Q9WU78
SS
Gene name |
Pdcd6ip (Aip1, Alix) |
Protein name |
Programmed cell death 6-interacting protein |
Names |
ALG-2-interacting protein 1 , ALG-2-interacting protein X , E2F1-inducible protein , Eig2 |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:18571 |
EC number |
|
Protein Class |
|
Descriptions
The adaptor protein PDCD6IP(ALIX) encodes a programmed cell death 6-interacting protein, which is involved in diverse cellular processes including cytokinesis, apoptosis, and junction integrity maintenance. PDCD6IP is composed of several domains (Bro1 domain containing patch 1 and 2, V domain, and proline-rich domain (PRD)). PRD contains multiple partner-protein-docking sites. PDCD6IP links retroviruses to ESCRT machinery during retroviral budding. This function of PDCD6IP requires its interaction with the ESCRT-III component CHMP4 at the N-terminal Bro1 domain and retroviral Gag protein at the middle of V domain. <br>The autoinhibited closed form of PDCD6IP is maintained via the intramolecular interaction between the patch 2 site of the Bro1 domain and TSG101-docking site (TDS) within the PRD domain, which prevents it from interacting with other partner proteins and inhibiting association with the membrane. <br>Though only the TDS was confirmed as an autoinhibitory region, since Bro1 domain has a protein-binding site for CHMP4, Bro1 domain may be an autoinhibitory region as well as a target element of TDS.
Autoinhibitory domains (AIDs)
Target domain |
712-720 (TSG101 docking site) |
Relief mechanism |
Partner binding |
Assay |
|
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for Q9WU78
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9WU78-F1 | Predicted | AlphaFoldDB |
37 variants for Q9WU78
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3389078966 | 113 | L>P | No | EVA | |
| rs3389054819 | 114 | A>T | No | EVA | |
| rs3400795708 | 151 | K>* | No | EVA | |
| rs3389083191 | 208 | M>V | No | EVA | |
| rs3389078927 | 212 | I>N | No | EVA | |
| rs3389078934 | 217 | A>V | No | EVA | |
| rs3389047053 | 222 | D>Y | No | EVA | |
| rs3389080197 | 244 | T>A | No | EVA | |
| rs3389080205 | 249 | Q>H | No | EVA | |
| rs3389081800 | 270 | F>* | No | EVA | |
| rs3389047058 | 275 | A>T | No | EVA | |
| rs3413091393 | 285 | K>R | No | EVA | |
| rs30522518 | 296 | N>K | No | EVA | |
| rs3389067446 | 296 | N>S | No | EVA | |
| rs3399607107 | 303 | K>I | No | EVA | |
| rs3389081872 | 368 | A>* | No | EVA | |
| rs3389067353 | 368 | A>D | No | EVA | |
| rs3389078924 | 370 | F>Y | No | EVA | |
| rs3389080780 | 374 | K>N | No | EVA | |
| rs3389088915 | 378 | V>I | No | EVA | |
| rs3389088936 | 380 | R>I | No | EVA | |
| rs3400749978 | 410 | G>A | No | EVA | |
| rs3400367614 | 410 | G>R | No | EVA | |
| rs3389058640 | 506 | D>E | No | EVA | |
| rs3389080787 | 514 | Q>H | No | EVA | |
| rs3399607088 | 538 | N>K | No | EVA | |
| rs46037244 | 573 | L>M | No | EVA | |
| rs3389080180 | 670 | L>* | No | EVA | |
| rs3389058655 | 671 | K>N | No | EVA | |
| rs3389078886 | 671 | K>R | No | EVA | |
| rs3389054884 | 676 | F>L | No | EVA | |
| rs3400367634 | 687 | F>L | No | EVA | |
| rs3389067431 | 707 | K>E | No | EVA | |
| rs3400154831 | 754 | P>T | No | EVA | |
| rs3389078898 | 802 | P>S | No | EVA | |
| rs3389081849 | 820 | M>I | No | EVA | |
| rs3389081806 | 827 | Y>H | No | EVA |
No associated diseases with Q9WU78
Functions
9 GO annotations of cellular component
| Name | Definition |
|---|---|
| actomyosin | Any complex of actin, myosin, and accessory proteins. |
