Reviewed, UniProtKB/Swiss-Prot Q9SWW6 (CESA7_ARATH)

Names and origin

Protein names

Recommended name:
    Cellulose synthase A catalytic subunit 7 [UDP-forming]
      Short name=AtCesA7
    EC=2.4.1.12
Alternative name(s):
    Protein IRREGULAR XYLEM 3
      Short name=AtIRX3
    Protein FRAGILE FIBER 5

Gene names

Name:	CESA7
Synonyms:	FRA5, IRX3
Ordered Locus Names:	At5g17420
ORF Names:	T10B6.80

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	1026 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.5 Ref.7 Ref.9 Ref.12 Ref.14
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.
Pathway	Glycan metabolism; plant cellulose biosynthesis.
Subunit structure	Interacts with CESA4 and CESA8. Assembly with CESA4 and CESA8 is required for functional complex and localization in secondary cell wall deposition sites. Ref.7 Ref.11 Ref.13
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 and flowers, but not in leaves, roots and shoots. Ref.7 Ref.13 Ref.1 Ref.8 Ref.10
Developmental stage	Not found in embryos. Increasing amount as stems mature. Ref.7 Ref.1
Post-translational modification	Phosphorylated protein may be subject to proteasome degradation. Ref.15
Disruption phenotype	Enhanced resistance to the pathogens Ralstonia solanacearum and Plectosphaerella cucumerina. Ref.12
Sequence similarities	Belongs to the glycosyltransferase 2 family. Plant cellulose synthase subfamily. Contains 1 RING-type zinc finger.

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 Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	cellulose biosynthetic process Ref.9 Inferred from mutant phenotype. Source: TAIR rhamnogalacturonan I side chain metabolic process Inferred from mutant phenotype. Source: TAIR secondary cell wall biogenesis Ref.1 Inferred from mutant phenotype. Source: TAIR
Cellular component	chloroplast 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 protein binding Inferred from electronic annotation. Source: InterPro 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 – 1026

1026

Cellulose synthase A catalytic subunit 7 [UDP-forming]

PRO_0000166373

Regions

Topological domain

1 – 233

233

Cytoplasmic Potential

Transmembrane

234 – 252

19

Potential

Topological domain

253 – 262

10

Extracellular Potential

Transmembrane

263 – 283

21

Potential

Topological domain

284 – 804

521

Cytoplasmic Potential

Transmembrane

805 – 825

21

Potential

Topological domain

826 – 836

11

Extracellular Potential

Transmembrane

837 – 857

21

Potential

Topological domain

858 – 872

15

Cytoplasmic Potential

Transmembrane

873 – 893

21

Potential

Topological domain

894 – 922

29

Extracellular Potential

Transmembrane

923 – 943

21

Potential

Topological domain

944 – 954

11

Cytoplasmic Potential

Transmembrane

955 – 975

21

Potential

Topological domain

976 – 984

9

Extracellular Potential

Transmembrane

985 – 1005

21

Potential

Topological domain

1006 – 1026

21

Cytoplasmic Potential

Zinc finger

37 – 83

47

RING-type; degenerate

Coiled coil

412 – 433

22

Potential

Compositional bias

611 – 638

28

Lys-rich

Sites

Active site

358

1

Potential

Active site

726

1

Potential

Metal binding

37

1

Zinc 1

Metal binding

40

1

Zinc 1

Metal binding

56

1

Zinc 2

Metal binding

59

1

Zinc 2

Metal binding

64

1

Zinc 1

Metal binding

67

1

Zinc 1

Metal binding

79

1

Zinc 2

Metal binding

82

1

Zinc 2

Binding site

524

1

Substrate Potential

Binding site

526

1

Substrate Potential

Amino acid modifications

Modified residue

185

1

Phosphoserine Ref.15

Glycosylation

900

1

N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis

557

1

P → T in fra5; dominant negative effect on cellulose synthesis. Ref.12

Sequence conflict

660

1

S → F in AAD32031. Ref.1

Sequence conflict

895

1

A → T in BAD94098. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

1026

Helix Strand Turn

Details...

