Q17GS9
Gene name |
arm |
Protein name |
Armadillo segment polarity protein |
Names |
|
Species |
Aedes aegypti (Yellowfever mosquito) (Culex aegypti) |
KEGG Pathway |
aag:5576477 |
EC number |
|
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 Q17GS9
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q17GS9-F1 | Predicted | AlphaFoldDB |
No variants for Q17GS9
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q17GS9 | |||||
No associated diseases with Q17GS9
4 regional properties for Q17GS9
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| repeat | Armadillo | 146 - 395 | IPR000225-1 |
| repeat | Armadillo | 405 - 484 | IPR000225-2 |
| repeat | Armadillo | 482 - 592 | IPR000225-3 |
| repeat | Armadillo | 593 - 675 | IPR000225-4 |
Functions
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| adherens junction | A cell-cell junction composed of the epithelial cadherin-catenin complex. The epithelial cadherins, or E-cadherins, of each interacting cell extend through the plasma membrane into the extracellular space and bind to each other. The E-cadherins bind to catenins on the cytoplasmic side of the membrane, where the E-cadherin-catenin complex binds to cytoskeletal components and regulatory and signaling molecules. |
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
1 GO annotations of molecular function
| Name | Definition |
|---|---|
| cadherin binding | Binding to cadherin, a type I membrane protein involved in cell adhesion. |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| canonical Wnt signaling pathway | The series of molecular signals initiated by binding of a Wnt protein to a frizzled family receptor on the surface of the target cell, followed by propagation of the signal via beta-catenin, and ending with a change in transcription of target genes. In this pathway, the activated receptor signals via downstream effectors that result in the inhibition of beta-catenin phosphorylation, thereby preventing degradation of beta-catenin. Stabilized beta-catenin can then accumulate and travel to the nucleus to trigger changes in transcription of target genes. |
| cell adhesion | The attachment of a cell, either to another cell or to an underlying substrate such as the extracellular matrix, via cell adhesion molecules. |
| neuroblast fate commitment | The process in which the developmental fate of a cell becomes restricted such that it will differentiate into a neuroblast. |
| segment polarity determination | Division of the 14 parasegments of the embryo into anterior and posterior compartments; exemplified by the actions of the segment polarity gene products. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSYQMPQNRT | MSHNPYNSSD | MPMPSAKEQT | LMWQQNSYLG | DSGIHSGAVT | QVPSLSGKDD |
| 70 | 80 | 90 | 100 | 110 | 120 |
| DMEDDPLMFD | MDQGFSQNFT | QDQVDDMNQQ | LSQTRSQRVR | AAMFPETLEE | GIEIPSTQFD |
| 130 | 140 | 150 | 160 | 170 | 180 |
| PQQPTAVQRL | SEPSQMLKHA | VVNLINYQDD | ADLATRAIPE | LIKLLNDEDQ | VVVSQAAMMV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| HQLSKKEASR | HAIMNSPQMV | AALVRALSQS | NDLETTKGAV | GTLHNLSHHR | QGLLAIFKSG |
| 250 | 260 | 270 | 280 | 290 | 300 |
| GIPALVKLLS | SPVESVLFYA | ITTLHNLLLH | QDGSKMAVRL | AGGLQKMVAL | LQRNNVKFLA |
| 310 | 320 | 330 | 340 | 350 | 360 |
| IVTDCLQILA | YGNQESKLII | LASTGPSELV | RIMRSYDYEK | LLWTTSRVLK | VLSVCSSNKP |
| 370 | 380 | 390 | 400 | 410 | 420 |
| AIVEAGGMQA | LAMHLGNPSQ | RLVQNCLWTL | RNLSDAATKV | DGLETLLSGL | VTVLGSSDVN |
| 430 | 440 | 450 | 460 | 470 | 480 |
| VVTCAAGILS | NLTCNNQRNK | VTVCQVGGVE | ALVGTIINAG | DREEITEPAV | CALRHLTSRH |
| 490 | 500 | 510 | 520 | 530 | 540 |
| PESESAQNIV | RNGYGLPVIV | KLLNPPSRWP | LIKAVIGLIR | NLALCPSNAA | PLREHGAIHL |
| 550 | 560 | 570 | 580 | 590 | 600 |
| LVRLLFKAFQ | DTQRQRSSVA | TNGSQPPGAY | ADGVRMEEIV | EGTVGALHIL | SKEELNRQLI |
| 610 | 620 | 630 | 640 | 650 | 660 |
| RQQNVISIFV | QLLFYNDIEN | IQRVAAGVLC | ELAVDKEVAE | MIEAEGATAP | LTELLNSANE |
| 670 | 680 | 690 | 700 | 710 | 720 |
| GVATYAAAVL | FKMSEDKSMD | YKKRFSSELT | TLPVFRDDTM | WNNGELGIGP | DLQDILSPDQ |
| 730 | 740 | 750 | 760 | 770 | 780 |
| AYEGLYGQGP | PSVHSSHGGR | AFQQGYDTLP | IDSMQGLEIG | GGGNAGPAGS | NPNAGNNPGA |
| 790 | 800 | 810 | 820 | 830 | |
| GGPPSGQPTS | PYAMDMDVGE | MDASELTFDH | LDVMPSPPQD | NNQVAAWYDT | DL |