Q9JLQ2
SS
Gene name |
Git2 |
Protein name |
ARF GTPase-activating protein GIT2 |
Names |
ARF GAP GIT2 , Cool-interacting tyrosine-phosphorylated protein 2 , CAT-2 , CAT2 , G protein-coupled receptor kinase-interactor 2 , GRK-interacting protein 2 |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:26431 |
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 |
258-348 (C-terminal SHD domain) |
Relief mechanism |
Partner binding, PTM |
Assay |
|
Accessory elements
No accessory elements
References
- Yeon JH et al. (2016) "Systems-wide Identification of cis-Regulatory Elements in Proteins", Cell systems, 2, 89-100
- Totaro A et al. (2007) "Identification of an intramolecular interaction important for the regulation of GIT1 functions", Molecular biology of the cell, 18, 5124-38
- Di Cesare A et al. (2000) "p95-APP1 links membrane transport to Rac-mediated reorganization of actin", Nature cell biology, 2, 521-30
Autoinhibited structure
Activated structure
2 structures for Q9JLQ2
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 6JMT | X-ray | 280 A | A/B/C/D/E/F | 1-359 | PDB |
| AF-Q9JLQ2-F1 | Predicted | AlphaFoldDB |
30 variants for Q9JLQ2
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs232016228 | 15 | N>S | No | EVA | |
| rs3388772167 | 131 | K>E | No | EVA | |
| rs3388786168 | 158 | Q>H | No | EVA | |
| rs3388778692 | 204 | V>F | No | EVA | |
| rs3388783738 | 224 | Y>* | No | EVA | |
| rs3388753733 | 370 | L>I | No | EVA | |
| rs3388764435 | 402 | V>E | No | EVA | |
| rs3388783853 | 444 | T>I | No | EVA | |
| rs3388781196 | 501 | A>P | No | EVA | |
| rs32133813 | 502 | L>F | No | EVA | |
| rs3395680317 | 502 | L>H | No | EVA | |
| rs3396022492 | 503 | V>M | No | EVA | |
| rs3396093968 | 504 | T>N | No | EVA | |
| rs3395898912 | 504 | T>P | No | EVA | |
| rs3388786188 | 525 | R>* | No | EVA | |
| rs3388783442 | 525 | R>L | No | EVA | |
| rs3388781195 | 530 | L>M | No | EVA | |
| rs3388786255 | 538 | E>K | No | EVA | |
| rs241189796 | 562 | R>Q | No | EVA | |
| rs3388753669 | 577 | E>K | No | EVA | |
| rs224515638 | 585 | T>A | No | EVA | |
| rs3396002194 | 591 | D>V | No | EVA | |
| rs3396002175 | 591 | D>Y | No | EVA | |
| rs3388772099 | 594 | R>L | No | EVA | |
| rs3388774795 | 645 | V>M | No | EVA | |
| rs3388783684 | 652 | L>P | No | EVA | |
| rs3388786173 | 671 | S>T | No | EVA | |
| rs228259171 | 672 | S>N | No | EVA | |
| rs3388784267 | 695 | A>T | No | EVA | |
| rs3388788725 | 707 | S>R | No | EVA |
No associated diseases with Q9JLQ2
12 regional properties for Q9JLQ2
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Actinin-type actin-binding domain, conserved site | 52 - 61 | IPR001589-1 |
| conserved_site | Actinin-type actin-binding domain, conserved site | 126 - 150 | IPR001589-2 |
| domain | Calponin homology domain | 50 - 154 | IPR001715-1 |
| domain | Calponin homology domain | 163 - 269 | IPR001715-2 |
| repeat | Spectrin repeat | 293 - 402 | IPR002017-1 |
| repeat | Spectrin repeat | 413 - 517 | IPR002017-2 |
| repeat | Spectrin repeat | 530 - 639 | IPR002017-3 |
| repeat | Spectrin repeat | 650 - 751 | IPR002017-4 |
| domain | EF-hand domain | 765 - 841 | IPR002048 |
