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Protein

Cellulose synthase A catalytic subunit 6 [UDP-forming]

Gene

CESA6

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. The presence of each protein CESA1 and CESA6 is critical for cell expansion. The hypocotyl elongation is based on a CESA6-dependent cell elongation in dark and a CESA6-independent cell elongation in light. The transition between these two mechanisms requires photosynthesis and PHYB, but not CRY1. The CESA6-dependent cell elongation seems to be independent of gibberellic acid, auxin and ethylene. May be involved in sensitivity to isoxaben. Associates with and moves along cortical microtubules for the process of cellulose deposition.7 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)DescriptionActionsGraphical viewLength
Metal bindingi39Zinc 1By similarity1
Metal bindingi42Zinc 1By similarity1
Metal bindingi58Zinc 2By similarity1
Metal bindingi61Zinc 2By similarity1
Metal bindingi66Zinc 1By similarity1
Metal bindingi69Zinc 1By similarity1
Metal bindingi81Zinc 2By similarity1
Metal bindingi84Zinc 2By similarity1
Active sitei396Sequence analysis1
Binding sitei562SubstrateSequence analysis1
Binding sitei564SubstrateSequence analysis1
Active sitei785Sequence analysis1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri39 – 85RING-type; degeneratePROSITE-ProRule annotationAdd BLAST47

GO - Molecular functioni

GO - Biological processi

  • cell growth Source: TAIR
  • cellulose biosynthetic process Source: TAIR
  • cell wall organization Source: UniProtKB-KW
  • cortical microtubule organization Source: TAIR
  • plant-type primary 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-2363.
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 6 [UDP-forming] (EC:2.4.1.12)
Short name:
AtCesA6
Alternative name(s):
AraxCelA
Isoxaben-resistant protein 2
Protein PROCUSTE 1
Protein QUILL
Gene namesi
Name:CESA6
Synonyms:IXR2, PRC1, QUI
Ordered Locus Names:At5g64740
ORF Names:MVP7.7
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G64740.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 277CytoplasmicSequence analysisAdd BLAST277
Transmembranei278 – 298HelicalSequence analysisAdd BLAST21
Topological domaini299 – 300ExtracellularSequence analysis2
Transmembranei301 – 321HelicalSequence analysisAdd BLAST21
Topological domaini322 – 868CytoplasmicSequence analysisAdd BLAST547
Transmembranei869 – 889HelicalSequence analysisAdd BLAST21
Topological domaini890 – 894ExtracellularSequence analysis5
Transmembranei895 – 915HelicalSequence analysisAdd BLAST21
Topological domaini916 – 930CytoplasmicSequence analysisAdd BLAST15
Transmembranei931 – 951HelicalSequence analysisAdd BLAST21
Topological domaini952 – 980ExtracellularSequence analysisAdd BLAST29
Transmembranei981 – 1001HelicalSequence analysisAdd BLAST21
Topological domaini1002 – 1012CytoplasmicSequence analysisAdd BLAST11
Transmembranei1013 – 1033HelicalSequence analysisAdd BLAST21
Topological domaini1034 – 1042ExtracellularSequence analysis9
Transmembranei1043 – 1063HelicalSequence analysisAdd BLAST21
Topological domaini1064 – 1084CytoplasmicSequence analysisAdd BLAST21

GO - Cellular componenti

  • cellulose synthase complex Source: TAIR
  • Golgi apparatus Source: TAIR
  • integral component of plasma membrane Source: UniProtKB
  • membrane Source: TAIR
  • plasma membrane Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1064R → W in ixr2-1; confers resistance to the herbicide isoxaben. Can complement prc1. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001663721 – 1084Cellulose synthase A catalytic subunit 6 [UDP-forming]Add BLAST1084

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Glycosylationi958N-linked (GlcNAc...)Sequence analysis1

Post-translational modificationi

S-acylated.1 Publication

Keywords - PTMi

Acetylation, Glycoprotein, Lipoprotein

Proteomic databases

PaxDbiQ94JQ6.

PTM databases

iPTMnetiQ94JQ6.

Expressioni

Tissue specificityi

Expressed in germinating seeds, seedlings, roots, stems, leaves and flowers. Not present in mature flowers.2 Publications

Developmental stagei

Not found in embryos. 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.1 Publication

Gene expression databases

ExpressionAtlasiQ94JQ6. baseline and differential.
GenevisibleiQ94JQ6. AT.

Interactioni

Subunit structurei

Interacts with CESA1 and CESA3. Interacts with STL1 and STL2, but not with GOT1 (PubMed:27277162). Binds to CSI1 and CSI3 (PubMed:20616083, PubMed:24368796).5 Publications

Protein-protein interaction databases

BioGridi21837. 11 interactors.
DIPiDIP-46438N.
STRINGi3702.AT5G64740.1.

Structurei

3D structure databases

ProteinModelPortaliQ94JQ6.
SMRiQ94JQ6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili450 – 476Sequence analysisAdd BLAST27
Coiled coili675 – 703Sequence analysisAdd BLAST29

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi649 – 687Lys-richAdd BLAST39

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri39 – 85RING-type; degeneratePROSITE-ProRule annotationAdd BLAST47

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix, Zinc-finger

Phylogenomic databases

eggNOGiENOG410IER8. Eukaryota.
COG1215. LUCA.
HOGENOMiHOG000241942.
InParanoidiQ94JQ6.
KOiK10999.
OMAiVHPMPYT.
OrthoDBiEOG093600TW.
PhylomeDBiQ94JQ6.

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.

Q94JQ6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNTGGRLIAG SHNRNEFVLI NADENARIRS VQELSGQTCQ ICRDEIELTV
60 70 80 90 100
DGEPFVACNE CAFPVCRPCY EYERREGNQA CPQCKTRFKR LKGSPRVEGD
110 120 130 140 150
EEEDDIDDLD NEFEYGNNGI GFDQVSEGMS ISRRNSGFPQ SDLDSAPPGS
160 170 180 190 200
QIPLLTYGDE DVEISSDRHA LIVPPSLGGH GNRVHPVSLS DPTVAAHPRP
210 220 230 240 250
MVPQKDLAVY GYGSVAWKDR MEEWKRKQNE KLQVVRHEGD PDFEDGDDAD
260 270 280 290 300
FPMMDEGRQP LSRKIPIKSS KINPYRMLIV LRLVILGLFF HYRILHPVKD
310 320 330 340 350
AYALWLISVI CEIWFAVSWV LDQFPKWYPI ERETYLDRLS LRYEKEGKPS
360 370 380 390 400
GLSPVDVFVS TVDPLKEPPL ITANTVLSIL AVDYPVDKVA CYVSDDGAAM
410 420 430 440 450
LTFEALSETA EFARKWVPFC KKYCIEPRAP EWYFCHKMDY LKNKVHPAFV
460 470 480 490 500
RERRAMKRDY EEFKVKINAL VATAQKVPED GWTMQDGTPW PGNSVRDHPG
510 520 530 540 550
MIQVFLGSDG VRDVENNELP RLVYVSREKR PGFDHHKKAG AMNSLIRVSG
560 570 580 590 600
VLSNAPYLLN VDCDHYINNS KALREAMCFM MDPQSGKKIC YVQFPQRFDG
610 620 630 640 650
IDRHDRYSNR NVVFFDINMK GLDGLQGPIY VGTGCVFRRQ ALYGFDAPKK
660 670 680 690 700
KKGPRKTCNC WPKWCLLCFG SRKNRKAKTV AADKKKKNRE ASKQIHALEN
710 720 730 740 750
IEEGRVTKGS NVEQSTEAMQ MKLEKKFGQS PVFVASARME NGGMARNASP
760 770 780 790 800
ACLLKEAIQV ISCGYEDKTE WGKEIGWIYG SVTEDILTGF KMHSHGWRSV
810 820 830 840 850
YCTPKLAAFK GSAPINLSDR LHQVLRWALG SVEIFLSRHC PIWYGYGGGL
860 870 880 890 900
KWLERLSYIN SVVYPWTSLP LIVYCSLPAI CLLTGKFIVP EISNYASILF
910 920 930 940 950
MALFSSIAIT GILEMQWGKV GIDDWWRNEQ FWVIGGVSAH LFALFQGLLK
960 970 980 990 1000
VLAGVDTNFT VTSKAADDGE FSDLYLFKWT SLLIPPMTLL IINVIGVIVG
1010 1020 1030 1040 1050
VSDAISNGYD SWGPLFGRLF FALWVIIHLY PFLKGLLGKQ DRMPTIIVVW
1060 1070 1080
SILLASILTL LWVRVNPFVA KGGPILEICG LDCL
Length:1,084
Mass (Da):122,502
Last modified:August 30, 2005 - v2
Checksum:i1520439A5053608C
GO

Sequence cautioni

The sequence AAC29067 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAK53023 differs from that shown. Reason: Frameshift at position 645.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti198P → R in AAC29067 (Ref. 4) Curated1
Sequence conflicti200P → L in AAC29067 (Ref. 4) Curated1
Sequence conflicti263R → M in AAC29067 (Ref. 4) Curated1
Sequence conflicti706 – 710VTKGS → GHKVL in AAC29067 (Ref. 4) Curated5
Sequence conflicti724E → Q in AAC29067 (Ref. 4) Curated1
Sequence conflicti727F → Y in AAC29067 (Ref. 4) Curated1
Sequence conflicti739M → L in AAC29067 (Ref. 4) Curated1
Sequence conflicti763C → R in AAC29067 (Ref. 4) Curated1
Sequence conflicti790F → S in AAC29067 (Ref. 4) Curated1
Sequence conflicti799S → H in AAC29067 (Ref. 4) Curated1
Sequence conflicti810K → E in AAK53023 (PubMed:14593172).Curated1
Sequence conflicti810K → E in AAN28896 (PubMed:14593172).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB025637 Genomic DNA. Translation: BAB10307.1.
CP002688 Genomic DNA. Translation: AED97945.1.
AK229477 mRNA. Translation: BAF01335.1.
AF062485 mRNA. Translation: AAC29067.1. Different initiation.
AF375439 mRNA. Translation: AAK53023.1. Frameshift.
AY143957 mRNA. Translation: AAN28896.1.
PIRiT52028.
RefSeqiNP_201279.1. NM_125870.3.
UniGeneiAt.9777.

Genome annotation databases

EnsemblPlantsiAT5G64740.1; AT5G64740.1; AT5G64740.
GeneIDi836595.
GrameneiAT5G64740.1; AT5G64740.1; AT5G64740.
KEGGiath:AT5G64740.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB025637 Genomic DNA. Translation: BAB10307.1.
CP002688 Genomic DNA. Translation: AED97945.1.
AK229477 mRNA. Translation: BAF01335.1.
AF062485 mRNA. Translation: AAC29067.1. Different initiation.
AF375439 mRNA. Translation: AAK53023.1. Frameshift.
AY143957 mRNA. Translation: AAN28896.1.
PIRiT52028.
RefSeqiNP_201279.1. NM_125870.3.
UniGeneiAt.9777.

3D structure databases

ProteinModelPortaliQ94JQ6.
SMRiQ94JQ6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi21837. 11 interactors.
DIPiDIP-46438N.
STRINGi3702.AT5G64740.1.

Protein family/group databases

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

PTM databases

iPTMnetiQ94JQ6.

Proteomic databases

PaxDbiQ94JQ6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G64740.1; AT5G64740.1; AT5G64740.
GeneIDi836595.
GrameneiAT5G64740.1; AT5G64740.1; AT5G64740.
KEGGiath:AT5G64740.

Organism-specific databases

TAIRiAT5G64740.

Phylogenomic databases

eggNOGiENOG410IER8. Eukaryota.
COG1215. LUCA.
HOGENOMiHOG000241942.
InParanoidiQ94JQ6.
KOiK10999.
OMAiVHPMPYT.
OrthoDBiEOG093600TW.
PhylomeDBiQ94JQ6.

Enzyme and pathway databases

UniPathwayiUPA00695.
BioCyciMetaCyc:MONOMER-2363.
BRENDAi2.4.1.12. 399.

Miscellaneous databases

PROiQ94JQ6.

Gene expression databases

ExpressionAtlasiQ94JQ6. baseline and differential.
GenevisibleiQ94JQ6. 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 nameiCESA6_ARATH
AccessioniPrimary (citable) accession number: Q94JQ6
Secondary accession number(s): O65338, Q0WNG4, Q9FGF9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: August 30, 2005
Last modified: November 30, 2016
This is version 114 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.