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
10 structures for A0PFK7
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 5ADX | EM | 400 A | L | 2-271 | PDB |
| 5AFU | EM | 350 A | L | 2-271 | PDB |
| 6F1T | EM | 350 A | L | 1-272 | PDB |
| 6F1U | EM | 340 A | L | 1-271 | PDB |
| 6F38 | EM | 670 A | L | 1-272 | PDB |
| 6F3A | EM | 820 A | L | 1-272 | PDB |
| 6ZNL | EM | 380 A | L | 1-272 | PDB |
| 7Z8F | EM | 2000 A | L | 1-272 | PDB |
| 7Z8I | EM | 330 A | L | 1-272 | PDB |
| AF-A0PFK7-F1 | Predicted | AlphaFoldDB |
No variants for A0PFK7
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A0PFK7 | |||||
No associated diseases with A0PFK7
1 regional properties for A0PFK7
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | F-actin capping protein, beta subunit, conserved site | 62 - 67 | IPR019771 |
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| F-actin capping protein complex | A heterodimer consisting of alpha and beta subunits that binds to and caps the barbed ends of actin filaments, thereby regulating the polymerization of actin monomers but not severing actin filaments. |
| sarcomere | The repeating unit of a myofibril in a muscle cell, composed of an array of overlapping thick and thin filaments between two adjacent Z discs. |
| WASH complex | A protein complex that localizes at the surface of endosomes, where it recruits and activates the Arp2/3 complex to induce actin polymerization. In human, the WASH complex is composed of F-actin-capping protein subunits alpha and beta, WASH1, FAM21, KIAA1033, KIAA0196 and CCDC53. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| actin binding | Binding to monomeric or multimeric forms of actin, including actin filaments. |
| actin filament binding | Binding to an actin filament, also known as F-actin, a helical filamentous polymer of globular G-actin subunits. |
7 GO annotations of biological process
| Name | Definition |
|---|---|
| actin cytoskeleton organization | A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures comprising actin filaments and their associated proteins. |
| barbed-end actin filament capping | The binding of a protein or protein complex to the barbed (or plus) end of an actin filament, thus preventing the addition, exchange or removal of further actin subunits. |
| cell morphogenesis | The developmental process in which the size or shape of a cell is generated and organized. |
| cytoskeleton organization | A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures. |
| negative regulation of filopodium assembly | Any process that stops, prevents, or reduces the frequency, rate or extent of the assembly of a filopodium, a thin, stiff protrusion extended by the leading edge of a motile cell such as a crawling fibroblast or amoeba, or an axonal growth cone. |
| regulation of cell morphogenesis | Any process that modulates the frequency, rate or extent of cell morphogenesis. Cell morphogenesis is the developmental process in which the shape of a cell is generated and organized. |
| regulation of lamellipodium assembly | Any process that modulates the rate, frequency or extent of the formation of a lamellipodium, a thin sheetlike extension of the surface of a migrating cell. |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MGDQQLDCAL | DLMRRLPPQQ | IEKNLSDLID | LVPSLCEDLL | SSVDQPLKIA | RDKVVGKDYL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LCDYNRDGDS | YRSPWSNKYD | PPLEDGAMPS | ARLRKLEVEA | NNAFDQYRDL | YFEGGVSSVY |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LWDLDHGFAG | VILIKKAGDG | SKKIKGCWDS | IHVVEVQEKS | SGRTAHYKLT | STVMLWLQTN |
| 190 | 200 | 210 | 220 | 230 | 240 |
| KSGSGTMNLG | GSLTRQMEKD | ETVSDCSPHI | ANIGRLVEDM | ENKIRSTLNE | IYFGKTKDIV |
| 250 | 260 | 270 | |||
| NGLRSLDAIP | DNHKFKQLQR | ELSQVLTQRQ | VYIQPDN |