Q06846
PR
Gene name |
RPH3A |
Protein name |
Rabphilin-3A |
Names |
Exophilin-1 |
Species |
Bos taurus (Bovine) |
KEGG Pathway |
bta:282044 |
EC number |
|
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for Q06846
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q06846-F1 | Predicted | AlphaFoldDB |
No variants for Q06846
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q06846 | |||||
No associated diseases with Q06846
4 regional properties for Q06846
Functions
6 GO annotations of cellular component
| Name | Definition |
|---|---|
| anchoring junction | A cell junction that mechanically attaches a cell (and its cytoskeleton) to neighboring cells or to the extracellular matrix. |
| dendritic spine | A small, membranous protrusion from a dendrite that forms a postsynaptic compartment, typically receiving input from a single presynapse. They function as partially isolated biochemical and an electrical compartments. Spine morphology is variable:they can be thin, stubby, mushroom, or branched, with a continuum of intermediate morphologies. They typically terminate in a bulb shape, linked to the dendritic shaft by a restriction. Spine remodeling is though to be involved in synaptic plasticity. |
| extrinsic component of synaptic vesicle membrane | The component of the synaptic vesicle membrane consisting of gene products and protein complexes that are loosely bound to one of its surfaces, but not integrated into the hydrophobic region. |
| neuron projection | A prolongation or process extending from a nerve cell, e.g. an axon or dendrite. |
| postsynaptic membrane | A specialized area of membrane facing the presynaptic membrane on the tip of the nerve ending and separated from it by a minute cleft (the synaptic cleft). Neurotransmitters cross the synaptic cleft and transmit the signal to the postsynaptic membrane. |
| 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. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| calcium ion binding | Binding to a calcium ion (Ca2+). |
| calcium-dependent phospholipid binding | Binding to a phospholipid, a class of lipids containing phosphoric acid as a mono- or diester, in the presence of calcium. |
| small GTPase binding | Binding to a small monomeric GTPase. |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| exocytosis | A process of secretion by a cell that results in the release of intracellular molecules (e.g. hormones, matrix proteins) contained within a membrane-bounded vesicle. Exocytosis can occur either by full fusion, when the vesicle collapses into the plasma membrane, or by a kiss-and-run mechanism that involves the formation of a transient contact, a pore, between a granule (for exemple of chromaffin cells) and the plasma membrane. The latter process most of the time leads to only partial secretion of the granule content. Exocytosis begins with steps that prepare vesicles for fusion with the membrane (tethering and docking) and ends when molecules are secreted from the cell. |
| intracellular protein transport | The directed movement of proteins in a cell, including the movement of proteins between specific compartments or structures within a cell, such as organelles of a eukaryotic cell. |
| regulation of calcium ion-dependent exocytosis | Any process that modulates the frequency, rate or extent of calcium ion-dependent exocytosis. |
| spontaneous neurotransmitter secretion | Neurotransmitter secretion that occurs in the absence of the action of a secretagogue or a presynaptic action potential. |
5 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q14183 | DOC2A | Double C2-like domain-containing protein alpha | Homo sapiens (Human) | PR |
| Q9Y2J0 | RPH3A | Rabphilin-3A | Homo sapiens (Human) | PR |
| Q7TNF0 | Doc2a | Double C2-like domain-containing protein alpha | Mus musculus (Mouse) | PR |
| P47708 | Rph3a | Rabphilin-3A | Mus musculus (Mouse) | PR |
| P47709 | Rph3a | Rabphilin-3A | Rattus norvegicus (Rat) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MTDTVFSSSS | SRWMCPSDRP | LQSNDKEQLQ | TGWSVHPSGQ | PDRQRKQEEL | TDEEKEIINR |
| 70 | 80 | 90 | 100 | 110 | 120 |
| VIARAEKMEE | MEQERIGRLV | DRLENMRKNV | AGDGVNRCIL | CGEQLGMLGS | ACVVCEDCKK |
| 130 | 140 | 150 | 160 | 170 | 180 |
| NVCTKCGVET | SNNRPHPVWL | CKICIEQREV | WKRSGAWFFK | GFPKQVLPQP | MPIKKNKPQQ |
| 190 | 200 | 210 | 220 | 230 | 240 |
| PVSEPVPAAP | EPATPEPKHP | ARAPTRGDTE | DRRGPGQKTG | PDMTSAPGRG | SYGPPVRRAS |
| 250 | 260 | 270 | 280 | 290 | 300 |
| EARMSSSGRD | SDSWDQGHGM | AAGDPSQSPA | GLRRANSVQA | SRPAPASMQS | PAPPQPGQPG |
| 310 | 320 | 330 | 340 | 350 | 360 |
| PPGGSRPSPG | PTGRFPDQRP | EVAPSDPDYT | GAAAQPREER | TGGIGGYSAA | GTREDRAGHP |
| 370 | 380 | 390 | 400 | 410 | 420 |
| PGSYTQASAA | APQPVVASAR | QPPPPEEDEE | EANSYDSDEA | TTLGALEFSL | LYDQDNSSLH |
| 430 | 440 | 450 | 460 | 470 | 480 |
| CTIIKAKGLK | PMDSNGLADP | YVKLHLLPGA | SKSNKLRTKT | LRNTRNPIWN | ETLVYHGITD |
| 490 | 500 | 510 | 520 | 530 | 540 |
| EDMQRKTLRI | SVCDEDKFGH | NEFIGETRFS | LKKLKPNQRK | NFNICLERVI | PMKRAGTTGS |
| 550 | 560 | 570 | 580 | 590 | 600 |
| ARGMALYEEE | QVERIGDIEE | RGKILVSLMY | STQQGGLIVG | IIRCVHLAAM | DANGYSDPFV |
| 610 | 620 | 630 | 640 | 650 | 660 |
| KLWLKPDMGK | KAKHKTQIKK | KTLNPEFNEE | FFYDIKHSDL | AKKSLDISVW | DYDIGKSNDY |
| 670 | 680 | 690 | 700 | ||
| IGGCQLGISA | KGERLKHWYE | CLKNKDKKIE | RWHQLQNENH | VSSD |