Q71LX4
Gene name |
Tln2 |
Protein name |
Talin-2 |
Names |
|
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:70549 |
EC number |
|
Protein Class |
FERM DOMAIN CONTAINING PROTEIN (PTHR45858) |
Descriptions
Farp2 is a Dbl-family quinine nucleotide exchange factor (GEF) that contains a 4.1, ezrin, radixin and moesin (FERM) domain, a Dbl-homology (DH) domain and two pleckstrin homology (PH) domains. Farp2 activates Rac1 or Cdc42 in response to upstream signals, thereby regulating neuronal axon guidance and bone homeostasis. The GEF substrate-binding site is blocked collectively by the last helix (Helix α6, 727-745, pseudosubstrate-like interaction) in the DH domain and the two PH domains (760-1025). Helix α6 and PH2 domain each can independently inhibit GEF activity of FARP2, and full activation of FARP2 requires releasing of both these two inhibitory elements. FARP2 activation involves membrane localization, binding of activators and tyrosine phosphorylation.
Autoinhibitory domains (AIDs)
Target domain |
317-406 (Talin head, FERM F3 subdomain) |
Relief mechanism |
Ligand binding, Partner binding |
Assay |
|
Accessory elements
No accessory elements
References
- Goult BT et al. (2009) "The structure of an interdomain complex that regulates talin activity", The Journal of biological chemistry, 284, 15097-106
- Haage A et al. (2020) "Precise coordination of cell-ECM adhesion is essential for efficient melanoblast migration during development", Development (Cambridge, England), 147,
- Song X et al. (2012) "A novel membrane-dependent on/off switch mechanism of talin FERM domain at sites of cell adhesion", Cell research, 22, 1533-45
- Goksoy E et al. (2008) "Structural basis for the autoinhibition of talin in regulating integrin activation", Molecular cell, 31, 124-33
- Zeng Y et al. (2015) "The conformational states of talin autoinhibition complex and its activation under forces", Science China. Life sciences, 58, 694-703
- Kopp PM et al. (2010) "Studies on the morphology and spreading of human endothelial cells define key inter- and intramolecular interactions for talin1", European journal of cell biology, 89, 661-73
- Liao Z et al. (2021) "Optogenetics-based localization of talin to the plasma membrane promotes activation of β3 integrins", The Journal of biological chemistry, 296, 100675
- Zhang H et al. (2016) "Structural and Functional Analysis of a Talin Triple-Domain Module Suggests an Alternative Talin Autoinhibitory Configuration", Structure (London, England : 1993), 24, 721-729
- Dedden D et al. (2019) "The Architecture of Talin1 Reveals an Autoinhibition Mechanism", Cell, 179, 120-131.e13
Autoinhibited structure
Activated structure
2 structures for Q71LX4
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 3G9W | X-ray | 216 A | A/B | 198-408 | PDB |
| AF-Q71LX4-F1 | Predicted | AlphaFoldDB |
No variants for Q71LX4
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q71LX4 | |||||
No associated diseases with Q71LX4
10 regional properties for Q71LX4
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Dbl homology (DH) domain | 538 - 729 | IPR000219 |
| domain | FERM domain | 44 - 324 | IPR000299 |
| domain | Pleckstrin homology domain | 758 - 857 | IPR001849-1 |
| domain | Pleckstrin homology domain | 930 - 1029 | IPR001849-2 |
| domain | FERM adjacent | 332 - 378 | IPR014847 |
| domain | FERM, N-terminal | 48 - 110 | IPR018979 |
| conserved_site | FERM conserved site | 98 - 127 | IPR019747 |
| domain | FERM central domain | 129 - 234 | IPR019748 |
| domain | Band 4.1 domain | 40 - 234 | IPR019749 |
| domain | FARP1/FARP2/FRMD7, FERM domain C-lobe | 221 - 341 | IPR041788 |
Functions
| Description | ||
|---|---|---|
| EC Number | ||
| Subcellular Localization |
|
|
| PANTHER Family | PTHR45858 | FERM DOMAIN CONTAINING PROTEIN |
| PANTHER Subfamily | PTHR45858:SF4 | FERM, ARHGEF AND PLECKSTRIN DOMAIN-CONTAINING PROTEIN 2 |
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
7 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| 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. |
