLLEN 5) (AtRSW5)

 CESA3_ARATH             Reviewed;        1065 AA.
Q941L0; O48948; Q0WLU1; Q9FHK6;
30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
30-AUG-2005, sequence version 2.
25-OCT-2017, entry version 129.
RecName: Full=Cellulose synthase A catalytic subunit 3 [UDP-forming];
Short=AtCesA3;
EC=2.4.1.12;
AltName: Full=Constitutive expression of VSP1 protein 1;
AltName: Full=Isoxaben-resistant protein 1;
Short=Ath-B;
AltName: Full=Protein ECTOPIC LIGNIN 1;
AltName: Full=Protein RADIALLY SWOLLEN 5;
Short=AtRSW5;
Name=CESA3; Synonyms=ATHB, CEV1, ELI1, IXR1, RSW5;
OrderedLocusNames=At5g05170; ORFNames=K2A11.4;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
PubMed=9445479; DOI=10.1126/science.279.5351.717;
Arioli T., Peng L., Betzner A.S., Burn J., Wittke W., Herth W.,
Camilleri C., Hoefte H., Plazinski J., Birch R., Cork A., Glover J.,
Redmond J., Williamson R.E.;
"Molecular analysis of cellulose biosynthesis in Arabidopsis.";
Science 279:717-720(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10470850; DOI=10.1093/dnares/6.3.183;
Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
Miyajima N., Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. IX.
Sequence features of the regions of 1,011,550 bp covered by seventeen
P1 and TAC clones.";
DNA Res. 6:183-195(1999).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 635-1065.
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[6]
GENE FAMILY, AND NOMENCLATURE.
PubMed=11178255; DOI=10.1186/gb-2000-1-4-reviews3001;
Richmond T.;
"Higher plant cellulose synthases.";
Genome Biol. 1:REVIEWS3001.1-REVIEWS3001.6(2000).
[7]
FUNCTION, MUTAGENESIS OF GLY-617, AND DISRUPTION PHENOTYPE.
PubMed=11340179; DOI=10.1105/tpc.13.5.1025;
Ellis C., Turner J.G.;
"The Arabidopsis mutant cev1 has constitutively active jasmonate and
ethylene signal pathways and enhanced resistance to pathogens.";
Plant Cell 13:1025-1033(2001).
[8]
TISSUE SPECIFICITY, AND MUTAGENESIS OF THR-942 AND GLY-998.
PubMed=11517344; DOI=10.1073/pnas.191361598;
Scheible W.-R., Eshed R., Richmond T., Delmer D., Somerville C.;
"Modifications of cellulose synthase confer resistance to isoxaben and
thiazolidinone herbicides in Arabidopsis Ixr1 mutants.";
Proc. Natl. Acad. Sci. U.S.A. 98:10079-10084(2001).
[9]
MUTAGENESIS OF GLY-617.
PubMed=12437300; DOI=10.1094/MPMI.2002.15.10.1025;
Ellis C., Karafyllidis I., Turner J.G.;
"Constitutive activation of jasmonate signaling in an Arabidopsis
mutant correlates with enhanced resistance to Erysiphe cichoracearum,
Pseudomonas syringae, and Myzus persicae.";
Mol. Plant Microbe Interact. 15:1025-1030(2002).
[10]
FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF GLY-617.
PubMed=12119374; DOI=10.1105/tpc.002022;
Ellis C., Karafyllidis I., Wasternack C., Turner J.G.;
"The Arabidopsis mutant cev1 links cell wall signaling to jasmonate
and ethylene responses.";
Plant Cell 14:1557-1566(2002).
[11]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=12068120; DOI=10.1104/pp.010931;
Burn J.E., Hocart C.H., Birch R.J., Cork A.C., Williamson R.E.;
"Functional analysis of the cellulose synthase genes CesA1, CesA2, and
CesA3 in Arabidopsis.";
Plant Physiol. 129:797-807(2002).
