CESA7_ARATH
ID CESA7_ARATH Reviewed; 1026 AA.
AC Q9SWW6; Q56ZZ5; Q9XHP6;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Cellulose synthase A catalytic subunit 7 [UDP-forming] {ECO:0000303|PubMed:11178255, ECO:0000303|PubMed:12805608};
DE Short=AtCesA7 {ECO:0000303|PubMed:11178255, ECO:0000303|PubMed:12805608};
DE EC=2.4.1.12;
DE AltName: Full=Protein FRAGILE FIBER 5 {ECO:0000303|PubMed:12805608};
DE AltName: Full=Protein IRREGULAR XYLEM 3 {ECO:0000303|PubMed:10330464};
DE Short=AtIRX3 {ECO:0000303|PubMed:10330464};
GN Name=CESA7 {ECO:0000303|PubMed:11178255, ECO:0000303|PubMed:12805608};
GN Synonyms=FRA5 {ECO:0000303|PubMed:12805608},
GN IRX3 {ECO:0000303|PubMed:10330464};
GN OrderedLocusNames=At5g17420 {ECO:0000312|Araport:AT5G17420};
GN ORFNames=T10B6.80 {ECO:0000312|EMBL:CAC01737.1};
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 [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=10330464; DOI=10.2307/3870813;
RA Taylor N.G., Scheible W.-R., Cutler S., Somerville C.R., Turner S.R.;
RT "The irregular xylem3 locus of Arabidopsis encodes a cellulose synthase
RT required for secondary cell wall synthesis.";
RL Plant Cell 11:769-780(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
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 776-1026.
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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 [7]
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 [8]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INTERACTION WITH
RP CESA8.
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 [9]
RP TISSUE SPECIFICITY.
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 [10]
RP FUNCTION.
RX PubMed=12165296; DOI=10.1016/s0031-9422(02)00199-1;
RA Ha M.-A., MacKinnon I.M., Sturcova A., Apperley D.C., McCann M.C.,
RA Turner S.R., Jarvis M.C.;
RT "Structure of cellulose-deficient secondary cell walls from the irx3 mutant
RT of Arabidopsis thaliana.";
RL Phytochemistry 61:7-14(2002).
RN [11]
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 [12]
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 [13]
RP FUNCTION, AND MUTAGENESIS OF PRO-557.
RX PubMed=12805608; DOI=10.1104/pp.102.019331;
RA Zhong R., Morrison W.H. III, Freshour G.D., Hahn M.G., Ye Z.-H.;
RT "Expression of a mutant form of cellulose synthase AtCesA7 causes dominant
RT negative effect on cellulose biosynthesis.";
RL Plant Physiol. 132:786-795(2003).
RN [14]
RP TISSUE SPECIFICITY, AND INTERACTION WITH CESA4 AND CESA8.
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 [15]
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 [16]
RP PHOSPHORYLATION AT SER-185, AND IDENTIFICATION 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 [17]
RP INTERACTION WITH TED6.
RX PubMed=19383897; DOI=10.1105/tpc.108.059154;
RA Endo S., Pesquet E., Yamaguchi M., Tashiro G., Sato M., Toyooka K.,
RA Nishikubo N., Udagawa-Motose M., Kubo M., Fukuda H., Demura T.;
RT "Identifying new components participating in the secondary cell wall
RT formation of vessel elements in zinnia and Arabidopsis.";
RL Plant Cell 21:1155-1165(2009).
RN [18]
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 [19]
RP SUBCELLULAR LOCATION, S-ACYLATION, AND MUTAGENESIS OF CYS-621; CYS-623;
RP CYS-624; CYS-626; CYS-1022 AND CYS-1026.
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).
RN [20]
RP STRUCTURE BY NMR OF 26-105, AND ZINC-BINDING SITES CYS-37; CYS-40; CYS-56;
RP CYS-59; CYS-64; CYS-67; CYS-79 AND CYS-82.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of ring-finger in the catalytic subunit (Irx3) of
RT cellulose synthase.";
RL Submitted (MAY-2004) to the PDB data bank.
