Q0V8F1
Gene name |
CORO7 |
Protein name |
Coronin-7 |
Names |
Crn7 |
Species |
Bos taurus (Bovine) |
KEGG Pathway |
bta:527934 |
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 Q0V8F1
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q0V8F1-F1 | Predicted | AlphaFoldDB |
No variants for Q0V8F1
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q0V8F1 | |||||
No associated diseases with Q0V8F1
9 regional properties for Q0V8F1
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| repeat | WD40 repeat | 66 - 107 | IPR001680-1 |
| repeat | WD40 repeat | 115 - 154 | IPR001680-2 |
| repeat | WD40 repeat | 157 - 196 | IPR001680-3 |
| repeat | WD40 repeat | 525 - 564 | IPR001680-4 |
| repeat | WD40 repeat | 574 - 656 | IPR001680-5 |
| repeat | WD40 repeat | 660 - 704 | IPR001680-6 |
| domain | Domain of unknown function DUF1899 | 3 - 64 | IPR015048-1 |
| domain | Domain of unknown function DUF1899 | 457 - 523 | IPR015048-2 |
| conserved_site | WD40 repeat, conserved site | 601 - 615 | IPR019775 |
Functions
4 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasmic vesicle | A vesicle found in the cytoplasm of a cell. |
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| Golgi membrane | The lipid bilayer surrounding any of the compartments of the Golgi apparatus. |
| trans-Golgi network | The network of interconnected tubular and cisternal structures located within the Golgi apparatus on the side distal to the endoplasmic reticulum, from which secretory vesicles emerge. The trans-Golgi network is important in the later stages of protein secretion where it is thought to play a key role in the sorting and targeting of secreted proteins to the correct destination. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| actin binding | Binding to monomeric or multimeric forms of actin, including actin filaments. |
| actin filament binding | Binding to an actin filament, also known as F-actin, a helical filamentous polymer of globular G-actin subunits. |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| actin filament organization | A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures comprising actin filaments. Includes processes that control the spatial distribution of actin filaments, such as organizing filaments into meshworks, bundles, or other structures, as by cross-linking. |
| actin filament polymerization | Assembly of actin filaments by the addition of actin monomers to a filament. |
| Golgi to endosome transport | The directed movement of substances from the Golgi to early sorting endosomes. Clathrin vesicles transport substances from the trans-Golgi to endosomes. |
| 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. |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MNRFKVSKFR | HTEARQPRRE | AWIGDIRAGT | APSCGNHIKA | SCSLIAFNSD | HPGVLGIVPL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| ESQGEDKRQV | THLGCHSDLV | TDLDFSPFDD | FLLATASADR | TVKLWRLPLS | GQALPSGPGL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LLGPEDAQVE | VLQFHPTADG | VLLSAAGRAV | KVWDATKQQP | LTELATHGDL | VQGAAWSRDG |
| 190 | 200 | 210 | 220 | 230 | 240 |
| ALLGTTCKDK | QLRIFDPRAK | PEAAQSTPAH | ENSRDGRLVW | TGTQEYLVST | GFNQMREREV |
| 250 | 260 | 270 | 280 | 290 | 300 |
| KLWDTRLFSA | ALTSLTLDTS | PRSLVPLLDP | DSGLLVLAGK | GENQLYCYEA | APQQPALSPV |
| 310 | 320 | 330 | 340 | 350 | 360 |
| TQCLLESVLR | GAALVPRRAL | AVMGCEVLRV | LQLSDTAIVP | ISYHVPRKTV | EFHEDLFPDT |
| 370 | 380 | 390 | 400 | 410 | 420 |
| AGCVPASDPH | AWWAGSDQQV | QRVSLHPARR | AHPSFTSCLA | PPAELTPATA | QPAGTPEGFS |
| 430 | 440 | 450 | 460 | 470 | 480 |
| STPSSLTSPS | TPSSLGPSLT | STSGIGTSPS | QRSLQSLLGP | SSKFRHAQGS | VLHRDSHITN |
| 490 | 500 | 510 | 520 | 530 | 540 |
| LKGLNLTTPG | ESDGFCANQL | RVAVPLLSSG | GQVAVLELRK | PGRLPDTALP | TLQNGVAVTD |
| 550 | 560 | 570 | 580 | 590 | 600 |
| LAWDPFDPHR | LAVAGEDARI | RLWRVPPDGL | QEVLTMPEAV | LTGHTEKIYS | LRFHPLAADV |
| 610 | 620 | 630 | 640 | 650 | 660 |
| LASSSYDLTV | RIWDLKVGAE | QLRLQGHRDQ | IFGLAWSPDG | QQLATVCKDG | RLRIYEPRGS |
| 670 | 680 | 690 | 700 | 710 | 720 |
| PEPLQEGPGP | EGARGARVVW | VCDGHYLLVS | GFDSRSERQL | LLYSAKALAG | GPSAVLGLDV |
| 730 | 740 | 750 | 760 | 770 | 780 |
| APSTLLPSYD | PDTGLVLLTG | KGDTRVFLYE | LLPGAPFFLE | CNSFTSPDPH | KGFILLPKTE |
| 790 | 800 | 810 | 820 | 830 | 840 |
| CDVREVEFAR | CLRLRQTSLE | PVAFRLPRVR | KEFFQDDVFP | DTTVSWEPAL | SAEAWLGGAN |
| 850 | 860 | 870 | 880 | 890 | 900 |
| GTPRLLSLQP | PGMTPVSQAP | REAPARRAPS | SVYLEEKSDQ | QKKEELLSAM | VAKLGNREDP |
| 910 | |||||
| LPQDSFEGVD | EDEWD |