[12]
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=12481071; DOI=10.1104/pp.102.010603;
Beeckman T., Przemeck G.K.H., Stamatiou G., Lau R., Terryn N.,
De Rycke R., Inze D., Berleth T.;
"Genetic complexity of cellulose synthase A gene function in
Arabidopsis embryogenesis.";
Plant Physiol. 130:1883-1893(2002).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=cv. La-0;
PubMed=14506206; DOI=10.1074/mcp.T300006-MCP200;
Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
"Large-scale analysis of in vivo phosphorylated membrane proteins by
immobilized metal ion affinity chromatography and mass spectrometry.";
Mol. Cell. Proteomics 2:1234-1243(2003).
[14]
FUNCTION, AND MUTAGENESIS OF SER-301.
PubMed=12713541; DOI=10.1046/j.1365-313X.2003.01729.x;
Cano-Delgado A., Penfield S., Smith C., Catley M., Bevan M.;
"Reduced cellulose synthesis invokes lignification and defense
responses in Arabidopsis thaliana.";
Plant J. 34:351-362(2003).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; SER-151 AND SER-216,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15308754; DOI=10.1105/tpc.104.023150;
Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
"Phosphoproteomics of the Arabidopsis plasma membrane and a new
phosphorylation site database.";
Plant Cell 16:2394-2405(2004).
[16]
MUTAGENESIS OF PRO-1056.
PubMed=16891551; DOI=10.1104/pp.106.084004;
Wang J., Howles P.A., Cork A.H., Birch R.J., Williamson R.E.;
"Chimeric proteins suggest that the catalytic and/or C-terminal
domains give CesA1 and CesA3 access to their specific sites in the
cellulose synthase of primary walls.";
Plant Physiol. 142:685-695(2006).
[17]
PHOSPHORYLATION AT SER-3; SER-151; SER-211 AND SER-216, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=17427041; DOI=10.1007/s11103-007-9142-2;
Taylor N.G.;
"Identification of cellulose synthase AtCesA7 (IRX3) in vivo
phosphorylation sites -- a potential role in regulating protein
degradation.";
Plant Mol. Biol. 64:161-171(2007).
[18]
FUNCTION, AND SUBUNIT.
PubMed=17878302; DOI=10.1073/pnas.0706592104;
Persson S., Paredez A., Carroll A., Palsdottir H., Doblin M.,
Poindexter P., Khitrov N., Auer M., Somerville C.R.;
"Genetic evidence for three unique components in primary cell-wall
cellulose synthase complexes in Arabidopsis.";
Proc. Natl. Acad. Sci. U.S.A. 104:15566-15571(2007).
[19]
FUNCTION, AND INTERACTION WITH CESA1 AND CESA6.
PubMed=17878303; DOI=10.1073/pnas.0706569104;
Desprez T., Juraniec M., Crowell E.F., Jouy H., Pochylova Z.,
Parcy F., Hoefte H., Gonneau M., Vernhettes S.;
"Organization of cellulose synthase complexes involved in primary cell
wall synthesis in Arabidopsis thaliana.";
Proc. Natl. Acad. Sci. U.S.A. 104:15572-15577(2007).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151 AND SER-216, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19376835; DOI=10.1104/pp.109.138677;
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
Grossmann J., Gruissem W., Baginsky S.;
"Large-scale Arabidopsis phosphoproteome profiling reveals novel
chloroplast kinase substrates and phosphorylation networks.";
Plant Physiol. 150:889-903(2009).
[21]
INTERACTION WITH CSI1.
STRAIN=cv. Columbia;
PubMed=20616083; DOI=10.1073/pnas.1007092107;
Gu Y., Kaplinsky N., Bringmann M., Cobb A., Carroll A.,
Sampathkumar A., Baskin T.I., Persson S., Somerville C.R.;
"Identification of a cellulose synthase-associated protein required
for cellulose biosynthesis.";
Proc. Natl. Acad. Sci. U.S.A. 107:12866-12871(2010).
[22]
INTERACTION WITH CSI1 AND CSI3.