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:12165296,
CC ECO:0000269|PubMed:12805608, ECO:0000269|PubMed:17351116,
CC 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:0000269|Ref.20};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|Ref.20};
CC -!- PATHWAY: Glycan metabolism; plant cellulose biosynthesis.
CC -!- SUBUNIT: Interacts with CESA4 and CESA8. Assembly with CESA4 and CESA8
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). Binds to TED6 (PubMed:19383897).
CC {ECO:0000269|PubMed:11148295, ECO:0000269|PubMed:12538856,
CC ECO:0000269|PubMed:12897249, ECO:0000269|PubMed:19383897,
CC ECO:0000269|PubMed:27277162}.
CC -!- INTERACTION:
CC Q9SWW6; Q84JA6: CESA4; NbExp=7; IntAct=EBI-4477361, EBI-8579072;
CC Q9SWW6; Q8LPK5: CESA8; NbExp=7; IntAct=EBI-4477361, EBI-8579199;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27387950};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Confined to secondary cell wall developing tissues
CC such as xylems and interfascicular regions. Expressed in young plants,
CC stems and flowers, but not in leaves, roots and shoots.
CC {ECO:0000269|PubMed:10330464, ECO:0000269|PubMed:11148295,
CC ECO:0000269|PubMed:11517344, 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:10330464, ECO:0000269|PubMed:11148295}.
CC -!- PTM: Phosphorylated protein may be subject to proteasome degradation.
CC {ECO:0000269|PubMed:17427041}.
CC -!- PTM: S-acylated at Cys-621, Cys-623, Cys-624, Cys-626, Cys-1022 and
CC Cys-1026. The ratio of acylation by either palmitate or stearate is
CC unknown. S-acylation is essential for plasma membrane localization.
CC {ECO:0000269|PubMed:27387950}.
CC -!- DISRUPTION PHENOTYPE: Reduced plant size, reduced content of cellulose,
CC collapsed xylem vessels and wilting of inflorescence stems
CC (PubMed:9165747). Enhanced resistance to the pathogens Ralstonia
CC solanacearum and Plectosphaerella cucumerina (PubMed:17351116).
CC {ECO:0000269|PubMed:17351116, ECO:0000269|PubMed:9165747}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. Plant
CC cellulose synthase subfamily. {ECO:0000305}.
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DR EMBL; AF088917; AAD32031.1; -; mRNA.
DR EMBL; AF091713; AAD40885.1; -; Genomic_DNA.
DR EMBL; AL391142; CAC01737.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92424.1; -; Genomic_DNA.
DR EMBL; AY139754; AAM98075.1; -; mRNA.
DR EMBL; BT004543; AAO42789.1; -; mRNA.
DR EMBL; AK220815; BAD94098.1; -; mRNA.
DR PIR; T51579; T51579.
DR RefSeq; NP_197244.1; NM_121748.4.
DR PDB; 1WEO; NMR; -; A=26-105.
DR PDBsum; 1WEO; -.
DR AlphaFoldDB; Q9SWW6; -.
DR SMR; Q9SWW6; -.
DR BioGRID; 16884; 13.
DR IntAct; Q9SWW6; 9.
DR MINT; Q9SWW6; -.
DR STRING; 3702.AT5G17420.1; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR TCDB; 4.D.3.1.7; the glycan glucosyl transferase (opgh) family.
DR iPTMnet; Q9SWW6; -.
DR SwissPalm; Q9SWW6; -.
DR PaxDb; Q9SWW6; -.
DR PRIDE; Q9SWW6; -.
DR ProteomicsDB; 220389; -.
DR EnsemblPlants; AT5G17420.1; AT5G17420.1; AT5G17420.
DR GeneID; 831608; -.
