Descriptions
The cytosolic adaptors GGA1-3 mediate sorting of transmembrane proteins. GGA1 contains an autoinhibitory region that is activated by the phosphorylation of a serine positioned three residues upstream of the DXXLL motif. Autoinhibition is achieved by the interaction between DXXLL site and the VHS domain in CGGA1, and the phosphoserine upstream of the DXXLL motif facilitates this interaction.
Autoinhibitory domains (AIDs)
Target domain |
5-146 (VHS domain) |
Relief mechanism |
PTM |
Assay |
|
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for A0A0G2JV04
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A0A0G2JV04-F1 | Predicted | AlphaFoldDB |
1 variants for A0A0G2JV04
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs198464089 | 383 | T>M | No | EVA |
No associated diseases with A0A0G2JV04
7 regional properties for A0A0G2JV04
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | VHS domain | 5 - 146 | IPR002014 |
| domain | GAT domain | 171 - 299 | IPR004152 |
| domain | Clathrin adaptor, alpha/beta/gamma-adaptin, appendage, Ig-like subdomain | 595 - 719 | IPR008152 |
| domain | Gamma-adaptin ear (GAE) domain | 598 - 719 | IPR008153 |
| domain | N-terminal extension of GAT domain | 169 - 207 | IPR041198 |
| domain | GGA3, GAT domain | 213 - 299 | IPR044111 |
| domain | GGA3, VHS domain | 6 - 146 | IPR046996 |
Functions
7 GO annotations of cellular component
| Name | Definition |
|---|---|
| early endosome | A membrane-bounded organelle that receives incoming material from primary endocytic vesicles that have been generated by clathrin-dependent and clathrin-independent endocytosis; vesicles fuse with the early endosome to deliver cargo for sorting into recycling or degradation pathways. |
| early endosome membrane | The lipid bilayer surrounding an early endosome. |
| lysosome | A small lytic vacuole that has cell cycle-independent morphology found in most animal cells and that contains a variety of hydrolases, most of which have their maximal activities in the pH range 5-6. The contained enzymes display latency if properly isolated. About 40 different lysosomal hydrolases are known and lysosomes have a great variety of morphologies and functions. |
| protein-containing complex | A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together. |
| recycling endosome | An organelle consisting of a network of tubules that functions in targeting molecules, such as receptors transporters and lipids, to the plasma membrane. |
| recycling endosome membrane | The lipid bilayer surrounding a recycling endosome. |
| trans-Golgi network | The network of interconnected tubular and cisternal structures located within the Golgi apparatus on the side distal to the endoplasmic reticulum, from which secretory vesicles emerge. The trans-Golgi network is important in the later stages of protein secretion where it is thought to play a key role in the sorting and targeting of secreted proteins to the correct destination. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| phosphatidylinositol binding | Binding to an inositol-containing glycerophospholipid, i.e. phosphatidylinositol (PtdIns) and its phosphorylated derivatives. |
| protein-containing complex binding | Binding to a macromolecular complex. |
| small GTPase binding | Binding to a small monomeric GTPase. |
| ubiquitin binding | Binding to ubiquitin, a protein that when covalently bound to other cellular proteins marks them for proteolytic degradation. |
11 GO annotations of biological process
| Name | Definition |
|---|---|
| endocytic recycling | The directed movement of membrane-bounded vesicles from endosomes back to the plasma membrane, a trafficking pathway that promotes the recycling of internalized transmembrane proteins. |
| Golgi to plasma membrane protein transport | The directed movement of proteins from the Golgi to the plasma membrane in transport vesicles that move from the trans-Golgi network to the plasma membrane. |
| Golgi to plasma membrane transport | The directed movement of substances from the Golgi to the plasma membrane in transport vesicles that move from the trans-Golgi network to the plasma membrane, where they fuse and release their contents by exocytosis. |
| negative regulation of amyloid-beta formation | Any process that stops, prevents or reduces the frequency, rate or extent of amyloid-beta formation. |
| positive regulation of protein catabolic process | Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of a protein by the destruction of the native, active configuration, with or without the hydrolysis of peptide bonds. |
| protein catabolic process | The chemical reactions and pathways resulting in the breakdown of a protein by the destruction of the native, active configuration, with or without the hydrolysis of peptide bonds. |
| protein destabilization | Any process that decreases the stability of a protein, making it more vulnerable to degradative processes or aggregation. |
| protein localization to cell surface | A process in which a protein is transported to, or maintained in, a location within the external part of the cell wall and/or plasma membrane. |
| protein localization to lysosome | A process in which a protein is transported to, or maintained in, a location within a lysosome. |
| protein targeting to lysosome | The process of directing proteins towards the lysosome using signals contained within the protein. |
| regulation of protein stability | Any process that affects the structure and integrity of a protein, altering the likelihood of its degradation or aggregation. |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAEAEGESLE | SWLNKATNPS | NRQEDWEYII | GFCDQINKEL | EGPQIAVRLL | AHKIQSPQEW |
| 70 | 80 | 90 | 100 | 110 | 120 |
| EAVQALTVLE | ACMKNCGRRL | HNEVGKFRFL | NELIKVVSPK | YLGDRVSEKV | KAKVIELLFS |
| 130 | 140 | 150 | 160 | 170 | 180 |
| WTLALPEEAK | IKDAYHMLKR | QGIVQSDPPI | PMDRTLIPSP | PPRPKNPVFD | DEEKSKLLAK |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LLRSKNPDDL | QEANQLIKSM | VKEDEARIQK | VTKRLHTLEE | VNNNVKLLHE | MLLHYSQEFS |
| 250 | 260 | 270 | 280 | 290 | 300 |
| SEADKELMKE | LFDRCENKRR | TLFKLASETE | DNDNSLGDIL | QASDNLSRVI | NSYKTIIEGQ |
| 310 | 320 | 330 | 340 | 350 | 360 |
| IINGEVTTST | VPDSEGNSHC | GNQGALIDLA | ELDTPSSSSP | VLAPAPAPPT | SGIPILPPPP |
| 370 | 380 | 390 | 400 | 410 | 420 |
| QTSGPPRSRS | SSQAEAPSGP | DSTNNALSLL | DEELLCLGLS | DPAPTAPKES | AGNSPWHLFQ |
| 430 | 440 | 450 | 460 | 470 | 480 |
| NEPSSDLDFF | SPRLVSAASC | PSEGSLLPPP | VSTSSLSQAP | LPAAFPAPVV | PASAVTHSTG |
| 490 | 500 | 510 | 520 | 530 | 540 |
| SFTFSSGPAP | ALVPKAEPEG | PEYPSSSISH | RLDALDQLLE | EAKVTSGLVK | PVSCFSPGPT |
| 550 | 560 | 570 | 580 | 590 | 600 |
| ASPLLPASTP | ARPLLPFSTG | PGSPLFQSPA | FQSQGSPQKG | PELSLASVHV | PLESIKPSSA |
| 610 | 620 | 630 | 640 | 650 | 660 |
| LPVTAYDKNG | FRILFHFAKE | CPPGRPDVLV | VVVSMLNTAP | LPVKSIVLQA | AVPKSMKVKL |
| 670 | 680 | 690 | 700 | 710 | 720 |
| QPPSGTELSP | FSPIQPPAAI | TQVMLLANPM | KEKVRLRYKL | TFALGEQLST | ELGEVDQFPP |
| VEQWGNL |