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Protein

Cellulose synthase A catalytic subunit 3 [UDP-forming]

Gene

CESA3

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.6 Publications

Catalytic activityi

UDP-glucose + (1,4-beta-D-glucosyl)(n) = UDP + (1,4-beta-D-glucosyl)(n+1).

Cofactori

Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit.By similarity

Pathwayi: plant cellulose biosynthesis

This protein is involved in the pathway plant cellulose biosynthesis, which is part of Glycan metabolism.
View all proteins of this organism that are known to be involved in the pathway plant cellulose biosynthesis and in Glycan metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi20 – 201Zinc 1By similarity
Metal bindingi23 – 231Zinc 1By similarity
Metal bindingi39 – 391Zinc 2By similarity
Metal bindingi42 – 421Zinc 2By similarity
Metal bindingi47 – 471Zinc 1By similarity
Metal bindingi50 – 501Zinc 1By similarity
Metal bindingi62 – 621Zinc 2By similarity
Metal bindingi65 – 651Zinc 2By similarity
Active sitei379 – 3791Sequence analysis
Binding sitei545 – 5451SubstrateSequence analysis
Binding sitei547 – 5471SubstrateSequence analysis
Active sitei765 – 7651Sequence analysis

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri20 – 6647RING-type; degeneratePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • cellulose biosynthetic process Source: TAIR
  • cell wall organization Source: UniProtKB-KW
  • defense response Source: TAIR
  • plant-type primary cell wall biogenesis Source: TAIR
  • plant-type secondary cell wall biogenesis Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Cell wall biogenesis/degradation, Cellulose biosynthesis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-2362.
BRENDAi2.4.1.12. 399.
UniPathwayiUPA00695.

Protein family/group databases

CAZyiGT2. Glycosyltransferase Family 2.
TCDBi4.D.3.1.4. the glycan glucosyl transferase (opgh) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Cellulose synthase A catalytic subunit 3 [UDP-forming] (EC:2.4.1.12)
Short name:
AtCesA3
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 namesi
Name:CESA3
Synonyms:ATHB, CEV1, ELI1, IXR1, RSW5
Ordered Locus Names:At5g05170
ORF Names:K2A11.4
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G05170.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 260260CytoplasmicSequence analysisAdd
BLAST
Transmembranei261 – 28121HelicalSequence analysisAdd
BLAST
Topological domaini282 – 2832ExtracellularSequence analysis
Transmembranei284 – 30421HelicalSequence analysisAdd
BLAST
Topological domaini305 – 842538CytoplasmicSequence analysisAdd
BLAST
Transmembranei843 – 86321HelicalSequence analysisAdd
BLAST
Topological domaini864 – 87411ExtracellularSequence analysisAdd
BLAST
Transmembranei875 – 89521HelicalSequence analysisAdd
BLAST
Topological domaini896 – 91015CytoplasmicSequence analysisAdd
BLAST
Transmembranei911 – 93121HelicalSequence analysisAdd
BLAST
Topological domaini932 – 96130ExtracellularSequence analysisAdd
BLAST
Transmembranei962 – 98221HelicalSequence analysisAdd
BLAST
Topological domaini983 – 99311CytoplasmicSequence analysisAdd
BLAST
Transmembranei994 – 101421HelicalSequence analysisAdd
BLAST
Topological domaini1015 – 10239ExtracellularSequence analysis
Transmembranei1024 – 104421HelicalSequence analysisAdd
BLAST
Topological domaini1045 – 106521CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • endosome Source: TAIR
  • Golgi apparatus Source: TAIR
  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: TAIR
  • plasmodesma Source: TAIR
  • trans-Golgi network Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

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.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi301 – 3011S → F in eli1-1; reduced cellulose synthesis and aberrant deposition of lignin. 1 Publication
Mutagenesisi522 – 5221A → V in eli1-2; reduced cellulose synthesis and aberrant deposition of lignin.
Mutagenesisi617 – 6171G → E in cev1; reduced amount of crystalline cellulose in roots. 3 Publications
Mutagenesisi942 – 9421T → I in ixr1-2; confers resistance to the herbicides isoxaben and thiazolidinones. 1 Publication
Mutagenesisi998 – 9981G → D in ixr1-1; confers resistance to the herbicides isoxaben and thiazolidinones. 1 Publication
Mutagenesisi1056 – 10561P → S in rsw5; reduction of cellulose synthesis, and temperature sensitive. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10651065Cellulose synthase A catalytic subunit 3 [UDP-forming]PRO_0000166369Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei3 – 31PhosphoserineCombined sources1 Publication
Modified residuei151 – 1511PhosphoserineCombined sources1 Publication
Modified residuei211 – 2111Phosphoserine1 Publication
Modified residuei216 – 2161PhosphoserineCombined sources1 Publication
Glycosylationi938 – 9381N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ941L0.
PRIDEiQ941L0.

