CESA9_ORYSJ
ID CESA9_ORYSJ Reviewed; 1055 AA.
AC Q69P51; B7F6V1;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Cellulose synthase A catalytic subunit 9 [UDP-forming];
DE EC=2.4.1.12;
DE AltName: Full=OsCesA9;
GN Name=CESA9; OrderedLocusNames=Os09g0422500, LOC_Os09g25490;
GN ORFNames=OJ1740_D06.31, OsJ_028258, P0418B08.2;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=12970476; DOI=10.1104/pp.103.022442;
RA Tanaka K., Murata K., Yamazaki M., Onosato K., Miyao A., Hirochika H.;
RT "Three distinct rice cellulose synthase catalytic subunit genes required
RT for cellulose synthesis in the secondary wall.";
RL Plant Physiol. 133:73-83(2003).
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 (By similarity). Involved
CC in the secondary cell wall formation. {ECO:0000250,
CC ECO:0000269|PubMed:12970476}.
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 -!- DISRUPTION PHENOTYPE: Plants develop a brittle culm (bc) phenotype with
CC a reduction of up to 90% percent of cellulose content in culm.
CC {ECO:0000269|PubMed:12970476}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. Plant
CC cellulose synthase subfamily. {ECO:0000305}.
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DR EMBL; AP005420; BAD33412.1; -; Genomic_DNA.
DR EMBL; AP005579; BAD33645.1; -; Genomic_DNA.
DR EMBL; AP008215; BAF25121.1; -; Genomic_DNA.
DR EMBL; AP014965; BAT08137.1; -; Genomic_DNA.
DR EMBL; CM000146; EAZ44775.1; -; Genomic_DNA.
DR EMBL; AK121170; BAH00349.1; -; mRNA.
DR RefSeq; XP_015612279.1; XM_015756793.1.
DR AlphaFoldDB; Q69P51; -.
DR SMR; Q69P51; -.
DR STRING; 4530.OS09T0422500-01; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR PaxDb; Q69P51; -.
DR PRIDE; Q69P51; -.
DR EnsemblPlants; Os09t0422500-01; Os09t0422500-01; Os09g0422500.
DR GeneID; 4347093; -.
DR Gramene; Os09t0422500-01; Os09t0422500-01; Os09g0422500.
DR KEGG; osa:4347093; -.
DR eggNOG; ENOG502QQXZ; Eukaryota.
DR HOGENOM; CLU_001418_0_1_1; -.
DR InParanoid; Q69P51; -.
DR OMA; NGQVCEI; -.
DR OrthoDB; 679241at2759; -.
DR PlantReactome; R-OSA-1119314; Cellulose biosynthesis.
DR UniPathway; UPA00695; -.
DR Proteomes; UP000000763; Chromosome 9.
DR Proteomes; UP000007752; Chromosome 9.
DR Proteomes; UP000059680; Chromosome 9.
DR Genevisible; Q69P51; OS.
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; IMP:UniProtKB.
DR GO; GO:0009833; P:plant-type primary cell wall biogenesis; IBA:GO_Central.
DR GO; GO:0009834; P:plant-type secondary cell wall biogenesis; IMP:UniProtKB.
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..1055
FT /note="Cellulose synthase A catalytic subunit 9 [UDP-
FT forming]"
FT /id="PRO_0000319370"
FT TOPO_DOM 1..268
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 290..291
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..312
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 313..831
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 832..852
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 853..860
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 861..881
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 882..899
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 900..920
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 921..951
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 952..972
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 973..983
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 984..1004
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1005..1013
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1014..1034
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1035..1055
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ZN_FING 37..83
FT /note="RING-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT COILED 439..468
FT /evidence="ECO:0000255"
FT ACT_SITE 387
FT /evidence="ECO:0000255"
FT ACT_SITE 753
FT /evidence="ECO:0000255"
FT BINDING 37
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 40
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 56
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 59
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 67
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 553
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 555
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT CARBOHYD 927
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1055 AA; 118697 MW; 8D050CC7A365D9EC CRC64;
MEASAGLVAG SHNRNELVLI RGHEEPKPLR ALSGQVCEIC GDEVGRTVDG DLFVACNECG
FPVCRPCYEY ERREGTQNCP QCKTRYKRLK GSPRVPGDED EEDIDDLEHE FNIDDEKQKQ
LQQDQDGMQN SHITEAMLHG KMSYGRGPDD GDGNSTPLPP IITGARSVPV SGEFPISNSH
GHGEFSSSLH KRIHPYPVSE PGSAKWDEKK EVSWKERMDD WKSKQGIVAG GAPDPDDYDA
DVPLNDEARQ PLSRKVSIAS SKVNPYRMVI ILRLVVLGFF LRYRILHPVP DAIPLWLTSI
ICEIWFAVSW ILDQFPKWYP IDRETYLDRL SLRYEREGEP SLLSAVDLFV STVDPLKEPP
LVTANTVLSI LAVDYPVDKV SCYVSDDGAS MLTFESLSET AEFARKWVPF CKKFSIEPRA
PEFYFSQKVD YLKDKVHPNF VQERRAMKRE YEEFKVRINA LVAKAQKVPA EGWIMKDGTP
WPGNNTRDHP GMIQVFLGHS GGHDTEGNEL PRLVYVSREK RPGFQHHKKA GAMNALIRVS
AVLTNAPFML NLDCDHYINN SKAIREAMCF LMDPQVGRKV CYVQFPQRFD GIDVHDRYAN
RNTVFFDINM KGLDGIQGPV YVGTGCVFRR QALYGYNPPK GPKRPKMVTC DCCPCFGRKK
RKHGKDGLPE AVAADGGMDS DKEMLMSQMN FEKRFGQSAA FVTSTLMEEG GVPPSSSPAA
LLKEAIHVIS CGYEDKTDWG LELGWIYGSI TEDILTGFKM HCRGWRSVYC MPKRAAFKGS
APINLSDRLN QVLRWALGSV EIFFSRHSPL LYGYKNGNLK WLERFSYINT TIYPFTSLPL
LAYCTLPAVC LLTGKFIMPP ISTFASLFFI ALFISIFATG ILEMRWSGVS IEEWWRNEQF
WVIGGVSAHL FAVVQGLLKV LAGIDTNFTV TSKATGDEDD EFAELYAFKW TTLLIPPTTL
LILNIIGVVA GVSDAINNGS EAWGPLFGKL FFAFWVIVHL YPFLKGLMGR QNRTPTIVVI
WSVLLASIFS LLWVRIDPFT IKARGPDVRQ CGINC
