Q9D2V7
Gene name |
Coro7 |
Protein name |
Coronin-7 |
Names |
Crn7, 70 kDa WD repeat tumor rejection antigen homolog |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:78885 |
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 Q9D2V7
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9D2V7-F1 | Predicted | AlphaFoldDB |
59 variants for Q9D2V7
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs47868465 | 2 | S>N | No | EVA | |
| rs3389358625 | 22 | W>* | No | EVA | |
| rs3389399152 | 25 | D>V | No | EVA | |
| rs3389348202 | 32 | P>L | No | EVA | |
| rs235497919 | 61 | E>K | No | EVA | |
| rs3389348154 | 68 | R>S | No | EVA | |
| rs3389313910 | 121 | V>S | No | EVA | |
| rs3389406974 | 122 | L>R | No | EVA | |
| rs3389358645 | 123 | G>C | No | EVA | |
| rs3389313893 | 132 | L>M | No | EVA | |
| rs3389348172 | 140 | G>E* | No | EVA | |
| rs3389395110 | 143 | V>G | No | EVA | |
| rs3389395500 | 148 | K>R | No | EVA | |
| rs3389348152 | 165 | E>* | No | EVA | |
| rs3413134963 | 168 | K>Q | No | EVA | |
| rs3389390892 | 176 | W>L | No | EVA | |
| rs3389348126 | 180 | G>E | No | EVA | |
| rs3389390874 | 205 | Q>* | No | EVA | |
| rs3412902596 | 208 | Q>R | No | EVA | |
| rs3389395107 | 229 | S>P | No | EVA | |
| rs3389388483 | 233 | N>D | No | EVA | |
| rs3389395134 | 248 | F>I | No | EVA | |
| rs3389388463 | 259 | T>I | No | EVA | |
| rs3389399150 | 260 | S>Y | No | EVA | |
| rs3389348128 | 288 | Y>C | No | EVA | |
| rs3389358529 | 298 | S>I | No | EVA | |
| rs3389390854 | 334 | S>G | No | EVA | |
| rs3389395163 | 340 | P>L | No | EVA | |
| rs3389399185 | 342 | S>G | No | EVA | |
| rs51648975 | 350 | V>I | No | EVA | |
| rs3389348216 | 373 | W>* | No | EVA | |
| rs3389391131 | 384 | S>G | No | EVA | |
| rs264509048 | 410 | V>A | No | EVA | |
| rs3389412649 | 477 | L>F | No | EVA | |
| rs3389367180 | 477 | L>P | No | EVA | |
| rs3389399226 | 521 | V>M | No | EVA | |
| rs3389395568 | 531 | P>L | No | EVA | |
| rs46299316 | 542 | T>A | No | EVA | |
| rs3389398144 | 549 | W>* | No | EVA | |
| rs3389388466 | 658 | V>G | No | EVA | |
| rs3389406887 | 677 | E>D | No | EVA | |
| rs261425482 | 685 | V>I | No | EVA | |
| rs3389377190 | 686 | W>* | No | EVA | |
| rs223399162 | 701 | R>Q | No | EVA | |
| rs3389388448 | 729 | S>L | No | EVA | |
| rs3389391136 | 781 | L>F | No | EVA | |
| rs3389395124 | 792 | V>M | No | EVA | |
| rs3412564235 | 817 | K>R | No | EVA | |
| rs3406270812 | 849 | P>T | No | EVA | |
| rs52050677 | 850 | R>Q | No | EVA | |
| rs13473982 | 851 | L>V | No | EVA | |
| rs3389399159 | 857 | P>S | No | EVA | |
| rs3389367165 | 859 | M>I | No | EVA | |
| rs3389412650 | 860 | T>S | No | EVA | |
| rs238246985 | 867 | R>H | No | EVA | |
| rs3389398145 | 874 | A>V | No | EVA | |
| rs3389406893 | 888 | Q>L | No | EVA | |
| rs3389391132 | 892 | E>D | No | EVA | |
| rs3389377251 | 903 | N>D | No | EVA |
No associated diseases with Q9D2V7
11 regional properties for Q9D2V7
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| repeat | WD40 repeat | 66 - 108 | IPR001680-1 |
| repeat | WD40 repeat | 115 - 154 | IPR001680-2 |
| repeat | WD40 repeat | 157 - 205 | IPR001680-3 |
| repeat | WD40 repeat | 531 - 570 | IPR001680-4 |
| repeat | WD40 repeat | 580 - 662 | IPR001680-5 |
| domain | Domain of unknown function DUF1899 | 3 - 64 | IPR015048-1 |
| domain | Domain of unknown function DUF1899 | 463 - 529 | IPR015048-2 |
| conserved_site | WD40 repeat, conserved site | 607 - 621 | IPR019775 |
| repeat | G-protein beta WD-40 repeat | 93 - 107 | IPR020472-1 |