| bicellular tight junction | An occluding cell-cell junction that is composed of a branching network of sealing strands that completely encircles the apical end of each cell in an epithelial sheet; the outer leaflets of the two interacting plasma membranes are seen to be tightly apposed where sealing strands are present. Each sealing strand is composed of a long row of transmembrane adhesion proteins embedded in each of the two interacting plasma membranes. |
| centrosome | A structure comprised of a core structure (in most organisms, a pair of centrioles) and peripheral material from which a microtubule-based structure, such as a spindle apparatus, is organized. Centrosomes occur close to the nucleus during interphase in many eukaryotic cells, though in animal cells it changes continually during the cell-division cycle. |
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| endosome | A vacuole to which materials ingested by endocytosis are delivered. |
| extracellular exosome | A vesicle that is released into the extracellular region by fusion of the limiting endosomal membrane of a multivesicular body with the plasma membrane. Extracellular exosomes, also simply called exosomes, have a diameter of about 40-100 nm. |
| Flemming body | A cell part that is the central region of the midbody characterized by a gap in alpha-tubulin staining. It is a dense structure of antiparallel microtubules from the central spindle in the middle of the intercellular bridge. |
| melanosome | A tissue-specific, membrane-bounded cytoplasmic organelle within which melanin pigments are synthesized and stored. Melanosomes are synthesized in melanocyte cells. |
| myelin sheath | An electrically insulating fatty layer that surrounds the axons of many neurons. It is an outgrowth of glial cells |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| identical protein binding | Binding to an identical protein or proteins. |
| protein dimerization activity | The formation of a protein dimer, a macromolecular structure consists of two noncovalently associated identical or nonidentical subunits. |
| SH3 domain binding | Binding to a SH3 domain (Src homology 3) of a protein, small protein modules containing approximately 50 amino acid residues found in a great variety of intracellular or membrane-associated proteins. |
10 GO annotations of biological process
| Name | Definition |
|---|---|
| actomyosin contractile ring assembly | The process of assembly of a ring composed of actin, myosin, and associated proteins that will function in cytokinesis. |
| apoptotic process | A programmed cell death process which begins when a cell receives an internal (e.g. DNA damage) or external signal (e.g. an extracellular death ligand), and proceeds through a series of biochemical events (signaling pathway phase) which trigger an execution phase. The execution phase is the last step of an apoptotic process, and is typically characterized by rounding-up of the cell, retraction of pseudopodes, reduction of cellular volume (pyknosis), chromatin condensation, nuclear fragmentation (karyorrhexis), plasma membrane blebbing and fragmentation of the cell into apoptotic bodies. When the execution phase is completed, the cell has died. |
| bicellular tight junction assembly | The aggregation, arrangement and bonding together of a set of components to form a tight junction, an occluding cell-cell junction that is composed of a branching network of sealing strands that completely encircles the apical end of each cell in an epithelial sheet. |
