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Protein

Cellulose synthase A catalytic subunit 7 [UDP-forming]

Gene

CESA7

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 secondary cell wall formation. Required for the xylem cell wall thickening.5 Publications

Catalytic activityi

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

Cofactori

Zn2+Note: Binds 2 Zn2+ ions per subunit.

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 bindingi37Zinc 1Combined sources1 Publication1
Metal bindingi40Zinc 1Combined sources1 Publication1
Metal bindingi56Zinc 2Combined sources1 Publication1
Metal bindingi59Zinc 2Combined sources1 Publication1
Metal bindingi64Zinc 1Combined sources1 Publication1
Metal bindingi67Zinc 1Combined sources1 Publication1
Metal bindingi79Zinc 2Combined sources1 Publication1
Metal bindingi82Zinc 2Combined sources1 Publication1
Active sitei358Sequence analysis1
Binding sitei524SubstrateSequence analysis1
Binding sitei526SubstrateSequence analysis1
Active sitei726Sequence analysis1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri37 – 83RING-type; degeneratePROSITE-ProRule annotationAdd BLAST47

GO - Molecular functioni

GO - Biological processi

  • cellulose biosynthetic process Source: TAIR
  • plant-type cell wall biogenesis Source: TAIR
  • plant-type primary cell wall biogenesis Source: GO_Central
  • plant-type secondary cell wall biogenesis Source: TAIR
  • rhamnogalacturonan I side chain metabolic process 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-2365.
BRENDAi2.4.1.12. 399.
UniPathwayiUPA00695.

Protein family/group databases

CAZyiGT2. Glycosyltransferase Family 2.
TCDBi4.D.3.1.7. the glycan glucosyl transferase (opgh) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Cellulose synthase A catalytic subunit 7 [UDP-forming] (EC:2.4.1.12)
Short name:
AtCesA7
Alternative name(s):
Protein FRAGILE FIBER 5
Protein IRREGULAR XYLEM 3
Short name:
AtIRX3
Gene namesi
Name:CESA7
Synonyms:FRA5, IRX3
Ordered Locus Names:At5g17420
ORF Names:T10B6.80
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G17420.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 233CytoplasmicSequence analysisAdd BLAST233
Transmembranei234 – 252HelicalSequence analysisAdd BLAST19
Topological domaini253 – 262ExtracellularSequence analysis10
Transmembranei263 – 283HelicalSequence analysisAdd BLAST21
Topological domaini284 – 804CytoplasmicSequence analysisAdd BLAST521
Transmembranei805 – 825HelicalSequence analysisAdd BLAST21
Topological domaini826 – 836ExtracellularSequence analysisAdd BLAST11
Transmembranei837 – 857HelicalSequence analysisAdd BLAST21
Topological domaini858 – 872CytoplasmicSequence analysisAdd BLAST15
Transmembranei873 – 893HelicalSequence analysisAdd BLAST21
Topological domaini894 – 922ExtracellularSequence analysisAdd BLAST29
Transmembranei923 – 943HelicalSequence analysisAdd BLAST21
Topological domaini944 – 954CytoplasmicSequence analysisAdd BLAST11
Transmembranei955 – 975HelicalSequence analysisAdd BLAST21
Topological domaini976 – 984ExtracellularSequence analysis9
Transmembranei985 – 1005HelicalSequence analysisAdd BLAST21
Topological domaini1006 – 1026CytoplasmicSequence analysisAdd BLAST21

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Reduced plant size, reduced content of cellulose, collapsed xylem vessels and wilting of inflorescence stems (PubMed:9165747). Enhanced resistance to the pathogens Ralstonia solanacearum and Plectosphaerella cucumerina (PubMed:17351116).2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi557P → T in fra5; dominant negative effect on cellulose synthesis. 1 Publication1
Mutagenesisi621C → S: Unable to localize to the plasma membrane and impaired function as cellulose synthase; when associated with S-623; S-624 and S-626. Abolishes S-acylation. 1 Publication1
Mutagenesisi623C → S: Unable to localize to the plasma membrane and impaired function as cellulose synthase; when associated with S-621; S-624 and S-626. Abolishes S-acylation. 1 Publication1
Mutagenesisi624C → S: Unable to localize to the plasma membrane and impaired function as cellulose synthase; when associated with S-621; S-623 and S-626. Abolishes S-acylation. 1 Publication1
Mutagenesisi626C → S: Unable to localize to the plasma membrane and impaired function as cellulose synthase; when associated with S-621; S-623 and S-624. Abolishes S-acylation. 1 Publication1
Mutagenesisi1022C → S: Impaired function as cellulose synthase. Abolishes S-acylation. Unable to localize to the plasma membrane; when associated with S-1026. 1 Publication1
Mutagenesisi1026C → S: Impaired function as cellulose synthase. Abolishes S-acylation. Unable to localize to the plasma membrane; when associated with S-1022. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001663731 – 1026Cellulose synthase A catalytic subunit 7 [UDP-forming]Add BLAST1026

