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 P36366
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P36366-F1 | Predicted | AlphaFoldDB |
2 variants for P36366
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| 522 | V>L | B form [UniProt] | No | ||
| 530 | S>F | B form [UniProt] | No |
No associated diseases with P36366
No regional properties for P36366
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for P36366 | |||
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| endoplasmic reticulum membrane | The lipid bilayer surrounding the endoplasmic reticulum. |
| 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. |
| membrane | A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| flavin adenine dinucleotide binding | Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2. |
| N,N-dimethylaniline monooxygenase activity | Catalysis of the reaction: N,N-dimethylaniline + NADPH + H+ + O2 = N,N-dimethylaniline N-oxide + NADP+ + H2O. |
| NADP binding | Binding to nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NADP+, or the reduced form, NADPH. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| NADPH oxidation | A metabolic process that results in the oxidation of reduced nicotinamide adenine dinucleotide, NADPH, to the oxidized form, NADP. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAKKVAVIGA | GVSGLISLKC | CVDEGLEPTC | FERTEDIGGL | WRFKENVEDG | RASIYKSVIT |
| 70 | 80 | 90 | 100 | 110 | 120 |
| NTSKEMSCFS | DFPMPEDFPN | FLHNSKLLEY | FRLFAKKFDL | LKYIQFQTTV | LTVKKHPDFS |
| 130 | 140 | 150 | 160 | 170 | 180 |
| SSGQWEVVTQ | SDGKEQSAVF | DAVMVCSGHH | ILPHIPLKSF | PGIERFKGQY | FHSRQYKHPA |
| 190 | 200 | 210 | 220 | 230 | 240 |
| GFEGKRILVI | GIGNSASDIA | SELSKNAAQV | FISTRNGSWV | MSRISEDGYP | WDMVFHTRFK |
| 250 | 260 | 270 | 280 | 290 | 300 |
| SMLRNILPRT | VSKWMMEQQL | NRWFNHANYS | LEPKNKYLMK | EPILNDDLPS | RILYGAVKVK |
| 310 | 320 | 330 | 340 | 350 | 360 |
| SRVTQLTETS | ALFEDGTVEE | DIDVIVFATG | YTFSFPFLEE | SLVKIEHNMV | SLYKYMFPPQ |
| 370 | 380 | 390 | 400 | 410 | 420 |
| LEKPTLTCMG | LIQPLGSIFP | TVELQARWAT | RVFKGLCHLP | SEKTMMEDII | KRNEKRIDLF |
| 430 | 440 | 450 | 460 | 470 | 480 |
| GESQSQIVQT | NYVDYLDELA | LEIGAKPDLI | SFLLKDPELA | VKLCFGPCNS | YQYRLVGPGQ |
| 490 | 500 | 510 | 520 | 530 | |
| WEGARRAILT | QKQRILKPLK | TRSVKAAPNL | SASFLMKILA | LVAVFVAFFS | QLYGF |