Reviewed, UniProtKB/Swiss-Prot O48947 (CESA2_ARATH)

Names and origin

Protein names

Recommended 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

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	1084 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 primary cell wall formation. Ref.6 Ref.8 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	Homodimer Probable. Interaction through zinc finger domain Probable.
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.8 Ref.5 Ref.7
Developmental stage	Expressed throughout the embryo during all steps of embryogenesis, and decrease toward the bent-cotyledon stage. Ref.7
Disruption phenotype	Plants display reduced cellulose synthesis affecting microtubule orientation, general cell size, hypocotyl growth and seeds production. Partially redundant with CESA6. Ref.8
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
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW cellulose biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from direct assay. Source: TAIR
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 – 1084	1084	Cellulose synthase A catalytic subunit 2 [UDP-forming]		PRO_0000166368
Regions
	Topological domain	1 – 278	278	Cytoplasmic Potential
	Transmembrane	279 – 299	21	Potential
	Topological domain	300 – 301	2	Extracellular Potential
	Transmembrane	302 – 322	21	Potential
	Topological domain	323 – 867	545	Cytoplasmic Potential
	Transmembrane	868 – 888	21	Potential
	Topological domain	889 – 893	5	Extracellular Potential
	Transmembrane	894 – 914	21	Potential
	Topological domain	915 – 929	15	Cytoplasmic Potential
	Transmembrane	930 – 950	21	Potential
	Topological domain	951 – 979	29	Extracellular Potential
	Transmembrane	980 – 1000	21	Potential
	Topological domain	1001 – 1011	11	Cytoplasmic Potential
	Transmembrane	1012 – 1032	21	Potential
	Topological domain	1033 – 1041	9	Extracellular Potential
	Transmembrane	1042 – 1062	21	Potential
	Topological domain	1063 – 1084	22	Cytoplasmic Potential
	Zinc finger	39 – 85	47	RING-type; degenerate
	Coiled coil	451 – 477	27	Potential
	Compositional bias	650 – 692	43	Lys-rich
Sites
	Active site	397	1	Potential
	Active site	784	1	Potential
	Metal binding	39	1	Zinc 1 By similarity
	Metal binding	42	1	Zinc 1 By similarity
	Metal binding	58	1	Zinc 2 By similarity
	Metal binding	61	1	Zinc 2 By similarity
	Metal binding	66	1	Zinc 1 By similarity
	Metal binding	69	1	Zinc 1 By similarity
	Metal binding	81	1	Zinc 2 By similarity
	Metal binding	84	1	Zinc 2 By similarity
	Binding site	563	1	Substrate Potential
	Binding site	565	1	Substrate Potential
Amino acid modifications
	Glycosylation	957	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	O48947-1 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: 2F9B22D168D734E0	FASTA	1,084	122,069
	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

References

	« Hide 'large scale' referencesShow '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. , 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] OF 577-1084. Strain: cv. Columbia.
[4]	"Higher plant cellulose synthases." Richmond T. Genome Biol. 1:REVIEWS3001.1-REVIEWS3001.6(2000) [PubMed: 11178255] [Abstract] Cited for: GENE FAMILY, NOMENCLATURE.
[5]	"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.
[6]	"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.
[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, DEVELOPMENTAL STAGE.
[8]	"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.
[9]	"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.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF027173 mRNA. Translation: AAC39335.1. AL050351 Genomic DNA. Translation: CAB43650.1. AL161595 Genomic DNA. Translation: CAB80598.1. AY059858 mRNA. Translation: AAL24340.1. Different initiation. AY093308 mRNA. Translation: AAM13307.1.
IPI	IPI00521119.
PIR	T08583.
RefSeq	NP_195645.1.
UniGene	At.3315
3D structure databases
SMR	O48947. Positions 29-97.
ModBase	Search...
Protein family/group databases
CAZy	GT2. Glycosyltransferase Family 2.
Proteomic databases
PRIDE	O48947.
Genome annotation databases
GeneID	830090.
GenomeReviews	Gene locus AT4G39350 in contig CT486007_GR.
KEGG	ath:AT4G39350.
NMPDR	fig|3702.1.peg.22070.
Organism-specific databases
GeneFarm	5085. 484.
TAIR	At4g39350.
Phylogenomic databases
OMA	O48947. GKTCNCW.
Enzyme and pathway databases
BRENDA	2.4.1.12. 302.
Gene expression databases
GermOnline	AT4G39350. 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

CESA2_ARATH

Accession

Primary (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:	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)