PubMed=24368796; DOI=10.1105/tpc.113.116715;
Lei L., Li S., Du J., Bashline L., Gu Y.;
"Cellulose synthase INTERACTIVE3 regulates cellulose biosynthesis in
both a microtubule-dependent and microtubule-independent manner in
Arabidopsis.";
Plant Cell 25:4912-4923(2013).
[23]
INTERACTION WITH STL1 AND STL2, AND LACK OF INTERACTION WITH GOT1.
PubMed=27277162; DOI=10.1038/ncomms11656;
Zhang Y., Nikolovski N., Sorieul M., Vellosillo T., McFarlane H.E.,
Dupree R., Kesten C., Schneider R., Driemeier C., Lathe R.,
Lampugnani E., Yu X., Ivakov A., Doblin M.S., Mortimer J.C.,
Brown S.P., Persson S., Dupree P.;
"Golgi-localized STELLO proteins regulate the assembly and trafficking
of cellulose synthase complexes in Arabidopsis.";
Nat. Commun. 7:11656-11656(2016).
-!- FUNCTION: Catalytic subunit of cellulose synthase terminal
complexes ('rosettes'), required for beta-1,4-glucan microfibril
crystallization, a major mechanism of the cell wall formation.
Involved in the primary cell wall formation, especially in roots.
{ECO:0000269|PubMed:11340179, ECO:0000269|PubMed:12068120,
ECO:0000269|PubMed:12119374, ECO:0000269|PubMed:12713541,
ECO:0000269|PubMed:17878302, ECO:0000269|PubMed:17878303}.
-!- CATALYTIC ACTIVITY: UDP-glucose + (1,4-beta-D-glucosyl)(n) = UDP +
(1,4-beta-D-glucosyl)(n+1).
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
-!- PATHWAY: Glycan metabolism; plant cellulose biosynthesis.
-!- SUBUNIT: Interacts with CESA1 and CESA6. Interacts with STL1 and
STL2, but not with GOT1 (PubMed:27277162). Binds to CSI1 and CSI3
(PubMed:20616083, PubMed:24368796). {ECO:0000269|PubMed:17878302,
ECO:0000269|PubMed:17878303, ECO:0000269|PubMed:20616083,
ECO:0000269|PubMed:24368796, ECO:0000269|PubMed:27277162}.
-!- INTERACTION:
Q94JQ6:CESA6; NbExp=2; IntAct=EBI-4448240, EBI-15659159;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass
membrane protein {ECO:0000305}.
-!- TISSUE SPECIFICITY: Expressed in young plants, flowers and roots,
and to a lower extent in leaves and stems. Localized in all cells
except meristematic cells. Accumulates particularly in root caps,
root hairs, epidermal layer, midveins of leaves and anthers. Not
present in old tissues. {ECO:0000269|PubMed:11517344,
ECO:0000269|PubMed:12068120, ECO:0000269|PubMed:12119374,
ECO:0000269|PubMed:12481071}.
-!- DEVELOPMENTAL STAGE: Mostly expressed in cotyledons during all
steps of embryogenesis, and decrease toward the bent-cotyledon
stage. {ECO:0000269|PubMed:12481071}.
-!- DISRUPTION PHENOTYPE: Mutants cev1 are dark green and contains
more jasmonates and ethylene, that leads to shorter and thickened
hypocotyls and roots, with prolific root hairs, and the
accumulation of purple anthocyanins. They exhibit constitutive and
high expression in leaves lamina of vegetative storage proteins
(VSP1 and VSP2), basic chitinase CHI-B and plant defensin PDF1.2.
In addition, this mutation confers resistance to powdery mildew
pathogens such as E.cichoracearum, E.orontii and O.lycopersicum,
to the bacterial pathogen P.syringae pv maculicola, and also to
the green peach aphid M.persicae. {ECO:0000269|PubMed:11340179}.
-!- SIMILARITY: Belongs to the glycosyltransferase 2 family. Plant
cellulose synthase subfamily. {ECO:0000305}.
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EMBL; AF027174; AAC39336.1; -; mRNA.
EMBL; AB018111; BAB09693.1; -; Genomic_DNA.
