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Q8LPK5 (CESA8_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cellulose synthase A catalytic subunit 8 [UDP-forming]

Short name=AtCesA8
EC=2.4.1.12
Alternative name(s):
Protein IRREGULAR XYLEM 1
Short name=AtIRX1
Protein LEAF WILTING 2
Gene names
Name:CESA8
Synonyms:IRX1, LEW2
Ordered Locus Names:At4g18780
ORF Names:F28A21.190
OrganismArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length985 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.5 Ref.10 Ref.11

Catalytic activity

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

Cofactor

Binds 2 zinc ions per subunit By similarity.

Pathway

Glycan metabolism; plant cellulose biosynthesis.

Subunit structure

Interacts with CESA4 and CESA7. Assembly with CESA4 and CESA7 is required for functional complex and localization in secondary cell wall deposition sites. Ref.1 Ref.8 Ref.9

Subcellular location

Cell membrane; Multi-pass membrane protein Probable.

Tissue specificity

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. Ref.1 Ref.7 Ref.9

Developmental stage

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

Disruption phenotype

Enhanced resistance to the pathogens Ralstonia solanacearum and Plectosphaerella cucumerina. Ref.11

Sequence similarities

Belongs to the glycosyltransferase 2 family. Plant cellulose synthase subfamily.

Contains 1 RING-type zinc finger.

Sequence caution

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

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

Ontologies

Keywords
   Biological processCell wall biogenesis/degradation
Cellulose biosynthesis
   Cellular componentCell membrane
Membrane
   DomainCoiled coil
Transmembrane
Transmembrane helix
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionGlycosyltransferase
Transferase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processcellular cell wall organization

Inferred from electronic annotation. Source: UniProtKB-KW

cellulose biosynthetic process

Inferred from mutant phenotype Ref.5. Source: TAIR

defense response to bacterium

Inferred from mutant phenotype Ref.11. Source: TAIR

defense response to fungus

Inferred from mutant phenotype Ref.11. Source: TAIR

positive regulation of abscisic acid biosynthetic process

Inferred from genetic interaction Ref.11. Source: TAIR

response to osmotic stress

Inferred from mutant phenotype Ref.10. Source: TAIR

response to water deprivation

Inferred from mutant phenotype Ref.10. Source: TAIR

secondary cell wall biogenesis

Inferred from mutant phenotype Ref.5. Source: TAIR

   Cellular componentcell wall

Inferred from direct assay. Source: TAIR

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncellulose synthase (UDP-forming) activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 985985Cellulose synthase A catalytic subunit 8 [UDP-forming]
PRO_0000166374

Regions

Topological domain1 – 179179Cytoplasmic Potential
Transmembrane180 – 20021Helical; Potential
Topological domain201 – 2088Extracellular Potential
Transmembrane209 – 22921Helical; Potential
Topological domain230 – 767538Cytoplasmic Potential
Transmembrane768 – 78821Helical; Potential
Topological domain789 – 7935Extracellular Potential
Transmembrane794 – 81421Helical; Potential
Topological domain815 – 82915Cytoplasmic Potential
Transmembrane830 – 85021Helical; Potential
Topological domain851 – 87929Extracellular Potential
Transmembrane880 – 90021Helical; Potential
Topological domain901 – 91111Cytoplasmic Potential
Transmembrane912 – 93221Helical; Potential
Topological domain933 – 9419Extracellular Potential
Transmembrane942 – 96221Helical; Potential
Topological domain963 – 98523Cytoplasmic Potential
Zinc finger9 – 5547RING-type; degenerate
Coiled coil358 – 38528 Potential
Compositional bias122 – 14019Lys-rich
Compositional bias565 – 5695Poly-Ser

Sites

Active site3041 Potential
Active site6831 Potential
Metal binding91Zinc 1 By similarity
Metal binding121Zinc 1 By similarity
Metal binding281Zinc 2 By similarity
Metal binding311Zinc 2 By similarity
Metal binding361Zinc 1 By similarity
Metal binding391Zinc 1 By similarity
Metal binding511Zinc 2 By similarity
Metal binding541Zinc 2 By similarity
Binding site4701Substrate Potential
Binding site4721Substrate Potential

Amino acid modifications

Glycosylation8571N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis6791S → L in irx1-2; reduced levels of crystalline cellulose in secondary cell wall. Ref.1 Ref.5
Mutagenesis6831D → N in irx1-1; reduced levels of crystalline cellulose in secondary cell wall. Ref.1 Ref.5
Mutagenesis8021L → F in lew2-2; enhanced tolerance to drought, salt and osmotic stresses. Higher accumulation of abscisic acid (ABA), proline and soluble sugars. Ref.10
Sequence conflict181V → A in AAK08700. Ref.1
Sequence conflict144 – 1452HE → QD in AAK08700. Ref.1
Sequence conflict1481I → V in AAK08700. Ref.1
Sequence conflict1571T → M in AAK08700. Ref.1
Sequence conflict5831S → A in AAK08700. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8LPK5 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: D299F357625768E0

FASTA985111,521
        10         20         30         40         50         60 
MMESRSPICN TCGEEIGVKS NGEFFVACHE CSFPICKACL EYEFKEGRRI CLRCGNPYDE 

