Q5RAB8
Gene name |
FARP1 |
Protein name |
FERM, ARHGEF and pleckstrin domain-containing protein 1 |
Names |
FERM, RhoGEF and pleckstrin domain-containing protein 1 |
Species |
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) |
KEGG Pathway |
pon:100172691 |
EC number |
|
Protein Class |
|
Descriptions
Autoinhibitory domains (AIDs)
Target domain |
540-730 (DH domain) |
Relief mechanism |
PTM |
Assay |
|
Target domain |
540-730 (DH domain) |
Relief mechanism |
PTM |
Assay |
|
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for Q5RAB8
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q5RAB8-F1 | Predicted | AlphaFoldDB |
No variants for Q5RAB8
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q5RAB8 | |||||
No associated diseases with Q5RAB8
11 regional properties for Q5RAB8
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Dbl homology (DH) domain | 540 - 730 | IPR000219 |
| domain | FERM domain | 40 - 320 | IPR000299 |
| domain | Pleckstrin homology domain | 759 - 858 | IPR001849-1 |
| domain | Pleckstrin homology domain | 932 - 1031 | IPR001849-2 |
| domain | FERM adjacent | 328 - 374 | IPR014847 |
| domain | FERM, N-terminal | 44 - 106 | IPR018979 |
| domain | FERM, C-terminal PH-like domain | 234 - 324 | IPR018980 |
| conserved_site | FERM conserved site | 94 - 123 | IPR019747 |
| domain | FERM central domain | 125 - 230 | IPR019748 |
| domain | Band 4.1 domain | 36 - 230 | IPR019749 |
| domain | FARP1/FARP2/FRMD7, FERM domain C-lobe | 217 - 337 | IPR041788 |
Functions
6 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoskeleton | A cellular structure that forms the internal framework of eukaryotic and prokaryotic 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. |
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| dendrite | A neuron projection that has a short, tapering, morphology. Dendrites receive and integrate signals from other neurons or from sensory stimuli, and conduct nerve impulses towards the axon or the cell body. In most neurons, the impulse is conveyed from dendrites to axon via the cell body, but in some types of unipolar neuron, the impulse does not travel via the cell body. |
| dendritic spine | A small, membranous protrusion from a dendrite that forms a postsynaptic compartment, typically receiving input from a single presynapse. They function as partially isolated biochemical and an electrical compartments. Spine morphology is variable:they can be thin, stubby, mushroom, or branched, with a continuum of intermediate morphologies. They typically terminate in a bulb shape, linked to the dendritic shaft by a restriction. Spine remodeling is though to be involved in synaptic plasticity. |
| extrinsic component of cytoplasmic side of plasma membrane | The component of a plasma membrane consisting of gene products and protein complexes that are loosely bound to its cytoplasmic surface, but not integrated into the hydrophobic region. |
| filopodium | Thin, stiff, actin-based protrusion extended by the leading edge of a motile cell such as a crawling fibroblast or amoeba, or an axonal or dendritic growth cone, or a dendritic shaft. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| cytoskeletal protein binding | Binding to a protein component of a cytoskeleton (actin, microtubule, or intermediate filament cytoskeleton). |
| guanyl-nucleotide exchange factor activity | Stimulates the exchange of GDP to GTP on a signaling GTPase, changing its conformation to its active form. Guanine nucleotide exchange factors (GEFs) act by stimulating the release of guanosine diphosphate (GDP) to allow binding of guanosine triphosphate (GTP), which is more abundant in the cell under normal cellular physiological conditions. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| dendrite morphogenesis | The process in which the anatomical structures of a dendrite are generated and organized. |
| synapse assembly | The aggregation, arrangement and bonding together of a set of components to form a synapse. This process ends when the synapse is mature (functional). |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MGEIEQRPTP | GSRLGAPENS | GISTLERGQK | PPPTPSGKLV | SIKIQMLDDT | QEAFEVPQRA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| PGKVLLDAVC | NHLNLVEGDY | FGLECPDHKK | ITVWLDLLKP | LVKQIRRPKH | VVVKFVVKFF |
| 130 | 140 | 150 | 160 | 170 | 180 |
| PPDHTQLQEE | LTRYLFALQV | KQDLAQGRLT | CNDTSAALLI | SHIVQSEIGD | FDEALDREHL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| AKNKYIPQQD | ALEDKIVEFH | HNHIGQTPAE | SDFQLLEIAR | RLEMYGIRLH | PAKDREGTKI |
| 250 | 260 | 270 | 280 | 290 | 300 |
| NLAVANTGIL | VFQGFTKINA | FNWAKVRKLS | FKRKRFLIKL | RPDANSAYQD | TLEFLMASRD |
| 310 | 320 | 330 | 340 | 350 | 360 |
| FCKSFWKICV | EHHAFFRLFE | EPKPKPKPVL | FSRGSSFRFS | GRTQKQVLDY | VKEGGHKKVQ |
| 370 | 380 | 390 | 400 | 410 | 420 |
| FERKHSKIHS | IRSLASQPTE | LYSEVLEQSQ | QSASLTFGEG | AESPGGQSCQ | QGKEPKVSPG |
| 430 | 440 | 450 | 460 | 470 | 480 |
| EPGSHPSPVP | RRSPAGNKQA | DGAASAPTEE | EEEVVKDRTQ | QSKPQPPQPS | TGSLTGSPHL |
| 490 | 500 | 510 | 520 | 530 | 540 |
| SELSVNSQGG | VAPANVTLSP | NLSPDTKQAS | PLISPLLNDQ | ACPRTDDEDE | GRRKRFPTDK |
| 550 | 560 | 570 | 580 | 590 | 600 |
| AYFIAKEVST | TERTYLKDLE | VITSWFQSAV | SKEDAMPEAL | KSLIFPNFEP | LHKFHTNFLK |
| 610 | 620 | 630 | 640 | 650 | 660 |
| EIEQRLALWE | GRSNAQIRDY | QRIGDVMLKN | IQGMKHLAVH | LWKHSEALEA | LENGIKSSRR |
| 670 | 680 | 690 | 700 | 710 | 720 |
| LENFCRDFEL | QKVCYLPLNT | FLLRPLHRHM | HYKQVLERLC | KHHPPSHADF | RDCRAALAGI |
| 730 | 740 | 750 | 760 | 770 | 780 |
| TEMVAQLHGT | MIKMENFQKL | HELKKDLIGI | DNLVVPGREF | IRLGSLSKLS | GKGLQQRMFF |
| 790 | 800 | 810 | 820 | 830 | 840 |
| LFNDVLLYTS | RGLTASNQFK | VHGQLPLYGM | TIKESEDEWG | VPHCLTLRGQ | RQSIIVAASS |
| 850 | 860 | 870 | 880 | 890 | 900 |
| RSEMEKWVED | IQMAIDLAEK | NSSLAPEFLA | SSPPDNKSPD | EATAADQESE | DDLSASRTSL |
| 910 | 920 | 930 | 940 | 950 | 960 |
| ERQAPHRGNT | MVHVCWHRNT | SVSMVDFSVA | VENQLSGNLL | RKFKNSNGWQ | KLWVVFTNFC |
| 970 | 980 | 990 | 1000 | 1010 | 1020 |
| LFFYKSHQDN | HPLASLPLLG | YSLTIPTESE | NIHKDYVFKL | HFKSHVYYFR | AESEYTFERW |
| 1030 | 1040 | ||||
| MEVIRSATSS | ASRVHVSSHK | ESLVY |