Q9JID2
SS
Gene name |
Gna11 |
Protein name |
Guanine nucleotide-binding protein subunit alpha-11 |
Names |
G alpha-11 , G-protein subunit alpha-11 |
Species |
Rattus norvegicus (Rat) |
KEGG Pathway |
rno:81662 |
EC number |
|
Protein Class |
|
Descriptions
The Gα subunits of heterotrimeric G proteins are GTP hydrolyases which, upon receptor activation, bind to GTP and regulate effector molecules. Gα-catalyzed hydrolysis of GTP to GDP releases the Gα-GDP product complex from effector and allows its sequestration by inhibitory Gβγ subunits. In Gia1-GppNHp complex, Gln204 of Gia1 interacts with nucleophilic water (Wnuc), participating directly in the Gia1-GTP ground state but must reorient to stabilize the transition state. RGS4, a member of the RGS family of G protein stimulatory factors, accelerates hydrolysis of GTP by Gia1 by destabilizing the ground-state conformation of Gln204. Insertion of Asn128 of RGS4 into the active site enhances catalysis by aiding in binding, orienting, and polarizing Wnuc in the pre-transition state complex. Asn128 of RGS4 displaces the side chain of Gln204 from its anti-catalytic position in the ground state, freeing it to participate in stabilization of the transition state.
Autoinhibitory domains (AIDs)
Target domain |
184-354 (P-loop containing nucleoside triphosphate hydrolase domain) |
Relief mechanism |
Partner binding |
Assay |
|
Accessory elements
No accessory elements
References
- Coleman DE et al. (1999) "Structure of Gialpha1.GppNHp, autoinhibition in a galpha protein-substrate complex", The Journal of biological chemistry, 274, 16669-72
- Lutz S et al. (2007) "Structure of Galphaq-p63RhoGEF-RhoA complex reveals a pathway for the activation of RhoA by GPCRs", Science (New York, N.Y.), 318, 1923-7
Autoinhibited structure
Activated structure
1 structures for Q9JID2
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9JID2-F1 | Predicted | AlphaFoldDB |
No variants for Q9JID2
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q9JID2 | |||||
No associated diseases with Q9JID2
5 regional properties for Q9JID2
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | EF-hand domain | 33 - 104 | IPR002048-1 |
| domain | EF-hand domain | 106 - 177 | IPR002048-2 |
| binding_site | EF-Hand 1, calcium-binding site | 46 - 58 | IPR018247-1 |
| binding_site | EF-Hand 1, calcium-binding site | 119 - 131 | IPR018247-2 |
| binding_site | EF-Hand 1, calcium-binding site | 155 - 167 | IPR018247-3 |
4 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| heterotrimeric G-protein complex | Any of a family of heterotrimeric GTP-binding and hydrolyzing proteins; they belong to a superfamily of GTPases that includes monomeric proteins such as EF-Tu and RAS. Heterotrimeric G-proteins consist of three subunits; the alpha subunit contains the guanine nucleotide binding site and possesses GTPase activity; the beta and gamma subunits are tightly associated and function as a beta-gamma heterodimer; extrinsic plasma membrane proteins (cytoplasmic face) that function as a complex to transduce signals from G protein-coupled receptors to an effector protein. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
| 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. |
10 GO annotations of molecular function
| Name | Definition |
|---|---|
| alkylglycerophosphoethanolamine phosphodiesterase activity | Catalysis of the reaction |
| enzyme regulator activity | Binds to and modulates the activity of an enzyme. |
| G protein activity | A molecular function regulator that cycles between active GTP-bound and inactive GDP-bound states. In its active state, binds to a variety of effector proteins to regulate cellular processes. Intrinsic GTPase activity returns the G protein to its GDP-bound state. The return to the GDP-bound state can be accelerated by the action of a GTPase-activating protein (GAP). |
| G protein-coupled receptor binding | Binding to a G protein-coupled receptor. |
| G-protein beta/gamma-subunit complex binding | Binding to a complex of G-protein beta/gamma subunits. |
| GTP binding | Binding to GTP, guanosine triphosphate. |
| GTPase activity | Catalysis of the reaction |
| guanyl nucleotide binding | Binding to a guanyl nucleotide, consisting of guanosine esterified with (ortho)phosphate. |
