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 Q27319
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q27319-F1 | Predicted | AlphaFoldDB |
No variants for Q27319
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q27319 | |||||
No associated diseases with Q27319
6 regional properties for Q27319
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Gelsolin-like domain | 22 - 103 | IPR007123-1 |
| domain | Gelsolin-like domain | 146 - 208 | IPR007123-2 |
| domain | Gelsolin-like domain | 271 - 339 | IPR007123-3 |
| domain | Gelsolin-like domain | 416 - 495 | IPR007123-4 |
| domain | Gelsolin-like domain | 550 - 584 | IPR007123-5 |
| domain | Gelsolin-like domain | 647 - 720 | IPR007123-6 |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| cytoskeleton | A cellular structure that forms the internal framework of eukaryotic and prokaryotic cells. The cytoskeleton includes intermediate filaments, microfilaments, microtubules, the microtrabecular lattice, and other structures characterized by a polymeric filamentous nature and long-range order within the cell. The various elements of the cytoskeleton not only serve in the maintenance of cellular shape but also have roles in other cellular functions, including cellular movement, cell division, endocytosis, and movement of organelles. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| actin filament binding | Binding to an actin filament, also known as F-actin, a helical filamentous polymer of globular G-actin subunits. |
| metal ion binding | Binding to a metal ion. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| actin filament capping | The binding of a protein or protein complex to the end of an actin filament, thus preventing the addition, exchange or removal of further actin subunits. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MVPAFEGAGA | VEGLTIWRIE | NFEVVPYPKE | KYGQFYQGDS | YIVLYTRDVN | GNLSWDLHFW |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LGSETSQDEA | GTAAIKTVEL | DDQLGGVPVQ | HREVEGHETS | LFLSRFKKGV | RYLKGGVASG |
| 130 | 140 | 150 | 160 | 170 | 180 |
| FHHVDPDAPY | PARLFHVKGR | RNIRIRQVEV | GVGSMNKGDC | FILDCGSQVY | AYMGPSSRKM |
| 190 | 200 | 210 | 220 | 230 | 240 |
| DRLKAIQAAN | PVRADDHAGK | AKVIVIDETA | SGSEAGESSP | GLGGGSPDDV | ADEDTGVDDS |
| 250 | 260 | 270 | 280 | 290 | 300 |
| AFERSEVNVV | TLHHIFEDGD | GVIQTNMIGE | KPLLQSMLDS | GDCFLLDTGV | GVYVWIGSGS |
| 310 | 320 | 330 | 340 | 350 | 360 |
| SKKEKVKSME | LAAGYMEKKG | YPTYTNVQRV | VEKAEPAVFK | AYFKTWREPQ | EQIGLGRVFT |
| 370 | 380 | 390 | 400 | 410 | 420 |
| QRQMSAVSAT | ETDFDVSSLH | AEKRRLLQKN | AGPAFALCPI | MVLARRNLGP | LRTLKLEPVD |
| 430 | 440 | 450 | 460 | 470 | 480 |
| ESTHGFFFGG | DSYVLKYIYE | VNGNERYILY | FWQGCASSQD | EKASSAIHTV | RLDNELCGKA |
| 490 | 500 | 510 | 520 | 530 | 540 |
| VQVRVVQGYE | PAHFLRIFKG | RMVIFLGGKA | SGFKNVHDHD | TYDVDGTRLF | RVRGTCDFDT |
| 550 | 560 | 570 | 580 | 590 | 600 |
| RAIQQTEVAG | SLNSDDVFVL | ETPGKTYLWI | GKGASEEEKA | MGEKVVELVS | PGRDMVTVAE |
| 610 | 620 | 630 | 640 | 650 | 660 |
| GEEDDDFWGG | LGGKGDYQTA | RDLDRPLLYP | RLFHCTISPA | GCLRVNEMSD | FAQEDLNEDD |
| 670 | 680 | 690 | 700 | 710 | 720 |
| VMVLDSGDEV | YVWVGQGSDD | QEKEKAFTMA | ENYIKTDPTE | RTLDATVILR | INQGEEPAAF |
| 730 | 740 | 750 | |||
| TSIFPAWNPD | MWQKGLVSYD | DMKAQVPETN | AAVE |