CESA2_ARATH
ID CESA2_ARATH Reviewed; 1084 AA.
AC O48947; Q93YP8;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Cellulose synthase A catalytic subunit 2 [UDP-forming];
DE Short=AtCesA2;
DE Short=Ath-A;
DE EC=2.4.1.12;
GN Name=CESA2; Synonyms=ATHA; OrderedLocusNames=At4g39350; ORFNames=T22F8.250;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=9445479; DOI=10.1126/science.279.5351.717;
RA Arioli T., Peng L., Betzner A.S., Burn J., Wittke W., Herth W.,
RA Camilleri C., Hoefte H., Plazinski J., Birch R., Cork A., Glover J.,
RA Redmond J., Williamson R.E.;
RT "Molecular analysis of cellulose biosynthesis in Arabidopsis.";
RL Science 279:717-720(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 577-1084.
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11178255; DOI=10.1186/gb-2000-1-4-reviews3001;
RA Richmond T.;
RT "Higher plant cellulose synthases.";
RL Genome Biol. 1:REVIEWS3001.1-REVIEWS3001.6(2000).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=11517344; DOI=10.1073/pnas.191361598;
RA Scheible W.-R., Eshed R., Richmond T., Delmer D., Somerville C.;
RT "Modifications of cellulose synthase confer resistance to isoxaben and
RT thiazolidinone herbicides in Arabidopsis Ixr1 mutants.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:10079-10084(2001).
RN [7]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12068120; DOI=10.1104/pp.010931;
RA Burn J.E., Hocart C.H., Birch R.J., Cork A.C., Williamson R.E.;
RT "Functional analysis of the cellulose synthase genes CesA1, CesA2, and
RT CesA3 in Arabidopsis.";
RL Plant Physiol. 129:797-807(2002).
RN [8]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=12481071; DOI=10.1104/pp.102.010603;
RA Beeckman T., Przemeck G.K.H., Stamatiou G., Lau R., Terryn N., De Rycke R.,
RA Inze D., Berleth T.;
RT "Genetic complexity of cellulose synthase A gene function in Arabidopsis
RT embryogenesis.";
RL Plant Physiol. 130:1883-1893(2002).
RN [9]
RP FUNCTION, SUBUNIT, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=17085513; DOI=10.1104/pp.106.088393;
RA Chu Z., Chen H., Zhang Y., Zhang Z., Zheng N., Yin B., Yan H., Zhu L.,
RA Zhao X., Yuan M., Zhang X., Xie Q.;
RT "Knockout of the AtCESA2 gene affects microtubule orientation and causes
RT abnormal cell expansion in Arabidopsis.";
RL Plant Physiol. 143:213-224(2007).
RN [10]
RP FUNCTION.
RX PubMed=17878303; DOI=10.1073/pnas.0706569104;
RA Desprez T., Juraniec M., Crowell E.F., Jouy H., Pochylova Z., Parcy F.,
RA Hoefte H., Gonneau M., Vernhettes S.;
RT "Organization of cellulose synthase complexes involved in primary cell wall
RT synthesis in Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:15572-15577(2007).
CC -!- FUNCTION: Catalytic subunit of cellulose synthase terminal complexes
CC ('rosettes'), required for beta-1,4-glucan microfibril crystallization,
CC a major mechanism of the cell wall formation. Involved in the primary
CC cell wall formation. {ECO:0000269|PubMed:12068120,
CC ECO:0000269|PubMed:17085513, ECO:0000269|PubMed:17878303}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->4)-
CC beta-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:19929, Rhea:RHEA-
CC COMP:10033, Rhea:RHEA-COMP:10034, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:18246, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.12;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC -!- PATHWAY: Glycan metabolism; plant cellulose biosynthesis.
CC -!- SUBUNIT: Homodimer. Interaction through zinc finger domain.
CC {ECO:0000305|PubMed:17085513}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Strongly and ubiquitously expressed. Localized in
CC some dividing and expanding cells, as well as in vascular tissues.
CC {ECO:0000269|PubMed:11517344, ECO:0000269|PubMed:12068120,
CC ECO:0000269|PubMed:12481071, ECO:0000269|PubMed:17085513}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout the embryo during all steps
CC of embryogenesis, and decrease toward the bent-cotyledon stage.
CC {ECO:0000269|PubMed:12481071}.
CC -!- DISRUPTION PHENOTYPE: Plants display reduced cellulose synthesis
CC affecting microtubule orientation, general cell size, hypocotyl growth
CC and seeds production. Partially redundant with CESA6.
CC {ECO:0000269|PubMed:17085513}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. Plant
CC cellulose synthase subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL24340.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF027173; AAC39335.1; -; mRNA.
DR EMBL; AL050351; CAB43650.1; -; Genomic_DNA.
DR EMBL; AL161595; CAB80598.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE87059.1; -; Genomic_DNA.
DR EMBL; AY059858; AAL24340.1; ALT_INIT; mRNA.
DR EMBL; AY093308; AAM13307.1; -; mRNA.
DR PIR; T08583; T08583.
DR RefSeq; NP_195645.1; NM_120095.4.
DR AlphaFoldDB; O48947; -.
DR SMR; O48947; -.
DR BioGRID; 15370; 18.
DR IntAct; O48947; 17.