| fascia adherens | A cell-cell junction that contains the transmembrane protein N-cadherin, which interacts with identical molecules from neighbouring cells to form a tight mechanical intercellular link; forms a large portion of the intercalated disc, the structure at which myofibrils terminate in cardiomyocytes. |
| focal adhesion | A cell-substrate junction that anchors the cell to the extracellular matrix and that forms a point of termination of actin filaments. In insects focal adhesion has also been referred to as hemi-adherens junction (HAJ). |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
| ruffle | Projection at the leading edge of a crawling cell; the protrusions are supported by a microfilament meshwork. |
| synapse | The junction between an axon of one neuron and a dendrite of another neuron, a muscle fiber or a glial cell. As the axon approaches the synapse it enlarges into a specialized structure, the presynaptic terminal bouton, which contains mitochondria and synaptic vesicles. At the tip of the terminal bouton is the presynaptic membrane; facing it, and separated from it by a minute cleft (the synaptic cleft) is a specialized area of membrane on the receiving cell, known as the postsynaptic membrane. In response to the arrival of nerve impulses, the presynaptic terminal bouton secretes molecules of neurotransmitters into the synaptic cleft. These diffuse across the cleft and transmit the signal to the postsynaptic membrane. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| actin filament binding | Binding to an actin filament, also known as F-actin, a helical filamentous polymer of globular G-actin subunits. |
| integrin binding | Binding to an integrin. |
| structural constituent of cytoskeleton | The action of a molecule that contributes to the structural integrity of a cytoskeletal structure. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| cell-cell adhesion | The attachment of one cell to another cell via adhesion molecules. |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MGEIEGTYRA | LPTSGTRLGG | QTAIGVSTLE | PEQSLSPRMQ | EKHMRIRVKL | LDSTVELFDI |
| 70 | 80 | 90 | 100 | 110 | 120 |
| EPKCDGQVLL | TQVWKHLNLI | ECDYFGLEFK | NVQSYWIWLE | PMKPIIRQVR | KPKNAVLRLA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| VKFFPPDPGQ | LQEEYTRYLF | ALQLKRDLLE | ERLTCTANTA | ALLISHLLQS | EIGDYDETLD |
| 190 | 200 | 210 | 220 | 230 | 240 |
| REHLKANEYL | PNQEKSLEKI | LDFHQRHTGQ | TPAESDFQVL | EIARKLEMYG | IRFHMASDRE |
| 250 | 260 | 270 | 280 | 290 | 300 |
| GTKINLAVSH | MGVLVFQGTT | KINTFNWSKV | RKLSFKRKRF | LIKLHPEVHG | PYQDTLEFLL |
| 310 | 320 | 330 | 340 | 350 | 360 |
| GSRDECKNFW | KICVEYHTFF | RLSDQPKPKA | KAVFFSRGSS | FRYSGRTQKQ | LVDYVKDGGM |
| 370 | 380 | 390 | 400 | 410 | 420 |
| KRIPYERRHS | KTRTSLHALT | VDLPKQSVSF | TDGLRTSASL | SSANVSFYPP | PSSSLSPPGL |
| 430 | 440 | 450 | 460 | 470 | 480 |
| PNLKDSSSSL | VDPQAPVIKS | TAAERSSGPS | SSDGPSTQSA | HLPGPPVLRP | GPGFSMDSPQ |
| 490 | 500 | 510 | 520 | 530 | 540 |
| PSPSSLKSHL | SLCPELQAAL | STAEQGASPV | LSPVLSGAGT | ARMDNQEEQK | HKHMPEDEAY |
| 550 | 560 | 570 | 580 | 590 | 600 |
| FIAKEILATE | RTYLKDLEVI | TVWFRSVLIK | EEAMPAALMA | LLFSNIDPVY | EFHRGFLHEV |
| 610 | 620 | 630 | 640 | 650 | 660 |
| EQRLALWEGP | SSAHLKGDHQ | RIGDILLRNM | RQLKEFTSYF | QRHDEVLTEL | EKATKHCKKL |
| 670 | 680 | 690 | 700 | 710 | 720 |
| EAVYKEFELQ | KVCYLPLNTF | LLKPVQRLVH | YRLLLSRLCA | HYSPGHRDYA | DCHEALKAIT |
| 730 | 740 | 750 | 760 | 770 | 780 |
| EVTTELQQSL | TRLENLQKLT | ELQRDLVGVE | NLIAPGREFI | REGCLHKLTK | KGLQQRMFFL |
| 790 | 800 | 810 | 820 | 830 | 840 |
| FSDMLLYTSK | SVTGASHFRI | RGFLPLRGML | VEESENEWSV | PHCFTIYAAQ | KTIVVAASTR |
| 850 | 860 | 870 | 880 | 890 | 900 |
| LEKEKWMQDL | NAAIQAAKTI | GDSPPVLLGG | PVYTRTPRSS | DEVSLEESED | GRGNRGSLEG |
| 910 | 920 | 930 | 940 | 950 | 960 |
| NSQHRANTTM | HVCWYRNTSV | SRADHSAAVE | NQLSGYLLRK | FKNSNGWQKL | WVVFTNFCLF |
| 970 | 980 | 990 | 1000 | 1010 | 1020 |
| FYKTHQDDYP | LASLPLLGYS | VSLPREADSI | HKDYVFKLQF | KSHVYFFRAE | SKYTFERWMD |
| 1030 | 1040 | 1050 | 1060 | ||
| VIKRASSSPG | RPPSFTQDCS | HHSPGLEAEI | REKEACPSPC | LDKNL |