DR Gramene; AT5G17420.1; AT5G17420.1; AT5G17420.
DR KEGG; ath:AT5G17420; -.
DR Araport; AT5G17420; -.
DR TAIR; locus:2178935; AT5G17420.
DR eggNOG; ENOG502QQXZ; Eukaryota.
DR HOGENOM; CLU_001418_0_2_1; -.
DR InParanoid; Q9SWW6; -.
DR OMA; NGQVCEI; -.
DR OrthoDB; 679241at2759; -.
DR PhylomeDB; Q9SWW6; -.
DR BioCyc; MetaCyc:MON-2365; -.
DR BRENDA; 2.4.1.12; 399.
DR UniPathway; UPA00695; -.
DR EvolutionaryTrace; Q9SWW6; -.
DR PRO; PR:Q9SWW6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9SWW6; baseline and differential.
DR Genevisible; Q9SWW6; AT.
DR GO; GO:0010330; C:cellulose synthase complex; IPI:TAIR.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA: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:0030244; P:cellulose biosynthetic process; IMP:TAIR.
DR GO; GO:0009832; P:plant-type cell wall biogenesis; 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:0010400; P:rhamnogalacturonan I side chain metabolic process; 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; Acetylation; Cell membrane; Cell wall biogenesis/degradation;
KW Cellulose biosynthesis; Coiled coil; Glycoprotein; Glycosyltransferase;
KW Lipoprotein; Membrane; Metal-binding; Phosphoprotein; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix; Zinc; Zinc-finger.
FT CHAIN 1..1026
FT /note="Cellulose synthase A catalytic subunit 7 [UDP-
FT forming]"
FT /id="PRO_0000166373"
FT TOPO_DOM 1..233
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..252
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 253..262
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 284..804
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 805..825
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 826..836
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 837..857
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 858..872
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 873..893
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 894..922
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 923..943
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 944..954
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 955..975
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 976..984
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 985..1005
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1006..1026
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ZN_FING 37..83
FT /note="RING-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT COILED 412..433
FT /evidence="ECO:0000255"
FT ACT_SITE 358
FT /evidence="ECO:0000255"
FT ACT_SITE 726
FT /evidence="ECO:0000255"
FT BINDING 37
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|Ref.20, ECO:0007744|PDB:1WEO"
FT BINDING 40
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|Ref.20, ECO:0007744|PDB:1WEO"
FT BINDING 56
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|Ref.20, ECO:0007744|PDB:1WEO"
FT BINDING 59
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|Ref.20, ECO:0007744|PDB:1WEO"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|Ref.20, ECO:0007744|PDB:1WEO"
FT BINDING 67
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|Ref.20, ECO:0007744|PDB:1WEO"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|Ref.20, ECO:0007744|PDB:1WEO"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|Ref.20, ECO:0007744|PDB:1WEO"
FT BINDING 524
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 526
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O48946"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17427041"
FT CARBOHYD 900
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 557
FT /note="P->T: In fra5; dominant negative effect on cellulose
FT synthesis."
FT /evidence="ECO:0000269|PubMed:12805608"
FT MUTAGEN 621
FT /note="C->S: Unable to localize to the plasma membrane and
FT impaired function as cellulose synthase; when associated
FT with S-623; S-624 and S-626. Abolishes S-acylation."
FT /evidence="ECO:0000269|PubMed:27387950"
FT MUTAGEN 623
FT /note="C->S: Unable to localize to the plasma membrane and
FT impaired function as cellulose synthase; when associated
FT with S-621; S-624 and S-626. Abolishes S-acylation."
FT /evidence="ECO:0000269|PubMed:27387950"
FT MUTAGEN 624
FT /note="C->S: Unable to localize to the plasma membrane and
FT impaired function as cellulose synthase; when associated
FT with S-621; S-623 and S-626. Abolishes S-acylation."
