Cellulose synthase A catalytic subunit 4 [UDP-forming] - Arabidopsis thaliana (Mouse-ear cress)

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Reviewed, UniProtKB/Swiss-Prot Q84JA6 (CESA4_ARATH)

Last modified June 16, 2009. Version 50. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Cellulose synthase A catalytic subunit 4 [UDP-forming]
      Short name=AtCesA4
    EC=2.4.1.12
Alternative name(s):
    Protein IRREGULAR XYLEM 5
      Short name=AtIRX5

Gene names

Name:	CESA4
Synonyms:	IRX5
Ordered Locus Names:	At5g44030
ORF Names:	MRH10.14

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

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Protein attributes

Sequence length	1049 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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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.9
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 CESA7 and CESA8. Assembly with CESA7 and CESA8 is required for functional complex and localization in secondary cell wall deposition sites. Ref.1 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 roots, hypocotyls, leaves, inflorescences and flowers. Ref.1 Ref.6 Ref.7
Developmental stage	Not expressed in embryos. In young leaves, localized in transient patches along the vascular system. In young inflorescence stems, observed in vascular bundles of primary xylems. In maturing inflorescence stems, most pronounced in regions of developing interfascicular fibers. Ref.6
Disruption phenotype	Enhanced resistance to the pathogens Ralstonia solanacearum and Plectosphaerella cucumerina. Ref.9
Sequence similarities	Belongs to the glycosyltransferase 2 family. Plant cellulose synthase subfamily. Contains 1 RING-type zinc finger.
Sequence caution	The sequence BAB09063.1 differs from that shown. Reason: Erroneous gene model prediction.

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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	Complete proteome
Gene Ontology (GO)
Biological process	cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW cellulose biosynthetic process Ref.1 Inferred from mutant phenotype. Source: TAIR defense response to bacterium Ref.9 Inferred from mutant phenotype. Source: TAIR defense response to fungus Ref.9 Inferred from mutant phenotype. Source: TAIR secondary cell wall biogenesis Ref.1 Inferred from mutant phenotype. Source: TAIR
Cellular component	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...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1049

1049

Cellulose synthase A catalytic subunit 4 [UDP-forming]

PRO_0000166370

Regions

Topological domain

1 – 215

215

Cytoplasmic Potential

Transmembrane

216 – 236

Potential

Topological domain

237 – 239

Extracellular Potential

Transmembrane

240 – 260

Potential

Topological domain

261 – 831

571

Cytoplasmic Potential

Transmembrane

832 – 852

Potential

Topological domain

853 – 857

Extracellular Potential

Transmembrane

858 – 878

Potential

Topological domain

879 – 895

Cytoplasmic Potential

Transmembrane

896 – 916

Potential

Topological domain

917 – 945

Extracellular Potential

Transmembrane

946 – 966

Potential

Topological domain

967 – 977

Cytoplasmic Potential

Transmembrane

978 – 998

Potential

Topological domain

999 – 1007

Extracellular Potential

Transmembrane

1008 – 1028

Potential

Topological domain

1029 – 1049

Cytoplasmic Potential

Zinc finger

23 – 69

RING-type; degenerate

Coiled coil

389 – 416

Potential

Compositional bias

597 – 608

Cys-rich

Compositional bias

616 – 644

Lys-rich

Sites

Active site

335

Potential

Active site

748

Potential

Metal binding

Zinc 1 By similarity

Metal binding

Zinc 1 By similarity

Metal binding

Zinc 2 By similarity

Metal binding

Zinc 2 By similarity

Metal binding

Zinc 1 By similarity

Metal binding

Zinc 1 By similarity

Metal binding

Zinc 2 By similarity

Metal binding

Zinc 2 By similarity

Binding site

501

Substrate Potential

Binding site

503

Substrate Potential

Amino acid modifications

Modified residue

135

Phosphoserine Ref.10

Glycosylation

921

N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis

989 – 1049

Missing in irx5-2; reduced levels of crystalline cellulose in secondary cell wall, dwarf and dark green, with irregular xylems and thinner cell walls in xylem and interfascicular tissues. Ref.1

Sequence conflict

127

W → C in AAO15532. Ref.1

Sequence conflict

191

Y → EL in AAO15532. Ref.1

Sequence conflict

542

L → H in AAO15532. Ref.1

Sequence conflict

616 – 618

KSD → HKSKSSDS in AAO15532. Ref.1

Sequence conflict

630

F → L in AAO15532. Ref.1

Sequence conflict

637

T → N in AAO15532. Ref.1

Sequence conflict

655

S → A in AAO15532. Ref.1

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Sequences

Sequence

Length

Mass (Da)

Tools

Q84JA6-1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: D6D2B1B73BBC3E41
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FASTA

1,049

119,599

        10         20         30         40         50         60 
MEPNTMASFD DEHRHSSFSA KICKVCGDEV KDDDNGQTFV ACHVCVYPVC KPCYEYERSN 

        70         80         90        100        110        120 
GNKCCPQCNT LYKRHKGSPK IAGDEENNGP DDSDDELNIK YRQDGSSIHQ NFAYGSENGD 

