CESA4_ORYSI
ID CESA4_ORYSI Reviewed; 989 AA.
AC A2WV32; A6N152; B8A9F7;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Cellulose synthase A catalytic subunit 4 [UDP-forming];
DE EC=2.4.1.12;
DE AltName: Full=OsCesA4;
GN Name=CESA4; ORFNames=OsI_03742;
OS Oryza sativa subsp. indica (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=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 296-574.
RA Kumari S., Panjabi V., Singla-Pareek S.L., Sopory S.K., Pareek A.;
RT "A comparative transcriptome map of early and late salinity stress
RT responses in contrasting genotypes of Oryza sativa L.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
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).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18037139; DOI=10.1016/s1673-8527(07)60115-5;
RA Yan C., Yan S., Zeng X., Zhang Z., Gu M.;
RT "Fine mapping and isolation of Bc7(t), allelic to OsCesA4.";
RL J. Genet. Genomics 34:1019-1027(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 (By similarity). Involved
CC in the secondary cell wall formation. {ECO:0000250,
CC ECO:0000269|PubMed:12970476, ECO:0000269|PubMed:18037139}.
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 80 percent of cellulose content in culm.
CC {ECO:0000269|PubMed:12970476, ECO:0000269|PubMed:18037139}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. Plant
CC cellulose synthase subfamily. {ECO:0000305}.
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DR EMBL; CM000126; EEC71479.1; -; Genomic_DNA.
DR EMBL; EF576384; ABR25972.1; -; mRNA.
DR AlphaFoldDB; A2WV32; -.
DR SMR; A2WV32; -.
DR STRING; 39946.A2WV32; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR EnsemblPlants; BGIOSGA004463-TA; BGIOSGA004463-PA; BGIOSGA004463.
DR Gramene; BGIOSGA004463-TA; BGIOSGA004463-PA; BGIOSGA004463.
DR HOGENOM; CLU_001418_0_0_1; -.
DR OMA; CATPYDE; -.
DR UniPathway; UPA00695; -.
DR Proteomes; UP000007015; Chromosome 1.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016760; F:cellulose synthase (UDP-forming) activity; IEA:UniProtKB-EC.
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:0042742; P:defense response to bacterium; IEA:EnsemblPlants.
DR GO; GO:0050832; P:defense response to fungus; IEA:EnsemblPlants.
DR GO; GO:0009834; P:plant-type secondary cell wall biogenesis; IMP:UniProtKB.
DR GO; GO:0006970; P:response to osmotic stress; IEA:EnsemblPlants.
DR GO; GO:0009414; P:response to water deprivation; IEA:EnsemblPlants.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR005150; Cellulose_synth.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF03552; Cellulose_synt; 1.
DR SUPFAM; SSF53448; SSF53448; 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..989
FT /note="Cellulose synthase A catalytic subunit 4 [UDP-
FT forming]"
FT /id="PRO_0000319362"
FT TOPO_DOM 1..184
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 206..213
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 235..772
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 773..793
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 794..798
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 799..819
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 820..835
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 836..856
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 857..884
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 885..905
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 906..916
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 917..937
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 938..946
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 947..967
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 968..989
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ZN_FING 9..47
FT /note="RING-type; degenerate"
FT REGION 138..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 362..389
FT /evidence="ECO:0000255"
FT ACT_SITE 308
FT /evidence="ECO:0000255"
FT ACT_SITE 688
FT /evidence="ECO:0000255"
FT BINDING 9
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 12
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 20
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 23
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 28
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 31
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 43
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 46
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 474
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 476
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT CARBOHYD 862
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 989 AA; 111085 MW; FF07A9EFF1A00139 CRC64;
MMESGVPPCA ACGDDAHAAC RACSYALCKA CLDEDAAEGR TTCARCGGEY GAPDPAHGQG
AVVEEEVEES HEPVASGVRE RVTMASQLSD HQDEGVHART MSTHARTISS VSGVGSELND
ESGKPIWKNR VESWKEKKKE KKASAKKAAA KAQAPPVEEQ IMDEKDLTDA YEPLSRIIPI
SKNKLTPYRA VIIMRLVVLG LFFHYRITNP VYSAFGLWMT SVICEIWFGF SWILDQFPKW
CPINRETYVD RLIARYGDGE DSGLAPVDFF VSTVDPLKEP PLITANTVLS ILAVDYPVEK
ISCYVSDDGS AMLTFESLAE TAEFARRWVP FCKKYSIEPR APEFYFSQKI DYLKDKIHPS
FVKERRAMKR DYEEYKVRIN ALVAKAQKTP EEGWIMQDGT PWPGNNPRDH PGMIQVFLGE
TGARDFDGNE LPRLVYVSRE KRPGYQHHKK AGAMNALVRV SAVLTNAPYI LNLDCDHYVN
NSKAVREAMC FMMDPSVGRD VCYVQFPQRF DGIDRSDRYA NRNVVFFDVN MKGLDGLQGP
VYVGTGCCFY RQALYGYGPP SLPALPKSSV CSWCCCCCPK KKAEKSEKEM HRDSRREDLE
SAIFNLREID NYDEYERSML ISQMSFEKSF GLSSVFIEST LMENGGVPES ANPSTLIKEA
IHVISCGYEE KTEWGKEIGW IYGSVTEDIL TGFKMHCRGW RSIYCMPIRP AFKGSAPINL
SDRLHQVLRW ALGSVEIFLS RHCPLWYGYG GGRLKWLQRL SYINTIVYPF TSLPLIAYCC
LPAICLLTGK FIIPTLSNAA TIWFLGLFIS IIVTSVLELR WSGIGIEDWW RNEQFWVIGG
VSAHLFAVFQ GILKMIAGLD TNFTVTAKAT DDTEFGELYV FKWTTVLIPP TSILVLNLVG
VVAGFSDALN SGYESWGPLF GKVFFAMWVI MHLYPFLKGL MGRQNRTPTI VVLWSVLLAS
VFSLLWVKID PFIGSSETTT TNSCANFDC
