O88302
SS
Gene name |
Gna15 |
Protein name |
Guanine nucleotide-binding protein subunit alpha-15 |
Names |
G alpha-15 , G-protein subunit alpha-15 |
Species |
Rattus norvegicus (Rat) |
KEGG Pathway |
rno:89788 |
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 |
187-369 (P-loop containing nucleoside triphosphate hydrolase domain) |
Relief mechanism |
Partner binding |
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
- 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 O88302
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-O88302-F1 | Predicted | AlphaFoldDB |
No variants for O88302
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for O88302 | |||||
No associated diseases with O88302
No regional properties for O88302
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for O88302 | |||
2 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. |
5 GO annotations of molecular function
| Name | Definition |
|---|---|
| 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 |
| metal ion binding | Binding to a metal ion. |
5 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). |
| calcium-mediated signaling | Any intracellular signal transduction in which the signal is passed on within the cell via calcium ions. |
| 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 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). |
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 |
| P29992 | GNA11 | Guanine nucleotide-binding protein subunit alpha-11 | 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 |
| P30679 | GNA15 | Guanine nucleotide-binding protein subunit alpha-15 | 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 |
| Q9JID2 | Gna11 | Guanine nucleotide-binding protein subunit alpha-11 | 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 |
| MARSLTWGCC | PWCLTEEEKT | AARIDQEINK | ILLEQKKQER | GELKLLLLGP | GESGKSTFIK |
| 70 | 80 | 90 | 100 | 110 | 120 |
| QMRIIHGAGY | SEEDRRAFRL | LVYQNIFVSM | QAMIEAMDRL | QIPFSRPDSK | QHASLVMTQD |
| 130 | 140 | 150 | 160 | 170 | 180 |
| PYKVSSFEKP | YAVAMQYLWR | DAGIRACYER | RREFHLLDSA | VYYLSHLERI | AEDDYIPTAQ |
| 190 | 200 | 210 | 220 | 230 | 240 |
| DVLRSRMPTT | GINEYCFSVQ | KTKLRIVDAG | GQKSERKKWI | HCFENVIALI | YLASLSEYDQ |
| 250 | 260 | 270 | 280 | 290 | 300 |
| CLEENSQENR | MKESLALFST | ILELPWFKST | SVILFLNKTD | ILEDKIHTSH | LASYFPSFQG |
| 310 | 320 | 330 | 340 | 350 | 360 |
| PRRDAEAAKR | FILDMYARVY | ASCAEPHDGG | RKGSRARRLF | AHFTCATDTH | SVRSVFKDVR |
| 370 | |||||
| DSVLARYLDE | INLL |