Q10484
Gene name |
scs22 (SPAC17C9.12) |
Protein name |
Vesicle-associated membrane protein-associated protein scs22 |
Names |
VAMP-associated protein scs22 |
Species |
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
KEGG Pathway |
spo:SPAC17C9.12 |
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 Q10484
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q10484-F1 | Predicted | AlphaFoldDB |
3 variants for Q10484
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| I_4479456_C_A | 76 | G>V | No | Jeffares_SNPs | |
| I_4478955_G_A | 216 | P>L | No | Jeffares_SNPs | |
| I_4478933_A_C | 223 | N>K | No | Jeffares_SNPs |
No associated diseases with Q10484
1 regional properties for Q10484
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Major sperm protein (MSP) domain | 1 - 121 | IPR000535 |
Functions
5 GO annotations of cellular component
| Name | Definition |
|---|---|
| cortical endoplasmic reticulum | A cortical network of highly dynamic tubules that are juxtaposed to the plasma membrane and undergo ring closure and tubule-branching movements. |
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| endoplasmic reticulum membrane | The lipid bilayer surrounding the endoplasmic reticulum. |
| integral component of endoplasmic reticulum membrane | The component of the endoplasmic reticulum 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. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| FFAT motif binding | Binding to a FFAT motif, a short motif containing diphenylalanine in an acidic tract that targets proteins to the cytosolic surface of the ER and to the nuclear membrane by binding directly to members of the VAP (VAMP-associated protein) protein family. |
| protein-membrane adaptor activity | The binding activity of a molecule that brings together a protein or a protein complex with a membrane, or bringing together two membranes, either via membrane lipid binding or by interacting with a membrane protein, to establish or maintain the localization of the protein, protein complex or organelle. |
5 GO annotations of biological process
| Name | Definition |
|---|---|
| endoplasmic reticulum membrane organization | A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of an endoplasmic reticulum membrane. |
| endoplasmic reticulum-plasma membrane tethering | The attachment of an endoplasmic reticulum membrane to the plasma membrane via molecular tethers. |
| maintenance of ER location | Any process in which the endoplasmic reticulum is maintained in a specific location within a cell and prevented from moving elsewhere. |
| phospholipid biosynthetic process | The chemical reactions and pathways resulting in the formation of a phospholipid, a lipid containing phosphoric acid as a mono- or diester. |
| reticulophagy | The selective autohagy process in which parts of the endoplasmic reticulum are loaded into autophagosomes, delivered to the vacuole, and degraded in response to changing cellular conditions. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MALECDSTIV | FPRPLTRLVK | CDLELRNTAP | YPIGFKVKTT | APKQYCVRPN | GGRIEANSAV |
| 70 | 80 | 90 | 100 | 110 | 120 |
| SVEVILQPLD | HEPAPGTKCR | DKFLVQSTEL | KPELQGMDIA | DIWTQVSKAN | ISERKIRCVY |
| 130 | 140 | 150 | 160 | 170 | 180 |
| SEGPSTANAH | ANAHHQPAQT | TTTSIPTSAT | DNYTTVNGNV | NQSYSKGIDG | TALPSTHANP |
| 190 | 200 | 210 | 220 | 230 | 240 |
| VAAPSTATTQ | HTQLPKTSAV | SHQKPHEAPS | TAVKAPTATV | AENEPYPKPQ | SVPTTTSPNN |
| 250 | 260 | 270 | 280 | 290 | 300 |
| ENNALRSTAN | VINNTRQSTA | TSPSMFAGNS | GNQIGLARVS | SSFGRPTSGA | KVVPQIHNTV |
| 310 | |||||
| TVQTAFLLAI | ICFLIGLLF |