O48946 (CESA1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cellulose synthase A catalytic subunit 1 [UDP-forming]
Short name=AtCesA1
EC=2.4.1.12

Alternative name(s):
Protein RADIALLY SWOLLEN 1
Short name=AtRSW1

Gene names

Name:	CESA1
Synonyms:	RSW1
Ordered Locus Names:	At4g32410
ORF Names:	F8B4.110

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	1081 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Required during embryogenesis for cell elongation, orientation of cell expansion and complex cell wall formations, such as interdigitated pattern of epidermal pavement cells, stomatal guard cells and trichomes. Plays a role in lateral roots formation, but seems not necessary for the development of tip-growing cells such as root hairs. The presence of each protein CESA1 and CESA6 is critical for cell expansion after germination. Ref.1 Ref.7 Ref.8 Ref.10 Ref.11 Ref.12 Ref.14 Ref.15 Ref.18 Ref.19
Catalytic activity	UDP-glucose + (1,4-beta-D-glucosyl)(n) = UDP + (1,4-beta-D-glucosyl)(n+1).
Cofactor	Binds 2 zinc ions per subunit By similarity.
Pathway	Glycan metabolism; plant cellulose biosynthesis.
Subunit structure	Interacts with CESA3 and CESA6. Assembly with CESA3 and CESA6 is required for functional complex in primary cell wall cellulose synthesis. Ref.18 Ref.19
Subcellular location	Cell membrane; Multi-pass membrane protein Probable.
Tissue specificity	Expressed in germinating seeds, seedlings, roots, stems, shoots leaves and flowers, but not in mature flowers. Ref.8 Ref.9 Ref.14 Ref.15
Developmental stage	Expressed throughout the embryo during all steps of embryogenesis, and decrease toward the bent-cotyledon stage. Higher levels in tissues undergoing primary cell wall formation, and drop of expression when secondary wall synthesis takes place. High levels in developing seedlings and elongating stems, with a decrease at later growth stages. Ref.8 Ref.15
Post-translational modification	Phosphorylation level varies significantly during early response to general elicitors.
Sequence similarities	Belongs to the glycosyltransferase 2 family. Plant cellulose synthase subfamily. Contains 1 RING-type zinc finger.
Sequence caution	The sequence BAD95078.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Cell wall biogenesis/degradation Cellulose biosynthesis
Cellular component	Cell membrane Membrane
Domain	Coiled coil Transmembrane Transmembrane helix Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Glycosyltransferase Transferase
PTM	Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellulose biosynthetic process Inferred from mutant phenotype Ref.14. Source: TAIR hyperosmotic salinity response Inferred from mutant phenotype PubMed 18408158. Source: TAIR primary cell wall biogenesis Inferred from mutant phenotype Ref.14. Source: TAIR
Cellular_component	Golgi apparatus Inferred from direct assay PubMed 16618929PubMed 22430844PubMed 22923678. Source: TAIR endosome Inferred from direct assay PubMed 22923678. Source: TAIR integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from direct assay Ref.16Ref.17. Source: TAIR trans-Golgi network Inferred from direct assay PubMed 22923678. Source: TAIR
Molecular_function	cellulose synthase (UDP-forming) activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1081	1081	Cellulose synthase A catalytic subunit 1 [UDP-forming]		PRO_0000166367
Regions
	Topological domain	1 – 270	270	Cytoplasmic Potential
	Transmembrane	271 – 291	21	Helical; Potential
	Topological domain	292 – 299	8	Extracellular Potential
	Transmembrane	300 – 320	21	Helical; Potential
	Topological domain	321 – 856	536	Cytoplasmic Potential
	Transmembrane	857 – 877	21	Helical; Potential
	Topological domain	878 – 889	12	Extracellular Potential
	Transmembrane	890 – 910	21	Helical; Potential
	Topological domain	911 – 925	15	Cytoplasmic Potential
	Transmembrane	926 – 946	21	Helical; Potential
	Topological domain	947 – 976	30	Extracellular Potential
	Transmembrane	977 – 997	21	Helical; Potential
	Topological domain	998 – 1008	11	Cytoplasmic Potential
	Transmembrane	1009 – 1029	21	Helical; Potential
	Topological domain	1030 – 1038	9	Extracellular Potential
	Transmembrane	1039 – 1059	21	Helical; Potential
	Topological domain	1060 – 1081	22	Cytoplasmic Potential
	Zinc finger	39 – 85	47	RING-type; degenerate
	Coiled coil	449 – 476	28	Potential
Sites
	Active site	395	1	Potential
	Active site	780	1	Potential
	Metal binding	39	1	Zinc 1 By similarity
	Metal binding	42	1	Zinc 1 By similarity
	Metal binding	58	1	Zinc 2 By similarity
	Metal binding	61	1	Zinc 2 By similarity
	Metal binding	66	1	Zinc 1 By similarity
	Metal binding	69	1	Zinc 1 By similarity
	Metal binding	81	1	Zinc 2 By similarity
	Metal binding	84	1	Zinc 2 By similarity
	Binding site	561	1	Substrate Potential
	Binding site	563	1	Substrate Potential
Amino acid modifications
	Modified residue	165	1	Phosphothreonine Ref.16
	Modified residue	167	1	Phosphoserine Ref.16 Ref.20
	Modified residue	180	1	Phosphoserine Ref.17 Ref.20
	Glycosylation	953	1	N-linked (GlcNAc...) Potential
Experimental info
	Mutagenesis	549	1	A → V in rsw1-1; temperature-sensitive disassembly of cellulose synthase complexes ('rosettes') and altered cellulose crystallinity, accumulation of noncrystalline beta-1,4-glucan, normal below 21 degrees Celsius but not above 30 degrees Celsius, accumulation of starch in roots, constitutive and high expression of vegetative storage proteins (VSP) and widespread morphological abnormalities. Ref.1 Ref.7 Ref.10 Ref.11 Ref.13
	Mutagenesis	631	1	G → S in rsw1-2; abnormal embryos, very short and stout plants, reduced crystalline cellulose deposition in cell walls, and restricted intercellular spaces due to increased cell junction thickness. Ref.12
	Mutagenesis	779	1	E → K in rsw1-45; abnormal embryos, short and stout plants, and reduced crystalline cellulose deposition in cell walls. Ref.15
	Mutagenesis	780	1	D → N in rsw1-20; abnormal embryos, short and stout plants, reduced crystalline cellulose deposition in cell walls, and restricted intercellular spaces due to increased cell junction thickness. Ref.15

Sequences

	Sequence		Length	Mass (Da)
	O48946 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: BDEB5D9DEE334D59	FASTA	1,081	122,237
	10 20 30 40 50 60 MEASAGLVAG SYRRNELVRI RHESDGGTKP LKNMNGQICQ ICGDDVGLAE TGDVFVACNE 70 80 90 100 110 120 CAFPVCRPCY EYERKDGTQC CPQCKTRFRR HRGSPRVEGD EDEDDVDDIE NEFNYAQGAN 130 140 150 160 170 180 KARHQRHGEE FSSSSRHESQ PIPLLTHGHT VSGEIRTPDT QSVRTTSGPL GPSDRNAISS 190 200 210 220 230 240 PYIDPRQPVP VRIVDPSKDL NSYGLGNVDW KERVEGWKLK QEKNMLQMTG KYHEGKGGEI 250 260 270 280 290 300 EGTGSNGEEL QMADDTRLPM SRVVPIPSSR LTPYRVVIIL RLIILCFFLQ YRTTHPVKNA 310 320 330 340 350 360 YPLWLTSVIC EIWFAFSWLL DQFPKWYPIN RETYLDRLAI RYDRDGEPSQ LVPVDVFVST 370 380 390 400 410 420 VDPLKEPPLV TANTVLSILS VDYPVDKVAC YVSDDGSAML TFESLSETAE FAKKWVPFCK 430 440 450 460 470 480 KFNIEPRAPE FYFAQKIDYL KDKIQPSFVK ERRAMKREYE EFKVRINALV AKAQKIPEEG 490 500 510 520 530 540 WTMQDGTPWP GNNTRDHPGM IQVFLGHSGG LDTDGNELPR LIYVSREKRP GFQHHKKAGA 550 560 570 580 590 600 MNALIRVSAV LTNGAYLLNV DCDHYFNNSK AIKEAMCFMM DPAIGKKCCY VQFPQRFDGI 610 620 630 640 650 660 DLHDRYANRN IVFFDINMKG LDGIQGPVYV GTGCCFNRQA LYGYDPVLTE EDLEPNIIVK 670 680 690 700 710 720 SCCGSRKKGK SSKKYNYEKR RGINRSDSNA PLFNMEDIDE GFEGYDDERS ILMSQRSVEK 730 740 750 760 770 780 RFGQSPVFIA ATFMEQGGIP PTTNPATLLK EAIHVISCGY EDKTEWGKEI GWIYGSVTED 790 800 810 820 830 840 ILTGFKMHAR GWISIYCNPP RPAFKGSAPI NLSDRLNQVL RWALGSIEIL LSRHCPIWYG 850 860 870 880 890 900 YHGRLRLLER IAYINTIVYP ITSIPLIAYC ILPAFCLITD RFIIPEISNY ASIWFILLFI 910 920 930 940 950 960 SIAVTGILEL RWSGVSIEDW WRNEQFWVIG GTSAHLFAVF QGLLKVLAGI DTNFTVTSKA 970 980 990 1000 1010 1020 TDEDGDFAEL YIFKWTALLI PPTTVLLVNL IGIVAGVSYA VNSGYQSWGP LFGKLFFALW 1030 1040 1050 1060 1070 1080 VIAHLYPFLK GLLGRQNRTP TIVIVWSVLL ASIFSLLWVR INPFVDANPN ANNFNGKGGV F

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular analysis of cellulose biosynthesis in Arabidopsis." 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. Science 279:717-720(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, MUTAGENESIS OF ALA-549. Strain: cv. Columbia.
[2]	"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R. Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[4]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." 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. Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs." 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. Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[6]	"Higher plant cellulose synthases." Richmond T. Genome Biol. 1:REVIEWS3001.1-REVIEWS3001.6(2000) [PubMed] [Europe PMC] [Abstract] Cited for: GENE FAMILY, NOMENCLATURE.
[7]	"Fractionation of carbohydrates in Arabidopsis root cell walls shows that three radial swelling loci are specifically involved in cellulose production." Peng L., Hocart C.H., Redmond J.W., Williamson R.E. Planta 211:406-414(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF ALA-549.
[8]	"PROCUSTE1 encodes a cellulose synthase required for normal cell elongation specifically in roots and dark-grown hypocotyls of Arabidopsis." Fagard M., Desnos T., Desprez T., Goubet F., Refregier G., Mouille G., McCann M., Rayon C., Vernhettes S., Hoefte H. Plant Cell 12:2409-2423(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[9]	"Modifications of cellulose synthase confer resistance to isoxaben and thiazolidinone herbicides in Arabidopsis Ixr1 mutants." Scheible W.-R., Eshed R., Richmond T., Delmer D., Somerville C. Proc. Natl. Acad. Sci. U.S.A. 98:10079-10084(2001) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[10]	"Morphology of rsw1, a cellulose-deficient mutant of Arabidopsis thaliana." Williamson R.E., Burn J.E., Birch R., Baskin T.I., Arioli T., Betzner A.S., Cork A. Protoplasma 215:116-127(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF ALA-549.
[11]	"Wall architecture in the cellulose-deficient rsw1 mutant of Arabidopsis thaliana: microfibrils but not microtubules lose their transverse alignment before microfibrils become unrecognizable in the mitotic and elongation zones of roots." Sugimoto K., Williamson R.E., Wasteneys G.O. Protoplasma 215:172-183(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF ALA-549.
[12]	"Alpha-glucosidase I is required for cellulose biosynthesis and morphogenesis in Arabidopsis." Gillmor C.S., Poindexter P., Lorieau J., Palcic M.M., Somerville C. J. Cell Biol. 156:1003-1013(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF GLY-631.
[13]	"The Arabidopsis mutant cev1 links cell wall signaling to jasmonate and ethylene responses." Ellis C., Karafyllidis I., Wasternack C., Turner J.G. Plant Cell 14:1557-1566(2002) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF ALA-549.
[14]	"Functional analysis of the cellulose synthase genes CesA1, CesA2, and CesA3 in Arabidopsis." Burn J.E., Hocart C.H., Birch R.J., Cork A.C., Williamson R.E. Plant Physiol. 129:797-807(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY.
[15]	"Genetic complexity of cellulose synthase A gene function in Arabidopsis embryogenesis." Beeckman T., Przemeck G.K.H., Stamatiou G., Lau R., Terryn N., De Rycke R., Inze D., Berleth T. Plant Physiol. 130:1883-1893(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, MUTAGENESIS OF GLU-779 AND ASP-780.
