CESAA_ARATH
ID CESAA_ARATH Reviewed; 1065 AA.
AC Q9SKJ5;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Probable cellulose synthase A catalytic subunit 10 [UDP-forming];
DE Short=AtCesA10;
DE Short=AtCesA13;
DE EC=2.4.1.12;
GN Name=CESA10; Synonyms=CESA13; OrderedLocusNames=At2g25540;
GN ORFNames=F13B15.20;
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=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 [5]
RP TISSUE SPECIFICITY.
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, flowers and
CC inflorescences. {ECO:0000269|PubMed:12068120,
CC ECO:0000269|PubMed:12481071}.
CC -!- DEVELOPMENTAL STAGE: Not found in embryos.
CC {ECO:0000269|PubMed:12068120}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. Plant
CC cellulose synthase subfamily. {ECO:0000305}.
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DR EMBL; AC006300; AAD20713.1; -; Genomic_DNA.
DR EMBL; CP002685; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; F84649; F84649.
DR AlphaFoldDB; Q9SKJ5; -.
DR SMR; Q9SKJ5; -.
DR STRING; 3702.AT2G25540.1; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR PaxDb; Q9SKJ5; -.
DR PeptideAtlas; Q9SKJ5; -.
DR PRIDE; Q9SKJ5; -.
DR ProteomicsDB; 241225; -.
DR Araport; AT2G25540; -.
DR TAIR; locus:2040080; AT2G25540.
DR eggNOG; ENOG502QQJD; Eukaryota.
DR HOGENOM; CLU_001418_0_2_1; -.
DR InParanoid; Q9SKJ5; -.
DR PhylomeDB; Q9SKJ5; -.
DR BioCyc; ARA:AT2G25540-MON; -.
DR UniPathway; UPA00695; -.
DR PRO; PR:Q9SKJ5; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SKJ5; baseline and differential.
DR Genevisible; Q9SKJ5; 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; 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 2: Evidence at transcript level;
KW Cell membrane; Cell wall biogenesis/degradation; Cellulose biosynthesis;
KW Coiled coil; Glycoprotein; Glycosyltransferase; Membrane; Metal-binding;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix; Zinc;
KW Zinc-finger.
FT CHAIN 1..1065
FT /note="Probable cellulose synthase A catalytic subunit 10
FT [UDP-forming]"
FT /id="PRO_0000166376"
FT TOPO_DOM 1..257
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 279..286
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..307
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 308..850
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 851..871
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 872..876
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 877..897
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 898..912
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 913..933
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 934..963
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 964..984
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 985..995
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 996..1016
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1017..1025
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1026..1046
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1047..1065
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ZN_FING 33..79
FT /note="RING-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT COILED 436..463
FT /evidence="ECO:0000255"
FT ACT_SITE 382
FT /evidence="ECO:0000255"
FT ACT_SITE 767
FT /evidence="ECO:0000255"
FT BINDING 33
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 36
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 52
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 55
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 548
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 550
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT CARBOHYD 940
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1065 AA; 120617 MW; F2AE36C9492A6076 CRC64;
MVAGSYRRYE FVRNRDDSDD GLKPLKDLNG QICQICGDDV GLTKTGNVFV ACNECGFPLC
QSCYEYERKD GSQCCPQCKA RFRRHNGSPR VEVDEKEDDV NDIENEFDYT QGNNKARLPH
RAEEFSSSSR HEESLPVSLL THGHPVSGEI PTPDRNATLS PCIDPQLPGI YQLLLLPVRI
LDPSKDLNSY GLVNVDWKKR IQGWKLKQDK NMIHMTGKYH EGKGGEFEGT GSNGDELQMV
DDARLPMSRV VHFPSARMTP YRIVIVLRLI ILGVFLHYRT THPVKDAYAL WLTSVICEIW
FAFSWLLDQF PKWYPINRET FLDRLALRYD RDGEPSQLAP VDVFVSTVDP MKEPPLVTAN
TVLSILAVDY PVDKVACYVS DDGSAMLTFE ALSETAEFSK KWVPFCKKFN IEPRAPEFYF
SQKIDYLKDK IQPSFVKERR AMKREYEEFK VRINILVAKA QKIPEDGWTM EDGTSWPGNN
PRDHPGMIQV FLGHSGGLDT DGNELPRLIY VSREKRPGFQ HHKKAGAMNA LIRVSAVLTN
GAYLLNVDCD HYFNNSKAIK EAMCFMMDPA IGKKCCYVQF PQRFDGIDLH DRYANRNTVF
FDINLKGLDG IQGPVYVGTG CCFNRQALYG YDPVLTEEDL EPNIIVKSCF GSRKKGKSRK
IPNYEDNRSI KRSDSNVPLF NMEDIDEDVE GYEDEMSLLV SQKRLEKRFG QSPVFIAATF
MEQGGLPSTT NPLTLLKEAI HVISCGYEAK TDWGKEIGWI YGSVTEDILT GFKMHARGWI
SIYCVPSRPA FKGSAPINLS DRLNQVLRWA LGSIEILLSR HCPIWYGYNG RLKLLERIAY
INTIVYPITS IPLLAYCMLP AFCLITNTFI IPEISNLASL CFMLLFASIY ASAILELKWS
DVALEDWWRN EQFWVIGGTS AHLFAVFQGL LKVFAGIDTN FTVTSKASDE DGDFAELYVF
KWTSLLIPPT TILLVNLVGI VAGVSYAINS GYQSWGPLMG KLLFAFWVVA HLYPFLKGLL
GRQNRTPTIV IVWSALLASI FSLLWVRINP FVSTTGVMSN SFMGE