| domain | EF-hand, Ca insensitive | 841 - 907 | IPR014837 |
| repeat | Spectrin/alpha-actinin | 296 - 754 | IPR018159 |
| binding_site | EF-Hand 1, calcium-binding site | 778 - 790 | IPR018247 |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| calyx of Held | The terminal specialization of a calyciferous axon which forms large synapses in the mammalian auditory central nervous system. |
| 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. |
| protein-containing complex binding | Binding to a macromolecular complex. |
| small GTPase binding | Binding to a small monomeric GTPase. |
7 GO annotations of biological process
| Name | Definition |
|---|---|
| behavioral response to pain | Any process that results in a change in the behavior of an organism as a result of a pain stimulus. Pain stimuli cause activation of nociceptors, peripheral receptors for pain, include receptors which are sensitive to painful mechanical stimuli, extreme heat or cold, and chemical stimuli. |
| 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.). |
| presynaptic modulation of chemical synaptic transmission | Any process, acting in the presynapse that results in modulation of chemical synaptic transmission. |
| 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 synaptic vesicle exocytosis | Any process that modulates the frequency, rate or extent of synaptic vesicle exocytosis. |
| 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 | |
| Q95RG8 | Git | ARF GTPase-activating protein Git | Drosophila melanogaster (Fruit fly) | SS |
| 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 |
| Q9Z272 | Git1 | ARF GTPase-activating protein GIT1 | Rattus norvegicus (Rat) | SS |
| Q66H91 | Git2 | ARF GTPase-activating protein GIT2 | Rattus norvegicus (Rat) | SS |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSKRLRSSDV | CADCNGPDPS | WASVNRGTFI | CDECCSVHRS | LGRHISQVRH | LKHTAWPPTL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LQMVETLYNN | GANSIWEHSL | LDPASIMSGR | RKANPQDKVH | PNKAEFIRAK | YQMLAFVHRL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| PCREDDSVTA | KDLSKQLHSS | VRTGNLETCL | RLLSLGAQAN | FFHPEKGSTP | LHVASKAGQI |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LQAELLAVYG | ADPGTQDSSG | KTPVDYARQG | GHHELAERLI | EIQYELTDRL | AFYLCGRKPD |
| 250 | 260 | 270 | 280 | 290 | 300 |
| HKSGQHFLIP | QRADSLDLSE | LAKAAKKKLQ | SLSNHLFEEL | AMDVYDEVDR | RETDAVWLAT |
| 310 | 320 | 330 | 340 | 350 | 360 |
| QNHSTLVTET | TVVPFLPVNP | EYSSTRNQGR | QKLARFNAHE | FATLVIDILS | DAKRRQQGSP |
| 370 | 380 | 390 | 400 | 410 | 420 |
| LSRSKDNVEL | ILRTVSTQHS | TESQDNDQPD | YDSVASDEDT | DVETRASKAN | RQKLQTLQSE |
| 430 | 440 | 450 | 460 | 470 | 480 |
| NSSLRRQATA | SACQVQTGSD | HKDTASHSSL | KRRPSARGSR | PMSMYETGSG | QKPYLPMGEA |
| 490 | 500 | 510 | 520 | 530 | 540 |
| SHPEESRTRL | QPFPTHIGRS | ALVTSSSSLP | SFPSTLSWSR | DESARRASRL | EKQNSTPESD |
| 550 | 560 | 570 | 580 | 590 | 600 |
| YDNTACDPEP | DDTGSTRKGR | QRSMLWQGDG | LLPDTAEPHS | VPSPTLPSTE | DVIRKTEQIT |
| 610 | 620 | 630 | 640 | 650 | 660 |
| KNIQELLRAA | QENKHDSYIP | CSERIHVAVT | EMAALFPKKP | KSDTVRTSLR | LLTSSAYRLQ |
| 670 | 680 | 690 | 700 | ||
| SECRKALPGD | SSLPTDVQLV | TQQVIQCAYD | IAKAAKQLVT | ITTKENSS |