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Protein

Cellulose synthase A catalytic subunit 8 [UDP-forming]

Gene

CESA8

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.4 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 bindingi9 – 91Zinc 1By similarity
Metal bindingi12 – 121Zinc 1By similarity
Metal bindingi28 – 281Zinc 2By similarity
Metal bindingi31 – 311Zinc 2By similarity
Metal bindingi36 – 361Zinc 1By similarity
Metal bindingi39 – 391Zinc 1By similarity
Metal bindingi51 – 511Zinc 2By similarity
Metal bindingi54 – 541Zinc 2By similarity
Active sitei304 – 3041Sequence analysis
Binding sitei470 – 4701SubstrateSequence analysis
Binding sitei472 – 4721SubstrateSequence analysis
Active sitei683 – 6831Sequence analysis

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri9 – 5547RING-type; degenerateAdd
BLAST

GO - Molecular functioni

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

GO - Biological processi

  • cellulose biosynthetic process Source: TAIR
  • cell wall organization Source: UniProtKB-KW
  • defense response to bacterium Source: TAIR
  • defense response to fungus Source: TAIR
  • plant-type secondary cell wall biogenesis Source: TAIR
  • response to osmotic stress Source: TAIR
  • response to water deprivation 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-2366.
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 8 [UDP-forming] (EC:2.4.1.12)
Short name:
AtCesA8
Alternative name(s):
Protein IRREGULAR XYLEM 1
Short name:
AtIRX1
Protein LEAF WILTING 2
Gene namesi
Name:CESA8
Synonyms:IRX1, LEW2
Ordered Locus Names:At4g18780
ORF Names:F28A21.190
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G18780.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 179179CytoplasmicSequence analysisAdd
BLAST
Transmembranei180 – 20021HelicalSequence analysisAdd
BLAST
Topological domaini201 – 2088ExtracellularSequence analysis
Transmembranei209 – 22921HelicalSequence analysisAdd
BLAST
Topological domaini230 – 767538CytoplasmicSequence analysisAdd
BLAST
Transmembranei768 – 78821HelicalSequence analysisAdd
BLAST
Topological domaini789 – 7935ExtracellularSequence analysis
Transmembranei794 – 81421HelicalSequence analysisAdd
BLAST
Topological domaini815 – 82915CytoplasmicSequence analysisAdd
BLAST
Transmembranei830 – 85021HelicalSequence analysisAdd
BLAST
Topological domaini851 – 87929ExtracellularSequence analysisAdd
BLAST
Transmembranei880 – 90021HelicalSequence analysisAdd
BLAST
Topological domaini901 – 91111CytoplasmicSequence analysisAdd
BLAST
Transmembranei912 – 93221HelicalSequence analysisAdd
BLAST
Topological domaini933 – 9419ExtracellularSequence analysis
Transmembranei942 – 96221HelicalSequence analysisAdd
BLAST
Topological domaini963 – 98523CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • cell wall Source: TAIR
  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: UniProtKB-SubCell
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
Mutagenesisi679 – 6791S → L in irx1-2; reduced levels of crystalline cellulose in secondary cell wall. 2 Publications
Mutagenesisi683 – 6831D → N in irx1-1; reduced levels of crystalline cellulose in secondary cell wall. 2 Publications
Mutagenesisi802 – 8021L → F in lew2-2; enhanced tolerance to drought, salt and osmotic stresses. Higher accumulation of abscisic acid (ABA), proline and soluble sugars. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 985985Cellulose synthase A catalytic subunit 8 [UDP-forming]PRO_0000166374Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi857 – 8571N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ8LPK5.
PRIDEiQ8LPK5.

Expressioni

Tissue specificityi

Confined to secondary cell wall developing tissues such as xylems and interfascicular regions. Expressed in young plants, stems, flowers and inflorescences, but not in leaves.3 Publications

Developmental stagei

Not found in embryos. Increasing amount as stems mature.1 Publication

Gene expression databases

ExpressionAtlasiQ8LPK5. baseline and differential.
GenevisibleiQ8LPK5. AT.

