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Protein

Cellulose synthase A catalytic subunit 4 [UDP-forming]

Gene

CESA4

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.2 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 bindingi23 – 231Zinc 1By similarity
Metal bindingi26 – 261Zinc 1By similarity
Metal bindingi42 – 421Zinc 2By similarity
Metal bindingi45 – 451Zinc 2By similarity
Metal bindingi50 – 501Zinc 1By similarity
Metal bindingi53 – 531Zinc 1By similarity
Metal bindingi65 – 651Zinc 2By similarity
Metal bindingi68 – 681Zinc 2By similarity
Active sitei335 – 3351Sequence analysis
Binding sitei501 – 5011SubstrateSequence analysis
Binding sitei503 – 5031SubstrateSequence analysis
Active sitei748 – 7481Sequence analysis

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri23 – 6947RING-type; degenerateAdd
BLAST

GO - Molecular functioni

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
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-2364.
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 4 [UDP-forming] (EC:2.4.1.12)
Short name:
AtCesA4
Alternative name(s):
Protein IRREGULAR XYLEM 5
Short name:
AtIRX5
Gene namesi
Name:CESA4
Synonyms:IRX5
Ordered Locus Names:At5g44030
ORF Names:MRH10.14
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G44030.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 215215CytoplasmicSequence analysisAdd
BLAST
Transmembranei216 – 23621HelicalSequence analysisAdd
BLAST
Topological domaini237 – 2393ExtracellularSequence analysis
Transmembranei240 – 26021HelicalSequence analysisAdd
BLAST
Topological domaini261 – 831571CytoplasmicSequence analysisAdd
BLAST
Transmembranei832 – 85221HelicalSequence analysisAdd
BLAST
Topological domaini853 – 8575ExtracellularSequence analysis
Transmembranei858 – 87821HelicalSequence analysisAdd
BLAST
Topological domaini879 – 89517CytoplasmicSequence analysisAdd
BLAST
Transmembranei896 – 91621HelicalSequence analysisAdd
BLAST
Topological domaini917 – 94529ExtracellularSequence analysisAdd
BLAST
Transmembranei946 – 96621HelicalSequence analysisAdd
BLAST
Topological domaini967 – 97711CytoplasmicSequence analysisAdd
BLAST
Transmembranei978 – 99821HelicalSequence analysisAdd
BLAST
Topological domaini999 – 10079ExtracellularSequence analysis
Transmembranei1008 – 102821HelicalSequence analysisAdd
BLAST
Topological domaini1029 – 104921CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

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
Mutagenesisi989 – 104961Missing 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. 1 PublicationAdd
BLAST

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10491049Cellulose synthase A catalytic subunit 4 [UDP-forming]PRO_0000166370Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei135 – 1351Phosphoserine1 Publication
Glycosylationi921 – 9211N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ84JA6.
PRIDEiQ84JA6.

PTM databases

iPTMnetiQ84JA6.

Expressioni

Tissue specificityi

Confined to secondary cell wall developing tissues such as xylems and interfascicular regions. Expressed in roots, hypocotyls, leaves, inflorescences and flowers.3 Publications

Developmental stagei

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.1 Publication

Gene expression databases

ExpressionAtlasiQ84JA6. baseline and differential.
GenevisibleiQ84JA6. AT.

Interactioni

Subunit structurei

Interacts with CESA7 and CESA8. Assembly with CESA7 and CESA8 is required for functional complex and localization in secondary cell wall deposition sites.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CESA7Q9SWW66EBI-8579072,EBI-4477361
CESA8Q8LPK54EBI-8579072,EBI-8579199

Protein-protein interaction databases

BioGridi19676. 7 interactions.
IntActiQ84JA6. 2 interactions.
MINTiMINT-6950789.
STRINGi3702.AT5G44030.1.