| metal ion binding | Binding to a metal ion. |
| protein-containing complex binding | Binding to a macromolecular complex. |
17 GO annotations of biological process
| Name | Definition |
|---|---|
| action potential | A process in which membrane potential cycles through a depolarizing spike, triggered in response to depolarization above some threshold, followed by repolarization. This cycle is driven by the flow of ions through various voltage gated channels with different thresholds and ion specificities. |
| adenylate cyclase-modulating G protein-coupled receptor signaling pathway | A G protein-coupled receptor signaling pathway in which the signal is transmitted via the activation or inhibition of adenylyl cyclase activity and a subsequent change in the intracellular concentration of cyclic AMP (cAMP). |
| cellular response to pH | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a pH stimulus. pH is a measure of the acidity or basicity of an aqueous solution. |
| cranial skeletal system development | The process whose specific outcome is the progression of a cranial skeletal system over time, from its formation to the mature structure. The cranial skeletal system is the skeletal subdivision of the head, and includes the skull (cranium plus mandible), pharyngeal and/or hyoid apparatus. |
| developmental pigmentation | The developmental process that results in the deposition of coloring matter in an organism, tissue or cell. |
| endothelin receptor signaling pathway | A G protein-coupled receptor signaling pathway initiated by endothelin binding to its receptor on the surface of a target cell, and ending with the regulation of a downstream cellular process, e.g. transcription. |
| G protein-coupled receptor signaling pathway | The series of molecular signals initiated by a ligand binding to its receptor, in which the activated receptor promotes the exchange of GDP for GTP on the alpha-subunit of an associated heterotrimeric G-protein complex. The GTP-bound activated alpha-G-protein then dissociates from the beta- and gamma-subunits to further transmit the signal within the cell. The pathway begins with receptor-ligand interaction, and ends with regulation of a downstream cellular process. The pathway can start from the plasma membrane, Golgi or nuclear membrane. |
| heart development | The process whose specific outcome is the progression of the heart over time, from its formation to the mature structure. The heart is a hollow, muscular organ, which, by contracting rhythmically, keeps up the circulation of the blood. |
| ion channel modulating, G protein-coupled receptor signaling pathway | The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, where the pathway proceeds through activation or inhibition of an ion channel. |
| ligand-gated ion channel signaling pathway | The series of molecular signals initiated by activation of a ligand-gated ion channel on the surface of a cell. The pathway begins with binding of an extracellular ligand to a ligand-gated ion channel and ends with a molecular function that directly regulates a downstream cellular process, e.g. transcription. |
| phospholipase C-activating dopamine receptor signaling pathway | A phospholipase C-activating receptor G protein-coupled receptor signaling pathway initiated by dopamine binding to its receptor on the surface of a target cell, and ending with the regulation of a downstream cellular process, e.g. transcription. |
| phospholipase C-activating G protein-coupled acetylcholine receptor signaling pathway | A phospholipase C-activating G protein-coupled receptor signaling pathway initiated by acetylcholine binding to its receptor on the surface of a target cell, and ending with the regulation of a downstream cellular process, e.g. transcription. |
| phospholipase C-activating G protein-coupled receptor signaling pathway | A G protein-coupled receptor signaling pathway in which the signal is transmitted via the activation of phospholipase C (PLC) and a subsequent increase in the intracellular concentration of inositol trisphosphate (IP3) and diacylglycerol (DAG). |
| positive regulation of insulin secretion | Any process that activates or increases the frequency, rate or extent of the regulated release of insulin. |
