CESA5_ARATH
ID CESA5_ARATH Reviewed; 1069 AA.
AC Q8L778; Q9FIB9;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Cellulose synthase A catalytic subunit 5 [UDP-forming];
DE Short=AtCesA5;
DE EC=2.4.1.12;
GN Name=CESA5; OrderedLocusNames=At5g09870; ORFNames=MYH9.8;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10048488; DOI=10.1093/dnares/5.6.379;
RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(1998).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 671-1069.
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 [4]
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 [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229 AND SER-230, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. La-0;
RX PubMed=14506206; DOI=10.1074/mcp.t300006-mcp200;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Large-scale analysis of in vivo phosphorylated membrane proteins by
RT immobilized metal ion affinity chromatography and mass spectrometry.";
RL Mol. Cell. Proteomics 2:1234-1243(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229 AND SER-230, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15308754; DOI=10.1105/tpc.104.023150;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Phosphoproteomics of the Arabidopsis plasma membrane and a new
RT phosphorylation site database.";
RL Plant Cell 16:2394-2405(2004).
RN [8]
RP PHOSPHORYLATION AT SER-229 AND SER-230, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=17427041; DOI=10.1007/s11103-007-9142-2;
RA Taylor N.G.;
RT "Identification of cellulose synthase AtCesA7 (IRX3) in vivo
RT phosphorylation sites -- a potential role in regulating protein
RT degradation.";
RL Plant Mol. Biol. 64:161-171(2007).
RN [9]
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. {ECO:0000250,
CC 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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in young plants, stems and flowers.
CC {ECO:0000269|PubMed:12481071}.
CC -!- DEVELOPMENTAL STAGE: Expressed at low levels in embryos.
CC {ECO:0000269|PubMed:12481071}.
CC -!- MISCELLANEOUS: Partially redundant with CESA6.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. Plant
CC cellulose synthase subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM97089.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAP68271.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB016893; BAB09408.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91458.1; -; Genomic_DNA.
DR EMBL; AY136423; AAM97089.1; ALT_INIT; mRNA.
DR EMBL; BT008832; AAP68271.1; ALT_INIT; mRNA.
DR RefSeq; NP_196549.1; NM_121024.3.
DR AlphaFoldDB; Q8L778; -.
DR SMR; Q8L778; -.
DR BioGRID; 16125; 1.
DR STRING; 3702.AT5G09870.1; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR iPTMnet; Q8L778; -.
DR PaxDb; Q8L778; -.
DR PRIDE; Q8L778; -.
DR ProteomicsDB; 220388; -.
DR EnsemblPlants; AT5G09870.1; AT5G09870.1; AT5G09870.
DR GeneID; 830847; -.
DR Gramene; AT5G09870.1; AT5G09870.1; AT5G09870.
DR KEGG; ath:AT5G09870; -.
DR Araport; AT5G09870; -.
DR TAIR; locus:2178193; AT5G09870.
DR eggNOG; ENOG502QQGG; Eukaryota.
DR HOGENOM; CLU_001418_0_0_1; -.
DR InParanoid; Q8L778; -.
DR OMA; VYCIPKL; -.
DR OrthoDB; 679241at2759; -.
DR PhylomeDB; Q8L778; -.
DR BioCyc; ARA:AT5G09870-MON; -.
DR UniPathway; UPA00695; -.
DR PRO; PR:Q8L778; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8L778; baseline and differential.
DR Genevisible; Q8L778; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
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; IMP:TAIR.
DR GO; GO:0010192; P:mucilage biosynthetic process; IMP:TAIR.
DR GO; GO:0009833; P:plant-type primary cell wall biogenesis; ISS:CACAO.
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; Phosphoprotein; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix; Zinc; Zinc-finger.
FT CHAIN 1..1069
FT /note="Cellulose synthase A catalytic subunit 5 [UDP-
FT forming]"
FT /id="PRO_0000166371"
FT TOPO_DOM 1..265
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 287..288
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 289..309
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 310..853
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 854..874
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 875..879
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 880..900
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 901..915
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 916..936
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 937..965
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 966..986
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 987..997
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 998..1018
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1019..1027
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1028..1048
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1049..1069
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 COILED 438..464
FT /evidence="ECO:0000255"
FT ACT_SITE 384
FT /evidence="ECO:0000255"
FT ACT_SITE 770
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 550
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 552
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O48946"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17427041,
FT ECO:0007744|PubMed:14506206, ECO:0007744|PubMed:15308754"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17427041,
FT ECO:0007744|PubMed:14506206, ECO:0007744|PubMed:15308754"
FT CARBOHYD 943
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1069 AA; 120862 MW; D03ED5C578DB3E7C CRC64;
MNTGGRLIAG SHNRNEFVLI NADESARIRS VEELSGQTCQ ICGDEIELSV DGESFVACNE
CAFPVCRPCY EYERREGNQS CPQCKTRYKR IKGSPRVEGD EEDDGIDDLD FEFDYSRSGL
ESETFSRRNS EFDLASAPPG SQIPLLTYGE EDVEISSDSH ALIVSPSPGH IHRVHQPHFP
DPAAHPRPMV PQKDLAVYGY GSVAWKDRME EWKRKQNEKY QVVKHDGDSS LGDGDDADIP
MMDEGRQPLS RKVPIKSSKI NPYRMLIVLR LVILGLFFHY RILHPVNDAY ALWLISVICE
IWFAVSWVLD QFPKWYPIER ETYLDRLSLR YEKEGKPSEL AGVDVFVSTV DPMKEPPLIT
ANTVLSILAV DYPVDRVACY VSDDGAAMLT FEALSETAEF ARKWVPFCKK YTIEPRAPEW
YFCHKMDYLK NKVHPAFVRE RRAMKRDYEE FKVKINALVA TAQKVPEEGW TMQDGTPWPG
NNVRDHPGMI QVFLGNNGVR DVENNELPRL VYVSREKRPG FDHHKKAGAM NSLIRVSGVL
SNAPYLLNVD CDHYINNSKA LREAMCFMMD PQSGKKICYV QFPQRFDGID KSDRYSNRNV
VFFDINMKGL DGLQGPIYVG TGCVFRRQAL YGFDAPKKKK TKRMTCNCWP KWCLFCCGLR
KNRKSKTTDK KKKNREASKQ IHALENIEEG TKGTNDAAKS PEAAQLKLEK KFGQSPVFVA
SAGMENGGLA RNASPASLLR EAIQVISCGY EDKTEWGKEI GWIYGSVTED ILTGFKMHSH
GWRSVYCTPK IPAFKGSAPI NLSDRLHQVL RWALGSVEIF LSRHCPIWYG YGGGLKWLER
LSYINSVVYP WTSIPLLVYC SLPAICLLTG KFIVPEISNY ASILFMALFG SIAVTGILEM
QWGKVGIDDW WRNEQFWVIG GVSAHLFALF QGLLKVLAGV ETNFTVTSKA ADDGEFSELY
IFKWTSLLIP PTTLLIINVI GVIVGISDAI SNGYDSWGPL FGRLFFAFWV ILHLYPFLKG
LLGKQDRMPT IILVWSILLA SILTLLWVRV NPFVAKGGPI LEICGLDCL