Interactioni

Subunit structurei

Interacts with CESA4 and CESA7. Assembly with CESA4 and CESA7 is required for functional complex and localization in secondary cell wall deposition sites.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CESA4Q84JA64EBI-8579199,EBI-8579072
CESA7Q9SWW67EBI-8579199,EBI-4477361

Protein-protein interaction databases

BioGridi12905. 17 interactions.
IntActiQ8LPK5. 2 interactions.
MINTiMINT-6950961.
STRINGi3702.AT4G18780.1.

Structurei

3D structure databases

ProteinModelPortaliQ8LPK5.
SMRiQ8LPK5. Positions 9-58, 679-820.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili358 – 38528Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi122 – 14019Lys-richAdd
BLAST
Compositional biasi565 – 5695Poly-Ser

Sequence similaritiesi

Contains 1 RING-type zinc finger.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri9 – 5547RING-type; degenerateAdd
BLAST

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix, Zinc-finger

Phylogenomic databases

eggNOGiENOG410IGV4. Eukaryota.
COG1215. LUCA.
HOGENOMiHOG000241942.
InParanoidiQ8LPK5.
KOiK10999.
OMAiWCGCCSC.
PhylomeDBiQ8LPK5.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Q8LPK5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMESRSPICN TCGEEIGVKS NGEFFVACHE CSFPICKACL EYEFKEGRRI
60 70 80 90 100
CLRCGNPYDE NVFDDVETKT SKTQSIVPTQ TNNTSQDSGI HARHISTVST
110 120 130 140 150
IDSELNDEYG NPIWKNRVES WKDKKDKKSK KKKKDPKATK AEQHEAQIPT
160 170 180 190 200
QQHMEDTPPN TESGATDVLS VVIPIPRTKI TSYRIVIIMR LIILALFFNY
210 220 230 240 250
RITHPVDSAY GLWLTSVICE IWFAVSWVLD QFPKWSPINR ETYIDRLSAR
260 270 280 290 300
FEREGEQSQL AAVDFFVSTV DPLKEPPLIT ANTVLSILAL DYPVDKVSCY
310 320 330 340 350
VSDDGAAMLS FESLVETADF ARKWVPFCKK YSIEPRAPEF YFSLKIDYLR
360 370 380 390 400
DKVQPSFVKE RRAMKRDYEE FKIRMNALVA KAQKTPEEGW TMQDGTSWPG
410 420 430 440 450
NNTRDHPGMI QVFLGYSGAR DIEGNELPRL VYVSREKRPG YQHHKKAGAE
460 470 480 490 500
NALVRVSAVL TNAPFILNLD CDHYVNNSKA VREAMCFLMD PVVGQDVCFV
510 520 530 540 550
QFPQRFDGID KSDRYANRNI VFFDVNMRGL DGIQGPVYVG TGTVFRRQAL
560 570 580 590 600
YGYSPPSKPR ILPQSSSSSC CCLTKKKQPQ DPSEIYKDAK REELDAAIFN
610 620 630 640 650
LGDLDNYDEY DRSMLISQTS FEKTFGLSTV FIESTLMENG GVPDSVNPST
660 670 680 690 700
LIKEAIHVIS CGYEEKTEWG KEIGWIYGSI TEDILTGFKM HCRGWRSIYC
710 720 730 740 750
MPLRPAFKGS APINLSDRLH QVLRWALGSV EIFLSRHCPL WYGCSGGRLK
760 770 780 790 800
LLQRLAYINT IVYPFTSLPL VAYCTLPAIC LLTGKFIIPT LSNLASMLFL
810 820 830 840 850
GLFISIILTS VLELRWSGVS IEDLWRNEQF WVIGGVSAHL FAVFQGFLKM
860 870 880 890 900
LAGLDTNFTV TSKTADDLEF GELYIVKWTT LLIPPTSLLI INLVGVVAGF
910 920 930 940 950
SDALNKGYEA WGPLFGKVFF AFWVILHLYP FLKGLMGRQN RTPTIVILWS
960 970 980
ILLASVFSLV WVRINPFVSK TDTTSLSLNC LLIDC
Length:985
Mass (Da):111,521
Last modified:October 1, 2002 - v1
Checksum:iD299F357625768E0
GO