Structurei

3D structure databases

ProteinModelPortaliQ84JA6.
SMRiQ84JA6. Positions 17-81, 739-848.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili389 – 41628Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi597 – 60812Cys-richAdd
BLAST
Compositional biasi616 – 64429Lys-richAdd
BLAST

Sequence similaritiesi

Contains 1 RING-type zinc finger.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri23 – 6947RING-type; degenerateAdd
BLAST

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix, Zinc-finger

Phylogenomic databases

eggNOGiENOG410IRAS. Eukaryota.
COG1215. LUCA.
HOGENOMiHOG000241942.
InParanoidiQ84JA6.
KOiK10999.
OMAiINDLWRN.
PhylomeDBiQ84JA6.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR005150. Cellulose_synth.
IPR027934. CES_Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF03552. Cellulose_synt. 1 hit.
PF14569. zf-UDP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q84JA6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEPNTMASFD DEHRHSSFSA KICKVCGDEV KDDDNGQTFV ACHVCVYPVC
60 70 80 90 100
KPCYEYERSN GNKCCPQCNT LYKRHKGSPK IAGDEENNGP DDSDDELNIK
110 120 130 140 150
YRQDGSSIHQ NFAYGSENGD YNSKQQWRPN GRAFSSTGSV LGKDFEAERD
160 170 180 190 200
GYTDAEWKER VDKWKARQEK RGLVTKGEQT NEDKEDDEEE YLDAEARQPL
210 220 230 240 250
WRKVPISSSK ISPYRIVIVL RLVILVFFFR FRILTPAKDA YPLWLISVIC
260 270 280 290 300
EIWFALSWIL DQFPKWFPIN RETYLDRLSM RFERDGEKNK LAPVDVFVST
310 320 330 340 350
VDPLKEPPII TANTILSILA VDYPVNKVSC YVSDDGASML LFDTLSETSE
360 370 380 390 400
FARRWVPFCK KYNVEPRAPE FYFSEKIDYL KDKVQTTFVK DRRAMKREYE
410 420 430 440 450
EFKVRINALV AKAQKKPEEG WVMQDGTPWP GNNTRDHPGM IQVYLGKEGA
460 470 480 490 500
FDIDGNELPR LVYVSREKRP GYAHHKKAGA MNAMVRVSAV LTNAPFMLNL
510 520 530 540 550
DCDHYINNSK AIRESMCFLM DPQLGKKLCY VQFPQRFDGI DLNDRYANRN
560 570 580 590 600
IVFFDINMRG LDGIQGPVYV GTGCVFNRPA LYGYEPPVSE KRKKMTCDCW
610 620 630 640 650
PSWICCCCGG GNRNHKSDSS KKKSGIKSLF SKLKKKTKKK SDDKTMSSYS
660 670 680 690 700
RKRSSTEAIF DLEDIEEGLE GYDELEKSSL MSQKNFEKRF GMSPVFIAST
710 720 730 740 750
LMENGGLPEA TNTSSLIKEA IHVISCGYEE KTEWGKEIGW IYGSVTEDIL
760 770 780 790 800
TGFRMHCRGW KSVYCMPKRP AFKGSAPINL SDRLHQVLRW ALGSVEIFFS
810 820 830 840 850
RHCPLWYAWG GKLKILERLA YINTIVYPFT SIPLLAYCTI PAVCLLTGKF
860 870 880 890 900
IIPTINNFAS IWFLALFLSI IATAILELRW SGVSINDLWR NEQFWVIGGV
910 920 930 940 950
SAHLFAVFQG LLKVLFGVDT NFTVTSKGAS DEADEFGDLY LFKWTTLLIP
960 970 980 990 1000
PTTLIILNMV GVVAGVSDAI NNGYGSWGPL FGKLFFAFWV IVHLYPFLKG
1010 1020 1030 1040
LMGRQNRTPT IVVLWSILLA SIFSLVWVRI DPFLPKQTGP LLKQCGVDC
Length:1,049
Mass (Da):119,599
Last modified:June 1, 2003 - v1
Checksum:iD6D2B1B73BBC3E41
GO