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei185Phosphoserine1 Publication1
Glycosylationi900N-linked (GlcNAc...)Sequence analysis1

Post-translational modificationi

Phosphorylated protein may be subject to proteasome degradation.1 Publication
S-acylated at Cys-621, Cys-623, Cys-624, Cys-626, Cys-1022 and Cys-1026. The ratio of acylation by either palmitate or stearate is unknown. S-acylation is essential for plasma membrane localization.1 Publication

Keywords - PTMi

Acetylation, Glycoprotein, Lipoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ9SWW6.

PTM databases

iPTMnetiQ9SWW6.

Expressioni

Tissue specificityi

Confined to secondary cell wall developing tissues such as xylems and interfascicular regions. Expressed in young plants, stems and flowers, but not in leaves, roots and shoots.5 Publications

Developmental stagei

Not found in embryos. Increasing amount as stems mature.2 Publications

Gene expression databases

ExpressionAtlasiQ9SWW6. baseline and differential.
GenevisibleiQ9SWW6. AT.

Interactioni

Subunit structurei

Interacts with CESA4 and CESA8. Assembly with CESA4 and CESA8 is required for functional complex and localization in secondary cell wall deposition sites. Interacts with STL1 and STL2, but not with GOT1 (PubMed:27277162).4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CESA4Q84JA66EBI-4477361,EBI-8579072
CESA8Q8LPK57EBI-4477361,EBI-8579199

Protein-protein interaction databases

BioGridi16884. 13 interactors.
IntActiQ9SWW6. 3 interactors.
MINTiMINT-6950921.
STRINGi3702.AT5G17420.1.

Structurei

Secondary structure

11026
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi38 – 40Combined sources3
Beta strandi48 – 52Combined sources5
Beta strandi57 – 59Combined sources3
Helixi65 – 73Combined sources9
Turni80 – 82Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WEONMR-A26-105[»]
ProteinModelPortaliQ9SWW6.
SMRiQ9SWW6.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9SWW6.

Family & Domainsi

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili412 – 433Sequence analysisAdd BLAST22

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi611 – 638Lys-richAdd BLAST28

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri37 – 83RING-type; degeneratePROSITE-ProRule annotationAdd BLAST47

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix, Zinc-finger

Phylogenomic databases

eggNOGiENOG410II8I. Eukaryota.
COG1215. LUCA.
HOGENOMiHOG000241942.
InParanoidiQ9SWW6.
KOiK10999.
OMAiPLEGWIM.
OrthoDBiEOG093600SP.
PhylomeDBiQ9SWW6.

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.