Beta strand

38 – 40

3

Beta strand

48 – 52

5

Beta strand

57 – 59

3

Helix

65 – 73

9

Turn

80 – 82

3

Sequences

	Sequence		Length	Mass (Da)
	Q9SWW6-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 503BFBC78BE6E511	FASTA	1,026	115,798
	10 20 30 40 50 60 MEASAGLVAG SHNRNELVVI HNHEEPKPLK NLDGQFCEIC GDQIGLTVEG DLFVACNECG 70 80 90 100 110 120 FPACRPCYEY ERREGTQNCP QCKTRYKRLR GSPRVEGDED EEDIDDIEYE FNIEHEQDKH 130 140 150 160 170 180 KHSAEAMLYG KMSYGRGPED DENGRFPPVI AGGHSGEFPV GGGYGNGEHG LHKRVHPYPS 190 200 210 220 230 240 SEAGSEGGWR ERMDDWKLQH GNLGPEPDDD PEMGLIDEAR QPLSRKVPIA SSKINPYRMV 250 260 270 280 290 300 IVARLVILAV FLRYRLLNPV HDALGLWLTS VICEIWFAVS WILDQFPKWF PIERETYLDR 310 320 330 340 350 360 LSLRYEREGE PNMLAPVDVF VSTVDPLKEP PLVTSNTVLS ILAMDYPVEK ISCYVSDDGA 370 380 390 400 410 420 SMLTFESLSE TAEFARKWVP FCKKFSIEPR APEMYFTLKV DYLQDKVHPT FVKERRAMKR 430 440 450 460 470 480 EYEEFKVRIN AQVAKASKVP LEGWIMQDGT PWPGNNTKDH PGMIQVFLGH SGGFDVEGHE 490 500 510 520 530 540 LPRLVYVSRE KRPGFQHHKK AGAMNALVRV AGVLTNAPFM LNLDCDHYVN NSKAVREAMC 550 560 570 580 590 600 FLMDPQIGKK VCYVQFPQRF DGIDTNDRYA NRNTVFFDIN MKGLDGIQGP VYVGTGCVFK 610 620 630 640 650 660 RQALYGYEPP KGPKRPKMIS CGCCPCFGRR RKNKKFSKND MNGDVAALGG AEGDKEHLMS 670 680 690 700 710 720 EMNFEKTFGQ SSIFVTSTLM EEGGVPPSSS PAVLLKEAIH VISCGYEDKT EWGTELGWIY 730 740 750 760 770 780 GSITEDILTG FKMHCRGWRS IYCMPKRPAF KGSAPINLSD RLNQVLRWAL GSVEIFFSRH 790 800 810 820 830 840 SPLWYGYKGG KLKWLERFAY ANTTIYPFTS IPLLAYCILP AICLLTDKFI MPPISTFASL 850 860 870 880 890 900 FFISLFMSII VTGILELRWS GVSIEEWWRN EQFWVIGGIS AHLFAVVQGL LKILAGIDTN 910 920 930 940 950 960 FTVTSKATDD DDFGELYAFK WTTLLIPPTT VLIINIVGVV AGISDAINNG YQSWGPLFGK 970 980 990 1000 1010 1020 LFFSFWVIVH LYPFLKGLMG RQNRTPTIVV IWSVLLASIF SLLWVRIDPF VLKTKGPDTS KCGINC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 10330464] [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: 11130714] [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]	"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.
[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.
[6]	"Higher plant cellulose synthases." Richmond T. Genome Biol. 1:REVIEWS3001.1-REVIEWS3001.6(2000) [PubMed: 11178255] [Abstract] Cited for: GENE FAMILY, NOMENCLATURE.
[7]	"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: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INTERACTION WITH CESA8.
[8]	"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: 11517344] [Abstract] Cited for: TISSUE SPECIFICITY.
[9]	"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: 12165296] [Abstract] Cited for: FUNCTION.
[10]	"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.
[11]	"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.
[12]	"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: 12805608] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF PRO-557, DISRUPTION PHENOTYPE.
[13]	"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 CESA8.
[14]	"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.
[15]	"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: 17427041] [Abstract] Cited for: PHOSPHORYLATION AT SER-185, MASS SPECTROMETRY.
[16]	"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.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AF088917 mRNA. Translation: AAD32031.1.
AF091713 Genomic DNA. Translation: AAD40885.1.
AL391142 Genomic DNA. Translation: CAC01737.1.
AY139754 mRNA. Translation: AAM98075.1.
BT004543 mRNA. Translation: AAO42789.1.
AK220815 mRNA. Translation: BAD94098.1.

IPI

IPI00527128.

PIR

T51579.

RefSeq

NP_197244.1.

UniGene

At.25558

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1WEO	NMR	-	A	26-105	[»]

ModBase

Search...

Protein family/group databases

CAZy

GT2. Glycosyltransferase Family 2.

Proteomic databases

PRIDE

Q9SWW6.

Genome annotation databases

GeneID

831608.

GenomeReviews

Gene locus AT5G17420 in contig BA000015_GR.

KEGG

ath:AT5G17420.

NMPDR

fig|3702.1.peg.23909.

Organism-specific databases

GeneFarm

5090. 484.

TAIR

At5g17420.

Phylogenomic databases

OMA

Q9SWW6. AVFLRYR.

Enzyme and pathway databases

BRENDA

2.4.1.12. 302.

Gene expression databases

GermOnline

AT5G17420. Arabidopsis thaliana.

Family and domain databases

InterPro

IPR005150. Cellulose_synth.
IPR001841. Znf_RING.
IPR017907. Znf_RING_CS.
[Graphical view]

Pfam

PF03552. Cellulose_synt. 1 hit.
[Graphical view]

SMART

SM00184. RING. 1 hit.
[Graphical view]

PROSITE

PS00518. ZF_RING_1. False negative.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

CESA7_ARATH

Accession

Primary (citable) accession number: Q9SWW6
Secondary accession number(s): Q56ZZ5, Q9XHP6

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2005
Last sequence update:	May 1, 2000
Last modified:	June 16, 2009
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)