CESA1_ORYSI
ID CESA1_ORYSI Reviewed; 1076 AA.
AC A2Y0X2;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Probable cellulose synthase A catalytic subunit 1 [UDP-forming];
DE EC=2.4.1.12;
DE AltName: Full=OsCesA1;
GN Name=CESA1; ORFNames=OsI_017965;
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: 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. {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}.
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; CM000130; EAY96732.1; -; Genomic_DNA.
DR AlphaFoldDB; A2Y0X2; -.
DR SMR; A2Y0X2; -.
DR STRING; 39946.A2Y0X2; -.
DR iPTMnet; A2Y0X2; -.
DR PRIDE; A2Y0X2; -.
DR EnsemblPlants; BGIOSGA018714-TA; BGIOSGA018714-PA; BGIOSGA018714.
DR Gramene; BGIOSGA018714-TA; BGIOSGA018714-PA; BGIOSGA018714.
DR HOGENOM; CLU_001418_0_2_1; -.
DR OMA; HESDGGT; -.
DR UniPathway; UPA00695; -.
DR Proteomes; UP000007015; Chromosome 5.
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; Glycoprotein; Glycosyltransferase; Membrane; Metal-binding;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix; Zinc;
KW Zinc-finger.
FT CHAIN 1..1076
FT /note="Probable cellulose synthase A catalytic subunit 1
FT [UDP-forming]"
FT /id="PRO_0000319357"
FT TOPO_DOM 1..267
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 268..288
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 289..296
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 297..317
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 318..851
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 852..872
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 873..884
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 885..905
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 906..920
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 921..941
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 942..971
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 972..992
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 993..1003
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1004..1024
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1025..1033
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1034..1054
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1055..1076
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ZN_FING 41..87
FT /note="RING-type; degenerate"
FT REGION 119..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 446..473
FT /evidence="ECO:0000255"
FT ACT_SITE 392
FT /evidence="ECO:0000255"
FT ACT_SITE 775
FT /evidence="ECO:0000255"
FT BINDING 41
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 44
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 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 558
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 560
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT CARBOHYD 948
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1076 AA; 121268 MW; 6B40F19DAEDF1AEC CRC64;
MAANAGMVAG SRNRNEFVMI RPDGDAPPPA KPGKSVNGQV CQICGDTVGV SATGDVFVAC
NECAFPVCRP CYEYERKEGN QCCPQCKTRY KRHKGSPRVQ GDEEEEDVDD LDNEFNYKHG
NGKGPEWQIQ RQGEDVDLSS SSRHEQHRIP RLTSGQQISG EIPDASPDRH SIRSGTSSYV
DPSVPVPVRI VDPSKDLNSY GINSVDWQER VASWRNKQDK NMMQVANKYP EARGGDMEGT
GSNGEDMQMV DDARLPLSRI VPIPSNQLNL YRIVIILRLI ILMFFFQYRV THPVRDAYGL
WLVSVICEIW FALSWLLDQF PKWYPINRET YLDRLALRYD REGEPSQLAP IDVFVSTVDP
LKEPPLITAN TVLSILAVDY PVDKVSCYVS DDGSAMLTFE ALSETAEFAR KWVPFCKKHN
IEPRAPEFYF AQKIDYLKDK IQPSFVKERR AMKREYEEFK VRINALVAKA QKVPEEGWTM
ADGTAWPGNN PRDHPGMIQV FLGHSGGLDT DGNELPRLVY VSREKRPGFQ HHKKAGAMNA
LIRVSAVLTN GAYLLNVDCD HYFNSSKALR EAMCFMMDPA LGRKTCYVQF PQRFDGIDLH
DRYANRNIVF FDINMKGLDG IQGPVYVGTG CCFNRQALYG YDPVLTEADL EPNIVVKSCC
GGRKKKSKSY MDSKNRMMKR TESSAPIFNM EDIEEGIEGY EDERSVLMSQ KRLEKRFGQS
PIFIASTFMT QGGIPPSTNP ASLLKEAIHV ISCGYEDKTE WGKEIGWIYG SVTEDILTGF
KMHARGWISI YCMPPRPCFK GSAPINLSDR LNQVLRWALG SVEILLSRHC PIWYGYNGRL
KLLERLAYIN TIVYPITSIP LIAYCVLPAI CLLTNKFIIP EISNYAGMFF ILLFASIFAT
GILELRWSGV GIEDWWRNEQ FWVIGGTSAH LFAVFQGLLK VLAGIDTNFT VTSKASDEDG
DFAELYVFKW TSLLIPPTTV LVINLVGMVA GISYAINSGY QSWGPLFGKL FFSIWVILHL
YPFLKGLMGR QNRTPTIVIV WSILLASIFS LLWVKIDPFI SPTQKAVALG QCGVNC