DR STRING; 3702.AT4G39350.1; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR iPTMnet; O48947; -.
DR PaxDb; O48947; -.
DR PRIDE; O48947; -.
DR ProteomicsDB; 220608; -.
DR EnsemblPlants; AT4G39350.1; AT4G39350.1; AT4G39350.
DR GeneID; 830090; -.
DR Gramene; AT4G39350.1; AT4G39350.1; AT4G39350.
DR KEGG; ath:AT4G39350; -.
DR Araport; AT4G39350; -.
DR TAIR; locus:2136308; AT4G39350.
DR eggNOG; ENOG502QQGG; Eukaryota.
DR HOGENOM; CLU_001418_0_0_1; -.
DR InParanoid; O48947; -.
DR OMA; HSEIDSF; -.
DR OrthoDB; 679241at2759; -.
DR PhylomeDB; O48947; -.
DR BioCyc; ARA:AT4G39350-MON; -.
DR UniPathway; UPA00695; -.
DR PRO; PR:O48947; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O48947; baseline and differential.
DR Genevisible; O48947; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0016760; F:cellulose synthase (UDP-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0016759; F:cellulose synthase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0030244; P:cellulose biosynthetic process; IBA:GO_Central.
DR GO; GO:0009833; P:plant-type primary cell wall biogenesis; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR005150; Cellulose_synth.
DR InterPro; IPR027934; CES_Znf_RING.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF03552; Cellulose_synt; 1.
DR Pfam; PF14569; zf-UDP; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell membrane; Cell wall biogenesis/degradation;
KW Cellulose biosynthesis; Coiled coil; Glycoprotein; Glycosyltransferase;
KW Membrane; Metal-binding; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix; Zinc; Zinc-finger.
FT CHAIN 1..1084
FT /note="Cellulose synthase A catalytic subunit 2 [UDP-
FT forming]"
FT /id="PRO_0000166368"
FT TOPO_DOM 1..278
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 279..299
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 300..301
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 302..322
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 323..867
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 868..888
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 889..893
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 894..914
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 915..929
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 930..950
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 951..979
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 980..1000
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1001..1011
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1012..1032
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1033..1041
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1042..1062
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1063..1084
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ZN_FING 39..85
FT /note="RING-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 230..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 451..477
FT /evidence="ECO:0000255"
FT ACT_SITE 397
FT /evidence="ECO:0000255"
FT ACT_SITE 784
FT /evidence="ECO:0000255"
FT BINDING 39
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 42
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 58
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 61
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 563
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 565
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O48946"
FT CARBOHYD 957
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1084 AA; 122069 MW; 2F9B22D168D734E0 CRC64;
MNTGGRLIAG SHNRNEFVLI NADESARIRS VQELSGQTCQ ICGDEIELTV SSELFVACNE
CAFPVCRPCY EYERREGNQA CPQCKTRYKR IKGSPRVDGD DEEEEDIDDL EYEFDHGMDP
EHAAEAALSS RLNTGRGGLD SAPPGSQIPL LTYCDEDADM YSDRHALIVP PSTGYGNRVY
PAPFTDSSAP PQARSMVPQK DIAEYGYGSV AWKDRMEVWK RRQGEKLQVI KHEGGNNGRG
SNDDDELDDP DMPMMDEGRQ PLSRKLPIRS SRINPYRMLI LCRLAILGLF FHYRILHPVN
DAYGLWLTSV ICEIWFAVSW ILDQFPKWYP IERETYLDRL SLRYEKEGKP SGLAPVDVFV
STVDPLKEPP LITANTVLSI LAVDYPVDKV ACYVSDDGAA MLTFEALSDT AEFARKWVPF
CKKFNIEPRA PEWYFSQKMD YLKNKVHPAF VRERRAMKRD YEEFKVKINA LVATAQKVPE
EGWTMQDGTP WPGNNVRDHP GMIQVFLGHS GVRDTDGNEL PRLVYVSREK RPGFDHHKKA
GAMNSLIRVS AVLSNAPYLL NVDCDHYINN SKAIRESMCF MMDPQSGKKV CYVQFPQRFD
GIDRHDRYSN RNVVFFDINM KGLDGIQGPI YVGTGCVFRR QALYGFDAPK KKKPPGKTCN
CWPKWCCLCC GLRKKSKTKA KDKKTNTKET SKQIHALENV DEGVIVPVSN VEKRSEATQL
KLEKKFGQSP VFVASAVLQN GGVPRNASPA CLLREAIQVI SCGYEDKTEW GKEIGWIYGS
VTEDILTGFK MHCHGWRSVY CMPKRAAFKG SAPINLSDRL HQVLRWALGS VEIFLSRHCP
IWYGYGGGLK WLERFSYINS VVYPWTSLPL IVYCSLPAVC LLTGKFIVPE ISNYAGILFM
LMFISIAVTG ILEMQWGGVG IDDWWRNEQF WVIGGASSHL FALFQGLLKV LAGVNTNFTV
TSKAADDGAF SELYIFKWTT LLIPPTTLLI INIIGVIVGV SDAISNGYDS WGPLFGRLFF
ALWVIVHLYP FLKGMLGKQD KMPTIIVVWS ILLASILTLL WVRVNPFVAK GGPVLEICGL
NCGN
