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O48947 (CESA2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 88. 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
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 2 [UDP-forming]
Short name=AtCesA2
Short name=Ath-A
EC=2.4.1.12
Gene names
Name:CESA2
Synonyms:ATHA
Ordered Locus Names:At4g39350
ORF Names:T22F8.250
OrganismArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length1084 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 primary cell wall formation. Ref.7 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

Homodimer Probable. Interaction through zinc finger domain Probable. Ref.9

Subcellular location

Cell membrane; Multi-pass membrane protein Probable.

Tissue specificity

Strongly and ubiquitously expressed. Localized in some dividing and expanding cells, as well as in vascular tissues. Ref.6 Ref.7 Ref.8 Ref.9

Developmental stage

Expressed throughout the embryo during all steps of embryogenesis, and decrease toward the bent-cotyledon stage. Ref.8

Disruption phenotype

Plants display reduced cellulose synthesis affecting microtubule orientation, general cell size, hypocotyl growth and seeds production. Partially redundant with CESA6. Ref.9

Sequence similarities

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

Contains 1 RING-type zinc finger.

Sequence caution

The sequence AAL24340.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10841084Cellulose synthase A catalytic subunit 2 [UDP-forming]
PRO_0000166368

Regions

Topological domain1 – 278278Cytoplasmic Potential
Transmembrane279 – 29921Helical; Potential
Topological domain300 – 3012Extracellular Potential
Transmembrane302 – 32221Helical; Potential
Topological domain323 – 867545Cytoplasmic Potential
Transmembrane868 – 88821Helical; Potential
Topological domain889 – 8935Extracellular Potential
Transmembrane894 – 91421Helical; Potential
Topological domain915 – 92915Cytoplasmic Potential
Transmembrane930 – 95021Helical; Potential
Topological domain951 – 97929Extracellular Potential
Transmembrane980 – 100021Helical; Potential
Topological domain1001 – 101111Cytoplasmic Potential
Transmembrane1012 – 103221Helical; Potential
Topological domain1033 – 10419Extracellular Potential
Transmembrane1042 – 106221Helical; Potential
Topological domain1063 – 108422Cytoplasmic Potential
Zinc finger39 – 8547RING-type; degenerate
Coiled coil451 – 47727 Potential
Compositional bias650 – 69243Lys-rich

Sites

Active site3971 Potential
Active site7841 Potential
Metal binding391Zinc 1 By similarity
Metal binding421Zinc 1 By similarity
Metal binding581Zinc 2 By similarity
Metal binding611Zinc 2 By similarity
Metal binding661Zinc 1 By similarity
Metal binding691Zinc 1 By similarity
Metal binding811Zinc 2 By similarity
Metal binding841Zinc 2 By similarity
Binding site5631Substrate Potential
Binding site5651Substrate Potential

Amino acid modifications

Glycosylation9571N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
O48947 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 2F9B22D168D734E0

FASTA1,084122,069
        10         20         30         40         50         60 
MNTGGRLIAG SHNRNEFVLI NADESARIRS VQELSGQTCQ ICGDEIELTV SSELFVACNE 

        70         80         90        100        110        120 
CAFPVCRPCY EYERREGNQA CPQCKTRYKR IKGSPRVDGD DEEEEDIDDL EYEFDHGMDP 

       130        140        150        160        170        180 
EHAAEAALSS RLNTGRGGLD SAPPGSQIPL LTYCDEDADM YSDRHALIVP PSTGYGNRVY 

       190        200        210        220        230        240 
PAPFTDSSAP PQARSMVPQK DIAEYGYGSV AWKDRMEVWK RRQGEKLQVI KHEGGNNGRG 

       250        260        270        280        290        300 
SNDDDELDDP DMPMMDEGRQ PLSRKLPIRS SRINPYRMLI LCRLAILGLF FHYRILHPVN 

       310        320        330        340        350        360 
DAYGLWLTSV ICEIWFAVSW ILDQFPKWYP IERETYLDRL SLRYEKEGKP SGLAPVDVFV 

       370        380        390        400        410        420 
STVDPLKEPP LITANTVLSI LAVDYPVDKV ACYVSDDGAA MLTFEALSDT AEFARKWVPF 

       430        440        450        460        470        480 
CKKFNIEPRA PEWYFSQKMD YLKNKVHPAF VRERRAMKRD YEEFKVKINA LVATAQKVPE 

       490        500        510        520        530        540 
EGWTMQDGTP WPGNNVRDHP GMIQVFLGHS GVRDTDGNEL PRLVYVSREK RPGFDHHKKA 

       550        560        570        580        590        600 
GAMNSLIRVS AVLSNAPYLL NVDCDHYINN SKAIRESMCF MMDPQSGKKV CYVQFPQRFD 

       610        620        630        640        650        660 
GIDRHDRYSN RNVVFFDINM KGLDGIQGPI YVGTGCVFRR QALYGFDAPK KKKPPGKTCN 