PTM databases

iPTMnetiQ941L0.
SwissPalmiQ941L0.

Expressioni

Tissue specificityi

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.4 Publications

Developmental stagei

Mostly expressed in cotyledons during all steps of embryogenesis, and decrease toward the bent-cotyledon stage.1 Publication

Gene expression databases

ExpressionAtlasiQ941L0. baseline and differential.
GenevisibleiQ941L0. AT.

Interactioni

Subunit structurei

Interacts with CESA1 and CESA6.2 Publications

Protein-protein interaction databases

BioGridi15678. 45 interactions.
DIPiDIP-46437N.
IntActiQ941L0. 1 interaction.
STRINGi3702.AT5G05170.1.

Structurei

3D structure databases

ProteinModelPortaliQ941L0.
SMRiQ941L0. Positions 3-78.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili433 – 45725Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi633 – 66432Lys-richAdd
BLAST

Sequence similaritiesi

Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri20 – 6647RING-type; degeneratePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix, Zinc-finger

Phylogenomic databases

eggNOGiENOG410II8I. Eukaryota.
COG1215. LUCA.
HOGENOMiHOG000241942.
InParanoidiQ941L0.
KOiK10999.
OMAiVHGEENE.
OrthoDBiEOG093600MD.
PhylomeDBiQ941L0.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR005150. Cellulose_synth.
IPR027934. CES_Znf_RING.
IPR029044. Nucleotide-diphossugar_trans.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF03552. Cellulose_synt. 1 hit.
PF14569. zf-UDP. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 3 hits.
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q941L0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MESEGETAGK PMKNIVPQTC QICSDNVGKT VDGDRFVACD ICSFPVCRPC
60 70 80 90 100
YEYERKDGNQ SCPQCKTRYK RLKGSPAIPG DKDEDGLADE GTVEFNYPQK
110 120 130 140 150
EKISERMLGW HLTRGKGEEM GEPQYDKEVS HNHLPRLTSR QDTSGEFSAA
160 170 180 190 200
SPERLSVSST IAGGKRLPYS SDVNQSPNRR IVDPVGLGNV AWKERVDGWK
210 220 230 240 250
MKQEKNTGPV STQAASERGG VDIDASTDIL ADEALLNDEA RQPLSRKVSI
260 270 280 290 300
PSSRINPYRM VIMLRLVILC LFLHYRITNP VPNAFALWLV SVICEIWFAL
310 320 330 340 350
SWILDQFPKW FPVNRETYLD RLALRYDREG EPSQLAAVDI FVSTVDPLKE
360 370 380 390 400
PPLVTANTVL SILAVDYPVD KVSCYVSDDG AAMLSFESLA ETSEFARKWV
410 420 430 440 450
PFCKKYSIEP RAPEWYFAAK IDYLKDKVQT SFVKDRRAMK REYEEFKIRI
460 470 480 490 500
NALVSKALKC PEEGWVMQDG TPWPGNNTRD HPGMIQVFLG QNGGLDAEGN
510 520 530 540 550
ELPRLVYVSR EKRPGFQHHK KAGAMNALVR VSAVLTNGPF ILNLDCDHYI
560 570 580 590 600
NNSKALREAM CFLMDPNLGK QVCYVQFPQR FDGIDKNDRY ANRNTVFFDI
610 620 630 640 650
NLRGLDGIQG PVYVGTGCVF NRTALYGYEP PIKVKHKKPS LLSKLCGGSR
660 670 680 690 700
KKNSKAKKES DKKKSGRHTD STVPVFNLDD IEEGVEGAGF DDEKALLMSQ
710 720 730 740 750
MSLEKRFGQS AVFVASTLME NGGVPPSATP ENLLKEAIHV ISCGYEDKSD
760 770 780 790 800
WGMEIGWIYG SVTEDILTGF KMHARGWRSI YCMPKLPAFK GSAPINLSDR
810 820 830 840 850
LNQVLRWALG SVEILFSRHC PIWYGYNGRL KFLERFAYVN TTIYPITSIP
860 870 880 890 900
LLMYCTLPAV CLFTNQFIIP QISNIASIWF LSLFLSIFAT GILEMRWSGV
910 920 930 940 950
GIDEWWRNEQ FWVIGGVSAH LFAVFQGILK VLAGIDTNFT VTSKASDEDG
960 970 980 990 1000
DFAELYLFKW TTLLIPPTTL LIVNLVGVVA GVSYAINSGY QSWGPLFGKL
1010 1020 1030 1040 1050
FFAFWVIVHL YPFLKGLMGR QNRTPTIVVV WSVLLASIFS LLWVRIDPFT
1060
SRVTGPDILE CGINC
Length:1,065
Mass (Da):119,683
Last modified:August 30, 2005 - v2
Checksum:i3AA4714CE3C4D581
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti377 – 3771S → F in AAC39336 (PubMed:9445479).Curated
Sequence conflicti479 – 4791R → G in AAC39336 (PubMed:9445479).Curated
Sequence conflicti858 – 8581P → L in AAC39336 (PubMed:9445479).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF027174 mRNA. Translation: AAC39336.1.
AB018111 Genomic DNA. Translation: BAB09693.1.
CP002688 Genomic DNA. Translation: AED90836.1.
AY045960 mRNA. Translation: AAK76634.2.
BT002335 mRNA. Translation: AAN86168.1.
AK230097 mRNA. Translation: BAF01916.1.
PIRiT52054.
RefSeqiNP_196136.1. NM_120599.3.
UniGeneiAt.24338.