FT /evidence="ECO:0000269|PubMed:27387950"
FT MUTAGEN 626
FT /note="C->S: Unable to localize to the plasma membrane and
FT impaired function as cellulose synthase; when associated
FT with S-621; S-623 and S-624. Abolishes S-acylation."
FT /evidence="ECO:0000269|PubMed:27387950"
FT MUTAGEN 1022
FT /note="C->S: Impaired function as cellulose synthase.
FT Abolishes S-acylation. Unable to localize to the plasma
FT membrane; when associated with S-1026."
FT /evidence="ECO:0000269|PubMed:27387950"
FT MUTAGEN 1026
FT /note="C->S: Impaired function as cellulose synthase.
FT Abolishes S-acylation. Unable to localize to the plasma
FT membrane; when associated with S-1022."
FT /evidence="ECO:0000269|PubMed:27387950"
FT CONFLICT 660
FT /note="S -> F (in Ref. 1; AAD32031)"
FT /evidence="ECO:0000305"
FT CONFLICT 895
FT /note="A -> T (in Ref. 5; BAD94098)"
FT /evidence="ECO:0000305"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:1WEO"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:1WEO"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:1WEO"
FT HELIX 65..73
FT /evidence="ECO:0007829|PDB:1WEO"
FT TURN 80..82
FT /evidence="ECO:0007829|PDB:1WEO"
SQ SEQUENCE 1026 AA; 115798 MW; 503BFBC78BE6E511 CRC64;
MEASAGLVAG SHNRNELVVI HNHEEPKPLK NLDGQFCEIC GDQIGLTVEG DLFVACNECG
FPACRPCYEY ERREGTQNCP QCKTRYKRLR GSPRVEGDED EEDIDDIEYE FNIEHEQDKH
KHSAEAMLYG KMSYGRGPED DENGRFPPVI AGGHSGEFPV GGGYGNGEHG LHKRVHPYPS
SEAGSEGGWR ERMDDWKLQH GNLGPEPDDD PEMGLIDEAR QPLSRKVPIA SSKINPYRMV
IVARLVILAV FLRYRLLNPV HDALGLWLTS VICEIWFAVS WILDQFPKWF PIERETYLDR
LSLRYEREGE PNMLAPVDVF VSTVDPLKEP PLVTSNTVLS ILAMDYPVEK ISCYVSDDGA
SMLTFESLSE TAEFARKWVP FCKKFSIEPR APEMYFTLKV DYLQDKVHPT FVKERRAMKR
EYEEFKVRIN AQVAKASKVP LEGWIMQDGT PWPGNNTKDH PGMIQVFLGH SGGFDVEGHE
LPRLVYVSRE KRPGFQHHKK AGAMNALVRV AGVLTNAPFM LNLDCDHYVN NSKAVREAMC
FLMDPQIGKK VCYVQFPQRF DGIDTNDRYA NRNTVFFDIN MKGLDGIQGP VYVGTGCVFK
RQALYGYEPP KGPKRPKMIS CGCCPCFGRR RKNKKFSKND MNGDVAALGG AEGDKEHLMS
EMNFEKTFGQ SSIFVTSTLM EEGGVPPSSS PAVLLKEAIH VISCGYEDKT EWGTELGWIY
GSITEDILTG FKMHCRGWRS IYCMPKRPAF KGSAPINLSD RLNQVLRWAL GSVEIFFSRH
SPLWYGYKGG KLKWLERFAY ANTTIYPFTS IPLLAYCILP AICLLTDKFI MPPISTFASL
FFISLFMSII VTGILELRWS GVSIEEWWRN EQFWVIGGIS AHLFAVVQGL LKILAGIDTN
FTVTSKATDD DDFGELYAFK WTTLLIPPTT VLIINIVGVV AGISDAINNG YQSWGPLFGK
LFFSFWVIVH LYPFLKGLMG RQNRTPTIVV IWSVLLASIF SLLWVRIDPF VLKTKGPDTS
KCGINC
