CESA6_ORYSJ
ID CESA6_ORYSJ Reviewed; 1092 AA.
AC Q6YVM4; B9FWG3;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Probable cellulose synthase A catalytic subunit 6 [UDP-forming];
DE EC=2.4.1.12;
DE AltName: Full=OsCesA6;
GN Name=CESA6; OrderedLocusNames=Os07g0252400, LOC_Os07g14850;
GN ORFNames=OsJ_23733 {ECO:0000312|EMBL:EEE66900.1}, P0669H03.13;
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; AP005824; BAC84511.1; -; Genomic_DNA.
DR EMBL; AP008213; BAF21217.1; -; Genomic_DNA.
DR EMBL; AP014963; BAT00852.1; -; Genomic_DNA.
DR EMBL; CM000144; EEE66900.1; -; Genomic_DNA.
DR EMBL; AK100914; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015647044.1; XM_015791558.1.
DR AlphaFoldDB; Q6YVM4; -.
DR SMR; Q6YVM4; -.
DR STRING; 4530.OS07T0252400-01; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR PaxDb; Q6YVM4; -.
DR PRIDE; Q6YVM4; -.
DR EnsemblPlants; Os07t0252400-01; Os07t0252400-01; Os07g0252400.
DR GeneID; 4342850; -.
DR Gramene; Os07t0252400-01; Os07t0252400-01; Os07g0252400.
DR KEGG; osa:4342850; -.
DR eggNOG; ENOG502QQGG; Eukaryota.
DR HOGENOM; CLU_001418_0_1_1; -.
DR InParanoid; Q6YVM4; -.
DR OMA; EIERINM; -.
DR OrthoDB; 679241at2759; -.
DR UniPathway; UPA00695; -.
DR Proteomes; UP000000763; Chromosome 7.
DR Proteomes; UP000007752; Chromosome 7.
DR Proteomes; UP000059680; Chromosome 7.
DR ExpressionAtlas; Q6YVM4; baseline and differential.
DR Genevisible; Q6YVM4; 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; 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; Glycosyltransferase; Membrane; Metal-binding;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix; Zinc;
KW Zinc-finger.
FT CHAIN 1..1092
FT /note="Probable cellulose synthase A catalytic subunit 6
FT [UDP-forming]"
FT /id="PRO_0000319366"
FT TOPO_DOM 1..280
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 302..303
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 304..324
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 325..868
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 869..889
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 890..901
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 902..922
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 923..937
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 938..958
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 959..987
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 988..1008
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1009..1019
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1020..1040
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1041..1049
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1050..1070
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1071..1092
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ZN_FING 42..88
FT /note="RING-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 100..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 453..480
FT /evidence="ECO:0000255"
FT COMPBIAS 104..118
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 399
FT /evidence="ECO:0000255"
FT ACT_SITE 792
FT /evidence="ECO:0000255"
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 45
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 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
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 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 565
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 567
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT CONFLICT 412
FT /note="T -> A (in Ref. 5; AK100914)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1092 AA; 122410 MW; C6739B6FCB6A91D5 CRC64;
MEASAGLVAG SHNRNELVVI RRDGGGGGGV GGRRAAEAKA ACQICGDDVG EGPDGEPFVA
CNECAFPVCR NCYDYERREG SQACPQCKTR FKRLKGCPRV AGDEEEDGVD DLEGEFGLDG
REDDPQYIAE SMLRANMSYG RGGDLQPFQP IPNVPLLTNG QMVDDIPPEQ HALVPSYMGG
GGGGGKRIHP LPFADPSVPV QPRSMDPSKD LAAYGYGSVA WKERMEGWKQ KQERMQQLRS
EGGGDWDGDG DADLPLMDEA RQPLSRKVPI SSSRINPYRM IIIIRLVVLG FFFHYRVMHP
VNDAFALWLI SVICEIWFAM SWILDQFPKW LPIERETYLD RLSLRFDKEG QPSQLAPVDF
FVSTVDPSKE PPLVTANTVL SILSVDYPVE KVSCYVSDDG AAMLTFEALS ETSEFAKKWV
PFCKKFNIEP RAPEWYFQQK IDYLKDKVAA SFVRERRAMK RDYEEFKVRI NALVAKAQKV
PEEGWTMQDG SPWPGNNVRD HPGMIQVFLG QSGGRDVEGN ELPRLVYVSR EKRPGYNHHK
KAGAMNALVR VSAVLSNAPY LLNLDCDHYI NNSKAIREAM CFMMDPLVGK KVCYVQFPQR
FDGIDRHDRY ANRNVVFFDI NMKGLDGIQG PIYVGTGCVF RRQALYGYDA PKTKKPPSRT
CNCWPKWCCC CCCGNRHTKK KTTKPKPEKK KRLFFKKAEN QSPAYALGEI EEGAPGAETD
KAGIVNQQKL EKKFGQSSVF VASTLLENGG TLKSASPASL LKEAIHVISC GYEDKTDWGK
EIGWIYGSIT EDILTGFKMH CHGWRSIYCI PKRPAFKGSA PLNLSDRLHQ VLRWALGSVE
IFFSKHCPLW YGYGGGLKFL ERFSYINSIV YPWTSIPLLA YCTLPAICLL TGKFITPELT
NVASLWFMSL FICIFVTGIL EMRWSGVAID DWWRNEQFWV IGGVSSHLFA VFQGLLKVLA
GVDTSFTVTS KAGDDEEFSE LYTFKWTTLL IPPTTLLLLN FIGVVAGVSN AINNGYESWG
PLFGKLFFAF WVIVHLYPFL KGLVGRQNRT PTIVIVWSIL LASIFSLLWV RIDPFLAKNN
GPLLEECGLD CN
