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
0 structures for P12474
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|
No variants for P12474
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P12474 | |||||
No associated diseases with P12474
Functions
6 GO annotations of cellular component
| Name | Definition |
|---|---|
| host cell endoplasmic reticulum-Golgi intermediate compartment | A complex system of membrane-bounded compartments located between host cell endoplasmic reticulum (ER) and the host Golgi complex, with a distinctive membrane protein composition; involved in ER-to-Golgi transport. |
| host cell plasma membrane | The plasma membrane surrounding a host cell. |
| host cell rough endoplasmic reticulum | The irregular network of unit membranes, visible only by electron microscopy, that occurs in the host cell cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The host rough ER has ribosomes adhering to the outer surface. |
| host cytoskeleton | A cellular structure that forms the internal framework of eukaryotic and prokaryotic host cells. The cytoskeleton includes intermediate filaments, microfilaments, microtubules, the microtrabecular lattice, and other structures characterized by a polymeric filamentous nature and long-range order within the cell. The various elements of the cytoskeleton not only serve in the maintenance of cellular shape but also have roles in other cellular functions, including cellular movement, cell division, endocytosis, and movement of organelles. |
| membrane | A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it. |
| viral outer capsid | The outer layer of a double or triple concentric icosahedral capsid. Outer capsids are part of reoviridae and cystoviridae virions. |
No GO annotations of molecular function
| Name | Definition |
|---|---|
| No GO annotations for molecular function |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| permeabilization of host organelle membrane involved in viral entry into host cell | Induction of organellar membrane permeabilization triggered by an interaction between the host membrane and a membrane-penetration protein associated with a viral capsid. Results in release of the virus contents from an organelle into the host cell cytoplasm. |
| viral entry via permeabilization of inner membrane | The entry of a non-enveloped virus into the cytoplasm of a host prokaryotic cell, following fusion with the outer membrane, via permeabilization of the plasma (inner) membrane. In the case of some double stranded RNA viruses of prokaryotes this occurs via interaction of a membrane-interacting component of the capsid, leading to depolarization an permeabilization of the plasma membrane. |
| virion attachment to host cell | The process by which a virion protein binds to molecules on the host cellular surface or host cell surface projection. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MASLIYRQLL | ANSYAVNLSD | EIQSVGSGKN | QRVTVNPGPF | AQTGYAPVNW | GPGEVNDSTV |
| 70 | 80 | 90 | 100 | 110 | 120 |
| VQPVLDGPYQ | PAPFDLPVGN | WMLLAPTRPG | VVVEGTDNSG | RWLSVILIEP | GVASETRTYM |
| 130 | 140 | 150 | 160 | 170 | 180 |
| MFGSSKQVVV | SNVSDTKWKF | VEMVKTAVDG | DYAEWGTLLS | DTKLYGMMKY | GRRLFIYEGE |
| 190 | 200 | 210 | 220 | 230 | 240 |
| TPNATTKGYF | ITNYASAEVR | PYSDFYIISR | SQESACTEYI | NNGLPPIQNT | RNVVPVAISS |
| 250 | 260 | 270 | 280 | 290 | 300 |
| RSIKPREVQA | NEDIVVSKTS | LWKEMQYNRD | IIIRFKFDNS | IIKSGGLGYK | WAEISFKAAN |
| 310 | 320 | 330 | 340 | 350 | 360 |
| YQYNYMRDGE | EVTAHTTCSV | NGVNDFSFNG | GSLPTDFAIS | RYEVIKENSY | VYVDYWDDSQ |
| 370 | 380 | 390 | 400 | 410 | 420 |
| AFRNMVYVRS | LAANLNDVMC | SGGHYSFALP | VGQWPVMKGG | AVTLHTAGVT | LSTQFTDFVS |
| 430 | 440 | 450 | 460 | 470 | 480 |
| LNSLRFRFRL | AVEEPSFTIT | RTRVSKLYGL | PAANPNGGKE | YYEVAGRFSF | ISLVPSNDDY |
| 490 | 500 | 510 | 520 | 530 | 540 |
| QTPIMNSVTV | RQDLERRLNE | LREEFNNLSQ | EIAVSQLIDL | AMLPLDMFSM | FSGIESTVNA |
| 550 | 560 | 570 | 580 | 590 | 600 |
| AKSMATNVMR | KFKSSKLASS | VSMLTDSLSD | AASSIARSTS | VRSIGSTASA | WANISEQTQD |
| 610 | 620 | 630 | 640 | 650 | 660 |
| AVSEVATISS | QVSQISGRLR | LKEITTQTEG | MNFDDISAAV | LKAKIDRSIQ | VDQNALPDVI |
| 670 | 680 | 690 | 700 | 710 | 720 |
| TEASEKFIRN | RAYRVIDGDE | AFEAGTDGRF | FAYKVETLEE | MPFNMEKFAD | LVTNSPVISA |
| 730 | 740 | 750 | 760 | 770 | |
| IIDFKTLKNL | NDNYGITREQ | AFNLLRSDPK | VLRGFIDQNN | PIIKNRIEQL | IMQCRL |