Q872W1
Gene name |
apg-9 (atg17, B2G14.070, NCU08766) |
Protein name |
Autophagy-related protein 17 |
Names |
|
Species |
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) |
KEGG Pathway |
ncr:NCU08766 |
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 Q872W1
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q872W1-F1 | Predicted | AlphaFoldDB |
No variants for Q872W1
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q872W1 | |||||
No associated diseases with Q872W1
1 regional properties for Q872W1
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Autophagy protein ATG17-like domain | 80 - 494 | IPR045326 |
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| Atg1/ULK1 kinase complex | A protein complex consisting of Atg1 (or Atg1 homologs e.g. ULK1, ULK2 in mammals) and Atg13 along with other proteins that regulate its function (e.g. Atg17 in yeast or RB1CC1(FIP200) in mammals). This complex has serine/threonine protein kinase activity and is involved in autophagosome formation. |
| phagophore assembly site | Punctate structures proximal to the endoplasmic reticulum which are the sites where the Atg machinery assembles upon autophagy induction. |
| phagophore assembly site membrane | A cellular membrane associated with the phagophore assembly site. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| molecular adaptor activity | The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way. |
| protein kinase activator activity | Binds to and increases the activity of a protein kinase, an enzyme which phosphorylates a protein. |
6 GO annotations of biological process
| Name | Definition |
|---|---|
| activation of protein kinase activity | Any process that initiates the activity of an inactive protein kinase. |
| autophagosome assembly | The formation of a double membrane-bounded structure, the autophagosome, that occurs when a specialized membrane sac, called the isolation membrane, starts to enclose a portion of the cytoplasm. |
| autophagy of mitochondrion | The autophagic process in which mitochondria are delivered to a type of vacuole and degraded in response to changing cellular conditions. |
| autophagy of peroxisome | The process in which peroxisomes are delivered to a type of vacuole and degraded in response to changing nutrient conditions. |
| late nucleophagy | A type of nucleophagy, distinct from piecemeal microautophagy of the nucleus (PNM) where the nuclear material is delivered to the vacuole/lysosome for breakdown and recycling later than observed for PNM. |
| piecemeal microautophagy of the nucleus | Degradation of a cell nucleus by lysosomal microautophagy. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MASFHSHSPS | PPAALSPDDA | PQPRRPSRTS | LHDAAAAAAP | ALSPESPGHE | LEDGADSSEF |
| 70 | 80 | 90 | 100 | 110 | 120 |
| NADDVPVEVL | VKHLLAAKQS | LSSMTLVLRA | NDLATSARQM | HQEFVILSAQ | TAFLRHGILQ |
| 130 | 140 | 150 | 160 | 170 | 180 |
| ELHILHQLRR | GMARAYDNGT | RDFKHIIRTL | DTADGRLEKI | MQVLRKTTVE | NVFRQPGEEP |
| 190 | 200 | 210 | 220 | 230 | 240 |
| KCLLDFVDPK | IVEQVRDALK | ESIHELSAAK | TSFDGDLLRF | DTDLRTLTDA | MAAAASLANP |
| 250 | 260 | 270 | 280 | 290 | 300 |
| TTTTPDGYPP | DQRSIPNLLS | ALSEGSHLMA | EHLSSLTRHF | DMCVTAVRTT | EGGAALARRR |
| 310 | 320 | 330 | 340 | 350 | 360 |
| AAEATSSDED | QAPVSISGVI | SAQESESGPS | AFEPMDPLER | QELLHVVMRD | AAEVDDVVAD |
| 370 | 380 | 390 | 400 | 410 | 420 |
| IHNVLQQMEM | DHASLHSLFS | ASRASHAATL | TCFSMLEEVG | ARASSYVAAE | AEFMQRWEDE |
| 430 | 440 | 450 | 460 | 470 | 480 |
| KETIDENVSK | MDELKKFYEG | FLNAYGGLLL | EVERRRAVEG | KIDSIWRKAK | EQVDKLVEAD |
| 490 | 500 | 510 | 520 | 530 | 540 |
| KREREHFRLE | VGDYVPADLW | GVVDRPLGRW | AVVPLEDTRE | GSYEMEAHGE | PENEGKVETA |
| 550 | 560 | ||||
| YERETEPSTP | TPRKMPLNGP | GSAGERPF |