| extracellular exosome biogenesis | The assembly and secretion of an extracellular exosome, a membrane-bounded vesicle that is released into the extracellular region by fusion of the limiting endosomal membrane of a multivesicular body with the plasma membrane. |
| macroautophagy | The major inducible pathway for the general turnover of cytoplasmic constituents in eukaryotic cells, it is also responsible for the degradation of active cytoplasmic enzymes and organelles during nutrient starvation. Macroautophagy involves the formation of double-membrane-bounded autophagosomes which enclose the cytoplasmic constituent targeted for degradation in a membrane-bounded structure. Autophagosomes then fuse with a lysosome (or vacuole) releasing single-membrane-bounded autophagic bodies that are then degraded within the lysosome (or vacuole). Some types of macroautophagy, e.g. pexophagy, mitophagy, involve selective targeting of the targets to be degraded. |
| maintenance of epithelial cell apical/basal polarity | The maintenance of the apicobasal polarity of an epithelial cell. |
| mitotic cytokinesis | A cell cycle process that results in the division of the cytoplasm of a cell after mitosis, resulting in the separation of the original cell into two daughter cells. |
| multivesicular body sorting pathway | A vesicle-mediated transport process in which transmembrane proteins are ubiquitylated to facilitate their entry into luminal vesicles of multivesicular bodies (MVBs); upon subsequent fusion of MVBs with lysosomes or vacuoles, the cargo proteins are degraded. |
| 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. |
| regulation of membrane permeability | Any process that modulates the frequency, rate or extent of the passage or uptake of molecules by a membrane. |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MASFIWVQLK | KTSEVDLAKP | LVKFIQQTYP | SGGEEQAQYC | RAAEELSKLR | RSALGRPLDK |
| 70 | 80 | 90 | 100 | 110 | 120 |
| HEGALETLLR | YYDQICSIEP | KFPFSENQIC | LTFTWKDAFD | KGSLFGGSVK | LALASLGYEK |
| 130 | 140 | 150 | 160 | 170 | 180 |
| SCVLFNCAAL | ASQIAAEQNL | DNDEGLKTAA | KQYQFASGAF | LHIKDTVLSA | LSREPTVDIS |
| 190 | 200 | 210 | 220 | 230 | 240 |
| PDTVGTLSLI | MLAQAQEVFF | LKATRDKMKD | AIIAKLANQA | ADYFGDAFKQ | CQYKDTLPKE |
| 250 | 260 | 270 | 280 | 290 | 300 |
| VFPTLAAKQC | IMQANAEYHQ | SILAKQQKKF | GEEIARLQHA | AELIKNVASR | YDEYVNVKDF |
| 310 | 320 | 330 | 340 | 350 | 360 |
| SDKINRALTA | AKKDNDFIYH | DRVPDLKDLD | PIGKATLVKP | TPVNVPVSQK | FTDLFEKMVP |
| 370 | 380 | 390 | 400 | 410 | 420 |
| VSVQQSLAVF | SQRKADLVNR | SIAQMREATT | LANGVLASLN | LPAAIEDVSG | DTVPQSILTK |
| 430 | 440 | 450 | 460 | 470 | 480 |
| STSVVEQGGI | QTVDQLIKEL | PELLQRNREI | LEESLRLLDE | EEATDNDLRA | KFKDRWQRTP |
| 490 | 500 | 510 | 520 | 530 | 540 |
| SNDLYKPLRA | EGAKFRAVLD | KAVQADGQVK | ERYQSHRDTI | ALLCKPEPEL | NAAIPSANPA |
| 550 | 560 | 570 | 580 | 590 | 600 |
| KTMQGSEVVS | VLKSLLSNLD | EIKKERESLE | NDLKSVNFDM | TSKFLTALAQ | DGVINEEALS |
| 610 | 620 | 630 | 640 | 650 | 660 |
| VTELDRIYGG | LTSKVQESLK | KQEGLLKNIQ | VSHQEFSKMK | QSNNEANLRE | EVLKNLATAY |
| 670 | 680 | 690 | 700 | 710 | 720 |
| DNFVELVANL | KEGTKFYNEL | TEILVRFQNK | CSDIVFARKT | ERDELLKDLQ | QSIAREPSAP |
| 730 | 740 | 750 | 760 | 770 | 780 |
| SIPPPAYQSS | PAAGHAAAPP | TPAPRTMPPA | KPQPPARPPP | PVLPANRVPP | ASAAAAPAGV |
| 790 | 800 | 810 | 820 | 830 | 840 |
| GTASAAPPQT | PGSAPPPQAQ | GPPYPTYPGY | PGYCQMPMPM | GYNPYAYGQY | NMPYPPVYHQ |
| 850 | 860 | ||||
| SPGQAPYPGP | QQPTYPFPQP | PQQSYYPQQ |