Genome annotation databases

EnsemblPlantsiAT5G05170.1; AT5G05170.1; AT5G05170.
GeneIDi830399.
GrameneiAT5G05170.1; AT5G05170.1; AT5G05170.
KEGGiath:AT5G05170.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF027174 mRNA. Translation: AAC39336.1.
AB018111 Genomic DNA. Translation: BAB09693.1.
CP002688 Genomic DNA. Translation: AED90836.1.
AY045960 mRNA. Translation: AAK76634.2.
BT002335 mRNA. Translation: AAN86168.1.
AK230097 mRNA. Translation: BAF01916.1.
PIRiT52054.
RefSeqiNP_196136.1. NM_120599.3.
UniGeneiAt.24338.

3D structure databases

ProteinModelPortaliQ941L0.
SMRiQ941L0. Positions 3-78.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi15678. 45 interactions.
DIPiDIP-46437N.
IntActiQ941L0. 1 interaction.
STRINGi3702.AT5G05170.1.

Protein family/group databases

CAZyiGT2. Glycosyltransferase Family 2.
TCDBi4.D.3.1.4. the glycan glucosyl transferase (opgh) family.

PTM databases

iPTMnetiQ941L0.
SwissPalmiQ941L0.

Proteomic databases

PaxDbiQ941L0.
PRIDEiQ941L0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G05170.1; AT5G05170.1; AT5G05170.
GeneIDi830399.
GrameneiAT5G05170.1; AT5G05170.1; AT5G05170.
KEGGiath:AT5G05170.

Organism-specific databases

TAIRiAT5G05170.

Phylogenomic databases

eggNOGiENOG410II8I. Eukaryota.
COG1215. LUCA.
HOGENOMiHOG000241942.
InParanoidiQ941L0.
KOiK10999.
OMAiVHGEENE.
OrthoDBiEOG093600MD.
PhylomeDBiQ941L0.

Enzyme and pathway databases

UniPathwayiUPA00695.
BioCyciMetaCyc:MONOMER-2362.
BRENDAi2.4.1.12. 399.

Miscellaneous databases

PROiQ941L0.

Gene expression databases

ExpressionAtlasiQ941L0. baseline and differential.
GenevisibleiQ941L0. AT.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR005150. Cellulose_synth.
IPR027934. CES_Znf_RING.
IPR029044. Nucleotide-diphossugar_trans.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF03552. Cellulose_synt. 1 hit.
PF14569. zf-UDP. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 3 hits.
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCESA3_ARATH
AccessioniPrimary (citable) accession number: Q941L0
Secondary accession number(s): O48948, Q0WLU1, Q9FHK6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: August 30, 2005
Last modified: September 7, 2016
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.