CESA1_ARATH
ID CESA1_ARATH Reviewed; 1081 AA.
AC O48946; Q0WWU2; Q56WC7;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Cellulose synthase A catalytic subunit 1 [UDP-forming];
DE Short=AtCesA1;
DE EC=2.4.1.12;
DE AltName: Full=Protein RADIALLY SWOLLEN 1;
DE Short=AtRSW1;
GN Name=CESA1; Synonyms=RSW1; OrderedLocusNames=At4g32410; ORFNames=F8B4.110;
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], FUNCTION, AND MUTAGENESIS OF ALA-549.
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=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 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 [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, AND MUTAGENESIS OF ALA-549.
RX PubMed=10987560; DOI=10.1007/s004250000301;
RA Peng L., Hocart C.H., Redmond J.W., Williamson R.E.;
RT "Fractionation of carbohydrates in Arabidopsis root cell walls shows that
RT three radial swelling loci are specifically involved in cellulose
RT production.";
RL Planta 211:406-414(2000).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=11148287; DOI=10.2307/3871238;
RA Fagard M., Desnos T., Desprez T., Goubet F., Refregier G., Mouille G.,
RA McCann M., Rayon C., Vernhettes S., Hoefte H.;
RT "PROCUSTE1 encodes a cellulose synthase required for normal cell elongation
RT specifically in roots and dark-grown hypocotyls of Arabidopsis.";
RL Plant Cell 12:2409-2423(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, AND MUTAGENESIS OF ALA-549.
RX PubMed=11732051; DOI=10.1007/bf01280308;
RA Williamson R.E., Burn J.E., Birch R., Baskin T.I., Arioli T., Betzner A.S.,
RA Cork A.;
RT "Morphology of rsw1, a cellulose-deficient mutant of Arabidopsis
RT thaliana.";
RL Protoplasma 215:116-127(2001).
RN [11]
RP FUNCTION, AND MUTAGENESIS OF ALA-549.
RX PubMed=11732056; DOI=10.1007/bf01280312;
RA Sugimoto K., Williamson R.E., Wasteneys G.O.;
RT "Wall architecture in the cellulose-deficient rsw1 mutant of Arabidopsis
RT thaliana: microfibrils but not microtubules lose their transverse alignment
RT before microfibrils become unrecognizable in the mitotic and elongation
RT zones of roots.";
RL Protoplasma 215:172-183(2001).
RN [12]
RP FUNCTION, AND MUTAGENESIS OF GLY-631.
RX PubMed=11901167; DOI=10.1083/jcb.200111093;
RA Gillmor C.S., Poindexter P., Lorieau J., Palcic M.M., Somerville C.;
RT "Alpha-glucosidase I is required for cellulose biosynthesis and
RT morphogenesis in Arabidopsis.";
RL J. Cell Biol. 156:1003-1013(2002).
RN [13]
RP MUTAGENESIS OF ALA-549.
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 [14]
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 [15]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF
RP GLU-779 AND ASP-780.
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 [16]
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 [17]
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 [18]
RP FUNCTION, AND INTERACTION WITH CESA3 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 [19]
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 [20]
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 [21]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [22]
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 [23]
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 primary
CC cell wall formation. Required during embryogenesis for cell elongation,
CC orientation of cell expansion and complex cell wall formations, such as
CC interdigitated pattern of epidermal pavement cells, stomatal guard
CC cells and trichomes. Plays a role in lateral roots formation, but seems
CC not necessary for the development of tip-growing cells such as root
CC hairs. The presence of each protein CESA1 and CESA6 is critical for
CC cell expansion after germination. {ECO:0000269|PubMed:10987560,
CC ECO:0000269|PubMed:11148287, ECO:0000269|PubMed:11732051,
CC ECO:0000269|PubMed:11732056, ECO:0000269|PubMed:11901167,
CC ECO:0000269|PubMed:12068120, ECO:0000269|PubMed:12481071,
CC ECO:0000269|PubMed:17878302, ECO:0000269|PubMed:17878303,
CC ECO:0000269|PubMed:9445479}.
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 CESA3 and CESA6. Assembly with CESA3 and CESA6
CC is required for functional complex in primary cell wall cellulose
CC synthesis. Interacts with STL1 and STL2, but not with GOT1
CC (PubMed:27277162). Binds to CSI1 (PubMed:20616083).