Q9SWW6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEASAGLVAG SHNRNELVVI HNHEEPKPLK NLDGQFCEIC GDQIGLTVEG
60 70 80 90 100
DLFVACNECG FPACRPCYEY ERREGTQNCP QCKTRYKRLR GSPRVEGDED
110 120 130 140 150
EEDIDDIEYE FNIEHEQDKH KHSAEAMLYG KMSYGRGPED DENGRFPPVI
160 170 180 190 200
AGGHSGEFPV GGGYGNGEHG LHKRVHPYPS SEAGSEGGWR ERMDDWKLQH
210 220 230 240 250
GNLGPEPDDD PEMGLIDEAR QPLSRKVPIA SSKINPYRMV IVARLVILAV
260 270 280 290 300
FLRYRLLNPV HDALGLWLTS VICEIWFAVS WILDQFPKWF PIERETYLDR
310 320 330 340 350
LSLRYEREGE PNMLAPVDVF VSTVDPLKEP PLVTSNTVLS ILAMDYPVEK
360 370 380 390 400
ISCYVSDDGA SMLTFESLSE TAEFARKWVP FCKKFSIEPR APEMYFTLKV
410 420 430 440 450
DYLQDKVHPT FVKERRAMKR EYEEFKVRIN AQVAKASKVP LEGWIMQDGT
460 470 480 490 500
PWPGNNTKDH PGMIQVFLGH SGGFDVEGHE LPRLVYVSRE KRPGFQHHKK
510 520 530 540 550
AGAMNALVRV AGVLTNAPFM LNLDCDHYVN NSKAVREAMC FLMDPQIGKK
560 570 580 590 600
VCYVQFPQRF DGIDTNDRYA NRNTVFFDIN MKGLDGIQGP VYVGTGCVFK
610 620 630 640 650
RQALYGYEPP KGPKRPKMIS CGCCPCFGRR RKNKKFSKND MNGDVAALGG
660 670 680 690 700
AEGDKEHLMS EMNFEKTFGQ SSIFVTSTLM EEGGVPPSSS PAVLLKEAIH
710 720 730 740 750
VISCGYEDKT EWGTELGWIY GSITEDILTG FKMHCRGWRS IYCMPKRPAF
760 770 780 790 800
KGSAPINLSD RLNQVLRWAL GSVEIFFSRH SPLWYGYKGG KLKWLERFAY
810 820 830 840 850
ANTTIYPFTS IPLLAYCILP AICLLTDKFI MPPISTFASL FFISLFMSII
860 870 880 890 900
VTGILELRWS GVSIEEWWRN EQFWVIGGIS AHLFAVVQGL LKILAGIDTN
910 920 930 940 950
FTVTSKATDD DDFGELYAFK WTTLLIPPTT VLIINIVGVV AGISDAINNG
960 970 980 990 1000
YQSWGPLFGK LFFSFWVIVH LYPFLKGLMG RQNRTPTIVV IWSVLLASIF
1010 1020
SLLWVRIDPF VLKTKGPDTS KCGINC
Length:1,026
Mass (Da):115,798
Last modified:May 1, 2000 - v1
Checksum:i503BFBC78BE6E511
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti660S → F in AAD32031 (PubMed:10330464).Curated1
Sequence conflicti895A → T in BAD94098 (Ref. 5) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF088917 mRNA. Translation: AAD32031.1.
AF091713 Genomic DNA. Translation: AAD40885.1.
AL391142 Genomic DNA. Translation: CAC01737.1.
CP002688 Genomic DNA. Translation: AED92424.1.
AY139754 mRNA. Translation: AAM98075.1.
BT004543 mRNA. Translation: AAO42789.1.
AK220815 mRNA. Translation: BAD94098.1.
PIRiT51579.
RefSeqiNP_197244.1. NM_121748.4.
UniGeneiAt.25558.
At.71017.

Genome annotation databases

EnsemblPlantsiAT5G17420.1; AT5G17420.1; AT5G17420.
GeneIDi831608.
GrameneiAT5G17420.1; AT5G17420.1; AT5G17420.
KEGGiath:AT5G17420.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF088917 mRNA. Translation: AAD32031.1.
AF091713 Genomic DNA. Translation: AAD40885.1.
AL391142 Genomic DNA. Translation: CAC01737.1.
CP002688 Genomic DNA. Translation: AED92424.1.
AY139754 mRNA. Translation: AAM98075.1.
BT004543 mRNA. Translation: AAO42789.1.
AK220815 mRNA. Translation: BAD94098.1.
PIRiT51579.
RefSeqiNP_197244.1. NM_121748.4.
UniGeneiAt.25558.
At.71017.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WEONMR-A26-105[»]
ProteinModelPortaliQ9SWW6.
SMRiQ9SWW6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi16884. 13 interactors.
IntActiQ9SWW6. 3 interactors.
MINTiMINT-6950921.
STRINGi3702.AT5G17420.1.

Protein family/group databases

CAZyiGT2. Glycosyltransferase Family 2.
TCDBi4.D.3.1.7. the glycan glucosyl transferase (opgh) family.

PTM databases

iPTMnetiQ9SWW6.

Proteomic databases

PaxDbiQ9SWW6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G17420.1; AT5G17420.1; AT5G17420.
GeneIDi831608.
GrameneiAT5G17420.1; AT5G17420.1; AT5G17420.
KEGGiath:AT5G17420.

Organism-specific databases

TAIRiAT5G17420.

Phylogenomic databases

eggNOGiENOG410II8I. Eukaryota.
COG1215. LUCA.
HOGENOMiHOG000241942.
InParanoidiQ9SWW6.
KOiK10999.
OMAiPLEGWIM.
OrthoDBiEOG093600SP.
PhylomeDBiQ9SWW6.

Enzyme and pathway databases

UniPathwayiUPA00695.
BioCyciMetaCyc:MONOMER-2365.
BRENDAi2.4.1.12. 399.

Miscellaneous databases

EvolutionaryTraceiQ9SWW6.
PROiQ9SWW6.

Gene expression databases

ExpressionAtlasiQ9SWW6. baseline and differential.
GenevisibleiQ9SWW6. 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 nameiCESA7_ARATH
AccessioniPrimary (citable) accession number: Q9SWW6
Secondary accession number(s): Q56ZZ5, Q9XHP6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: May 1, 2000
Last modified: November 30, 2016
This is version 137 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.