        70         80         90        100        110        120 
NVFDDVETKT SKTQSIVPTQ TNNTSQDSGI HARHISTVST IDSELNDEYG NPIWKNRVES 

       130        140        150        160        170        180 
WKDKKDKKSK KKKKDPKATK AEQHEAQIPT QQHMEDTPPN TESGATDVLS VVIPIPRTKI 

       190        200        210        220        230        240 
TSYRIVIIMR LIILALFFNY RITHPVDSAY GLWLTSVICE IWFAVSWVLD QFPKWSPINR 

       250        260        270        280        290        300 
ETYIDRLSAR FEREGEQSQL AAVDFFVSTV DPLKEPPLIT ANTVLSILAL DYPVDKVSCY 

       310        320        330        340        350        360 
VSDDGAAMLS FESLVETADF ARKWVPFCKK YSIEPRAPEF YFSLKIDYLR DKVQPSFVKE 

       370        380        390        400        410        420 
RRAMKRDYEE FKIRMNALVA KAQKTPEEGW TMQDGTSWPG NNTRDHPGMI QVFLGYSGAR 

       430        440        450        460        470        480 
DIEGNELPRL VYVSREKRPG YQHHKKAGAE NALVRVSAVL TNAPFILNLD CDHYVNNSKA 

       490        500        510        520        530        540 
VREAMCFLMD PVVGQDVCFV QFPQRFDGID KSDRYANRNI VFFDVNMRGL DGIQGPVYVG 

       550        560        570        580        590        600 
TGTVFRRQAL YGYSPPSKPR ILPQSSSSSC CCLTKKKQPQ DPSEIYKDAK REELDAAIFN 

       610        620        630        640        650        660 
LGDLDNYDEY DRSMLISQTS FEKTFGLSTV FIESTLMENG GVPDSVNPST LIKEAIHVIS 

       670        680        690        700        710        720 
CGYEEKTEWG KEIGWIYGSI TEDILTGFKM HCRGWRSIYC MPLRPAFKGS APINLSDRLH 

       730        740        750        760        770        780 
QVLRWALGSV EIFLSRHCPL WYGCSGGRLK LLQRLAYINT IVYPFTSLPL VAYCTLPAIC 

       790        800        810        820        830        840 
LLTGKFIIPT LSNLASMLFL GLFISIILTS VLELRWSGVS IEDLWRNEQF WVIGGVSAHL 

       850        860        870        880        890        900 
FAVFQGFLKM LAGLDTNFTV TSKTADDLEF GELYIVKWTT LLIPPTSLLI INLVGVVAGF 

       910        920        930        940        950        960 
SDALNKGYEA WGPLFGKVFF AFWVILHLYP FLKGLMGRQN RTPTIVILWS ILLASVFSLV 

       970        980 
WVRINPFVSK TDTTSLSLNC LLIDC 

« Hide

References

« Hide 'large scale' references
[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: 11148295] [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. expand/collapse author list , 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: 10617198] [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. expand/collapse author list , 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: 14593172] [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: 9165747] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF SER-679 AND ASP-683.
[6]"Higher plant cellulose synthases."
Richmond T.
Genome Biol. 1:REVIEWS3001.1-REVIEWS3001.6(2000) [PubMed: 11178255] [Abstract]
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: 12481071] [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: 12897249] [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: 12538856] [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: 15998313] [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: 17351116] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
IPIIPI00540646.
PIRT04870.
RefSeqNP_567564.1. NM_117994.3.
UniGeneAt.66621.
At.68239.
At.72359.

3D structure databases

ProteinModelPortalQ8LPK5.
SMRQ8LPK5. Positions 2-63, 444-501.
ModBaseSearch...

Protein-protein interaction databases

MINTMINT-6950961.
STRINGQ8LPK5.

Protein family/group databases

CAZyGT2. Glycosyltransferase Family 2.

Proteomic databases

PRIDEQ8LPK5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G18780.1; AT4G18780.1; AT4G18780.
GeneID827612.
GenomeReviewsGene locus AT4G18780 in contig CT486007_GR.
KEGGath:AT4G18780.
NMPDRfig|3702.1.peg.19685.

Organism-specific databases

GeneFarm5091. 484.
TAIRAt4g18780.

Phylogenomic databases

eggNOGCOG1215.
GeneTreeEPGT00070000027964.
HOGENOMHBG744549.
InParanoidQ8LPK5.
OMAKVFFAFW.
PhylomeDBQ8LPK5.
ProtClustDBPLN02195.

Gene expression databases

GenevestigatorQ8LPK5.
GermOnlineAT4G18780. Arabidopsis thaliana.

Family and domain databases

InterProIPR005150. Cellulose_synth.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
Gene3DG3DSA:3.30.40.10. Znf_RING/FYVE/PHD. 1 hit.
KOK10999.
PfamPF03552. Cellulose_synt. 1 hit.
[Graphical view]
PROSITEPS00518. ZF_RING_1. False negative.
PS50089. ZF_RING_2. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCESA8_ARATH
AccessionPrimary (citable) accession number: Q8LPK5
Secondary accession number(s): Q9C5Z8, Q9SN37
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: October 1, 2002
Last modified: December 14, 2011
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families