Q95RG8
SS
Gene name |
Git (arfgap2, CG16728) |
Protein name |
ARF GTPase-activating protein Git |
Names |
ARF GAP GIT , dGIT protein , G protein-coupled receptor kinase interacting ArfGAP |
Species |
Drosophila melanogaster (Fruit fly) |
KEGG Pathway |
dme:Dmel_CG16728 |
EC number |
|
Protein Class |
|
Descriptions
G-protein coupled receptor kinase-interacting protein (GIT, p95-APP1) proteins include an N-terminal Arf GTPase-activating protein domain (Arf-GAP domain), three ankyrin repeats, a Spa2-homology domain (SHD), a coiled-coil domain including a leucine zipper required for dimerization, and a paxillin-binding site (PBS). To autoinhibit the C-terminal domain, the N-terminal GAP domain (1-124) interacts with the C-terminal domain. In addition, the interaction between the ankyrin repeats and SHD domain is probably the main intramolecular interface to keep the inactive conformation (GAP-C terminal domain interaction) of p95-APP1. Therefore, the SHD domain is essential in mediating the intramolecular interactions between the C-terminal half of GIT1 and the N-terminal part including GAP domain and ankyrin repeats.
Autoinhibitory domains (AIDs)
Target domain |
307-393 (C-terminal SHD domain) |
Relief mechanism |
Partner binding, PTM |
Assay |
|
Accessory elements
No accessory elements
References
Autoinhibited structure
Activated structure
1 structures for Q95RG8
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q95RG8-F1 | Predicted | AlphaFoldDB |
No variants for Q95RG8
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q95RG8 | |||||
No associated diseases with Q95RG8
5 regional properties for Q95RG8
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Arf GTPase activating protein | 32 - 168 | IPR001164 |
| repeat | Ankyrin repeat | 187 - 278 | IPR002110 |
| domain | GIT, Spa2 homology (SHD) domain | 314 - 344 | IPR013724-1 |
| domain | GIT, Spa2 homology (SHD) domain | 374 - 404 | IPR013724-2 |
| domain | ARF GTPase-activating protein GIT1, C-terminal | 612 - 730 | IPR022018 |
Functions
8 GO annotations of cellular component
| Name | Definition |
|---|---|
| cell leading edge | The area of a motile cell closest to the direction of movement. |
| centrosome | A structure comprised of a core structure (in most organisms, a pair of centrioles) and peripheral material from which a microtubule-based structure, such as a spindle apparatus, is organized. Centrosomes occur close to the nucleus during interphase in many eukaryotic cells, though in animal cells it changes continually during the cell-division cycle. |
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| focal adhesion | A cell-substrate junction that anchors the cell to the extracellular matrix and that forms a point of termination of actin filaments. In insects focal adhesion has also been referred to as hemi-adherens junction (HAJ). |
| lamellipodium | A thin sheetlike process extended by the leading edge of a migrating cell or extending cell process; contains a dense meshwork of actin filaments. |
| presynaptic active zone | A specialized region of the plasma membrane and cell cortex of a presynaptic neuron; encompasses a region of the plasma membrane where synaptic vesicles dock and fuse, and a specialized cortical cytoskeletal matrix. |
| spindle pole | Either of the ends of a spindle, where spindle microtubules are organized; usually contains a microtubule organizing center and accessory molecules, spindle microtubules and astral microtubules. |
| synapse | The junction between an axon of one neuron and a dendrite of another neuron, a muscle fiber or a glial cell. As the axon approaches the synapse it enlarges into a specialized structure, the presynaptic terminal bouton, which contains mitochondria and synaptic vesicles. At the tip of the terminal bouton is the presynaptic membrane; facing it, and separated from it by a minute cleft (the synaptic cleft) is a specialized area of membrane on the receiving cell, known as the postsynaptic membrane. In response to the arrival of nerve impulses, the presynaptic terminal bouton secretes molecules of neurotransmitters into the synaptic cleft. These diffuse across the cleft and transmit the signal to the postsynaptic membrane. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| GTPase activator activity | Binds to and increases the activity of a GTPase, an enzyme that catalyzes the hydrolysis of GTP. |
| metal ion binding | Binding to a metal ion. |
| molecular adaptor activity | The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way. |
| small GTPase binding | Binding to a small monomeric GTPase. |
11 GO annotations of biological process
| Name | Definition |
|---|---|