EMBL; CP002688; AED90836.1; -; Genomic_DNA.
EMBL; AY045960; AAK76634.2; -; mRNA.
EMBL; BT002335; AAN86168.1; -; mRNA.
EMBL; AK230097; BAF01916.1; -; mRNA.
PIR; T52054; T52054.
RefSeq; NP_196136.1; NM_120599.4.
UniGene; At.24338; -.
ProteinModelPortal; Q941L0; -.
SMR; Q941L0; -.
BioGrid; 15678; 46.
DIP; DIP-46437N; -.
IntAct; Q941L0; 3.
STRING; 3702.AT5G05170.1; -.
CAZy; GT2; Glycosyltransferase Family 2.
TCDB; 4.D.3.1.4; the glycan glucosyl transferase (opgh) family.
iPTMnet; Q941L0; -.
SwissPalm; Q941L0; -.
PaxDb; Q941L0; -.
EnsemblPlants; AT5G05170.1; AT5G05170.1; AT5G05170.
GeneID; 830399; -.
Gramene; AT5G05170.1; AT5G05170.1; AT5G05170.
KEGG; ath:AT5G05170; -.
Araport; AT5G05170; -.
TAIR; locus:2156789; AT5G05170.
eggNOG; ENOG410II8I; Eukaryota.
eggNOG; COG1215; LUCA.
HOGENOM; HOG000241942; -.
InParanoid; Q941L0; -.
KO; K10999; -.
OMA; GHVCQIC; -.
OrthoDB; EOG093600MD; -.
PhylomeDB; Q941L0; -.
BioCyc; MetaCyc:MONOMER-2362; -.
BRENDA; 2.4.1.12; 399.
UniPathway; UPA00695; -.
PRO; PR:Q941L0; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q941L0; baseline and differential.
Genevisible; Q941L0; AT.
GO; GO:0005768; C:endosome; IDA:TAIR.
GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0009506; C:plasmodesma; IDA:TAIR.
GO; GO:0005802; C:trans-Golgi network; IDA:TAIR.
GO; GO:0016760; F:cellulose synthase (UDP-forming) activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
GO; GO:0030244; P:cellulose biosynthetic process; IMP:TAIR.
GO; GO:0006952; P:defense response; TAS:TAIR.
GO; GO:0009833; P:plant-type primary cell wall biogenesis; IMP:TAIR.
GO; GO:0009834; P:plant-type secondary cell wall biogenesis; IMP:TAIR.
Gene3D; 3.30.40.10; -; 1.
Gene3D; 3.90.550.10; -; 1.
InterPro; IPR005150; Cellulose_synth.
InterPro; IPR027934; CES_Znf_RING.
InterPro; IPR029044; Nucleotide-diphossugar_trans.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
Pfam; PF03552; Cellulose_synt; 1.
Pfam; PF14569; zf-UDP; 1.
SUPFAM; SSF53448; SSF53448; 3.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
Cell membrane; Cell wall biogenesis/degradation;
Cellulose biosynthesis; Coiled coil; Complete proteome; Glycoprotein;
Glycosyltransferase; Membrane; Metal-binding; Phosphoprotein;
Reference proteome; Transferase; Transmembrane; Transmembrane helix;
Zinc; Zinc-finger.
CHAIN 1 1065 Cellulose synthase A catalytic subunit 3
[UDP-forming].
/FTId=PRO_0000166369.
TOPO_DOM 1 260 Cytoplasmic. {ECO:0000255}.
TRANSMEM 261 281 Helical. {ECO:0000255}.
TOPO_DOM 282 283 Extracellular. {ECO:0000255}.
TRANSMEM 284 304 Helical. {ECO:0000255}.
TOPO_DOM 305 842 Cytoplasmic. {ECO:0000255}.
TRANSMEM 843 863 Helical. {ECO:0000255}.
TOPO_DOM 864 874 Extracellular. {ECO:0000255}.
TRANSMEM 875 895 Helical. {ECO:0000255}.
TOPO_DOM 896 910 Cytoplasmic. {ECO:0000255}.
