CESA7_ORYSJ
ID CESA7_ORYSJ Reviewed; 1063 AA.
AC Q9AV71; B7EKJ9; Q7XDK9;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Cellulose synthase A catalytic subunit 7 [UDP-forming];
DE EC=2.4.1.12;
DE AltName: Full=OsCesA7;
GN Name=CESA7; OrderedLocusNames=Os10g0467800, LOC_Os10g32980;
GN ORFNames=OSJNBa0006L06.10;
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=12791992; DOI=10.1126/science.1083523;
RA Yu Y., Rambo T., Currie J., Saski C., Kim H.-R., Collura K., Thompson S.,
RA Simmons J., Yang T.-J., Nah G., Patel A.J., Thurmond S., Henry D.,
RA Oates R., Palmer M., Pries G., Gibson J., Anderson H., Paradkar M.,
RA Crane L., Dale J., Carver M.B., Wood T., Frisch D., Engler F.,
RA Soderlund C., Palmer L.E., Teytelman L., Nascimento L., De la Bastide M.,
RA Spiegel L., Ware D., O'Shaughnessy A., Dike S., Dedhia N., Preston R.,
RA Huang E., Ferraro K., Kuit K., Miller B., Zutavern T., Katzenberger F.,
RA Muller S., Balija V., Martienssen R.A., Stein L., Minx P., Johnson D.,
RA Cordum H., Mardis E., Cheng Z., Jiang J., Wilson R., McCombie W.R.,
RA Wing R.A., Yuan Q., Ouyang S., Liu J., Jones K.M., Gansberger K.,
RA Moffat K., Hill J., Tsitrin T., Overton L., Bera J., Kim M., Jin S.,
RA Tallon L., Ciecko A., Pai G., Van Aken S., Utterback T., Reidmuller S.,
RA Bormann J., Feldblyum T., Hsiao J., Zismann V., Blunt S., de Vazeille A.R.,
RA Shaffer T., Koo H., Suh B., Yang Q., Haas B., Peterson J., Pertea M.,
RA Volfovsky N., Wortman J., White O., Salzberg S.L., Fraser C.M., Buell C.R.,
RA Messing J., Song R., Fuks G., Llaca V., Kovchak S., Young S., Bowers J.E.,
RA Paterson A.H., Johns M.A., Mao L., Pan H., Dean R.A.;
RT "In-depth view of structure, activity, and evolution of rice chromosome
RT 10.";
RL Science 300:1566-1569(2003).
RN [2]
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 [3]
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 [4]
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 [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 75% 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC022457; AAK27814.1; -; Genomic_DNA.
DR EMBL; DP000086; AAP54202.1; -; Genomic_DNA.
DR EMBL; AP008216; BAF26725.1; -; Genomic_DNA.
DR EMBL; AP014966; BAT11225.1; -; Genomic_DNA.
DR EMBL; AK072259; BAG92896.1; -; mRNA.
DR RefSeq; XP_015614140.1; XM_015758654.1.
DR AlphaFoldDB; Q9AV71; -.
DR SMR; Q9AV71; -.
DR STRING; 4530.OS10T0467800-01; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR PaxDb; Q9AV71; -.
DR PRIDE; Q9AV71; -.
DR EnsemblPlants; Os10t0467800-01; Os10t0467800-01; Os10g0467800.
DR GeneID; 4348853; -.
DR Gramene; Os10t0467800-01; Os10t0467800-01; Os10g0467800.
DR KEGG; osa:4348853; -.
DR eggNOG; ENOG502QPUN; Eukaryota.
DR HOGENOM; CLU_001418_0_2_1; -.
DR InParanoid; Q9AV71; -.
DR OMA; ENGDYNP; -.
DR OrthoDB; 679241at2759; -.
DR PlantReactome; R-OSA-1119314; Cellulose biosynthesis.
DR UniPathway; UPA00695; -.
DR Proteomes; UP000000763; Chromosome 10.
DR Proteomes; UP000059680; Chromosome 10.
DR Genevisible; Q9AV71; 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..1063
FT /note="Cellulose synthase A catalytic subunit 7 [UDP-
FT forming]"
FT /id="PRO_0000319367"
FT TOPO_DOM 1..213
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 235..237
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 259..845
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 846..866
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 867..871
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 872..892
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 893..907
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 908..928
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 929..959
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 960..980
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 981..991
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 992..1012
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1013..1021
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1022..1042
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1043..1063
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ZN_FING 18..64
FT /note="RING-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 116..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 387..414
FT /evidence="ECO:0000255"
FT ACT_SITE 333
FT /evidence="ECO:0000255"
FT ACT_SITE 762
FT /evidence="ECO:0000255"
FT BINDING 18
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 21
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 37
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 40
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
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 48
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 499
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 501
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT CARBOHYD 935
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1063 AA; 119788 MW; BE02386EFAECDE4E CRC64;
MDTASVTGGE HKGKEKTCRV CGEEVAARED GKPFVACAEC GFPVCKPCYE YERSEGTQCC
PQCNTRYKRH KGCPRVEGDE DDGGDMDDFE EEFQIKSPTK QKPPHEPVNF DVYSENGEQP
AQKWRPGGPA LSSFTGSVAG KDLEQEREME GGMEWKDRID KWKTKQEKRG KLNRDDSDDD
DDKNDDEYML LAEARQPLWR KVPIPSSKIN PYRIVIVLRL VVLCFFLKFR ITTPAMDAVP
LWLASVICEL WFALSWILDQ LPKWSPVTRE TYLDRLALRY ERDGEPCRLA PIDFFVSTVD
PLKEPPIITA NTVLSILAVD YPVDRVSCYV SDDGASMLLF DTLSETAEFA RRWVPFCKKF
TIEPRAPEFY FSQKIDYLKD KVQPTFVKER RAMKREYEEF KVRINALVAK AQKKPEEGWV
MQDGTPWPGN NTRDHPGMIQ VYLGSQGALD VEGSELPRLV YVSREKRPGY NHHKKAGAMN
SLVRVSAVLT NAPFILNLDC DHYVNNSKAV REAMCFLMDK QLGKKLCYVQ FPQRFDGIDR
HDRYANRNTV FFDINMKGLD GIQGPVYVGT GTVFNRQALY GYDPPRPEKR PKMTCDCWPS
WCCCCCCFGG GKRGKSHKNK KGGGGGEGGG LDEPRRGLLG FYKKRSKKDK LGGGAASLAG
GKKGYRKHQR GFELEEIEEG LEGYDELERS SLMSQKSFEK RFGQSPVFIA STLVEDGGLP
QGAAADPAAL IKEAIHVISC GYEEKTEWGK EIGWIYGSVT EDILTGFKMH CRGWKSVYCT
PARAAFKGSA PINLSDRLHQ VLRWALGSVE IFMSRHCPLW YAYGGRLKWL ERFAYTNTIV
YPFTSIPLLA YCTIPAVCLL TGKFIIPTLN NLASIWFIAL FLSIIATGVL ELRWSGVSIE
DWWRNEQFWV IGGVSAHLFA VFQGLLKVLG GVDTNFTVTS KAAADETDAF GELYLFKWTT
LLVPPTTLII INMVGIVAGV SDAVNNGYGS WGPLFGKLFF SFWVILHLYP FLKGLMGRQN
RTPTIVVLWS ILLASIFSLV WVRIDPFIPK PKGPVLKPCG VSC