       670        680        690        700        710        720 
CWPKWCCLCC GLRKKSKTKA KDKKTNTKET SKQIHALENV DEGVIVPVSN VEKRSEATQL 

       730        740        750        760        770        780 
KLEKKFGQSP VFVASAVLQN GGVPRNASPA CLLREAIQVI SCGYEDKTEW GKEIGWIYGS 

       790        800        810        820        830        840 
VTEDILTGFK MHCHGWRSVY CMPKRAAFKG SAPINLSDRL HQVLRWALGS VEIFLSRHCP 

       850        860        870        880        890        900 
IWYGYGGGLK WLERFSYINS VVYPWTSLPL IVYCSLPAVC LLTGKFIVPE ISNYAGILFM 

       910        920        930        940        950        960 
LMFISIAVTG ILEMQWGGVG IDDWWRNEQF WVIGGASSHL FALFQGLLKV LAGVNTNFTV 

       970        980        990       1000       1010       1020 
TSKAADDGAF SELYIFKWTT LLIPPTTLLI INIIGVIVGV SDAISNGYDS WGPLFGRLFF 

      1030       1040       1050       1060       1070       1080 
ALWVIVHLYP FLKGMLGKQD KMPTIIVVWS ILLASILTLL WVRVNPFVAK GGPVLEICGL 


NCGN

« Hide

References

« Hide 'large scale' references
[1]"Molecular analysis of cellulose biosynthesis in Arabidopsis."
Arioli T., Peng L., Betzner A.S., Burn J., Wittke W., Herth W., Camilleri C., Hoefte H., Plazinski J., Birch R., Cork A., Glover J., Redmond J., Williamson R.E.
Science 279:717-720(1998) [PubMed: 9445479] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Columbia.
[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] OF 577-1084.
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]"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.
[7]"Functional analysis of the cellulose synthase genes CesA1, CesA2, and CesA3 in Arabidopsis."
Burn J.E., Hocart C.H., Birch R.J., Cork A.C., Williamson R.E.
Plant Physiol. 129:797-807(2002) [PubMed: 12068120] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[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: 12481071] [Abstract]
Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[9]"Knockout of the AtCESA2 gene affects microtubule orientation and causes abnormal cell expansion in Arabidopsis."
Chu Z., Chen H., Zhang Y., Zhang Z., Zheng N., Yin B., Yan H., Zhu L., Zhao X., Yuan M., Zhang X., Xie Q.
Plant Physiol. 143:213-224(2007) [PubMed: 17085513] [Abstract]
Cited for: FUNCTION, SUBUNIT, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
[10]"Organization of cellulose synthase complexes involved in primary cell wall synthesis in Arabidopsis thaliana."
Desprez T., Juraniec M., Crowell E.F., Jouy H., Pochylova Z., Parcy F., Hoefte H., Gonneau M., Vernhettes S.
Proc. Natl. Acad. Sci. U.S.A. 104:15572-15577(2007) [PubMed: 17878303] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF027173 mRNA. Translation: AAC39335.1.
AL050351 Genomic DNA. Translation: CAB43650.1.
AL161595 Genomic DNA. Translation: CAB80598.1.
CP002687 Genomic DNA. Translation: AEE87059.1.
AY059858 mRNA. Translation: AAL24340.1. Different initiation.
AY093308 mRNA. Translation: AAM13307.1.
IPIIPI00521119.
PIRT08583.
RefSeqNP_195645.1. NM_120095.3.
UniGeneAt.3315.

3D structure databases

ProteinModelPortalO48947.
SMRO48947. Positions 29-97.
ModBaseSearch...

Protein-protein interaction databases

STRINGO48947.

Protein family/group databases

CAZyGT2. Glycosyltransferase Family 2.

Proteomic databases

PRIDEO48947.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G39350.1; AT4G39350.1; AT4G39350.
GeneID830090.
GenomeReviewsGene locus AT4G39350 in contig CT486007_GR.
KEGGath:AT4G39350.
NMPDRfig|3702.1.peg.22070.

Organism-specific databases

GeneFarm5085. 484.
TAIRAt4g39350.

Phylogenomic databases

eggNOGCOG1215.
GeneTreeEPGT00070000027964.
HOGENOMHBG744549.
InParanoidO48947.
OMAIHALENV.
PhylomeDBO48947.
ProtClustDBPLN02436.

Gene expression databases

GenevestigatorO48947.
GermOnlineAT4G39350. Arabidopsis thaliana.

Family and domain databases

InterProIPR005150. Cellulose_synth.
IPR001841. Znf_RING.
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]
SMARTSM00184. RING. 1 hit.
[Graphical view]
PROSITEPS00518. ZF_RING_1. False negative.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCESA2_ARATH
AccessionPrimary (citable) accession number: O48947
Secondary accession number(s): Q93YP8
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: June 1, 1998
Last modified: December 14, 2011
This is version 88 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

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