CESA9_ARATH
ID CESA9_ARATH Reviewed; 1088 AA.
AC Q9SJ22;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Probable cellulose synthase A catalytic subunit 9 [UDP-forming];
DE Short=AtCesA9;
DE EC=2.4.1.12;
GN Name=CESA9; Synonyms=CESA09; OrderedLocusNames=At2g21770; ORFNames=F7D8.9;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 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 [4]
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).
CC -!- FUNCTION: Probable catalytic subunit of cellulose synthase terminal
CC complexes ('rosettes'), required for beta-1,4-glucan microfibril
CC crystallization, a major mechanism of the cell wall formation.
CC {ECO:0000250}.
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: Mostly expressed in cotyledons during all steps of
CC embryogenesis, and decrease toward the bent-cotyledon stage.
CC {ECO:0000269|PubMed:12481071}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. Plant
CC cellulose synthase subfamily. {ECO:0000305}.
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DR EMBL; AC007019; AAD20396.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07220.1; -; Genomic_DNA.
DR PIR; H84604; H84604.
DR RefSeq; NP_179768.1; NM_127746.2.
DR AlphaFoldDB; Q9SJ22; -.
DR SMR; Q9SJ22; -.
DR STRING; 3702.AT2G21770.1; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR iPTMnet; Q9SJ22; -.
DR PaxDb; Q9SJ22; -.
DR PRIDE; Q9SJ22; -.
DR ProteomicsDB; 241234; -.
DR EnsemblPlants; AT2G21770.1; AT2G21770.1; AT2G21770.
DR GeneID; 816713; -.
DR Gramene; AT2G21770.1; AT2G21770.1; AT2G21770.
DR KEGG; ath:AT2G21770; -.
DR Araport; AT2G21770; -.
DR TAIR; locus:2052576; AT2G21770.
DR eggNOG; ENOG502QQGG; Eukaryota.
DR HOGENOM; CLU_001418_0_1_1; -.
DR InParanoid; Q9SJ22; -.
DR OMA; GRTCNCW; -.
DR OrthoDB; 679241at2759; -.
DR PhylomeDB; Q9SJ22; -.
DR BioCyc; ARA:AT2G21770-MON; -.
DR UniPathway; UPA00695; -.
DR PRO; PR:Q9SJ22; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SJ22; baseline and differential.
DR Genevisible; Q9SJ22; 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 GO; GO:0010214; P:seed coat development; IMP:TAIR.
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; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF03552; Cellulose_synt; 1.
DR Pfam; PF14569; zf-UDP; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cell membrane; Cell wall biogenesis/degradation;
KW Cellulose biosynthesis; Glycoprotein; Glycosyltransferase; Membrane;
KW Metal-binding; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix; Zinc; Zinc-finger.
FT CHAIN 1..1088
FT /note="Probable cellulose synthase A catalytic subunit 9
FT [UDP-forming]"
FT /id="PRO_0000166375"
FT TOPO_DOM 1..283
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 284..304
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 305..306
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 328..871
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 872..892
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 893..897
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 898..918
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 919..933
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 934..954
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 955..983
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 984..1004
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1005..1015
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1016..1036
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1037..1045
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1046..1066
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1067..1088
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ZN_FING 39..85
FT /note="RING-type; degenerate"
FT ACT_SITE 402
FT /evidence="ECO:0000255"
FT ACT_SITE 788
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 568
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 570
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O48946"
FT CARBOHYD 961
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1088 AA; 123447 MW; 060571118600DC9F CRC64;
MNTGGRLIAG SHNRNEFVLI NADDTARIRS AEELSGQTCK ICRDEIELTD NGEPFIACNE
CAFPTCRPCY EYERREGNQA CPQCGTRYKR IKGSPRVEGD EEDDDIDDLE HEFYGMDPEH
VTEAALYYMR LNTGRGTDEV SHLYSASPGS EVPLLTYCDE DSDMYSDRHA LIVPPSTGLG
NRVHHVPFTD SFASIHTRPM VPQKDLTVYG YGSVAWKDRM EVWKKQQIEK LQVVKNERVN
DGDGDGFIVD ELDDPGLPMM DEGRQPLSRK LPIRSSRINP YRMLIFCRLA ILGLFFHYRI
LHPVNDAFGL WLTSVICEIW FAVSWILDQF PKWYPIERET YLDRLSLRYE KEGKPSELAP
VDVFVSTVDP LKEPPLITAN TVLSILAVDY PVEKVACYVS DDGAAMLTFE ALSYTAEFAR
KWVPFCKKFS IEPRAPEWYF SQKMDYLKHK VDPAFVMERR AMKRDYEEFK VKINALVSVS
QKVPEDGWTM QDGTPWPGNN VRDHPGMIQV FLGHSGVCDM DGNELPRLVY VSREKRPGFD
HHKKAGAMNS LIRVSAVLSN APYLLNVDCD HYINNSKAIR EAMCFMMDPQ SGKKICYVQF
PQRFDGIDRH DRYSNRNVVF FDINMKGLDG IQGPIYVGTG CVFRRQALYG FDAPKKKQPP
GRTCNCWPKW CCLCCGMRKK KTGKVKDNQR KKPKETSKQI HALEHIEEGL QVTNAENNSE
TAQLKLEKKF GQSPVLVAST LLLNGGVPSN VNPASLLRES IQVISCGYEE KTEWGKEIGW
IYGSVTEDIL TGFKMHCHGW RSVYCMPKRA AFKGSAPINL SDRLHQVLRW ALGSVEIFLS
RHCPIWYGYG GGLKWLERFS YINSVVYPWT SLPLLVYCSL PAICLLTGKF IVPEISNYAG
ILFLLMFMSI AVTGILEMQW GKIGIDDWWR NEQFWVIGGV SSHLFALFQG LLKVLAGVST
NFTVTSKAAD DGEFSELYIF KWTSLLIPPT TLLIINIVGV IVGVSDAINN GYDSWGPLFG
RLFFALWVIV HLYPFLKGLL GKQDRVPTII LVWSILLASI LTLLWVRVNP FVSKDGPVLE
ICGLDCLK
