Q04584
Gene name |
ZYX |
Protein name |
Zyxin |
Names |
|
Species |
Gallus gallus (Chicken) |
KEGG Pathway |
gga:418300 |
EC number |
|
Protein Class |
ZYXIN/TRIP6 (PTHR24212) |

Descriptions
Zyxin is a LIM protein found prominently at sites of cell adhesion, faintly in leading lamellipodia, and transiently in cell nuclei. Zyxin displays an N-terminal proline-rich region and three C-terminal LIM domains that provide binding sites for several proteins associated with actin polymerization and intracellular signaling. The head-tail interaction of proline-rich region and LIM domains maintains zyxin in a closed conformation that limits access to binding partners.
Autoinhibitory domains (AIDs)
Target domain |
352-538 (LIM domains) |
Relief mechanism |
PTM, Partner binding |
Assay |
Deletion assay |
Target domain |
100-267 (Proline-rich region) |
Relief mechanism |
PTM, Partner binding |
Assay |
Deletion assay |
Accessory elements
No accessory elements
References
- Hansen MD et al. (2013) "Control of actin dynamics by allosteric regulation of actin binding proteins", International review of cell and molecular biology, 303, 1-25
- Nix DA et al. (2001) "Targeting of zyxin to sites of actin membrane interaction and to the nucleus", The Journal of biological chemistry, 276, 34759-67
- Acevedo LA et al. (2017) "A Noncanonical Binding Site in the EVH1 Domain of Vasodilator-Stimulated Phosphoprotein Regulates Its Interactions with the Proline Rich Region of Zyxin", Biochemistry, 56, 4626-4636
Autoinhibited structure

Activated structure

1 structures for Q04584
Entry ID | Method | Resolution | Chain | Position | Source |
---|---|---|---|---|---|
AF-Q04584-F1 | Predicted | AlphaFoldDB |
18 variants for Q04584
Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
---|---|---|---|---|---|
rs735970241 | 50 | S>L | No | EVA | |
rs737749657 | 50 | S>P | No | EVA | |
rs316602696 | 64 | R>S | No | EVA | |
rs739352340 | 70 | V>G | No | EVA | |
rs3384588466 | 76 | S>P | No | EVA | |
rs740118788 | 193 | T>P | No | EVA | |
rs740309975 | 211 | S>P | No | EVA | |
rs740521552 | 212 | V>A | No | EVA | |
rs733156959 | 217 | S>P | No | EVA | |
rs739466781 | 251 | T>A | No | EVA | |
rs738240054 | 262 | T>P | No | EVA | |
rs730960551 | 272 | R>L | No | EVA | |
rs731129850 | 357 | K>E | No | EVA | |
rs741331885 | 362 | T>P | No | EVA | |
rs734788887 | 363 | Q>P | No | EVA | |
rs732692579 | 376 | E>G | No | EVA | |
463 | D>V | No | |||
rs741644046 | 512 | L>F | No | EVA |
No associated diseases with Q04584
No regional properties for Q04584
Type | Name | Position | InterPro Accession |
---|---|---|---|
No domain, repeats, and functional sites for Q04584 |
Functions
Description | ||
---|---|---|
EC Number | ||
Subcellular Localization |
|
|
PANTHER Family | PTHR24212 | ZYXIN/TRIP6 |
PANTHER Subfamily | PTHR24212:SF1 | ZYXIN |
PANTHER Protein Class |
cytoskeletal protein
actin or actin-binding cytoskeletal protein |
|
PANTHER Pathway Category | No pathway information available |
4 GO annotations of cellular component
Name | Definition |
---|---|
cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
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). |
nucleus | A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. |
stress fiber | A contractile actin filament bundle that consists of short actin filaments with alternating polarity, cross-linked by alpha-actinin and possibly other actin bundling proteins, and with myosin present in a periodic distribution along the fiber. |
2 GO annotations of molecular function
Name | Definition |
---|---|
alpha-actinin binding | Binding to alpha-actinin, one of a family of proteins that cross-link F-actin as antiparallel homodimers. Alpha-actinin has a molecular mass of 93-103 KDa; at the N-terminus there are two calponin homology domains, at the C-terminus there are two EF-hands. These two domains are connected by the rod domain. This domain is formed by triple-helical spectrin repeats. |
metal ion binding | Binding to a metal ion. |
3 GO annotations of biological process
Name | Definition |
---|---|
cell adhesion | The attachment of a cell, either to another cell or to an underlying substrate such as the extracellular matrix, via cell adhesion molecules. |
integrin-mediated signaling pathway | The series of molecular signals initiated by an extracellular ligand binding to an integrin on the surface of a target cell, and ending with the regulation of a downstream cellular process, e.g. transcription. |
transforming growth factor beta receptor signaling pathway | The series of molecular signals initiated by an extracellular ligand binding to a transforming growth factor beta receptor on the surface of a target cell, and ending with the regulation of a downstream cellular process, e.g. transcription. |
4 homologous proteins in AiPD
10 | 20 | 30 | 40 | 50 | 60 |
MASPGTPGTR | MTTTVSINIS | TPSFYNPQKK | FAPVVAPKPK | VNPFKTGGTS | ESSQPQPPGT |
70 | 80 | 90 | 100 | 110 | 120 |
GAQRAQIGRV | GEIPVSVTAE | ELPLPPPPPP | GEELSFSSNC | AFPPPPPPFE | EPFPPAPDEA |
130 | 140 | 150 | 160 | 170 | 180 |
FPSPPPPPPP | MFDEGPALQI | PPGSTGSVEK | PLAPKAHVEI | SSAPRDPTPP | FPSKFTPKPS |
190 | 200 | 210 | 220 | 230 | 240 |
GTLSSKPPGL | DSTPAPAPWA | APQQRKEPLA | SVPPPPSLPS | QPTAKFTPPP | VASSPGSKPG |
250 | 260 | 270 | 280 | 290 | 300 |
ATVPMAPSNS | TRYPTSLQTQ | FTAPSPSGPL | SRPQPPNFTY | AQQWERPQVQ | EKPVPTEKSA |
310 | 320 | 330 | 340 | 350 | 360 |
AVKDMRRPTA | DPPKGNSPLT | MKEVEELELL | TQKLMKDMDH | PPPVEAATSE | LCGFCRKPLS |
370 | 380 | 390 | 400 | 410 | 420 |
RTQPAVRALD | CLFHVECFTC | FKCEKQLQGQ | QFYNVDEKPF | CEDCYAGTLE | KCSVCKQTIT |
430 | 440 | 450 | 460 | 470 | 480 |
DRMLKATGNS | YHPQCFTCVM | CHTPLEGASF | IVDQANQPHC | VDDYHRKYAP | RCSVCSEPIM |
490 | 500 | 510 | 520 | 530 | 540 |
PEPGKDETVR | VVALEKNFHM | KCYKCEDCGR | PLSIEADENG | CFPLDGHVLC | MKCHTVRAKT |
AC |