Reviewed, UniProtKB/Swiss-Prot Q8LPK5 (CESA8_ARATH)

Names and origin

Protein names

Recommended 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

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	985 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.4 Ref.9 Ref.10
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.7 Ref.8
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.8 Ref.6
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.10
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 process	Cell wall biogenesis/degradation Cellulose biosynthesis
Cellular component	Cell membrane Membrane
Domain	Coiled coil Transmembrane Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Glycosyltransferase Transferase
PTM	Glycoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW cellulose biosynthetic process Ref.4 Inferred from mutant phenotype. Source: TAIR defense response to bacterium Ref.10 Inferred from mutant phenotype. Source: TAIR defense response to fungus Ref.10 Inferred from mutant phenotype. Source: TAIR positive regulation of abscisic acid biosynthetic process Ref.10 Inferred from genetic interaction. Source: TAIR response to osmotic stress Ref.9 Inferred from mutant phenotype. Source: TAIR response to water deprivation Ref.9 Inferred from mutant phenotype. Source: TAIR secondary cell wall biogenesis Ref.4 Inferred from mutant phenotype. Source: TAIR
Cellular component	cell 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 function	cellulose synthase (UDP-forming) activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 985	985	Cellulose synthase A catalytic subunit 8 [UDP-forming]		PRO_0000166374
Regions
	Topological domain	1 – 179	179	Cytoplasmic Potential
	Transmembrane	180 – 200	21	Potential
	Topological domain	201 – 208	8	Extracellular Potential
	Transmembrane	209 – 229	21	Potential
	Topological domain	230 – 767	538	Cytoplasmic Potential
	Transmembrane	768 – 788	21	Potential
	Topological domain	789 – 793	5	Extracellular Potential
	Transmembrane	794 – 814	21	Potential
	Topological domain	815 – 829	15	Cytoplasmic Potential
	Transmembrane	830 – 850	21	Potential
	Topological domain	851 – 879	29	Extracellular Potential
	Transmembrane	880 – 900	21	Potential
	Topological domain	901 – 911	11	Cytoplasmic Potential
	Transmembrane	912 – 932	21	Potential
	Topological domain	933 – 941	9	Extracellular Potential
	Transmembrane	942 – 962	21	Potential
	Topological domain	963 – 985	23	Cytoplasmic Potential
	Zinc finger	9 – 55	47	RING-type; degenerate
	Coiled coil	358 – 385	28	Potential
	Compositional bias	122 – 140	19	Lys-rich
	Compositional bias	565 – 569	5	Poly-Ser
Sites
	Active site	304	1	Potential
	Active site	683	1	Potential
	Metal binding	9	1	Zinc 1 By similarity
	Metal binding	12	1	Zinc 1 By similarity
	Metal binding	28	1	Zinc 2 By similarity
	Metal binding	31	1	Zinc 2 By similarity
	Metal binding	36	1	Zinc 1 By similarity
	Metal binding	39	1	Zinc 1 By similarity
	Metal binding	51	1	Zinc 2 By similarity
	Metal binding	54	1	Zinc 2 By similarity
	Binding site	470	1	Substrate Potential
	Binding site	472	1	Substrate Potential
Amino acid modifications
	Glycosylation	857	1	N-linked (GlcNAc...) Potential
Experimental info
	Mutagenesis	679	1	S → L in irx1-2; reduced levels of crystalline cellulose in secondary cell wall. Ref.1 Ref.4
	Mutagenesis	683	1	D → N in irx1-1; reduced levels of crystalline cellulose in secondary cell wall. Ref.1 Ref.4
	Mutagenesis	802	1	L → F in lew2-2; enhanced tolerance to drought, salt and osmotic stresses. Higher accumulation of abscisic acid (ABA), proline and soluble sugars. Ref.9
	Sequence conflict	18	1	V → A in AAK08700. Ref.1
	Sequence conflict	144 – 145	2	HE → QD in AAK08700. Ref.1
	Sequence conflict	148	1	I → V in AAK08700. Ref.1
	Sequence conflict	157	1	T → M in AAK08700. Ref.1
	Sequence conflict	583	1	S → A in AAK08700. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q8LPK5-1 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: D299F357625768E0	FASTA	985	111,521
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	"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: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"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.
[5]	"Higher plant cellulose synthases." Richmond T. Genome Biol. 1:REVIEWS3001.1-REVIEWS3001.6(2000) [PubMed: 11178255] [Abstract] Cited for: GENE FAMILY, NOMENCLATURE.
[6]	"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.
[7]	"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.
[8]	"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.
[9]	"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.
[10]	"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.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF267742 mRNA. Translation: AAK08700.1. AL035526 Genomic DNA. Translation: CAB37463.1. Sequence problems. AL161549 Genomic DNA. Translation: CAB78880.1. Sequence problems. AY099636 mRNA. Translation: AAM20487.1.
IPI	IPI00540646.
PIR	T04870.
RefSeq	NP_567564.1.
UniGene	At.66621 At.68239
3D structure databases
ModBase	Search...
Protein family/group databases
CAZy	GT2. Glycosyltransferase Family 2.
Genome annotation databases
GeneID	827612.
GenomeReviews	Gene locus AT4G18780 in contig CT486007_GR.
KEGG	ath:AT4G18780.
NMPDR	fig|3702.1.peg.19685.
Organism-specific databases
GeneFarm	5091. 484.
TAIR	At4g18780.
Phylogenomic databases
OMA	Q8LPK5. LDTNFTV.
Enzyme and pathway databases
BRENDA	2.4.1.12. 302.
Gene expression databases
GermOnline	AT4G18780. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR005150. Cellulose_synth. IPR017907. Znf_RING_CS. [Graphical view]
Pfam	PF03552. Cellulose_synt. 1 hit. [Graphical view]
PROSITE	PS00518. ZF_RING_1. False negative. PS50089. ZF_RING_2. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CESA8_ARATH

Accession

Primary (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:	June 16, 2009
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)