CC {ECO:0000269|PubMed:17878302, ECO:0000269|PubMed:17878303,
CC ECO:0000269|PubMed:20616083, ECO:0000269|PubMed:27277162}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in germinating seeds, seedlings, roots,
CC stems, shoots leaves and flowers, but not in mature flowers.
CC {ECO:0000269|PubMed:11148287, ECO:0000269|PubMed:11517344,
CC ECO:0000269|PubMed:12068120, ECO:0000269|PubMed:12481071}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout the embryo during all steps
CC of embryogenesis, and decrease toward the bent-cotyledon stage. Higher
CC levels in tissues undergoing primary cell wall formation, and drop of
CC expression when secondary wall synthesis takes place. High levels in
CC developing seedlings and elongating stems, with a decrease at later
CC growth stages. {ECO:0000269|PubMed:11148287,
CC ECO:0000269|PubMed:12481071}.
CC -!- PTM: S-acylated. {ECO:0000269|PubMed:27387950}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. Plant
CC cellulose synthase subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD95078.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF027172; AAC39334.1; -; Genomic_DNA.
DR EMBL; AL034567; CAA22568.1; -; Genomic_DNA.
DR EMBL; AL161581; CAB79958.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86053.1; -; Genomic_DNA.
DR EMBL; BT008654; AAP40467.1; -; mRNA.
DR EMBL; AK222115; BAD95078.1; ALT_INIT; mRNA.
DR EMBL; AK226243; BAE98406.1; -; mRNA.
DR PIR; T05351; T05351.
DR RefSeq; NP_194967.1; NM_119393.3.
DR AlphaFoldDB; O48946; -.
DR SMR; O48946; -.
DR BioGRID; 14662; 11.
DR DIP; DIP-59354N; -.
DR IntAct; O48946; 2.
DR STRING; 3702.AT4G32410.1; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR TCDB; 4.D.3.1.4; the glycan glucosyl transferase (opgh) family.
DR iPTMnet; O48946; -.
DR SwissPalm; O48946; -.
DR PaxDb; O48946; -.
DR PRIDE; O48946; -.
DR ProteomicsDB; 220543; -.
DR EnsemblPlants; AT4G32410.1; AT4G32410.1; AT4G32410.
DR GeneID; 829376; -.
DR Gramene; AT4G32410.1; AT4G32410.1; AT4G32410.
DR KEGG; ath:AT4G32410; -.
DR Araport; AT4G32410; -.
DR TAIR; locus:2127776; AT4G32410.
DR eggNOG; ENOG502QQJD; Eukaryota.
DR HOGENOM; CLU_001418_0_2_1; -.
DR InParanoid; O48946; -.
DR OMA; HESDGGT; -.
DR OrthoDB; 679241at2759; -.
DR PhylomeDB; O48946; -.
DR BioCyc; MetaCyc:MON-2361; -.
DR UniPathway; UPA00695; -.
DR PRO; PR:O48946; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O48946; baseline and differential.
DR Genevisible; O48946; 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: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:0042538; P:hyperosmotic salinity response; IMP:TAIR.
DR GO; GO:0009833; P:plant-type primary 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; 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 Acetylation; Cell membrane; Cell wall biogenesis/degradation;
KW Cellulose biosynthesis; Coiled coil; Glycoprotein; Glycosyltransferase;
KW Lipoprotein; Membrane; Metal-binding; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix; Zinc; Zinc-finger.
FT CHAIN 1..1081
FT /note="Cellulose synthase A catalytic subunit 1 [UDP-
FT forming]"
FT /id="PRO_0000166367"
FT TOPO_DOM 1..270
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 292..299
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 300..320
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 321..856
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 857..877
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 878..889
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 890..910
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 911..925
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 926..946
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 947..976
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 977..997
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 998..1008
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1009..1029
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1030..1038
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1039..1059
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1060..1081
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ZN_FING 39..85
FT /note="RING-type; degenerate"
FT REGION 117..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 449..476
FT /evidence="ECO:0000255"
FT COMPBIAS 153..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 395
FT /evidence="ECO:0000255"
FT ACT_SITE 780
FT /evidence="ECO:0000255"
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 42
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 58
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 61
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 561
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 563
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CARBOHYD 953
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 549
FT /note="A->V: In rsw1-1; temperature-sensitive disassembly
FT of cellulose synthase complexes ('rosettes') and altered
FT cellulose crystallinity, accumulation of noncrystalline
FT beta-1,4-glucan, normal below 21 degrees Celsius but not
FT above 30 degrees Celsius, accumulation of starch in roots,
FT constitutive and high expression of vegetative storage
FT proteins (VSP) and widespread morphological abnormalities."