TRANSMEM 911 931 Helical. {ECO:0000255}.
TOPO_DOM 932 961 Extracellular. {ECO:0000255}.
TRANSMEM 962 982 Helical. {ECO:0000255}.
TOPO_DOM 983 993 Cytoplasmic. {ECO:0000255}.
TRANSMEM 994 1014 Helical. {ECO:0000255}.
TOPO_DOM 1015 1023 Extracellular. {ECO:0000255}.
TRANSMEM 1024 1044 Helical. {ECO:0000255}.
TOPO_DOM 1045 1065 Cytoplasmic. {ECO:0000255}.
ZN_FING 20 66 RING-type; degenerate.
{ECO:0000255|PROSITE-ProRule:PRU00175}.
COILED 433 457 {ECO:0000255}.
COMPBIAS 633 664 Lys-rich.
ACT_SITE 379 379 {ECO:0000255}.
ACT_SITE 765 765 {ECO:0000255}.
METAL 20 20 Zinc 1. {ECO:0000250|UniProtKB:Q9SWW6}.
METAL 23 23 Zinc 1. {ECO:0000250|UniProtKB:Q9SWW6}.
METAL 39 39 Zinc 2. {ECO:0000250|UniProtKB:Q9SWW6}.
METAL 42 42 Zinc 2. {ECO:0000250|UniProtKB:Q9SWW6}.
METAL 47 47 Zinc 1. {ECO:0000250|UniProtKB:Q9SWW6}.
METAL 50 50 Zinc 1. {ECO:0000250|UniProtKB:Q9SWW6}.
METAL 62 62 Zinc 2. {ECO:0000250|UniProtKB:Q9SWW6}.
METAL 65 65 Zinc 2. {ECO:0000250|UniProtKB:Q9SWW6}.
BINDING 545 545 Substrate. {ECO:0000255}.
BINDING 547 547 Substrate. {ECO:0000255}.
MOD_RES 3 3 Phosphoserine.
{ECO:0000244|PubMed:15308754,
ECO:0000269|PubMed:17427041}.
MOD_RES 151 151 Phosphoserine.
{ECO:0000244|PubMed:14506206,
ECO:0000244|PubMed:15308754,
ECO:0000244|PubMed:19376835,
ECO:0000269|PubMed:17427041}.
MOD_RES 211 211 Phosphoserine.
{ECO:0000269|PubMed:17427041}.
MOD_RES 216 216 Phosphoserine.
{ECO:0000244|PubMed:15308754,
ECO:0000244|PubMed:19376835,
ECO:0000269|PubMed:17427041}.
CARBOHYD 938 938 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
MUTAGEN 301 301 S->F: In eli1-1; reduced cellulose
synthesis and aberrant deposition of
lignin. {ECO:0000269|PubMed:12713541}.
MUTAGEN 522 522 A->V: In eli1-2; reduced cellulose
synthesis and aberrant deposition of
lignin.
MUTAGEN 617 617 G->E: In cev1; reduced amount of
crystalline cellulose in roots.
{ECO:0000269|PubMed:11340179,
ECO:0000269|PubMed:12119374,
ECO:0000269|PubMed:12437300}.
MUTAGEN 942 942 T->I: In ixr1-2; confers resistance to
the herbicides isoxaben and
thiazolidinones.
{ECO:0000269|PubMed:11517344}.
MUTAGEN 998 998 G->D: In ixr1-1; confers resistance to
the herbicides isoxaben and
thiazolidinones.
{ECO:0000269|PubMed:11517344}.
MUTAGEN 1056 1056 P->S: In rsw5; reduction of cellulose
synthesis, and temperature sensitive.
{ECO:0000269|PubMed:16891551}.
CONFLICT 377 377 S -> F (in Ref. 1; AAC39336).
{ECO:0000305}.
CONFLICT 479 479 R -> G (in Ref. 1; AAC39336).
{ECO:0000305}.
CONFLICT 858 858 P -> L (in Ref. 1; AAC39336).
{ECO:0000305}.
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


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