| brain development | The process whose specific outcome is the progression of the brain over time, from its formation to the mature structure. Brain development begins with patterning events in the neural tube and ends with the mature structure that is the center of thought and emotion. The brain is responsible for the coordination and control of bodily activities and the interpretation of information from the senses (sight, hearing, smell, etc.). |
| mushroom body development | The process whose specific outcome is the progression of the mushroom body over time, from its formation to the mature structure. The mushroom body is composed of the prominent neuropil structures of the insect central brain, thought to be crucial for olfactory associated learning. These consist mainly of a bulbous calyx and tightly packaged arrays of thin parallel fibers of the Kenyon cells. |
| negative regulation of organ growth | Any process that stops, prevents, or reduces the frequency, rate or extent of growth of an organ of an organism. |
| positive regulation of hippo signaling | Any process that activates or increases the frequency, rate or extent of hippo signaling. |
| protein localization to presynapse | A process in which a protein is transported to, or maintained in, a location within a presynapse. |
| regulation of ARF protein signal transduction | Any process that modulates the frequency, rate or extent of ARF protein signal transduction. |
| regulation of G protein-coupled receptor signaling pathway | Any process that modulates the frequency, rate or extent of G protein-coupled receptor signaling pathway. |
| regulation of GTPase activity | Any process that modulates the rate of GTP hydrolysis by a GTPase. |
| somatic muscle development | The process whose specific outcome is the progression of the somatic muscle over time, from its formation to the mature structure. Somatic muscles are striated muscle structures that connect to the exoskeleton or cuticle. |
| synaptic vesicle cycle | A biological process in which synaptic vesicles are loaded with neurotransmitters, move to the active zone, exocytose and are then recycled via endocytosis, ultimately leading to reloading with neurotransmitters. |
| synaptic vesicle recycling | The trafficking of synaptic vesicles from the pre-synaptic membrane so the vesicle can dock and prime for another round of exocytosis and neurotransmitter release. Recycling occurs after synaptic vesicle exocytosis, and is necessary to replenish presynaptic vesicle pools, sustain transmitter release and preserve the structural integrity of the presynaptic membrane. Recycling can occur following transient fusion with the presynaptic membrane (kiss and run), or via endocytosis of presynaptic membrane. |
7 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q9DG15 | p95-APP1 | Gallus gallus (Chicken) | EV | |
| Q9Y2X7 | GIT1 | ARF GTPase-activating protein GIT1 | Homo sapiens (Human) | SS |
| Q14161 | GIT2 | ARF GTPase-activating protein GIT2 | Homo sapiens (Human) | SS |
| Q68FF6 | Git1 | ARF GTPase-activating protein GIT1 | Mus musculus (Mouse) | SS |
| Q9JLQ2 | Git2 | ARF GTPase-activating protein GIT2 | Mus musculus (Mouse) | SS |
| Q66H91 | Git2 | ARF GTPase-activating protein GIT2 | Rattus norvegicus (Rat) | SS |
| Q9Z272 | Git1 | ARF GTPase-activating protein GIT1 | Rattus norvegicus (Rat) | SS |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MCFASSIIEA | HRKLFIAPPD | LDHSDPATPT | ISTRSKMPRG | KSRLQTEVCG | DCGAGDPSWA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| SINRGILLCA | DCCSVHRSLG | RHISIVKSLR | QGNWEPSVLN | FVNSLNAHGA | NSVWEHHLLD |
| 130 | 140 | 150 | 160 | 170 | 180 |
| GSTNSTGGKH | VPRWRKPTPK | DALHPTKSDF | IKAKHVNLTF | VLKPSLQDDD | DGNGSAGCLE |
| 190 | 200 | 210 | 220 | 230 | 240 |
| QELSRQLHAS | VRTSNLETSL | RFLVQGADPN | YYHEDKLSTP | LHMAAKFGQA | SQIEMLLIYG |
| 250 | 260 | 270 | 280 | 290 | 300 |
| ADVNALDGNG | MTPLELARAN | NHNTIAERLL | DAMYDVTDRI | ITFLGGKKPD | HASGRHMIIP |
| 310 | 320 | 330 | 340 | 350 | 360 |
| DANGADISEQ | LKIARGKLQL | VPNKMFEELV | MDLYDEVDRR | ECEAIWSTST | LNADHATVPF |
| 370 | 380 | 390 | 400 | 410 | 420 |
| LPANPFLSAT | RNQGRQKLAR | FNRAEFTGLL | TDVLVDAMRR | QNMANLRPMD | APVAGHQSLQ |
| 430 | 440 | 450 | 460 | 470 | 480 |
| SLPYANNSML | LGSFEQGGHD | PNLSDDEPIY | DPVASDDDYA | PVPPMAQQAI | VHTPPRSANS |
| 490 | 500 | 510 | 520 | 530 | 540 |
| HNEMETLRKQ | LNDYKSEINQ | LKNVVQMLSS | ENTQLKSKFS | SASNNSVYDE | PLRIDLSLSS |
| 550 | 560 | 570 | 580 | 590 | 600 |
| PDTEHEPLSL | PEGGTANGES | GSSNDSSNQS | TIKRPASMYE | RRLVPNVAKG | NTDIRNTTSM |
| 610 | 620 | 630 | 640 | 650 | 660 |
| YQMAGDGKPF | GEEVKVRSDL | VTRRLKELIR | AMQPVPEDQK | QSIAPHGELI | RSAVTDLIAL |
| 670 | 680 | 690 | 700 | 710 | 720 |
| YANLPPNASD | PSRETLKLLT | RQNILIQHEC | ENLQKAIEAD | DKQAIQKNTL | EVRDCAFHIA |
| 730 | |||||
| SAIKTLVLQF | Y |