       130        140        150        160        170        180 
YNSKQQWRPN GRAFSSTGSV LGKDFEAERD GYTDAEWKER VDKWKARQEK RGLVTKGEQT 

       190        200        210        220        230        240 
NEDKEDDEEE YLDAEARQPL WRKVPISSSK ISPYRIVIVL RLVILVFFFR FRILTPAKDA 

       250        260        270        280        290        300 
YPLWLISVIC EIWFALSWIL DQFPKWFPIN RETYLDRLSM RFERDGEKNK LAPVDVFVST 

       310        320        330        340        350        360 
VDPLKEPPII TANTILSILA VDYPVNKVSC YVSDDGASML LFDTLSETSE FARRWVPFCK 

       370        380        390        400        410        420 
KYNVEPRAPE FYFSEKIDYL KDKVQTTFVK DRRAMKREYE EFKVRINALV AKAQKKPEEG 

       430        440        450        460        470        480 
WVMQDGTPWP GNNTRDHPGM IQVYLGKEGA FDIDGNELPR LVYVSREKRP GYAHHKKAGA 

       490        500        510        520        530        540 
MNAMVRVSAV LTNAPFMLNL DCDHYINNSK AIRESMCFLM DPQLGKKLCY VQFPQRFDGI 

       550        560        570        580        590        600 
DLNDRYANRN IVFFDINMRG LDGIQGPVYV GTGCVFNRPA LYGYEPPVSE KRKKMTCDCW 

       610        620        630        640        650        660 
PSWICCCCGG GNRNHKSDSS KKKSGIKSLF SKLKKKTKKK SDDKTMSSYS RKRSSTEAIF 

       670        680        690        700        710        720 
DLEDIEEGLE GYDELEKSSL MSQKNFEKRF GMSPVFIAST LMENGGLPEA TNTSSLIKEA 

       730        740        750        760        770        780 
IHVISCGYEE KTEWGKEIGW IYGSVTEDIL TGFRMHCRGW KSVYCMPKRP AFKGSAPINL 

       790        800        810        820        830        840 
SDRLHQVLRW ALGSVEIFFS RHCPLWYAWG GKLKILERLA YINTIVYPFT SIPLLAYCTI 

       850        860        870        880        890        900 
PAVCLLTGKF IIPTINNFAS IWFLALFLSI IATAILELRW SGVSINDLWR NEQFWVIGGV 

       910        920        930        940        950        960 
SAHLFAVFQG LLKVLFGVDT NFTVTSKGAS DEADEFGDLY LFKWTTLLIP PTTLIILNMV 

       970        980        990       1000       1010       1020 
GVVAGVSDAI NNGYGSWGPL FGKLFFAFWV IVHLYPFLKG LMGRQNRTPT IVVLWSILLA 

      1030       1040 
SIFSLVWVRI DPFLPKQTGP LLKQCGVDC

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH CESA7 AND CESA8, MUTAGENESIS OF 989-TRP--CYS-1049.
[2]	"Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence features of the regions of 1,044,062 bp covered by thirteen physically assigned P1 clones." Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N., Tabata S. DNA Res. 4:291-300(1997) [PubMed: 9405937] [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. 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. Shinozaki K. Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"Higher plant cellulose synthases." Richmond T. Genome Biol. 1:REVIEWS3001.1-REVIEWS3001.6(2000) [PubMed: 11178255] [Abstract] Cited for: GENE FAMILY, NOMENCLATURE.
[6]	"A comparative analysis of the plant cellulose synthase (CesA) gene family." Holland N., Holland D., Helentjaris T., Dhugga K.S., Xoconostle-Cazares B., Delmer D.P. Plant Physiol. 123:1313-1324(2000) [PubMed: 10938350] [Abstract] Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[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]	"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.
[10]	"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-135, MASS SPECTROMETRY.

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Cross-references

Sequence databases
	AF458083 mRNA. Translation: AAO15532.1. AB006703 Genomic DNA. Translation: BAB09063.1. Sequence problems. BT005710 mRNA. Translation: AAO64130.1. BT006111 mRNA. Translation: AAP04096.1. AK228561 mRNA. Translation: BAF00480.1.
IPI	IPI00537913.
RefSeq	NP_199216.2.
UniGene	At.71068
3D structure databases
ModBase	Search...
Protein family/group databases
CAZy	GT2. Glycosyltransferase Family 2.
Proteomic databases
PRIDE	Q84JA6.
Genome annotation databases
GeneID	834426.
GenomeReviews	Gene locus AT5G44030 in contig BA000015_GR.
KEGG	ath:AT5G44030.
NMPDR	fig\|3702.1.peg.26154.
Organism-specific databases
GeneFarm	5087. 484.
TAIR	At5g44030.
Phylogenomic databases
OMA	Q84JA6. LLAYCTI.
Enzyme and pathway databases
BRENDA	2.4.1.12. 302.
Gene expression databases
ArrayExpress	Q84JA6.
GermOnline	AT5G44030. 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...

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Entry information

Entry name

CESA4_ARATH

Accession

Primary (citable) accession number: Q84JA6
Secondary accession number(s): Q0WQW9, Q8GZN8, Q9FNC3

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2005
Last sequence update:	June 1, 2003
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)

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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

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents