CESA8_ORYSJ
ID CESA8_ORYSJ Reviewed; 1081 AA.
AC Q84ZN6; B7EKN8;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Probable cellulose synthase A catalytic subunit 8 [UDP-forming];
DE EC=2.4.1.12;
DE AltName: Full=OsCesA8;
GN Name=CESA8; OrderedLocusNames=Os07g0208500, LOC_Os07g10770;
GN ORFNames=OJ1136_A05.10, OJ1559_F09.120, OsJ_022567;
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).
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 -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. Plant
CC cellulose synthase subfamily. {ECO:0000305}.
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DR EMBL; AP003748; BAD30175.1; -; Genomic_DNA.
DR EMBL; AP003837; BAC57282.1; -; Genomic_DNA.
DR EMBL; AP008213; BAF21076.1; -; Genomic_DNA.
DR EMBL; AP014963; BAT00571.1; -; Genomic_DNA.
DR EMBL; CM000144; EAZ39084.1; -; Genomic_DNA.
DR EMBL; AK072356; BAG92935.1; -; mRNA.
DR RefSeq; XP_015646894.1; XM_015791408.1.
DR PDB; 5JNP; X-ray; 2.40 A; A/B=398-523.
DR PDBsum; 5JNP; -.
DR AlphaFoldDB; Q84ZN6; -.
DR SMR; Q84ZN6; -.
DR STRING; 4530.OS07T0208500-01; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR PaxDb; Q84ZN6; -.
DR PRIDE; Q84ZN6; -.
DR EnsemblPlants; Os07t0208500-01; Os07t0208500-01; Os07g0208500.
DR GeneID; 4342699; -.
DR Gramene; Os07t0208500-01; Os07t0208500-01; Os07g0208500.
DR KEGG; osa:4342699; -.
DR eggNOG; ENOG502QSUQ; Eukaryota.
DR HOGENOM; CLU_001418_0_1_1; -.
DR InParanoid; Q84ZN6; -.
DR OMA; SAQVCQI; -.
DR OrthoDB; 679241at2759; -.
DR BRENDA; 2.4.1.12; 4460.
DR PlantReactome; R-OSA-1119314; Cellulose biosynthesis.
DR UniPathway; UPA00695; -.
DR Proteomes; UP000000763; Chromosome 7.
DR Proteomes; UP000007752; Chromosome 7.
DR Proteomes; UP000059680; Chromosome 7.
DR ExpressionAtlas; Q84ZN6; baseline and differential.
DR Genevisible; Q84ZN6; 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; IBA:GO_Central.
DR GO; GO:0009833; P:plant-type primary cell wall biogenesis; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cell wall biogenesis/degradation;
KW Cellulose biosynthesis; Coiled coil; Glycoprotein; Glycosyltransferase;
KW Membrane; Metal-binding; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix; Zinc; Zinc-finger.
FT CHAIN 1..1081
FT /note="Probable cellulose synthase A catalytic subunit 8
FT [UDP-forming]"
FT /id="PRO_0000319368"
FT TOPO_DOM 1..277
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 299..300
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 301..321
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 322..864
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 865..885
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 886..890
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 891..911
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 912..926
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 927..947
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 948..977
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 978..998
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 999..1009
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1010..1030
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1031..1039
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1040..1060
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1061..1081
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ZN_FING 19..65
FT /note="RING-type; degenerate"
FT REGION 72..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 660..684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 450..477
FT /evidence="ECO:0000255"
FT ACT_SITE 396
FT /evidence="ECO:0000255"
FT ACT_SITE 781
FT /evidence="ECO:0000255"
FT BINDING 19
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 22
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 38
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 41
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="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 49
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
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 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 562
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 564
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT CARBOHYD 954
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT HELIX 403..423
FT /evidence="ECO:0007829|PDB:5JNP"
FT HELIX 430..435
FT /evidence="ECO:0007829|PDB:5JNP"
FT TURN 440..443
FT /evidence="ECO:0007829|PDB:5JNP"
FT HELIX 449..471
FT /evidence="ECO:0007829|PDB:5JNP"
SQ SEQUENCE 1081 AA; 120794 MW; BA17F2D40BFAA2EB CRC64;
MDGDADAVKS GRHGSGQACQ ICGDGVGTTA EGDVFAACDV CGFPVCRPCY EYERKDGTQA
CPQCKTKYKR HKGSPAIRGE EGEDTDADDV SDYNYPASGS ADQKQKIADR MRSWRMNAGG
GGDVGRPKYD SGEIGLTKYD SGEIPRGYIP SVTNSQISGE IPGASPDHHM MSPTGNIGKR
APFPYVNHSP NPSREFSGSI GNVAWKERVD GWKLKQDKGA IPMTNGTSIA PSEGRGVGDI
DASTDYNMED ALLNDETRQP LSRKVPLPSS RINPYRMVIV LRLVVLSIFL HYRITNPVRN
AYPLWLLSVI CEIWFALSWI LDQFPKWFPI NRETYLDRLA LRYDREGEPS QLAAVDIFVS
TVDPMKEPPL VTANTVLSIL AVDYPVDKVS CYVSDDGAAM LTFDALAETS EFARKWVPFV
KKYNIEPRAP EWYFSQKIDY LKDKVHPSFV KDRRAMKREY EEFKVRINGL VAKAQKVPEE
GWIMQDGTPW PGNNTRDHPG MIQVFLGHSG GLDTEGNELP RLVYVSREKR PGFQHHKKAG
AMNALVRVSA VLTNGQYMLN LDCDHYINNS KALREAMCFL MDPNLGRSVC YVQFPQRFDG
IDRNDRYANR NTVFFDINLR GLDGIQGPVY VGTGCVFNRT ALYGYEPPIK QKKKGSFLSS
LCGGRKKASK SKKKSSDKKK SNKHVDSAVP VFNLEDIEEG VEGAGFDDEK SLLMSQMSLE
KRFGQSAAFV ASTLMEYGGV PQSATPESLL KEAIHVISCG YEDKTEWGTE IGWIYGSVTE
DILTGFKMHA RGWRSIYCMP KRPAFKGSAP INLSDRLNQV LRWALGSVEI LFSRHCPIWY
GYGGRLKFLE RFAYINTTIY PLTSIPLLIY CVLPAICLLT GKFIIPEISN FASIWFISLF
ISIFATGILE MRWSGVGIDE WWRNEQFWVI GGISAHLFAV FQGLLKVLAG IDTNFTVTSK
ASDEDGDFAE LYMFKWTTLL IPPTTILIIN LVGVVAGISY AINSGYQSWG PLFGKLFFAF
WVIVHLYPFL KGLMGRQNRT PTIVVVWAIL LASIFSLLWV RIDPFTTRVT GPDTQTCGIN
C