Sequence cautioni

The sequence BAB09063.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti127 – 1271W → C in AAO15532 (PubMed:12538856).Curated
Sequence conflicti191 – 1911Y → EL in AAO15532 (PubMed:12538856).Curated
Sequence conflicti542 – 5421L → H in AAO15532 (PubMed:12538856).Curated
Sequence conflicti616 – 6183KSD → HKSKSSDS in AAO15532 (PubMed:12538856).Curated
Sequence conflicti630 – 6301F → L in AAO15532 (PubMed:12538856).Curated
Sequence conflicti637 – 6371T → N in AAO15532 (PubMed:12538856).Curated
Sequence conflicti655 – 6551S → A in AAO15532 (PubMed:12538856).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF458083 mRNA. Translation: AAO15532.1.
AB006703 Genomic DNA. Translation: BAB09063.1. Sequence problems.
CP002688 Genomic DNA. Translation: AED95050.1.
BT005710 mRNA. Translation: AAO64130.1.
BT006111 mRNA. Translation: AAP04096.1.
AK228561 mRNA. Translation: BAF00480.1.
RefSeqiNP_199216.2. NM_123770.3.
UniGeneiAt.49129.
At.71068.

Genome annotation databases

EnsemblPlantsiAT5G44030.1; AT5G44030.1; AT5G44030.
GeneIDi834426.
GrameneiAT5G44030.1; AT5G44030.1; AT5G44030.
KEGGiath:AT5G44030.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF458083 mRNA. Translation: AAO15532.1.
AB006703 Genomic DNA. Translation: BAB09063.1. Sequence problems.
CP002688 Genomic DNA. Translation: AED95050.1.
BT005710 mRNA. Translation: AAO64130.1.
BT006111 mRNA. Translation: AAP04096.1.
AK228561 mRNA. Translation: BAF00480.1.
RefSeqiNP_199216.2. NM_123770.3.
UniGeneiAt.49129.
At.71068.

3D structure databases

ProteinModelPortaliQ84JA6.
SMRiQ84JA6. Positions 17-81, 739-848.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi19676. 7 interactions.
IntActiQ84JA6. 2 interactions.
MINTiMINT-6950789.
STRINGi3702.AT5G44030.1.

Protein family/group databases

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

PTM databases

iPTMnetiQ84JA6.

Proteomic databases

PaxDbiQ84JA6.
PRIDEiQ84JA6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G44030.1; AT5G44030.1; AT5G44030.
GeneIDi834426.
GrameneiAT5G44030.1; AT5G44030.1; AT5G44030.
KEGGiath:AT5G44030.

Organism-specific databases

TAIRiAT5G44030.

Phylogenomic databases

eggNOGiENOG410IRAS. Eukaryota.
COG1215. LUCA.
HOGENOMiHOG000241942.
InParanoidiQ84JA6.
KOiK10999.
OMAiINDLWRN.
PhylomeDBiQ84JA6.

Enzyme and pathway databases

UniPathwayiUPA00695.
BioCyciMetaCyc:MONOMER-2364.
BRENDAi2.4.1.12. 399.

Miscellaneous databases

PROiQ84JA6.

Gene expression databases

ExpressionAtlasiQ84JA6. baseline and differential.
GenevisibleiQ84JA6. AT.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR005150. Cellulose_synth.
IPR027934. CES_Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF03552. Cellulose_synt. 1 hit.
PF14569. zf-UDP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [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. "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 (JUL-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  6. Cited for: GENE FAMILY, NOMENCLATURE.
  7. "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] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  8. "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.
  9. "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.
  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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  11. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-135, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiCESA4_ARATH
AccessioniPrimary (citable) accession number: Q84JA6
Secondary accession number(s): Q0WQW9, Q8GZN8, Q9FNC3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: June 1, 2003
Last modified: February 17, 2016
This is version 108 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.