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O48946 (CESA1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length1081 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10811081Cellulose synthase A catalytic subunit 1 [UDP-forming]
PRO_0000166367

Regions

Topological domain1 – 270270Cytoplasmic Potential
Transmembrane271 – 29121Helical; Potential
Topological domain292 – 2998Extracellular Potential
Transmembrane300 – 32021Helical; Potential
Topological domain321 – 856536Cytoplasmic Potential
Transmembrane857 – 87721Helical; Potential
Topological domain878 – 88912Extracellular Potential
Transmembrane890 – 91021Helical; Potential
Topological domain911 – 92515Cytoplasmic Potential
Transmembrane926 – 94621Helical; Potential
Topological domain947 – 97630Extracellular Potential
Transmembrane977 – 99721Helical; Potential
Topological domain998 – 100811Cytoplasmic Potential
Transmembrane1009 – 102921Helical; Potential
Topological domain1030 – 10389Extracellular Potential
Transmembrane1039 – 105921Helical; Potential
Topological domain1060 – 108122Cytoplasmic Potential
Zinc finger39 – 8547RING-type; degenerate
Coiled coil449 – 47628 Potential

Sites

Active site3951 Potential
Active site7801 Potential
Metal binding391Zinc 1 By similarity
Metal binding421Zinc 1 By similarity
Metal binding581Zinc 2 By similarity
Metal binding611Zinc 2 By similarity
Metal binding661Zinc 1 By similarity
Metal binding691Zinc 1 By similarity
Metal binding811Zinc 2 By similarity
Metal binding841Zinc 2 By similarity
Binding site5611Substrate Potential
Binding site5631Substrate Potential

Amino acid modifications

Modified residue1651Phosphothreonine Ref.16
Modified residue1671Phosphoserine Ref.16 Ref.20
Modified residue1801Phosphoserine Ref.17 Ref.20
Glycosylation9531N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis5491A → 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
Mutagenesis6311G → 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
Mutagenesis7791E → K in rsw1-45; abnormal embryos, short and stout plants, and reduced crystalline cellulose deposition in cell walls. Ref.15
Mutagenesis7801D → 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 LengthMass (Da)Tools
O48946 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: BDEB5D9DEE334D59

FASTA1,081122,237
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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.
IPIIPI00536785.
PIRT05351.
RefSeqNP_194967.1. NM_119393.2.
UniGeneAt.21246.

3D structure databases

ProteinModelPortalO48946.
SMRO48946. Positions 27-97, 535-591.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-59354N.

Protein family/group databases

CAZyGT2. Glycosyltransferase Family 2.

Proteomic databases

PaxDbO48946.
PRIDEO48946.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G32410.1; AT4G32410.1; AT4G32410.
GeneID829376.
KEGGath:AT4G32410.

Organism-specific databases

GeneFarm5084. 484.
TAIRAt4g32410.

Phylogenomic databases

eggNOGCOG1215.
HOGENOMHOG000241942.
InParanoidO48946.
KOK10999.
OMAKQDKNMM.
PhylomeDBO48946.
ProtClustDBPLN02400.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-2361.
UniPathwayUPA00695.

Gene expression databases

GenevestigatorO48946.
GermOnlineAT4G32410. Arabidopsis thaliana.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR005150. Cellulose_synth.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamPF03552. Cellulose_synt. 1 hit.
[Graphical view]
SMARTSM00184. RING. 1 hit.
[Graphical view]
PROSITEPS00518. ZF_RING_1. False negative.
PS50089. ZF_RING_2. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCESA1_ARATH
AccessionPrimary (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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families