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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: -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

  • cellulose synthase (UDP-forming) activity Source: UniProtKB-EC
  • cellulose synthase activity Source: GO_Central
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

Keywordsi

Molecular functionGlycosyltransferase, Transferase
Biological processCell wall biogenesis/degradation, Cellulose biosynthesis
LigandMetal-binding, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-2365
BRENDAi2.4.1.12 399
UniPathwayi
UPA00695

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

AraportiAT5G17420
TAIRilocus:2178935 AT5G17420

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte; Source: COMPARTMENTS

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

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...) asparagineSequence 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
SwissPalmiQ9SWW6

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

Protein-protein interaction databases

BioGridi16884, 13 interactors
IntActiQ9SWW6, 8 interactors
MINTiQ9SWW6
STRINGi3702.AT5G17420.1

Structurei

Secondary structure

11026
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

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
OMAiKVRINAQ
OrthoDBiEOG093600SP
PhylomeDBiQ9SWW6

Family and domain databases

Gene3Di3.30.40.10, 1 hit
3.90.550.10, 1 hit
InterProiView protein in InterPro
IPR005150 Cellulose_synth
IPR027934 CES_Znf_RING
IPR029044 Nucleotide-diphossugar_trans
IPR001841 Znf_RING
IPR013083 Znf_RING/FYVE/PHD
PfamiView protein in Pfam
PF03552 Cellulose_synt, 1 hit
PF14569 zf-UDP, 1 hit
SUPFAMiSSF53448 SSF53448, 1 hit
PROSITEiView protein in PROSITE
PS50089 ZF_RING_2, 1 hit

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

Similar proteinsi

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, 8 interactors
MINTiQ9SWW6
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
SwissPalmiQ9SWW6

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

AraportiAT5G17420
TAIRilocus:2178935 AT5G17420

Phylogenomic databases

eggNOGiENOG410II8I Eukaryota
COG1215 LUCA
HOGENOMiHOG000241942
InParanoidiQ9SWW6
KOiK10999
OMAiKVRINAQ
OrthoDBiEOG093600SP
PhylomeDBiQ9SWW6

Enzyme and pathway databases

UniPathwayi
UPA00695

BioCyciMetaCyc:MONOMER-2365
BRENDAi2.4.1.12 399

Miscellaneous databases

EvolutionaryTraceiQ9SWW6
PROiPR:Q9SWW6

Gene expression databases

ExpressionAtlasiQ9SWW6 baseline and differential
GenevisibleiQ9SWW6 AT

Family and domain databases

Gene3Di3.30.40.10, 1 hit
3.90.550.10, 1 hit
InterProiView protein in InterPro
IPR005150 Cellulose_synth
IPR027934 CES_Znf_RING
IPR029044 Nucleotide-diphossugar_trans
IPR001841 Znf_RING
IPR013083 Znf_RING/FYVE/PHD
PfamiView protein in Pfam
PF03552 Cellulose_synt, 1 hit
PF14569 zf-UDP, 1 hit
SUPFAMiSSF53448 SSF53448, 1 hit
PROSITEiView protein in PROSITE
PS50089 ZF_RING_2, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiCESA7_ARATH
AccessioniPrimary (citable) accession number: Q9SWW6
Secondary accession number(s): Q56ZZ5, Q9XHP6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: May 1, 2000
Last modified: November 7, 2018
This is version 148 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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Main funding by: National Institutes of Health

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