| repeat | G-protein beta WD-40 repeat | 141 - 155 | IPR020472-2 |
| repeat | G-protein beta WD-40 repeat | 607 - 621 | IPR020472-3 |
Functions
6 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 apparatus | A membrane-bound cytoplasmic organelle of the endomembrane system that further processes the core oligosaccharides (e.g. N-glycans) added to proteins in the endoplasmic reticulum and packages them into membrane-bound vesicles. The Golgi apparatus operates at the intersection of the secretory, lysosomal, and endocytic pathways. |
| Golgi membrane | The lipid bilayer surrounding any of the compartments of the Golgi apparatus. |
| integral component of membrane | The component of a 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. |
| 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. |
8 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. |
| cell migration | The controlled self-propelled movement of a cell from one site to a destination guided by molecular cues. Cell migration is a central process in the development and maintenance of multicellular organisms. |
| establishment of cell polarity | The specification and formation of anisotropic intracellular organization or cell growth patterns. |
| Golgi organization | A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the Golgi apparatus. |
| 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. |
| positive regulation of hippo signaling | Any process that activates or increases the frequency, rate or extent of hippo signaling. |
| 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. |
5 homologous proteins in AiPD
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSRFKVSKFR | HMEARPSRRE | AWISDIRAVT | TPTCGNHIKS | SCSLIAFNSD | RPGVLGVISL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| EGHEENKRHV | TYLGCHSDLV | TDLDFSPFDD | FLLASGSADR | TIKLWRLSGT | GEALPSVPGV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| VLGPEELPVE | VLQFHPTVDG | VLVSTAGKTV | KVWDVAKQQP | LTELEAHKDL | VQSAVWSRDG |
| 190 | 200 | 210 | 220 | 230 | 240 |
| AIVGTACKDK | QLRIFDPRAR | TQASQSTQAH | ENNRDIRLAW | TGIQEHLVST | GFNQMREREA |
| 250 | 260 | 270 | 280 | 290 | 300 |
| KLWDTRLFSS | ALASVTLDTS | PGPLIPLLDP | DSGLLVLAGK | GENQLYCYEV | TPQQPALSPV |
| 310 | 320 | 330 | 340 | 350 | 360 |
| TQCILENVLR | GAALVPRRAL | AVMSCEVLQV | LQLSDTAIIP | ISHHVPRKAV | EFHEDLFPDT |
| 370 | 380 | 390 | 400 | 410 | 420 |
| AGSVPASDAH | MWWAGDNQQV | QKVSLNPARR | PHPCFTSSLV | PTMEPAPDMV | QPAEMPRADT |
| 430 | 440 | 450 | 460 | 470 | 480 |
| DLSEGFSSPS | SLMSPSTPSS | LGPSLSSTSG | IGTSPSQRSL | QSLLGPSSKF | RHTQGSLLHR |
| 490 | 500 | 510 | 520 | 530 | 540 |
| DSHITNLKGL | NLTTPGESDG | FCANRLRVAV | PLLSSGGQVA | VLELQKPGRL | PDTALPTLQN |
| 550 | 560 | 570 | 580 | 590 | 600 |
| GTAVMDLVWD | PFDPHRLAVA | GEDARIRLWR | VPPGGLENVL | TTPETVLTGH | TEKIYSLRFH |
| 610 | 620 | 630 | 640 | 650 | 660 |
| PLAADVLASS | SYDLTVRIWD | LQTGAERLKL | QGHQDQIFSL | AWSPDGKQLA | TVCKDGHVRV |
| 670 | 680 | 690 | 700 | 710 | 720 |
| YEPRSSPLPL | QEGPGPEGGR | GARIVWVCDG | GCLLVSGFDS | RSERQLQLYI | ADALAQGPSA |
| 730 | 740 | 750 | 760 | 770 | 780 |
| LLGLDVAPST | LLPSYDPDTG | LVLLTGKGDT | RVFLYEVLPE | APFFLECNSF | TSPDPHKGFV |
| 790 | 800 | 810 | 820 | 830 | 840 |
| LLPKTECDIQ | DVEFARCLRL | RQTSLEPVAF | RLPRVRKEFF | QDDVFPDTAV | TWEPALSAKA |
| 850 | 860 | 870 | 880 | 890 | 900 |
| WFEGANGQPR | LLSLQPPGMT | PVSQAPREVP | ARRAPSSAQY | LEEKSDQQKK | EELLNAMVAK |
| 910 | 920 | ||||
| LGNREDPLPQ | DSFEGVDEDE | WD |