Q5R664
Gene name |
COPB2 |
Protein name |
Coatomer subunit beta' |
Names |
Beta'-coat protein, Beta'-COP |
Species |
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) |
KEGG Pathway |
pon:100173601 |
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 Q5R664
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q5R664-F1 | Predicted | AlphaFoldDB |
No variants for Q5R664
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q5R664 | |||||
No associated diseases with Q5R664
7 regional properties for Q5R664
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| repeat | WD40 repeat | 4 - 85 | IPR001680-1 |
| repeat | WD40 repeat | 88 - 127 | IPR001680-2 |
| repeat | WD40 repeat | 131 - 266 | IPR001680-3 |
| domain | Coatomer, WD associated region | 319 - 762 | IPR006692 |
| repeat | G-protein beta WD-40 repeat | 158 - 172 | IPR020472-1 |
| repeat | G-protein beta WD-40 repeat | 202 - 216 | IPR020472-2 |
| repeat | G-protein beta WD-40 repeat | 244 - 258 | IPR020472-3 |
Functions
4 GO annotations of cellular component
| Name | Definition |
|---|---|
| COPI-coated vesicle membrane | The lipid bilayer surrounding a COPI-coated vesicle. |
| 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. |
| membrane coat | Any of several different proteinaceous coats that can associate with membranes. Membrane coats include those formed by clathrin plus an adaptor complex, the COPI and COPII complexes, and possibly others. They are found associated with membranes on many vesicles as well as other membrane features such as pits and perhaps tubules. |
1 GO annotations of molecular function
| Name | Definition |
|---|---|
| structural molecule activity | The action of a molecule that contributes to the structural integrity of a complex or its assembly within or outside a cell. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| intracellular protein transport | The directed movement of proteins in a cell, including the movement of proteins between specific compartments or structures within a cell, such as organelles of a eukaryotic cell. |
| vesicle-mediated transport | A cellular transport process in which transported substances are moved in membrane-bounded vesicles; transported substances are enclosed in the vesicle lumen or located in the vesicle membrane. The process begins with a step that directs a substance to the forming vesicle, and includes vesicle budding and coating. Vesicles are then targeted to, and fuse with, an acceptor membrane. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MPLRLDIKRK | LTARSDRVKS | VDLHPTEPWM | LASLYNGSVC | VWNHETQTLV | KTFEVCDLPV |
| 70 | 80 | 90 | 100 | 110 | 120 |
| RAAKFVARKN | WVVTGADDMQ | IRVFNYNTLE | RVHMFEAHSD | YIRCIAVHPT | QPFILTSSDD |
| 130 | 140 | 150 | 160 | 170 | 180 |
| MLIKLWDWDK | KWSCSQVFEG | HTHYVMQIVI | NPKDNNQFAS | ASLDRTIKVW | QLGSSSPNFT |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LEGHEKGVNC | IDYYSGGDKP | YLISGADDRL | VKIWDYQNKT | CVQTLEGHAQ | NVSCASFHPE |
| 250 | 260 | 270 | 280 | 290 | 300 |
| LPIIITGSED | GTVRIWHSST | YRLESTLNYG | MERVWCVASL | RGSNNVALGY | DEGSIIVKLG |
| 310 | 320 | 330 | 340 | 350 | 360 |
| REEPAMSMDA | NGKIIWAKHS | EVQQANLKAM | GDAEIKDGER | LPLAVKDMGS | CEIYPQTIQH |
| 370 | 380 | 390 | 400 | 410 | 420 |
| NPNGRFVVVC | GDGEYIIYTA | MALRNKSFGS | AQEFAWAHDS | SEYAIRESNS | IVKIFKNFKE |
| 430 | 440 | 450 | 460 | 470 | 480 |
| KKSFKPDFGA | ESIYGGFLLG | VRSVNGLAFY | DWDNTELIRR | IEIQPKHIFW | SDSGELVCIA |
| 490 | 500 | 510 | 520 | 530 | 540 |
| TEESFFILKY | LSEKVLAVQE | THEGVTEDGI | EDAFEVLGEI | QEIVKTGLWV | GDCFIYTSSV |
| 550 | 560 | 570 | 580 | 590 | 600 |
| NRLNYYVGGE | IVTIAHLDRT | MYLLGYIPKD | NRLYLGDKEL | NIVSYSLLVS | VLEYQTAVMR |
| 610 | 620 | 630 | 640 | 650 | 660 |
| RDFSMADKVL | PTIPKEQRTR | VAHFLEKQGF | KQQALTVSTD | PEHRFELALQ | LGELKIAYQL |
| 670 | 680 | 690 | 700 | 710 | 720 |
| AVEAESEQKW | KQLAELAISK | CQFGLAQECL | HHAQDYGGLL | LLATASGNAN | MVNKLAEGAE |
| 730 | 740 | 750 | 760 | 770 | 780 |
| RDGKNNVAFM | SYFLQGKVDA | CLELLIRTGR | LPEAAFLART | YLPSQVSRVV | KLWRENLSKV |
| 790 | 800 | 810 | 820 | 830 | 840 |
| NQKAAESLAD | PTEYENLFPG | LKEAFVVEEW | VKETHAELWP | AKQYPLVTPN | EERNVMEEAK |
| 850 | 860 | 870 | 880 | 890 | 900 |
| GFQPSRSTAQ | QELDGKPASP | TPVIVASHTA | NKEEKSLLEL | EVDLDNLELV | DIDTTDINLD |
| EDILDD |