CESA5_ORYSI
ID CESA5_ORYSI Reviewed; 1092 AA.
AC A2XNT2;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Probable cellulose synthase A catalytic subunit 5 [UDP-forming];
DE EC=2.4.1.12;
DE AltName: Full=OsCesA5;
GN Name=CESA5; ORFNames=OsI_013725;
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; EAY92492.1; -; Genomic_DNA.
DR AlphaFoldDB; A2XNT2; -.
DR SMR; A2XNT2; -.
DR STRING; 39946.A2XNT2; -.
DR PRIDE; A2XNT2; -.
DR EnsemblPlants; BGIOSGA013897-TA; BGIOSGA013897-PA; BGIOSGA013897.
DR Gramene; BGIOSGA013897-TA; BGIOSGA013897-PA; BGIOSGA013897.
DR HOGENOM; CLU_001418_0_0_1; -.
DR OMA; CWPKWKN; -.
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; 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 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..1092
FT /note="Probable cellulose synthase A catalytic subunit 5
FT [UDP-forming]"
FT /id="PRO_0000319364"
FT TOPO_DOM 1..279
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 280..300
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 301..302
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 303..323
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 324..868
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 869..889
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 890..901
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 902..922
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 923..938
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 939..959
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 960..987
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 988..1008
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1009..1019
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1020..1040
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1041..1049
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1050..1070
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1071..1092
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 COILED 450..479
FT /evidence="ECO:0000255"
FT ACT_SITE 398
FT /evidence="ECO:0000255"
FT ACT_SITE 792
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 564
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 566
FT /ligand="substrate"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1092 AA; 123396 MW; A682D0A434BE24D0 CRC64;
MEASAGLVAG SHNRNELVVI RRDGEPGPKP VKHTNGQVCQ ICGDDVGLTP DGEPFVACNE
CAFPVCRDCY EYERREGTQN CPQCKTRFKR LKGCARVPGD EEEEDVDDLE NEFNWRDKTD
SQYVAESMLH GHMSYGRGGD LDGVPQHFQP IPNVPLLTNG EMADDIPPEQ HALVPSFMGG
GGKRIHPLPY ADPNLPVQPR SMDPSKDLAA YGYGSVAWKE RMESWKQKQE RLHQMRNDGG
GKDWDGDGDD ADLPLMDEAR QPLSRKIPIS SSLVNPYRMI IIIRLVVLGF FFHYRVMHPV
PDAFALWLIS VICEIWFAMS WILDQFPKWF PIERETYLDR LTLRFDKEGQ QSQLAPVDFF
VSTVDPMKEP PLVTANTVLS ILAVDYPVDK VSCYVSDDGA AMLTFEALSE TSEFAKKWVP
FCKRYSLEPR APEWYFQQKI DYLKDKVAPN FVRERRAMKR EYEEFKVRIN ALVAKAQKVP
EEGWTMQDGT PWPGNNVRDH PGMIQVFLGQ SGGHDVEGNE LPRLVYVSRE KRPGYNHHKK
AGAMNALVRV SAVLTNAPYM LNLDCDHYIN NSKAIKEAMC FMMDPLVGKK VCYVQFPQRF
DGIDRHDRYA NRNVVFFDIN MKGLDGIQGP IYVGTGCVFR RQALYGYDAP KSKKPPSRTC
NCWPKWCICC CCFGNRTNKK KTAKPKTEKK KRLFFKRAEN QSPAYALGEI DEGAPGAENE
KAGIVNQQKL EKKFGQSSVF VASTLLENGG TLKSASPASL LKEAIHVISC GYEDKTDWGK
EIGWIYGSVT EDILTGFKMH CHGWRSIYCI PKRAAFKGSA PLNLSDRLHQ VLRWALGSIE
IFFSNHCPLW YGYGGGLKCL ERFSYINSIV YPWTSIPLLA YCTLPAICLL TGKFITPELT
NIASLWFMSL FICIFATGIL EMRWSGVGID DWWRNEQFWV IGGVSSHLFA VFQGLLKVIA
GIDTSFTVTS KGGDDEEFSE LYTFKWTTLL IPPTTLLLLN FIGVVAGVSN AINNGYESWG
PLFGKLFFAF WVIVHLYPFL KGLVGRQNRT PTIVIVWSIL LASIFSLLWV RIDPFLAKND
GPLLEECGLD CN
