Q9USW2
Gene name |
inp2 (SPBC21B10.06c) |
Protein name |
Inheritance of peroxisomes protein 2 |
Names |
|
Species |
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
KEGG Pathway |
spo:SPBC21B10.06c |
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 Q9USW2
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9USW2-F1 | Predicted | AlphaFoldDB |
No variants for Q9USW2
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q9USW2 | |||||
No associated diseases with Q9USW2
No regional properties for Q9USW2
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for Q9USW2 | |||
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| cell division site | The eventual plane of cell division (also known as cell cleavage or cytokinesis) in a dividing cell. In Eukaryotes, the cleavage apparatus, composed of septin structures and the actomyosin contractile ring, forms along this plane, and the mitotic, or meiotic, spindle is aligned perpendicular to the division plane. In bacteria, the cell division site is generally located at mid-cell and is the site at which the cytoskeletal structure, the Z-ring, assembles. |
| cell tip | The region at the end of the longest axis of a cylindrical or elongated cell. |
| integral component of peroxisomal membrane | The component of the peroxisomal 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. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| myosin binding | Binding to a myosin; myosins are any of a superfamily of molecular motor proteins that bind to actin and use the energy of ATP hydrolysis to generate force and movement along actin filaments. |
| 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. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| peroxisome inheritance | The acquisition of peroxisomes by daughter cells from the mother cell after replication. In Saccharomyces cerevisiae, the number of peroxisomes cells is fairly constant; a subset of the organelles are targeted and segregated to the bud in a highly ordered, vectorial process. Efficient segregation of peroxisomes from mother to bud is dependent on the actin cytoskeleton, and active movement of peroxisomes along actin filaments is driven by the class V myosin motor protein, Myo2p. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MNVDTQLSRD | GLYSSLRTRY | KVYISMHAFA | IWHRFISFLA | IYLWPCIMGS | VNLNLQDREN |
| 70 | 80 | 90 | 100 | 110 | 120 |
| EYFFDSIQYI | IYTSELLVGD | HELQRSHHEE | QPSLVYPSSS | FSSTSKFWRY | FAYLLSLQIV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| IDFVLYKLSS | AMASLHYLKF | VKIIALSYIC | FSSLIRICHC | WTYFIRIMGL | SSLNKFVNLL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| HDFETTSNRV | YSQICELEAN | SAANRSRLMD | FLPANDPLLF | NLTEQNTLSY | ELSGLYEKLL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| PRYQLVLSRI | YPYAAASNLR | NLLSLYRLPN | CFGKLNSFDL | RKGSSTSLKR | SSMYLARKEN |
| 310 | 320 | 330 | 340 | 350 | 360 |
| QDFDDQSTQI | LNHIKTAYYE | LTIISKQVLC | CILSFPVDSF | LAERSSWLIV | HREVGDLSNA |
| 370 | 380 | 390 | 400 | 410 | 420 |
| LSVSMVRLVD | ILKFSVESVN | RNQHNTTSKP | FPRIMCKENL | RSLFNELHSV | MMETHESISS |
| 430 | 440 | 450 | 460 | ||
| YIQEGDNTAM | QTYAMDEYDQ | VGLLLKDLLS | EWDFNRALLL | NLQHMHRKRK |