Cellulose synthase A catalytic subunit 3 [UDP-forming] - Arabidopsis thaliana (Mouse-ear cress)

Contribute

Send feedback

Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q941L0 (CESA3_ARATH)

Last modified July 7, 2009. Version 56. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data |

Customize display

text xml rdf/xml gff fasta

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein names

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

Gene names

Name:	CESA3
Synonyms:	ATHB, CEV1, ELI1, IXR1, RSW5
Ordered Locus Names:	At5g05170
ORF Names:	K2A11.4

Organism

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

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Hide | Top

Protein attributes

Sequence length	1065 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

Hide | Top

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, especially in roots. Ref.6 Ref.9 Ref.10 Ref.17 Ref.18
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 CESA1 and CESA6. Ref.17 Ref.18
Subcellular location	Cell membrane; Multi-pass membrane protein Probable.
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. Ref.9 Ref.10 Ref.7 Ref.11
Developmental stage	Mostly expressed in cotyledons during all steps of embryogenesis, and decrease toward the bent-cotyledon stage. Ref.11
Post-translational modification	Phosphorylation level varies significantly during early response to general elicitors.
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. Ref.6
Sequence similarities	Belongs to the glycosyltransferase 2 family. Plant cellulose synthase subfamily. Contains 1 RING-type zinc finger.

Hide | Top

Ontologies

Keywords
Biological process	Cell wall biogenesis/degradation Cellulose biosynthesis
Cellular component	Cell membrane Membrane
Domain	Coiled coil Transmembrane Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Glycosyltransferase Transferase
PTM	Glycoprotein Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW cellulose biosynthetic process Ref.10 Inferred from mutant phenotype. Source: TAIR defense response Traceable author statement. Source: TAIR primary cell wall biogenesis Ref.10 Inferred from mutant phenotype. Source: TAIR
Cellular component	Golgi apparatus Inferred from direct assay. Source: TAIR integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Ref.15 Inferred from direct assay. Source: TAIR
Molecular function	cellulose synthase (UDP-forming) activity Inferred from electronic annotation. Source: EC protein binding Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1065

1065

Cellulose synthase A catalytic subunit 3 [UDP-forming]

PRO_0000166369

Regions

Topological domain

1 – 260

260

Cytoplasmic Potential

Transmembrane

261 – 281

Potential

Topological domain

282 – 283

Extracellular Potential

Transmembrane

284 – 304

Potential

Topological domain

305 – 842

538

Cytoplasmic Potential

Transmembrane

843 – 863

Potential

Topological domain

864 – 874

Extracellular Potential

Transmembrane

875 – 895

Potential

Topological domain

896 – 910

Cytoplasmic Potential

Transmembrane

911 – 931

Potential

Topological domain

932 – 961

Extracellular Potential

Transmembrane

962 – 982

Potential

Topological domain

983 – 993

Cytoplasmic Potential

Transmembrane

994 – 1014

Potential

Topological domain

1015 – 1023

Extracellular Potential

Transmembrane

1024 – 1044

Potential

Topological domain

1045 – 1065

Cytoplasmic Potential

Zinc finger

20 – 66

RING-type; degenerate

Coiled coil

433 – 457

Potential

Compositional bias

633 – 664

Lys-rich

Sites

Active site

379

Potential

Active site

765

Potential

Metal binding

Zinc 1 By similarity

Metal binding

Zinc 1 By similarity

Metal binding

Zinc 2 By similarity

Metal binding

Zinc 2 By similarity

Metal binding

Zinc 1 By similarity

Metal binding

Zinc 1 By similarity

Metal binding

Zinc 2 By similarity

Metal binding

Zinc 2 By similarity

Binding site

545

Substrate Potential

Binding site

547

Substrate Potential

Amino acid modifications

Modified residue

Phosphoserine Ref.13 Ref.16

Modified residue

151

Phosphoserine Ref.13 Ref.16 Ref.15

Modified residue

211

Phosphoserine Ref.13 Ref.16

Modified residue

216

Phosphoserine Ref.13 Ref.16

Glycosylation

938

N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis

301

S → F in eli1-1; reduced cellulose synthesis and aberrant deposition of lignin. Ref.12

Mutagenesis

522

A → V in eli1-2; reduced cellulose synthesis and aberrant deposition of lignin.

Mutagenesis

617

G → E in cev1; reduced amount of crystalline cellulose in roots. Ref.6 Ref.9 Ref.8

Mutagenesis

942

T → I in ixr1-2; confers resistance to the herbicides isoxaben and thiazolidinones. Ref.7

Mutagenesis

998

G → D in ixr1-1; confers resistance to the herbicides isoxaben and thiazolidinones. Ref.7

Mutagenesis

1056

P → S in rsw5; reduction of cellulose synthesis, and temperature sensitive. Ref.14

Sequence conflict

377

S → F in AAC39336. Ref.1

Sequence conflict

479

R → G in AAC39336. Ref.1

Sequence conflict

858

P → L in AAC39336. Ref.1

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

Q941L0-1 [UniParc].

Last modified August 30, 2005. Version 2.
Checksum: 3AA4714CE3C4D581
Show »

FASTA

1,065

119,683

        10         20         30         40         50         60 
MESEGETAGK PMKNIVPQTC QICSDNVGKT VDGDRFVACD ICSFPVCRPC YEYERKDGNQ 

        70         80         90        100        110        120 
SCPQCKTRYK RLKGSPAIPG DKDEDGLADE GTVEFNYPQK EKISERMLGW HLTRGKGEEM 

       130        140        150        160        170        180 
GEPQYDKEVS HNHLPRLTSR QDTSGEFSAA SPERLSVSST IAGGKRLPYS SDVNQSPNRR 

       190        200        210        220        230        240 
IVDPVGLGNV AWKERVDGWK MKQEKNTGPV STQAASERGG VDIDASTDIL ADEALLNDEA 

       250        260        270        280        290        300 
RQPLSRKVSI PSSRINPYRM VIMLRLVILC LFLHYRITNP VPNAFALWLV SVICEIWFAL 

       310        320        330        340        350        360 
SWILDQFPKW FPVNRETYLD RLALRYDREG EPSQLAAVDI FVSTVDPLKE PPLVTANTVL 

       370        380        390        400        410        420 
SILAVDYPVD KVSCYVSDDG AAMLSFESLA ETSEFARKWV PFCKKYSIEP RAPEWYFAAK 

       430        440        450        460        470        480 
IDYLKDKVQT SFVKDRRAMK REYEEFKIRI NALVSKALKC PEEGWVMQDG TPWPGNNTRD 

       490        500        510        520        530        540 
HPGMIQVFLG QNGGLDAEGN ELPRLVYVSR EKRPGFQHHK KAGAMNALVR VSAVLTNGPF 

       550        560        570        580        590        600 
ILNLDCDHYI NNSKALREAM CFLMDPNLGK QVCYVQFPQR FDGIDKNDRY ANRNTVFFDI 

       610        620        630        640        650        660 
NLRGLDGIQG PVYVGTGCVF NRTALYGYEP PIKVKHKKPS LLSKLCGGSR KKNSKAKKES 

       670        680        690        700        710        720 
DKKKSGRHTD STVPVFNLDD IEEGVEGAGF DDEKALLMSQ MSLEKRFGQS AVFVASTLME 

       730        740        750        760        770        780 
NGGVPPSATP ENLLKEAIHV ISCGYEDKSD WGMEIGWIYG SVTEDILTGF KMHARGWRSI 

       790        800        810        820        830        840 
YCMPKLPAFK GSAPINLSDR LNQVLRWALG SVEILFSRHC PIWYGYNGRL KFLERFAYVN 

       850        860        870        880        890        900 
TTIYPITSIP LLMYCTLPAV CLFTNQFIIP QISNIASIWF LSLFLSIFAT GILEMRWSGV 

       910        920        930        940        950        960 
GIDEWWRNEQ FWVIGGVSAH LFAVFQGILK VLAGIDTNFT VTSKASDEDG DFAELYLFKW 

       970        980        990       1000       1010       1020 
TTLLIPPTTL LIVNLVGVVA GVSYAINSGY QSWGPLFGKL FFAFWVIVHL YPFLKGLMGR 

