Q9CQV4
Gene name |
Retreg3 (Fam134c) |
Protein name |
Reticulophagy regulator 3 |
Names |
|
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:67998 |
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 Q9CQV4
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9CQV4-F1 | Predicted | AlphaFoldDB |
22 variants for Q9CQV4
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3389178224 | 54 | S>N | No | EVA | |
| rs3389178249 | 55 | R>L | No | EVA | |
| rs3389141016 | 69 | A>V | No | EVA | |
| rs3389207172 | 117 | P>Q | No | EVA | |
| rs3389214034 | 150 | S>G | No | EVA | |
| rs3389197062 | 158 | L>P | No | EVA | |
| rs3389178242 | 237 | K>N | No | EVA | |
| rs226735331 | 254 | T>M | No | EVA | |
| rs3389211585 | 312 | G>S | No | EVA | |
| rs3402705831 | 317 | D>A | No | EVA | |
| rs3389204414 | 318 | G>A | No | EVA | |
| rs3402034297 | 335 | S>Y | No | EVA | |
| rs3402817689 | 337 | N>K | No | EVA | |
| rs3402072756 | 338 | V>L | No | EVA | |
| rs3389211642 | 340 | P>H | No | EVA | |
| rs3389197021 | 373 | S>G | No | EVA | |
| rs3389138136 | 382 | L>F | No | EVA | |
| rs3389214007 | 404 | G>D | No | EVA | |
| rs3389197087 | 405 | M>I | No | EVA | |
| rs3402869858 | 416 | T>P | No | EVA | |
| rs13473314 | 425 | R>I | No | EVA | |
| rs3389138205 | 432 | R>W | No | EVA |
No associated diseases with Q9CQV4
Functions
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| endoplasmic reticulum | The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached). |
| 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. |
| protein-containing complex | A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together. |
1 GO annotations of molecular function
| Name | Definition |
|---|---|
| endoplasmic reticulum-autophagosome adaptor activity | The binding activity of a molecule that brings together an ER membrane and an autophagosome during reticulophagy. |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| collagen catabolic process | The proteolytic chemical reactions and pathways resulting in the breakdown of collagen in the extracellular matrix, usually carried out by proteases secreted by nearby cells. |
| endoplasmic reticulum organization | A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the endoplasmic reticulum. |
| positive regulation of neuron projection development | Any process that increases the rate, frequency or extent of neuron projection development. Neuron projection development is the process whose specific outcome is the progression of a neuron projection over time, from its formation to the mature structure. A neuron projection is any process extending from a neural cell, such as axons or dendrites (collectively called neurites). |
| 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. |
6 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q5E9K8 | RETREG1 | Reticulophagy regulator 1 | Bos taurus (Bovine) | PR |
| Q9H6L5 | RETREG1 | Reticulophagy regulator 1 | Homo sapiens (Human) | PR |
| Q86VR2 | RETREG3 | Reticulophagy regulator 3 | Homo sapiens (Human) | PR |
| Q6NS82 | Retreg2 | Reticulophagy regulator 2 | Mus musculus (Mouse) | PR |
| Q8VE91 | Retreg1 | Reticulophagy regulator 1 | Mus musculus (Mouse) | PR |
| Q0P4Z1 | retreg3 | Reticulophagy regulator 3 | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MEEAEGVAAA | PGPASGLAFR | GRRAMSGSWE | RDQQVEAAQR | TLVEVLGPYE | PLLSRVQAAL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| VWERPARSAL | WCLGLNAAFW | FFALTSLRFV | FLLAFSLMII | VCIDQWKNKI | WPEINVPRPD |
| 130 | 140 | 150 | 160 | 170 | 180 |
| ALDNESWGFV | HPRLLSVPEL | CHHVAEVWVS | GTIFIRNLLL | FKKQNPGKFC | LLSCGVLTFL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| AMLGRYIPGL | LLSYLMLVII | MMWPLAVYHR | LWDRAYVRLK | PVLQRLDFSV | RGYMMSKQRE |
| 250 | 260 | 270 | 280 | 290 | 300 |
| RQLRRRALHS | ERATDSHSDS | EEELAAFCPQ | LDDSTVAREL | AITDSEHSDA | EVSCTENGTF |
| 310 | 320 | 330 | 340 | 350 | 360 |
| NLSRGQTPLT | EGSEDLDGHS | DPEESFARDL | PDFPSINVDP | AGLDDEDDTS | IGMPSLMYRS |
| 370 | 380 | 390 | 400 | 410 | 420 |
| PPGAGDTQVL | PASRNEAALP | ELLLSSLPGG | SNLTSNLASL | VSQGMIQLAL | SEASQTDPSG |
| 430 | 440 | 450 | 460 | ||
| PPPRRATRGF | LRAPSSDLDT | DAEGDDFELL | DQSELNQLDP | ASSRSH |