O48946 · CESA1_ARATH
- ProteinCellulose synthase A catalytic subunit 1 [UDP-forming]
- GeneCESA1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1081 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalytic subunit of cellulose synthase terminal complexes ('rosettes'), required for beta-1,4-glucan microfibril crystallization, a major mechanism of the cell wall formation. Involved in the primary cell wall formation. Required during embryogenesis for cell elongation, orientation of cell expansion and complex cell wall formations, such as interdigitated pattern of epidermal pavement cells, stomatal guard cells and trichomes. Plays a role in lateral roots formation, but seems not necessary for the development of tip-growing cells such as root hairs. The presence of each protein CESA1 and CESA6 is critical for cell expansion after germination.
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 | 39 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 42 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 58 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 61 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 66 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 69 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 81 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 84 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 359 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 365 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 366 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Active site | 395 | |||||
Sequence: D | ||||||
Binding site | 395 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 536 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 537 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 561 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 780 | |||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endosome | |
Cellular Component | Golgi apparatus | |
Cellular Component | plasma membrane | |
Cellular Component | trans-Golgi network | |
Molecular Function | cellulose synthase (UDP-forming) activity | |
Molecular Function | metal ion binding | |
Biological Process | cell wall organization | |
Biological Process | cellulose biosynthetic process | |
Biological Process | hyperosmotic salinity response | |
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 nameCellulose synthase A catalytic subunit 1 [UDP-forming]
- EC number
- Short namesAtCesA1
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionO48946
- Secondary accessions
Proteomes
Organism-specific databases
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 | 1-270 | Cytoplasmic | ||||
Sequence: MEASAGLVAGSYRRNELVRIRHESDGGTKPLKNMNGQICQICGDDVGLAETGDVFVACNECAFPVCRPCYEYERKDGTQCCPQCKTRFRRHRGSPRVEGDEDEDDVDDIENEFNYAQGANKARHQRHGEEFSSSSRHESQPIPLLTHGHTVSGEIRTPDTQSVRTTSGPLGPSDRNAISSPYIDPRQPVPVRIVDPSKDLNSYGLGNVDWKERVEGWKLKQEKNMLQMTGKYHEGKGGEIEGTGSNGEELQMADDTRLPMSRVVPIPSSR | ||||||
Transmembrane | 271-291 | Helical | ||||
Sequence: LTPYRVVIILRLIILCFFLQY | ||||||
Topological domain | 292-299 | Extracellular | ||||
Sequence: RTTHPVKN | ||||||
Transmembrane | 300-320 | Helical | ||||
Sequence: AYPLWLTSVICEIWFAFSWLL | ||||||
Topological domain | 321-856 | Cytoplasmic | ||||
Sequence: DQFPKWYPINRETYLDRLAIRYDRDGEPSQLVPVDVFVSTVDPLKEPPLVTANTVLSILSVDYPVDKVACYVSDDGSAMLTFESLSETAEFAKKWVPFCKKFNIEPRAPEFYFAQKIDYLKDKIQPSFVKERRAMKREYEEFKVRINALVAKAQKIPEEGWTMQDGTPWPGNNTRDHPGMIQVFLGHSGGLDTDGNELPRLIYVSREKRPGFQHHKKAGAMNALIRVSAVLTNGAYLLNVDCDHYFNNSKAIKEAMCFMMDPAIGKKCCYVQFPQRFDGIDLHDRYANRNIVFFDINMKGLDGIQGPVYVGTGCCFNRQALYGYDPVLTEEDLEPNIIVKSCCGSRKKGKSSKKYNYEKRRGINRSDSNAPLFNMEDIDEGFEGYDDERSILMSQRSVEKRFGQSPVFIAATFMEQGGIPPTTNPATLLKEAIHVISCGYEDKTEWGKEIGWIYGSVTEDILTGFKMHARGWISIYCNPPRPAFKGSAPINLSDRLNQVLRWALGSIEILLSRHCPIWYGYHGRLRLLERIAYINT | ||||||
Transmembrane | 857-877 | Helical | ||||
Sequence: IVYPITSIPLIAYCILPAFCL | ||||||
Topological domain | 878-889 | Extracellular | ||||
Sequence: ITDRFIIPEISN | ||||||
Transmembrane | 890-910 | Helical | ||||
Sequence: YASIWFILLFISIAVTGILEL | ||||||
Topological domain | 911-925 | Cytoplasmic | ||||
Sequence: RWSGVSIEDWWRNEQ | ||||||
Transmembrane | 926-946 | Helical | ||||
Sequence: FWVIGGTSAHLFAVFQGLLKV | ||||||
Topological domain | 947-976 | Extracellular | ||||
Sequence: LAGIDTNFTVTSKATDEDGDFAELYIFKWT | ||||||
Transmembrane | 977-997 | Helical | ||||
Sequence: ALLIPPTTVLLVNLIGIVAGV | ||||||
Topological domain | 998-1008 | Cytoplasmic | ||||
Sequence: SYAVNSGYQSW | ||||||
Transmembrane | 1009-1029 | Helical | ||||
Sequence: GPLFGKLFFALWVIAHLYPFL | ||||||
Topological domain | 1030-1038 | Extracellular | ||||
Sequence: KGLLGRQNR | ||||||
Transmembrane | 1039-1059 | Helical | ||||
Sequence: TPTIVIVWSVLLASIFSLLWV | ||||||
Topological domain | 1060-1081 | Cytoplasmic | ||||
Sequence: RINPFVDANPNANNFNGKGGVF |
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 549 | In rsw1-1; temperature-sensitive disassembly of cellulose synthase complexes ('rosettes') and altered cellulose crystallinity, accumulation of noncrystalline beta-1,4-glucan, normal below 21 degrees Celsius but not above 30 degrees Celsius, accumulation of starch in roots, constitutive and high expression of vegetative storage proteins (VSP) and widespread morphological abnormalities. | ||||
Sequence: A → V | ||||||
Mutagenesis | 631 | In rsw1-2; abnormal embryos, very short and stout plants, reduced crystalline cellulose deposition in cell walls, and restricted intercellular spaces due to increased cell junction thickness. | ||||
Sequence: G → S | ||||||
Mutagenesis | 779 | In rsw1-45; abnormal embryos, short and stout plants, and reduced crystalline cellulose deposition in cell walls. | ||||
Sequence: E → K | ||||||
Mutagenesis | 780 | In rsw1-20; abnormal embryos, short and stout plants, reduced crystalline cellulose deposition in cell walls, and restricted intercellular spaces due to increased cell junction thickness. | ||||
Sequence: D → N |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 19 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for modified residue, chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 1 | N-acetylmethionine | ||||
Sequence: M | ||||||
Chain | PRO_0000166367 | 1-1081 | Cellulose synthase A catalytic subunit 1 [UDP-forming] | |||
Sequence: MEASAGLVAGSYRRNELVRIRHESDGGTKPLKNMNGQICQICGDDVGLAETGDVFVACNECAFPVCRPCYEYERKDGTQCCPQCKTRFRRHRGSPRVEGDEDEDDVDDIENEFNYAQGANKARHQRHGEEFSSSSRHESQPIPLLTHGHTVSGEIRTPDTQSVRTTSGPLGPSDRNAISSPYIDPRQPVPVRIVDPSKDLNSYGLGNVDWKERVEGWKLKQEKNMLQMTGKYHEGKGGEIEGTGSNGEELQMADDTRLPMSRVVPIPSSRLTPYRVVIILRLIILCFFLQYRTTHPVKNAYPLWLTSVICEIWFAFSWLLDQFPKWYPINRETYLDRLAIRYDRDGEPSQLVPVDVFVSTVDPLKEPPLVTANTVLSILSVDYPVDKVACYVSDDGSAMLTFESLSETAEFAKKWVPFCKKFNIEPRAPEFYFAQKIDYLKDKIQPSFVKERRAMKREYEEFKVRINALVAKAQKIPEEGWTMQDGTPWPGNNTRDHPGMIQVFLGHSGGLDTDGNELPRLIYVSREKRPGFQHHKKAGAMNALIRVSAVLTNGAYLLNVDCDHYFNNSKAIKEAMCFMMDPAIGKKCCYVQFPQRFDGIDLHDRYANRNIVFFDINMKGLDGIQGPVYVGTGCCFNRQALYGYDPVLTEEDLEPNIIVKSCCGSRKKGKSSKKYNYEKRRGINRSDSNAPLFNMEDIDEGFEGYDDERSILMSQRSVEKRFGQSPVFIAATFMEQGGIPPTTNPATLLKEAIHVISCGYEDKTEWGKEIGWIYGSVTEDILTGFKMHARGWISIYCNPPRPAFKGSAPINLSDRLNQVLRWALGSIEILLSRHCPIWYGYHGRLRLLERIAYINTIVYPITSIPLIAYCILPAFCLITDRFIIPEISNYASIWFILLFISIAVTGILELRWSGVSIEDWWRNEQFWVIGGTSAHLFAVFQGLLKVLAGIDTNFTVTSKATDEDGDFAELYIFKWTALLIPPTTVLLVNLIGIVAGVSYAVNSGYQSWGPLFGKLFFALWVIAHLYPFLKGLLGRQNRTPTIVIVWSVLLASIFSLLWVRINPFVDANPNANNFNGKGGVF | ||||||
Glycosylation | 953 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
S-acylated.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in germinating seeds, seedlings, roots, stems, shoots leaves and flowers, but not in mature flowers.
Developmental stage
Expressed throughout the embryo during all steps of embryogenesis, and decrease toward the bent-cotyledon stage. Higher levels in tissues undergoing primary cell wall formation, and drop of expression when secondary wall synthesis takes place. High levels in developing seedlings and elongating stems, with a decrease at later growth stages.
Gene expression databases
Interaction
Subunit
Interacts with CESA3 and CESA6. Assembly with CESA3 and CESA6 is required for functional complex in primary cell wall cellulose synthesis. Interacts with STL1 and STL2, but not with GOT1 (PubMed:27277162).
Binds to CSI1 (PubMed:20616083).
Interacts with PAT24/TIP1 (PubMed:35644016).
Binds to CSI1 (PubMed:20616083).
Interacts with PAT24/TIP1 (PubMed:35644016).
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for zinc finger, region, compositional bias, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Zinc finger | 39-85 | RING-type; degenerate | ||||
Sequence: CQICGDDVGLAETGDVFVACNECAFPVCRPCYEYERKDGTQCCPQCK | ||||||
Region | 117-195 | Disordered | ||||
Sequence: QGANKARHQRHGEEFSSSSRHESQPIPLLTHGHTVSGEIRTPDTQSVRTTSGPLGPSDRNAISSPYIDPRQPVPVRIVD | ||||||
Compositional bias | 153-174 | Polar residues | ||||
Sequence: GEIRTPDTQSVRTTSGPLGPSD | ||||||
Coiled coil | 449-476 | |||||
Sequence: VKERRAMKREYEEFKVRINALVAKAQKI |
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)122,237
- Last updated1998-06-01 v1
- ChecksumBDEB5D9DEE334D59
Sequence caution
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 153-174 | Polar residues | ||||
Sequence: GEIRTPDTQSVRTTSGPLGPSD |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF027172 EMBL· GenBank· DDBJ | AAC39334.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL034567 EMBL· GenBank· DDBJ | CAA22568.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL161581 EMBL· GenBank· DDBJ | CAB79958.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002687 EMBL· GenBank· DDBJ | AEE86053.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BT008654 EMBL· GenBank· DDBJ | AAP40467.1 EMBL· GenBank· DDBJ | mRNA | ||
AK222115 EMBL· GenBank· DDBJ | BAD95078.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK226243 EMBL· GenBank· DDBJ | BAE98406.1 EMBL· GenBank· DDBJ | mRNA |