Sequence cautioni

The sequence CAB37463.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAB78880.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti18 – 181V → A in AAK08700 (PubMed:11148295).Curated
Sequence conflicti144 – 1452HE → QD in AAK08700 (PubMed:11148295).Curated
Sequence conflicti148 – 1481I → V in AAK08700 (PubMed:11148295).Curated
Sequence conflicti157 – 1571T → M in AAK08700 (PubMed:11148295).Curated
Sequence conflicti583 – 5831S → A in AAK08700 (PubMed:11148295).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF267742 mRNA. Translation: AAK08700.1.
AL035526 Genomic DNA. Translation: CAB37463.1. Sequence problems.
AL161549 Genomic DNA. Translation: CAB78880.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE84089.1.
AY099636 mRNA. Translation: AAM20487.1.
PIRiT04870.
RefSeqiNP_567564.1. NM_117994.3.
UniGeneiAt.66621.
At.68239.

Genome annotation databases

EnsemblPlantsiAT4G18780.1; AT4G18780.1; AT4G18780.
GeneIDi827612.
GrameneiAT4G18780.1; AT4G18780.1; AT4G18780.
KEGGiath:AT4G18780.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF267742 mRNA. Translation: AAK08700.1.
AL035526 Genomic DNA. Translation: CAB37463.1. Sequence problems.
AL161549 Genomic DNA. Translation: CAB78880.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE84089.1.
AY099636 mRNA. Translation: AAM20487.1.
PIRiT04870.
RefSeqiNP_567564.1. NM_117994.3.
UniGeneiAt.66621.
At.68239.

3D structure databases

ProteinModelPortaliQ8LPK5.
SMRiQ8LPK5. Positions 9-58, 679-820.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi12905. 17 interactions.
IntActiQ8LPK5. 2 interactions.
MINTiMINT-6950961.
STRINGi3702.AT4G18780.1.

Protein family/group databases

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

Proteomic databases

PaxDbiQ8LPK5.
PRIDEiQ8LPK5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G18780.1; AT4G18780.1; AT4G18780.
GeneIDi827612.
GrameneiAT4G18780.1; AT4G18780.1; AT4G18780.
KEGGiath:AT4G18780.

Organism-specific databases

TAIRiAT4G18780.

Phylogenomic databases

eggNOGiENOG410IGV4. Eukaryota.
COG1215. LUCA.
HOGENOMiHOG000241942.
InParanoidiQ8LPK5.
KOiK10999.
OMAiWCGCCSC.
PhylomeDBiQ8LPK5.

Enzyme and pathway databases

UniPathwayiUPA00695.
BioCyciMetaCyc:MONOMER-2366.
BRENDAi2.4.1.12. 399.

Miscellaneous databases

PROiQ8LPK5.

Gene expression databases

ExpressionAtlasiQ8LPK5. baseline and differential.
GenevisibleiQ8LPK5. AT.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "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: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INTERACTION WITH CESA7, MUTAGENESIS OF SER-679 AND ASP-683.
  2. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1999) [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. "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, MUTAGENESIS OF SER-679 AND ASP-683.
  6. Cited for: GENE FAMILY, NOMENCLATURE.
  7. "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.
  8. "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.
  9. "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 CESA7.
  10. "Disruption of the cellulose synthase gene, AtCesA8/IRX1, enhances drought and osmotic stress tolerance in Arabidopsis."
    Chen Z., Hong X., Zhang H., Wang Y., Li X., Zhu J.-K., Gong Z.
    Plant J. 43:273-283(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF LEU-802.
  11. "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, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiCESA8_ARATH
AccessioniPrimary (citable) accession number: Q8LPK5
Secondary accession number(s): Q9C5Z8, Q9SN37
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: October 1, 2002
Last modified: February 17, 2016
This is version 106 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

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.