CESA2_ORYSI
ID CESA2_ORYSI Reviewed; 1073 AA.
AC A2XN66;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Probable cellulose synthase A catalytic subunit 2 [UDP-forming];
DE EC=2.4.1.12;
DE AltName: Full=OsCesA2;
GN Name=CESA2; ORFNames=OsI_013509;
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).
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; CM000128; EAY92276.1; -; Genomic_DNA.
DR AlphaFoldDB; A2XN66; -.
DR SMR; A2XN66; -.
DR STRING; 39946.A2XN66; -.
DR iPTMnet; A2XN66; -.
DR EnsemblPlants; BGIOSGA009600-TA; BGIOSGA009600-PA; BGIOSGA009600.
DR Gramene; BGIOSGA009600-TA; BGIOSGA009600-PA; BGIOSGA009600.
DR HOGENOM; CLU_001418_0_1_1; -.
DR OMA; EIPRVYI; -.
DR UniPathway; UPA00695; -.
DR Proteomes; UP000007015; Chromosome 3.
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; IEA:UniProtKB-KW.
DR GO; GO:0071669; P:plant-type cell wall organization or biogenesis; IEA:UniProt.
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 3: Inferred from homology;
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..1073
FT /note="Probable cellulose synthase A catalytic subunit 2
FT [UDP-forming]"
FT /id="PRO_0000319359"
FT TOPO_DOM 1..270
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 292..293
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..314
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 315..856
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 857..877
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 878..882
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 883..903
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 904..918
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 919..939
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 940..969
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 970..990
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 991..1001
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1002..1022
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1023..1031
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1032..1052
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1053..1073
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ZN_FING 13..59
FT /note="RING-type; degenerate"
FT REGION 66..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 655..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 443..470
FT /evidence="ECO:0000255"
FT ACT_SITE 389
FT /evidence="ECO:0000255"
FT ACT_SITE 773
FT /evidence="ECO:0000255"
FT BINDING 13
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 16
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 32
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 35
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="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 43
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 55
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 58
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 555
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 557
FT /ligand="substrate"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1073 AA; 120682 MW; 55B677033E77A7BE CRC64;
MDGAKSGKQC HVCQICGDGV GTAADGELFT ACDVCGFPVC RPCYEYERKD GSQACPQCKT
KYKRHKGSPP ILGDESDDVD ADDASDVNYP TSGNQDHKHK IAERMLTWRM NSGRNDDIVH
SKYDSGEIGH PKYDSGEIPR IYIPSLTHSQ ISGEIPGASP DHMMSPVGNI GRRGHPFPYV
NHSPNPSREF SGSLGNVAWK ERVDGWKMKD KGAIPMANGT SIAPSEGRGV GDIDASTDYN
MEDALLNDET RQPLSRKVPI SSSRINPYRM VIVLRLIVLC IFLHYRITNP VRNAYPLWLL
SVICEIWFAL SWILDQFPKW SPINRETYLD RLALRYDREG EPSQLAPVDI FVSTVDPMKE
PPLVTANTVL SILAVDYPVD KVSCYVSDDG AAMLTFDALA ETSEFARKWV PFCKKYSIEP
RAPEWYFAQK IDYLKDKVQA SFVKDRRAMK REYEEFKVRV NALVAKAQKV PEEGWIMQDG
TPWPGNNTRD HPGMIQVFLG HSGGLDTEGN ELPRLVYVSR EKRPGFQHHK KAGAMNALVR
VSAVLTNGQY LLNLDCDHYI NNSKALREAM CFLMDPNLGR RVCYVQFPQR FDGIDRNDRY
ANRNTVFFDI NLRGLDGLQG PVYVGTGCVF NRTALYGYEP PIKQKRPGYF SSLCGGRKKT
KKSKEKSTEK KKSHKHVDSS VPVFNLEDIE EGIEGSGFDD EKSLLMSQMS LEKRFGQSSV
FVASTLMEYG GVPQSATPES LLKEAIHVIS CGYEDKSDWG TEIGWIYGSV TEDILTGFKM
HARGWRSIYC MPKRPAFKGS APINLSDRLN QVLRWALGSV EILFSRHCPI WYGYGGRLKF
LERFAYINTT IYPLTSIPLL LYCILPAICL LTGKFIIPEI SNFASIWFIS LFLSIFATGI
LEMRWSGVGI DEWWRNEQFW VIGGISAHLF AVFQGLLKVL AGIDTSFTVT SKASDEEGDF
AELYMFKWTT LLIPPTTILI INLVGVVAGI SYAINSGYQS WGPLFGKLFF AFWVIVHLYP
FLKGLMGRQN RTPTIVVVWA ILLASIFSLL WVRIDPFTTR VTGPDTQKCG INC