      1030       1040       1050       1060 
QNRTPTIVVV WSVLLASIFS LLWVRIDPFT SRVTGPDILE CGINC

« Hide

Hide | Top

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: 9445479] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia.
[2]	"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." Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H., Miyajima N., Tabata S. DNA Res. 6:183-195(1999) [PubMed: 10470850] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"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. Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"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. Shinozaki K. Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 635-1065. Strain: cv. Columbia.
[5]	"Higher plant cellulose synthases." Richmond T. Genome Biol. 1:REVIEWS3001.1-REVIEWS3001.6(2000) [PubMed: 11178255] [Abstract] Cited for: GENE FAMILY, NOMENCLATURE.
[6]	"The Arabidopsis mutant cev1 has constitutively active jasmonate and ethylene signal pathways and enhanced resistance to pathogens." Ellis C., Turner J.G. Plant Cell 13:1025-1033(2001) [PubMed: 11340179] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF GLY-617, DISRUPTION PHENOTYPE.
[7]	"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: 11517344] [Abstract] Cited for: TISSUE SPECIFICITY, MUTAGENESIS OF THR-942 AND GLY-998.
[8]	"Constitutive activation of jasmonate signaling in an Arabidopsis mutant correlates with enhanced resistance to Erysiphe cichoracearum, Pseudomonas syringae, and Myzus persicae." Ellis C., Karafyllidis I., Turner J.G. Mol. Plant Microbe Interact. 15:1025-1030(2002) [PubMed: 12437300] [Abstract] Cited for: MUTAGENESIS OF GLY-617.
[9]	"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: 12119374] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY, MUTAGENESIS OF GLY-617.
[10]	"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: 12068120] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY.
[11]	"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: 12481071] [Abstract] Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[12]	"Reduced cellulose synthesis invokes lignification and defense responses in Arabidopsis thaliana." Cano-Delgado A., Penfield S., Smith C., Catley M., Bevan M. Plant J. 34:351-362(2003) [PubMed: 12713541] [Abstract] Cited for: FUNCTIO, MUTAGENESIS OF SER-301.
[13]	"Phosphoproteomics of the Arabidopsis plasma membrane and a new phosphorylation site database." Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C. Plant Cell 16:2394-2405(2004) [PubMed: 15308754] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; SER-151; SER-211 AND SER-216, MASS SPECTROMETRY.
[14]	"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." Wang J., Howles P.A., Cork A.H., Birch R.J., Williamson R.E. Plant Physiol. 142:685-695(2006) [PubMed: 16891551] [Abstract] Cited for: MUTAGENESIS OF PRO-1056.
[15]	"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: 17317660] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151, MASS SPECTROMETRY.
[16]	"Identification of cellulose synthase AtCesA7 (IRX3) in vivo phosphorylation sites -- a potential role in regulating protein degradation." Taylor N.G. Plant Mol. Biol. 64:161-171(2007) [PubMed: 17427041] [Abstract] Cited for: PHOSPHORYLATION AT SER-3; SER-151; SER-211 AND SER-216, MASS SPECTROMETRY.
[17]	"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: 17878302] [Abstract] Cited for: FUNCTION, SUBUNIT.
[18]	"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: 17878303] [Abstract] Cited for: FUNCTION, INTERACTION WITH CESA1 AND CESA6.

Hide | Top

Cross-references

Sequence databases
	AF027174 mRNA. Translation: AAC39336.1. AB018111 Genomic DNA. Translation: BAB09693.1. AY045960 mRNA. Translation: AAK76634.2. BT002335 mRNA. Translation: AAN86168.1. AK230097 mRNA. Translation: BAF01916.1.
IPI	IPI00528019.
PIR	T52054.
RefSeq	NP_196136.1.
UniGene	At.24338
3D structure databases
ModBase	Search...
Protein family/group databases
CAZy	GT2. Glycosyltransferase Family 2.
Proteomic databases
PRIDE	Q941L0.
Genome annotation databases
GeneID	830399.
GenomeReviews	Gene locus AT5G05170 in contig BA000015_GR.
KEGG	ath:AT5G05170.
NMPDR	fig\|3702.1.peg.22618.
Organism-specific databases
GeneFarm	5086. 484.
TAIR	At5g05170.
Phylogenomic databases
OMA	Q941L0. GGQVCQI.
Enzyme and pathway databases
BRENDA	2.4.1.12. 302.
Gene expression databases
GermOnline	AT5G05170. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR005150. Cellulose_synth. IPR001841. Znf_RING. IPR017907. Znf_RING_CS. [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. 1 hit. [Graphical view]
ProtoNet	Search...

Hide | Top

Entry information

Entry name

CESA3_ARATH

Accession

Primary (citable) accession number: Q941L0
Secondary accession number(s): O48948, Q0WLU1, Q9FHK6

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2005
Last sequence update:	August 30, 2005
Last modified:	July 7, 2009
This is version 56 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)

Hide | Top

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

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents