A2WV32
Gene name |
CESA4 (OsI_03742) |
Protein name |
Cellulose synthase A catalytic subunit 4 [UDP-forming] |
Names |
OsCesA4 |
Species |
Oryza sativa subsp indica (Rice) |
KEGG Pathway |
|
EC number |
2.4.1.12: Hexosyltransferases |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for A2WV32
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A2WV32-F1 | Predicted | AlphaFoldDB |
No variants for A2WV32
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A2WV32 | |||||
No associated diseases with A2WV32
No regional properties for A2WV32
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for A2WV32 | |||
Functions
| Description | ||
|---|---|---|
| EC Number | 2.4.1.12 | Hexosyltransferases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| integral component of membrane | The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| cellulose synthase (UDP-forming) activity | Catalysis of the reaction: UDP-glucose + ((1,4)-beta-D-glucosyl)(n) = UDP + ((1,4)-beta-D-glucosyl)(n+1). |
| metal ion binding | Binding to a metal ion. |
7 GO annotations of biological process
| Name | Definition |
|---|---|
| cell wall organization | A process that results in the assembly, arrangement of constituent parts, or disassembly of the cell wall, the rigid or semi-rigid envelope lying outside the cell membrane of plant, fungal and most prokaryotic cells, maintaining their shape and protecting them from osmotic lysis. |
| cellulose biosynthetic process | The chemical reactions and pathways resulting in the formation of cellulose, a linear beta1-4 glucan of molecular mass 50-400 kDa with the pyranose units in the -4C1 conformation. |
| defense response to bacterium | Reactions triggered in response to the presence of a bacterium that act to protect the cell or organism. |
| defense response to fungus | Reactions triggered in response to the presence of a fungus that act to protect the cell or organism. |
| plant-type secondary cell wall biogenesis | A cellular process that results in the biosynthesis of constituent macromolecules, assembly, and arrangement of constituent parts of inextensible cellulose- and pectin-containing cell walls that are formed between the plasma membrane and primary cell wall after cell expansion is complete. An example of this is found in Arabidopsis thaliana. |
| response to osmotic stress | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating an increase or decrease in the concentration of solutes outside the organism or cell. |
| response to water deprivation | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a water deprivation stimulus, prolonged deprivation of water. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MMESGVPPCA | ACGDDAHAAC | RACSYALCKA | CLDEDAAEGR | TTCARCGGEY | GAPDPAHGQG |
| 70 | 80 | 90 | 100 | 110 | 120 |
| AVVEEEVEES | HEPVASGVRE | RVTMASQLSD | HQDEGVHART | MSTHARTISS | VSGVGSELND |
| 130 | 140 | 150 | 160 | 170 | 180 |
| ESGKPIWKNR | VESWKEKKKE | KKASAKKAAA | KAQAPPVEEQ | IMDEKDLTDA | YEPLSRIIPI |
| 190 | 200 | 210 | 220 | 230 | 240 |
| SKNKLTPYRA | VIIMRLVVLG | LFFHYRITNP | VYSAFGLWMT | SVICEIWFGF | SWILDQFPKW |
| 250 | 260 | 270 | 280 | 290 | 300 |
| CPINRETYVD | RLIARYGDGE | DSGLAPVDFF | VSTVDPLKEP | PLITANTVLS | ILAVDYPVEK |
| 310 | 320 | 330 | 340 | 350 | 360 |
| ISCYVSDDGS | AMLTFESLAE | TAEFARRWVP | FCKKYSIEPR | APEFYFSQKI | DYLKDKIHPS |
| 370 | 380 | 390 | 400 | 410 | 420 |
| FVKERRAMKR | DYEEYKVRIN | ALVAKAQKTP | EEGWIMQDGT | PWPGNNPRDH | PGMIQVFLGE |
| 430 | 440 | 450 | 460 | 470 | 480 |
| TGARDFDGNE | LPRLVYVSRE | KRPGYQHHKK | AGAMNALVRV | SAVLTNAPYI | LNLDCDHYVN |
| 490 | 500 | 510 | 520 | 530 | 540 |
| NSKAVREAMC | FMMDPSVGRD | VCYVQFPQRF | DGIDRSDRYA | NRNVVFFDVN | MKGLDGLQGP |
| 550 | 560 | 570 | 580 | 590 | 600 |
| VYVGTGCCFY | RQALYGYGPP | SLPALPKSSV | CSWCCCCCPK | KKAEKSEKEM | HRDSRREDLE |
| 610 | 620 | 630 | 640 | 650 | 660 |
| SAIFNLREID | NYDEYERSML | ISQMSFEKSF | GLSSVFIEST | LMENGGVPES | ANPSTLIKEA |
| 670 | 680 | 690 | 700 | 710 | 720 |
| IHVISCGYEE | KTEWGKEIGW | IYGSVTEDIL | TGFKMHCRGW | RSIYCMPIRP | AFKGSAPINL |
| 730 | 740 | 750 | 760 | 770 | 780 |
| SDRLHQVLRW | ALGSVEIFLS | RHCPLWYGYG | GGRLKWLQRL | SYINTIVYPF | TSLPLIAYCC |
| 790 | 800 | 810 | 820 | 830 | 840 |
| LPAICLLTGK | FIIPTLSNAA | TIWFLGLFIS | IIVTSVLELR | WSGIGIEDWW | RNEQFWVIGG |
| 850 | 860 | 870 | 880 | 890 | 900 |
| VSAHLFAVFQ | GILKMIAGLD | TNFTVTAKAT | DDTEFGELYV | FKWTTVLIPP | TSILVLNLVG |
| 910 | 920 | 930 | 940 | 950 | 960 |
| VVAGFSDALN | SGYESWGPLF | GKVFFAMWVI | MHLYPFLKGL | MGRQNRTPTI | VVLWSVLLAS |
| 970 | 980 | ||||
| VFSLLWVKID | PFIGSSETTT | TNSCANFDC |