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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi37 – 371Zinc 1
Metal bindingi40 – 401Zinc 1
Metal bindingi56 – 561Zinc 2
Metal bindingi59 – 591Zinc 2
Metal bindingi64 – 641Zinc 1
Metal bindingi67 – 671Zinc 1
Metal bindingi79 – 791Zinc 2
Metal bindingi82 – 821Zinc 2
Active sitei358 – 3581Sequence analysis
Binding sitei524 – 5241SubstrateSequence analysis
Binding sitei526 – 5261SubstrateSequence analysis
Active sitei726 – 7261Sequence analysis

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri37 – 8347RING-type; degeneratePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • cellulose biosynthetic process Source: TAIR
  • plant-type cell wall biogenesis Source: TAIR
  • 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)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 233233CytoplasmicSequence analysisAdd
BLAST
Transmembranei234 – 25219HelicalSequence analysisAdd
BLAST
Topological domaini253 – 26210ExtracellularSequence analysis
Transmembranei263 – 28321HelicalSequence analysisAdd
BLAST
Topological domaini284 – 804521CytoplasmicSequence analysisAdd
BLAST
Transmembranei805 – 82521HelicalSequence analysisAdd
BLAST
Topological domaini826 – 83611ExtracellularSequence analysisAdd
BLAST
Transmembranei837 – 85721HelicalSequence analysisAdd
BLAST
Topological domaini858 – 87215CytoplasmicSequence analysisAdd
BLAST
Transmembranei873 – 89321HelicalSequence analysisAdd
BLAST
Topological domaini894 – 92229ExtracellularSequence analysisAdd
BLAST
Transmembranei923 – 94321HelicalSequence analysisAdd
BLAST
Topological domaini944 – 95411CytoplasmicSequence analysisAdd
BLAST
Transmembranei955 – 97521HelicalSequence analysisAdd
BLAST
Topological domaini976 – 9849ExtracellularSequence analysis
Transmembranei985 – 100521HelicalSequence analysisAdd
BLAST
Topological domaini1006 – 102621CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Enhanced resistance to the pathogens Ralstonia solanacearum and Plectosphaerella cucumerina.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi557 – 5571P → T in fra5; dominant negative effect on cellulose synthesis. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10261026Cellulose synthase A catalytic subunit 7 [UDP-forming]PRO_0000166373Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei185 – 1851Phosphoserine1 Publication
Glycosylationi900 – 9001N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

Phosphorylated protein may be subject to proteasome degradation.1 Publication

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ9SWW6.
PRIDEiQ9SWW6.

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.3 Publications

Binary interactionsi

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

Protein-protein interaction databases

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

Structurei

Secondary structure

1
1026
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi38 – 403Combined sources
Beta strandi48 – 525Combined sources
Beta strandi57 – 593Combined sources
Helixi65 – 739Combined sources
Turni80 – 823Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WEONMR-A26-105[»]
ProteinModelPortaliQ9SWW6.
SMRiQ9SWW6. Positions 26-95.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9SWW6.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili412 – 43322Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi611 – 63828Lys-richAdd
BLAST

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri37 – 8347RING-type; degeneratePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix, Zinc-finger

Phylogenomic databases

eggNOGiENOG410II8I. Eukaryota.
COG1215. LUCA.
HOGENOMiHOG000241942.
InParanoidiQ9SWW6.
KOiK10999.
OMAiPLEGWIM.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti660 – 6601S → F in AAD32031 (PubMed:10330464).Curated
Sequence conflicti895 – 8951A → T in BAD94098 (Ref. 5) Curated

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_121748.3.
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_121748.3.
UniGeneiAt.25558.
At.71017.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WEONMR-A26-105[»]
ProteinModelPortaliQ9SWW6.
SMRiQ9SWW6. Positions 26-95.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi16884. 13 interactions.
IntActiQ9SWW6. 3 interactions.
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.
PRIDEiQ9SWW6.

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.
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...

Publicationsi

« Hide 'large scale' publications
  1. "The irregular xylem3 locus of Arabidopsis encodes a cellulose synthase required for secondary cell wall synthesis."
    Taylor N.G., Scheible W.-R., Cutler S., Somerville C.R., Turner S.R.
    Plant Cell 11:769-780(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Strain: cv. Landsberg erecta.
  2. "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
    Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.
    , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
    Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "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.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "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.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 776-1026.
    Strain: cv. Columbia.
  6. "Collapsed xylem phenotype of Arabidopsis identifies mutants deficient in cellulose deposition in the secondary cell wall."
    Turner S.R., Somerville C.R.
    Plant Cell 9:689-701(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. Cited for: GENE FAMILY, NOMENCLATURE.
  8. "Multiple cellulose synthase catalytic subunits are required for cellulose synthesis in Arabidopsis."
    Taylor N.G., Laurie S., Turner S.R.
    Plant Cell 12:2529-2539(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INTERACTION WITH CESA8.
  9. "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] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  10. "Structure of cellulose-deficient secondary cell walls from the irx3 mutant of Arabidopsis thaliana."
    Ha M.-A., MacKinnon I.M., Sturcova A., Apperley D.C., McCann M.C., Turner S.R., Jarvis M.C.
    Phytochemistry 61:7-14(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  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] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  12. "Control of cellulose synthase complex localization in developing xylem."
    Gardiner J.C., Taylor N.G., Turner S.R.
    Plant Cell 15:1740-1748(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  13. "Expression of a mutant form of cellulose synthase AtCesA7 causes dominant negative effect on cellulose biosynthesis."
    Zhong R., Morrison W.H. III, Freshour G.D., Hahn M.G., Ye Z.-H.
    Plant Physiol. 132:786-795(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF PRO-557, DISRUPTION PHENOTYPE.
  14. "Interactions among three distinct CesA proteins essential for cellulose synthesis."
    Taylor N.G., Howells R.M., Huttly A.K., Vickers K., Turner S.R.
    Proc. Natl. Acad. Sci. U.S.A. 100:1450-1455(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, INTERACTION WITH CESA4 AND CESA8.
  15. "Impairment of cellulose synthases required for Arabidopsis secondary cell wall formation enhances disease resistance."
    Hernandez-Blanco C., Feng D.X., Hu J., Sanchez-Vallet A., Deslandes L., Llorente F., Berrocal-Lobo M., Keller H., Barlet X., Sanchez-Rodriguez C., Anderson L.K., Somerville S., Marco Y., Molina A.
    Plant Cell 19:890-903(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-185, IDENTIFICATION BY MASS SPECTROMETRY.
  17. "Solution structure of ring-finger in the catalytic subunit (Irx3) of cellulose synthase."
    RIKEN structural genomics initiative (RSGI)
    Submitted (MAY-2004) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 26-105.

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: May 11, 2016
This is version 133 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.