Q8K021
Gene name |
Scamp1 |
Protein name |
Secretory carrier-associated membrane protein 1 |
Names |
Secretory carrier membrane protein 1 |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:107767 |
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 Q8K021
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q8K021-F1 | Predicted | AlphaFoldDB |
7 variants for Q8K021
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3389294597 | 21 | P>Q | No | EVA | |
| rs3389254577 | 31 | P>Q | No | EVA | |
| rs3389294619 | 68 | E>D | No | EVA | |
| rs3389270659 | 253 | G>A | No | EVA | |
| rs3389304706 | 266 | I>V | No | EVA | |
| rs3389313467 | 331 | N>T | No | EVA | |
| rs3404513317 | 337 | Q>K | No | EVA |
No associated diseases with Q8K021
No regional properties for Q8K021
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for Q8K021 | |||
Functions
11 GO annotations of cellular component
| Name | Definition |
|---|---|
| clathrin-coated vesicle | A vesicle with a coat formed of clathrin connected to the membrane via one of the clathrin adaptor complexes. |
| cytoplasmic vesicle membrane | The lipid bilayer surrounding a cytoplasmic vesicle. |
| integral component of membrane | The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane. |
| integral component of synaptic vesicle membrane | The component of the synaptic vesicle membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane. |
| recycling endosome membrane | The lipid bilayer surrounding a recycling endosome. |
| 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. |
| synaptic vesicle | A secretory organelle, typically 50 nm in diameter, of presynaptic nerve terminals; accumulates in high concentrations of neurotransmitters and secretes these into the synaptic cleft by fusion with the 'active zone' of the presynaptic plasma membrane. |
| synaptic vesicle membrane | The lipid bilayer surrounding a synaptic vesicle. |
| trans-Golgi network | The network of interconnected tubular and cisternal structures located within the Golgi apparatus on the side distal to the endoplasmic reticulum, from which secretory vesicles emerge. The trans-Golgi network is important in the later stages of protein secretion where it is thought to play a key role in the sorting and targeting of secreted proteins to the correct destination. |
| trans-Golgi network membrane | The lipid bilayer surrounding any of the compartments that make up the trans-Golgi network. |
| zymogen granule membrane | The lipid bilayer surrounding a zymogen granule. |
1 GO annotations of molecular function
| Name | Definition |
|---|---|
| protein domain specific binding | Binding to a specific domain of a protein. |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| endocytosis | A vesicle-mediated transport process in which cells take up external materials or membrane constituents by the invagination of a small region of the plasma membrane to form a new membrane-bounded vesicle. |
| establishment of localization in cell | Any process, occuring in a cell, that localizes a substance or cellular component. This may occur via movement, tethering or selective degradation. |
| 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. |
| protein transport | The directed movement of proteins into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. |
3 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q969E2 | SCAMP4 | Secretory carrier-associated membrane protein 4 | Homo sapiens (Human) | PR |
| O15126 | SCAMP1 | Secretory carrier-associated membrane protein 1 | Homo sapiens (Human) | PR |
| Q9LR68 | SCAMP2 | Secretory carrier-associated membrane protein 2 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSDFDSNPFA | DPDLNNPFKD | PSVTQVTRNV | PPGLDEYNPF | SDSRTPPPGS | VKMPNVPNTQ |
| 70 | 80 | 90 | 100 | 110 | 120 |
| PAIMKPTEEH | PAYTQITKEH | ALAQAELLKR | QEELERKAAE | LDRREREMQN | LSQHGRKNNW |
| 130 | 140 | 150 | 160 | 170 | 180 |
| PPLPSNFPVG | PCFYQDFSVD | IPVEFQKTVK | LMYYLWMFHA | VTLFLNIFGC | LAWFCVDSSR |
| 190 | 200 | 210 | 220 | 230 | 240 |
| AVDFGLSILW | FLLFTPCSFV | CWYRPLYGAF | RSDSSFRFFV | FFFVYICQFA | VHVLQAAGFH |
| 250 | 260 | 270 | 280 | 290 | 300 |
| NWGNCGWISS | LTGLNKNIPV | GIMMIIIAAL | FTASAVISLV | MFKKVHGLYR | TTGASFEKAQ |
| 310 | 320 | 330 | |||
| QEFATGVMSN | KTVQTAAANA | ASTAATSAAQ | NAFKGNQM |