Q84ZN6 · CESA8_ORYSJ
- ProteinProbable cellulose synthase A catalytic subunit 8 [UDP-forming]
- GeneCESA8
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1081 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Probable catalytic subunit of cellulose synthase terminal complexes ('rosettes'), required for beta-1,4-glucan microfibril crystallization, a major mechanism of the cell wall formation.
Catalytic activity
- [(1->4)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->4)-beta-D-glucosyl](n+1) + H+ + UDP
[(1→4)-β-D-glucosyl](n) RHEA-COMP:10033 + CHEBI:58885 = [(1→4)-β-D-glucosyl](n+1) RHEA-COMP:10034 + CHEBI:15378 + CHEBI:58223
Cofactor
Protein has several cofactor binding sites:
Note: Binds 2 Zn2+ ions per subunit.
Pathway
Glycan metabolism; plant cellulose biosynthesis.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 19 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 22 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 38 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 41 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 46 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 49 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 61 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 64 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 360 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 366 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 367 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Active site | 396 | |||||
Sequence: D | ||||||
Binding site | 396 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 537 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 538 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 562 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 781 | |||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | plasma membrane | |
Molecular Function | cellulose synthase (UDP-forming) activity | |
Molecular Function | cellulose synthase activity | |
Molecular Function | metal ion binding | |
Biological Process | cell wall organization | |
Biological Process | cellulose biosynthetic process | |
Biological Process | plant-type primary cell wall biogenesis |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameProbable cellulose synthase A catalytic subunit 8 [UDP-forming]
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > BOP clade > Oryzoideae > Oryzeae > Oryzinae > Oryza > Oryza sativa
Accessions
- Primary accessionQ84ZN6
- Secondary accessions
Proteomes
Genome annotation databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-277 | Cytoplasmic | ||||
Sequence: MDGDADAVKSGRHGSGQACQICGDGVGTTAEGDVFAACDVCGFPVCRPCYEYERKDGTQACPQCKTKYKRHKGSPAIRGEEGEDTDADDVSDYNYPASGSADQKQKIADRMRSWRMNAGGGGDVGRPKYDSGEIGLTKYDSGEIPRGYIPSVTNSQISGEIPGASPDHHMMSPTGNIGKRAPFPYVNHSPNPSREFSGSIGNVAWKERVDGWKLKQDKGAIPMTNGTSIAPSEGRGVGDIDASTDYNMEDALLNDETRQPLSRKVPLPSSRINPYRM | ||||||
Transmembrane | 278-298 | Helical | ||||
Sequence: VIVLRLVVLSIFLHYRITNPV | ||||||
Topological domain | 299-300 | Extracellular | ||||
Sequence: RN | ||||||
Transmembrane | 301-321 | Helical | ||||
Sequence: AYPLWLLSVICEIWFALSWIL | ||||||
Topological domain | 322-864 | Cytoplasmic | ||||
Sequence: DQFPKWFPINRETYLDRLALRYDREGEPSQLAAVDIFVSTVDPMKEPPLVTANTVLSILAVDYPVDKVSCYVSDDGAAMLTFDALAETSEFARKWVPFVKKYNIEPRAPEWYFSQKIDYLKDKVHPSFVKDRRAMKREYEEFKVRINGLVAKAQKVPEEGWIMQDGTPWPGNNTRDHPGMIQVFLGHSGGLDTEGNELPRLVYVSREKRPGFQHHKKAGAMNALVRVSAVLTNGQYMLNLDCDHYINNSKALREAMCFLMDPNLGRSVCYVQFPQRFDGIDRNDRYANRNTVFFDINLRGLDGIQGPVYVGTGCVFNRTALYGYEPPIKQKKKGSFLSSLCGGRKKASKSKKKSSDKKKSNKHVDSAVPVFNLEDIEEGVEGAGFDDEKSLLMSQMSLEKRFGQSAAFVASTLMEYGGVPQSATPESLLKEAIHVISCGYEDKTEWGTEIGWIYGSVTEDILTGFKMHARGWRSIYCMPKRPAFKGSAPINLSDRLNQVLRWALGSVEILFSRHCPIWYGYGGRLKFLERFAYINTTIYPLTS | ||||||
Transmembrane | 865-885 | Helical | ||||
Sequence: IPLLIYCVLPAICLLTGKFII | ||||||
Topological domain | 886-890 | Extracellular | ||||
Sequence: PEISN | ||||||
Transmembrane | 891-911 | Helical | ||||
Sequence: FASIWFISLFISIFATGILEM | ||||||
Topological domain | 912-926 | Cytoplasmic | ||||
Sequence: RWSGVGIDEWWRNEQ | ||||||
Transmembrane | 927-947 | Helical | ||||
Sequence: FWVIGGISAHLFAVFQGLLKV | ||||||
Topological domain | 948-977 | Extracellular | ||||
Sequence: LAGIDTNFTVTSKASDEDGDFAELYMFKWT | ||||||
Transmembrane | 978-998 | Helical | ||||
Sequence: TLLIPPTTILIINLVGVVAGI | ||||||
Topological domain | 999-1009 | Cytoplasmic | ||||
Sequence: SYAINSGYQSW | ||||||
Transmembrane | 1010-1030 | Helical | ||||
Sequence: GPLFGKLFFAFWVIVHLYPFL | ||||||
Topological domain | 1031-1039 | Extracellular | ||||
Sequence: KGLMGRQNR | ||||||
Transmembrane | 1040-1060 | Helical | ||||
Sequence: TPTIVVVWAILLASIFSLLWV | ||||||
Topological domain | 1061-1081 | Cytoplasmic | ||||
Sequence: RIDPFTTRVTGPDTQTCGINC |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), glycosylation.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000319368 | 1-1081 | UniProt | Probable cellulose synthase A catalytic subunit 8 [UDP-forming] | |||
Sequence: MDGDADAVKSGRHGSGQACQICGDGVGTTAEGDVFAACDVCGFPVCRPCYEYERKDGTQACPQCKTKYKRHKGSPAIRGEEGEDTDADDVSDYNYPASGSADQKQKIADRMRSWRMNAGGGGDVGRPKYDSGEIGLTKYDSGEIPRGYIPSVTNSQISGEIPGASPDHHMMSPTGNIGKRAPFPYVNHSPNPSREFSGSIGNVAWKERVDGWKLKQDKGAIPMTNGTSIAPSEGRGVGDIDASTDYNMEDALLNDETRQPLSRKVPLPSSRINPYRMVIVLRLVVLSIFLHYRITNPVRNAYPLWLLSVICEIWFALSWILDQFPKWFPINRETYLDRLALRYDREGEPSQLAAVDIFVSTVDPMKEPPLVTANTVLSILAVDYPVDKVSCYVSDDGAAMLTFDALAETSEFARKWVPFVKKYNIEPRAPEWYFSQKIDYLKDKVHPSFVKDRRAMKREYEEFKVRINGLVAKAQKVPEEGWIMQDGTPWPGNNTRDHPGMIQVFLGHSGGLDTEGNELPRLVYVSREKRPGFQHHKKAGAMNALVRVSAVLTNGQYMLNLDCDHYINNSKALREAMCFLMDPNLGRSVCYVQFPQRFDGIDRNDRYANRNTVFFDINLRGLDGIQGPVYVGTGCVFNRTALYGYEPPIKQKKKGSFLSSLCGGRKKASKSKKKSSDKKKSNKHVDSAVPVFNLEDIEEGVEGAGFDDEKSLLMSQMSLEKRFGQSAAFVASTLMEYGGVPQSATPESLLKEAIHVISCGYEDKTEWGTEIGWIYGSVTEDILTGFKMHARGWRSIYCMPKRPAFKGSAPINLSDRLNQVLRWALGSVEILFSRHCPIWYGYGGRLKFLERFAYINTTIYPLTSIPLLIYCVLPAICLLTGKFIIPEISNFASIWFISLFISIFATGILEMRWSGVGIDEWWRNEQFWVIGGISAHLFAVFQGLLKVLAGIDTNFTVTSKASDEDGDFAELYMFKWTTLLIPPTTILIINLVGVVAGISYAINSGYQSWGPLFGKLFFAFWVIVHLYPFLKGLMGRQNRTPTIVVVWAILLASIFSLLWVRIDPFTTRVTGPDTQTCGINC | |||||||
Modified residue (large scale data) | 91 | PTMeXchange | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 131 | PTMeXchange | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 141 | PTMeXchange | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 189 | PTMeXchange | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 197 | PTMeXchange | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 718 | PTMeXchange | Phosphoserine | ||||
Sequence: S | |||||||
Glycosylation | 954 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for zinc finger, region, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Zinc finger | 19-65 | RING-type; degenerate | ||||
Sequence: CQICGDGVGTTAEGDVFAACDVCGFPVCRPCYEYERKDGTQACPQCK | ||||||
Region | 72-148 | Disordered | ||||
Sequence: KGSPAIRGEEGEDTDADDVSDYNYPASGSADQKQKIADRMRSWRMNAGGGGDVGRPKYDSGEIGLTKYDSGEIPRGY | ||||||
Coiled coil | 450-477 | |||||
Sequence: VKDRRAMKREYEEFKVRINGLVAKAQKV | ||||||
Region | 660-684 | Disordered | ||||
Sequence: SLCGGRKKASKSKKKSSDKKKSNKH |
Sequence similarities
Belongs to the glycosyltransferase 2 family. Plant cellulose synthase subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,081
- Mass (Da)120,794
- Last updated2003-06-01 v1
- ChecksumBA17F2D40BFAA2EB
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0P0X3V1 | A0A0P0X3V1_ORYSJ | Os07g0208500 | 294 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AP003748 EMBL· GenBank· DDBJ | BAD30175.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP003837 EMBL· GenBank· DDBJ | BAC57282.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP008213 EMBL· GenBank· DDBJ | BAF21076.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP014963 EMBL· GenBank· DDBJ | BAT00571.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CM000144 EMBL· GenBank· DDBJ | EAZ39084.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK072356 EMBL· GenBank· DDBJ | BAG92935.1 EMBL· GenBank· DDBJ | mRNA |