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   02-SEP-2026, entry version 170.
DE   RecName: Full=Cellulose synthase A catalytic subunit 7 [UDP-forming];
DE            EC=2.4.1.12 {ECO:0000305};
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|UniProtKB:Q9SWW6,
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) + UDP + H(+); 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         Evidence={ECO:0000305};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:Q941L0};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:Q9SWW6};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q9SWW6};
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}.
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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   AlphaFoldDB; Q9AV71; -.
DR   SMR; Q9AV71; -.
DR   FunCoup; Q9AV71; 159.
DR   STRING; 39947.Q9AV71; -.
DR   GlyCosmos; Q9AV71; 1 site, No reported glycans.
DR   PaxDb; 39947-Q9AV71; -.
DR   EnsemblPlants; Os10t0467800-01; Os10t0467800-01; Os10g0467800.
DR   Gramene; Os10t0467800-01; Os10t0467800-01; Os10g0467800.
DR   KEGG; dosa:Os10g0467800; -.
DR   eggNOG; ENOG502QPUN; Eukaryota.
DR   HOGENOM; CLU_001418_0_2_1; -.
DR   InParanoid; Q9AV71; -.
DR   OMA; EGSQCCP; -.
DR   OrthoDB; 2161379at2759; -.
DR   PlantReactome; R-OSA-1119314; Cellulose biosynthesis.
DR   UniPathway; UPA00695; -.
DR   Proteomes; UP000059680; Chromosome 10.
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:0030244; P:cellulose biosynthetic process; IMP:UniProtKB.
DR   GO; GO:0009834; P:plant-type secondary cell wall biogenesis; IMP:UniProtKB.
DR   CDD; cd16617; mRING-HC-C4C4_CesA; 1.
DR   FunFam; 3.30.40.10:FF:000558; Cellulose synthase; 1.
DR   FunFam; 3.90.550.10:FF:000009; Cellulose synthase; 1.
DR   Gene3D; 3.90.550.10; Spore Coat Polysaccharide Biosynthesis Protein SpsA, Chain A; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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   PANTHER; PTHR13301; X-BOX TRANSCRIPTION FACTOR-RELATED; 1.
DR   Pfam; PF03552; Cellulose_synt; 1.
DR   Pfam; PF14569; zf-UDP; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   SUPFAM; SSF57850; RING/U-box; 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; Manganese; Membrane;
KW   Metal-binding; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix; Zinc; 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   COMPBIAS        141..154
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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         297
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q941L0"
FT   BINDING         303
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q941L0"
FT   BINDING         304
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q941L0"
FT   BINDING         333
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q941L0"
FT   BINDING         474
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q941L0"
FT   BINDING         475
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:Q941L0"
FT   BINDING         499
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:Q941L0"
FT   CARBOHYD        935
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
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
//