CESA3_ORYSJ
ID CESA3_ORYSJ Reviewed; 1093 AA.
AC Q69V23; B7F6W2;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Probable cellulose synthase A catalytic subunit 3 [UDP-forming];
DE EC=2.4.1.12;
DE AltName: Full=OsCesA3;
GN Name=CESA3; OrderedLocusNames=Os07g0424400, LOC_Os07g24190;
GN ORFNames=P0409D09.11;
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 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AK073561; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AP004298; BAD30574.1; -; Genomic_DNA.
DR EMBL; AP008213; BAF21401.1; -; Genomic_DNA.
DR EMBL; AP014963; BAT01208.1; -; Genomic_DNA.
DR EMBL; AK073561; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK121193; BAH00360.1; -; mRNA.
DR RefSeq; XP_015646807.1; XM_015791321.1.
DR AlphaFoldDB; Q69V23; -.
DR SMR; Q69V23; -.
DR STRING; 4530.OS07T0424400-01; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR PaxDb; Q69V23; -.
DR EnsemblPlants; Os07t0424400-01; Os07t0424400-01; Os07g0424400.
DR EnsemblPlants; Os07t0424400-06; Os07t0424400-06; Os07g0424400.
DR GeneID; 4343049; -.
DR Gramene; Os07t0424400-01; Os07t0424400-01; Os07g0424400.
DR Gramene; Os07t0424400-06; Os07t0424400-06; Os07g0424400.
DR KEGG; osa:4343049; -.
DR eggNOG; ENOG502QQGG; Eukaryota.
DR HOGENOM; CLU_001418_0_0_1; -.
DR InParanoid; Q69V23; -.
DR OMA; MKHENGG; -.
DR OrthoDB; 679241at2759; -.
DR UniPathway; UPA00695; -.
DR Proteomes; UP000000763; Chromosome 7.
DR Proteomes; UP000059680; Chromosome 7.
DR ExpressionAtlas; Q69V23; baseline and differential.
DR Genevisible; Q69V23; 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..1093
FT /note="Probable cellulose synthase A catalytic subunit 3
FT [UDP-forming]"
FT /id="PRO_0000319361"
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..869
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 870..890
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 891..902
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 903..923
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 924..939
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 940..960
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 961..988
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 989..1009
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1010..1020
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1021..1041
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1042..1050
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1051..1071
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1072..1093
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ZN_FING 39..85
FT /note="RING-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 233..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 453..480
FT /evidence="ECO:0000255"
FT ACT_SITE 399
FT /evidence="ECO:0000255"
FT ACT_SITE 793
FT /evidence="ECO:0000255"
FT BINDING 39
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
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 58
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
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 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
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 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
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 565
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 567
FT /ligand="substrate"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1093 AA; 123503 MW; 33075A79C634AD31 CRC64;
MEASAGLVAG SHNRNELVVI RRDGDPGPKP LRQQNGQVCQ ICGDDVGLNP DGEPFVACNE
CAFPVCRDCY EYERREGTQN CPQCKTRFKR LRGCARVPGD EEEDGVDDLE NEFNWRDRND
SQYVAESMLH AHMSYGRGGV DVNGVPQPFQ PNPNVPLLTD GQMVDDIPPE QHALVPSFMG
GGGKRIHPLP YADPNLPVQP RSMDPSKDLA AYGYGSVAWK ERMESWKQKQ ERLHQMRNDG
GGKDWDGDGD DGDLPLMDEA RQPLSRKVPI PSSQINPYRM VIIIRLVVLG FFFHYRVMHP
VPDAFALWLI SVICEIWFAM SWILDQFPKW FPIERETYLD RLTLRFDKEG QTSQLAPIDF
FVSTVDPLKE PPLVTANTVL SILAVDYPVD KVSCYVSDDG AAMLTFEALS ETSEFAKKWV
PFCKKYSIEP RAPEWYFQQK IDYLKDKVAP YFVRERRAMK REYEEFKVRI NALVAKAQKV
PEEGWTMQDG TPWPGNNVRD HPGMIQVFLG QSGGHDIEGN ELPRLVYVSR EKRPGYNHHK
KAGAMNALVR VSAVLTNAPY MLNLDCDHYI NNSKAIKEAM CFMMDPLVGK KVCYVQFPQR
FDGIDRHDRY ANRNVVFFDI NMKGLDGIQG PIYVGTGCVF RRQALYGYDA PKTKKPPSRT
CNCWPKWCIC CCCFGDRKSK KKTTKPKTEK KKRSFFKRAE NQSPAYALGE IEEGAPGAEN
EKAGIVNQQK LEKKFGQSSV FVASTLLENG GTLKSASPAS LLKEAIHVIS CGYEDKTDWG
KEIGWIYGSV TEDILTGFKM HCHGWRSIYC IPKLPAFKGS APLNLSDRLH QVLRWALGSV
EIFFSNHCPL WYGYGGGLKC LERFSYINSI VYPFTSIPLL AYCTLPAICL LTGKFITPEL
TNVASLWFMS LFICIFATGI LEMRWSGVGI DDWWRNEQFW VIGGVSSHLF ALFQGLLKVI
AGIDTSFTVT SKGGDDEEFS ELYTFKWTTL LIPPTTLLLL NFIGVVAGVS NAINNGYESW
GPLFGKLFFA FWVIVHLYPF LKGLVGRQNR TPTIVIVWSI LLASIFSLLW VRIDPFLAKN
DGPLLEECGL DCN