| regulation of blood pressure | Any process that modulates the force with which blood travels through the circulatory system. The process is controlled by a balance of processes that increase pressure and decrease pressure. |
| regulation of melanocyte differentiation | Any process that modulates the frequency, rate or extent of melanocyte differentiation. |
| skeletal system development | The process whose specific outcome is the progression of the skeleton over time, from its formation to the mature structure. The skeleton is the bony framework of the body in vertebrates (endoskeleton) or the hard outer envelope of insects (exoskeleton or dermoskeleton). |
28 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| P38408 | GNA14 | Guanine nucleotide-binding protein subunit alpha-14 | Bos taurus (Bovine) | PR |
| P23625 | Galphaq | G protein alpha q subunit | Drosophila melanogaster (Fruit fly) | PR |
| P30679 | GNA15 | Guanine nucleotide-binding protein subunit alpha-15 | Homo sapiens (Human) | SS |
| P50148 | GNAQ | Guanine nucleotide-binding protein G | Homo sapiens (Human) | SS |
| O95837 | GNA14 | Guanine nucleotide-binding protein subunit alpha-14 | Homo sapiens (Human) | SS |
| P29992 | GNA11 | Guanine nucleotide-binding protein subunit alpha-11 | Homo sapiens (Human) | SS |
| P21279 | Gnaq | Guanine nucleotide-binding protein G(q) subunit alpha | Mus musculus (Mouse) | PR |
| P30678 | Gna15 | Guanine nucleotide-binding protein subunit alpha-15 | Mus musculus (Mouse) | PR |
| Q2PKF4 | GNAQ | Guanine nucleotide-binding protein G(q) subunit alpha | Sus scrofa (Pig) | PR |
| P93564 | GPA1 | Guanine nucleotide-binding protein alpha-1 subunit | Solanum tuberosum (Potato) | SS |
| Q6Q7Y5 | Gna13 | Guanine nucleotide-binding protein subunit alpha-13 | Rattus norvegicus (Rat) | SS |
| Q63210 | Gna12 | Guanine nucleotide-binding protein subunit alpha-12 | Rattus norvegicus (Rat) | SS |
| O88302 | Gna15 | Guanine nucleotide-binding protein subunit alpha-15 | Rattus norvegicus (Rat) | SS |
| P82471 | Gnaq | Guanine nucleotide-binding protein G | Rattus norvegicus (Rat) | SS |
| P38406 | Gnal | Guanine nucleotide-binding protein G | Rattus norvegicus (Rat) | SS |
| P29348 | Gnat3 | Guanine nucleotide-binding protein G | Rattus norvegicus (Rat) | SS |
| P04897 | Gnai2 | Guanine nucleotide-binding protein G | Rattus norvegicus (Rat) | SS |
| P08753 | Gnai3 | Guanine nucleotide-binding protein G | Rattus norvegicus (Rat) | SS |
| P19627 | Gnaz | Guanine nucleotide-binding protein G | Rattus norvegicus (Rat) | SS |
| P10824 | Gnai1 | Guanine nucleotide-binding protein G subunit alpha-1 | Rattus norvegicus (Rat) | EV |
| P59215 | Gnao1 | Guanine nucleotide-binding protein G | Rattus norvegicus (Rat) | SS |
| Q63803 | Gnas | Guanine nucleotide-binding protein G | Rattus norvegicus (Rat) | SS |
| Q0DJ33 | GPA1 | Guanine nucleotide-binding protein alpha-1 subunit | Oryza sativa subsp. japonica (Rice) | SS |
| P93163 | GPA2 | Guanine nucleotide-binding protein alpha-2 subunit | Glycine max (Soybean) (Glycine hispida) | SS |
| P49084 | GPA1 | Guanine nucleotide-binding protein alpha-1 subunit | Glycine max (Soybean) (Glycine hispida) | SS |
| O80462 | XLG1 | Extra-large guanine nucleotide-binding protein 1 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| P18064 | GPA1 | Guanine nucleotide-binding protein alpha-1 subunit | Arabidopsis thaliana (Mouse-ear cress) | SS |
| P26981 | GPA1 | Guanine nucleotide-binding protein alpha-1 subunit | Solanum lycopersicum (Tomato) (Lycopersicon esculentum) | SS |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MTLESMIACC | LSDEVKESKR | INAEIEKQLR | RDKRDARREL | KLLLLGTGES | GKSTFIKQMR |
| 70 | 80 | 90 | 100 | 110 | 120 |
| IIHGAGYSEE | DKRGFTKLVY | QNIFTAMQAV | VRAMDTLKIR | YKYEQNKANA | LLIREVDVEK |
| 130 | 140 | 150 | 160 | 170 | 180 |
| VTTFEHQYVN | AIKTLWSDPG | VQECYDRRRE | FQLSDSAKYY | LTDVDRIATV | GYLPTQQDVL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| RVRVPTTGII | EYPFDLENII | FRMVDVGGQR | SERRKWIHCF | ENVTSIMFLV | ALSEYDQVLV |
| 250 | 260 | 270 | 280 | 290 | 300 |
| ESDNENRMEE | SKALFRTIIT | YPWFQHSSVI | LFLNKKDLLE | DKILHSHLVD | YFPEFDGPQR |
| 310 | 320 | 330 | 340 | 350 | |
| DAQAAREFIL | KMFVDLNPDS | DKIIYSHFTC | ATDTENIRFV | FAAVKDTILQ | LNLKEYNLV |