FT /evidence="ECO:0000269|PubMed:10987560,
FT ECO:0000269|PubMed:11732051, ECO:0000269|PubMed:11732056,
FT ECO:0000269|PubMed:12119374, ECO:0000269|PubMed:9445479"
FT MUTAGEN 631
FT /note="G->S: In rsw1-2; abnormal embryos, very short and
FT stout plants, reduced crystalline cellulose deposition in
FT cell walls, and restricted intercellular spaces due to
FT increased cell junction thickness."
FT /evidence="ECO:0000269|PubMed:11901167"
FT MUTAGEN 779
FT /note="E->K: In rsw1-45; abnormal embryos, short and stout
FT plants, and reduced crystalline cellulose deposition in
FT cell walls."
FT /evidence="ECO:0000269|PubMed:12481071"
FT MUTAGEN 780
FT /note="D->N: In rsw1-20; abnormal embryos, short and stout
FT plants, reduced crystalline cellulose deposition in cell
FT walls, and restricted intercellular spaces due to increased
FT cell junction thickness."
FT /evidence="ECO:0000269|PubMed:12481071"
SQ SEQUENCE 1081 AA; 122237 MW; BDEB5D9DEE334D59 CRC64;
MEASAGLVAG SYRRNELVRI RHESDGGTKP LKNMNGQICQ ICGDDVGLAE TGDVFVACNE
CAFPVCRPCY EYERKDGTQC CPQCKTRFRR HRGSPRVEGD EDEDDVDDIE NEFNYAQGAN
KARHQRHGEE FSSSSRHESQ PIPLLTHGHT VSGEIRTPDT QSVRTTSGPL GPSDRNAISS
PYIDPRQPVP VRIVDPSKDL NSYGLGNVDW KERVEGWKLK QEKNMLQMTG KYHEGKGGEI
EGTGSNGEEL QMADDTRLPM SRVVPIPSSR LTPYRVVIIL RLIILCFFLQ YRTTHPVKNA
YPLWLTSVIC EIWFAFSWLL DQFPKWYPIN RETYLDRLAI RYDRDGEPSQ LVPVDVFVST
VDPLKEPPLV TANTVLSILS VDYPVDKVAC YVSDDGSAML TFESLSETAE FAKKWVPFCK
KFNIEPRAPE FYFAQKIDYL KDKIQPSFVK ERRAMKREYE EFKVRINALV AKAQKIPEEG
WTMQDGTPWP GNNTRDHPGM IQVFLGHSGG LDTDGNELPR LIYVSREKRP GFQHHKKAGA
MNALIRVSAV LTNGAYLLNV DCDHYFNNSK AIKEAMCFMM DPAIGKKCCY VQFPQRFDGI
DLHDRYANRN IVFFDINMKG LDGIQGPVYV GTGCCFNRQA LYGYDPVLTE EDLEPNIIVK
SCCGSRKKGK SSKKYNYEKR RGINRSDSNA PLFNMEDIDE GFEGYDDERS ILMSQRSVEK
RFGQSPVFIA ATFMEQGGIP PTTNPATLLK EAIHVISCGY EDKTEWGKEI GWIYGSVTED
ILTGFKMHAR GWISIYCNPP RPAFKGSAPI NLSDRLNQVL RWALGSIEIL LSRHCPIWYG
YHGRLRLLER IAYINTIVYP ITSIPLIAYC ILPAFCLITD RFIIPEISNY ASIWFILLFI
SIAVTGILEL RWSGVSIEDW WRNEQFWVIG GTSAHLFAVF QGLLKVLAGI DTNFTVTSKA
TDEDGDFAEL YIFKWTALLI PPTTVLLVNL IGIVAGVSYA VNSGYQSWGP LFGKLFFALW
VIAHLYPFLK GLLGRQNRTP TIVIVWSVLL ASIFSLLWVR INPFVDANPN ANNFNGKGGV
F