[16]	"Large-scale analysis of in vivo phosphorylated membrane proteins by immobilized metal ion affinity chromatography and mass spectrometry." Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C. Mol. Cell. Proteomics 2:1234-1243(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-165 AND SER-167, MASS SPECTROMETRY. Strain: cv. La-0.
[17]	"Quantitative phosphoproteomics of early elicitor signaling in Arabidopsis." Benschop J.J., Mohammed S., O'Flaherty M., Heck A.J.R., Slijper M., Menke F.L.H. Mol. Cell. Proteomics 6:1198-1214(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-180, MASS SPECTROMETRY. Strain: cv. Columbia.
[18]	"Genetic evidence for three unique components in primary cell-wall cellulose synthase complexes in Arabidopsis." Persson S., Paredez A., Carroll A., Palsdottir H., Doblin M., Poindexter P., Khitrov N., Auer M., Somerville C.R. Proc. Natl. Acad. Sci. U.S.A. 104:15566-15571(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBUNIT.
[19]	"Organization of cellulose synthase complexes involved in primary cell wall synthesis in Arabidopsis thaliana." Desprez T., Juraniec M., Crowell E.F., Jouy H., Pochylova Z., Parcy F., Hoefte H., Gonneau M., Vernhettes S. Proc. Natl. Acad. Sci. U.S.A. 104:15572-15577(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH CESA3 AND CESA6.
[20]	"Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks." Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S. Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167 AND SER-180, MASS SPECTROMETRY. Strain: cv. Columbia. Tissue: Seedling.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF027172 Genomic DNA. Translation: AAC39334.1. AL034567 Genomic DNA. Translation: CAA22568.1. AL161581 Genomic DNA. Translation: CAB79958.1. CP002687 Genomic DNA. Translation: AEE86053.1. BT008654 mRNA. Translation: AAP40467.1. AK222115 mRNA. Translation: BAD95078.1. Different initiation. AK226243 mRNA. Translation: BAE98406.1.
IPI	IPI00536785.
PIR	T05351.
RefSeq	NP_194967.1. NM_119393.2.
UniGene	At.21246.
3D structure databases
ProteinModelPortal	O48946.
SMR	O48946. Positions 27-97, 535-591.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-59354N.
Protein family/group databases
CAZy	GT2. Glycosyltransferase Family 2.
Proteomic databases
PaxDb	O48946.
PRIDE	O48946.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT4G32410.1; AT4G32410.1; AT4G32410.
GeneID	829376.
KEGG	ath:AT4G32410.
Organism-specific databases
GeneFarm	5084. 484.
TAIR	At4g32410.
Phylogenomic databases
eggNOG	COG1215.
HOGENOM	HOG000241942.
InParanoid	O48946.
KO	K10999.
OMA	KQDKNMM.
PhylomeDB	O48946.
ProtClustDB	PLN02400.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-2361.
UniPathway	UPA00695.
Gene expression databases
Genevestigator	O48946.
GermOnline	AT4G32410. Arabidopsis thaliana.
Family and domain databases
Gene3D	3.30.40.10. 1 hit.
InterPro	IPR005150. Cellulose_synth. IPR001841. Znf_RING. IPR013083. Znf_RING/FYVE/PHD. [Graphical view]
Pfam	PF03552. Cellulose_synt. 1 hit. [Graphical view]
SMART	SM00184. RING. 1 hit. [Graphical view]
PROSITE	PS00518. ZF_RING_1. False negative. PS50089. ZF_RING_2. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CESA1_ARATH

Accession

Primary (citable) accession number: O48946
Secondary accession number(s): Q0WWU2, Q56WC7

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2005
Last sequence update:	June 1, 1998
Last modified:	May 1, 2013
This is version 100 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program