P97694
Gene name |
Cyth1 (Pscd1, Sec7a) |
Protein name |
Cytohesin-1 |
Names |
PH, SEC7 and coiled-coil domain-containing protein 1 , SEC7 homolog A , rSec7-1 |
Species |
Rattus norvegicus (Rat) |
KEGG Pathway |
rno:116691 |
EC number |
|
Protein Class |
|
Descriptions
Autoinhibitory domains (AIDs)
Target domain |
59-247 (Sec7 domain) |
Relief mechanism |
Partner binding |
Assay |
|
Target domain |
59-247 (Sec7 domain) |
Relief mechanism |
Partner binding |
Assay |
|
Accessory elements
No accessory elements
References
- Yeon JH et al. (2016) "Systems-wide Identification of cis-Regulatory Elements in Proteins", Cell systems, 2, 89-100
- Malaby AW et al. (2013) "Structural basis for membrane recruitment and allosteric activation of cytohesin family Arf GTPase exchange factors", Proceedings of the National Academy of Sciences of the United States of America, 110, 14213-8
- DiNitto JP et al. (2007) "Structural basis and mechanism of autoregulation in 3-phosphoinositide-dependent Grp1 family Arf GTPase exchange factors", Molecular cell, 28, 569-83
Autoinhibited structure
Activated structure
1 structures for P97694
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P97694-F1 | Predicted | AlphaFoldDB |
No variants for P97694
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P97694 | |||||
No associated diseases with P97694
Functions
8 GO annotations of cellular component
| Name | Definition |
|---|---|
| adherens junction | A cell-cell junction composed of the epithelial cadherin-catenin complex. The epithelial cadherins, or E-cadherins, of each interacting cell extend through the plasma membrane into the extracellular space and bind to each other. The E-cadherins bind to catenins on the cytoplasmic side of the membrane, where the E-cadherin-catenin complex binds to cytoskeletal components and regulatory and signaling molecules. |
| bicellular tight junction | An occluding cell-cell junction that is composed of a branching network of sealing strands that completely encircles the apical end of each cell in an epithelial sheet; the outer leaflets of the two interacting plasma membranes are seen to be tightly apposed where sealing strands are present. Each sealing strand is composed of a long row of transmembrane adhesion proteins embedded in each of the two interacting plasma membranes. |
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| cytoplasmic side of plasma membrane | The leaflet the plasma membrane that faces the cytoplasm and any proteins embedded or anchored in it or attached to its surface. |
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| extrinsic component of presynaptic membrane | The component of the presynaptic membrane consisting of gene products and protein complexes that are loosely bound to one of its surfaces, but not integrated into the hydrophobic region. |
| neuromuscular junction | The junction between the axon of a motor neuron and a muscle fiber. In response to the arrival of action potentials, the presynaptic button releases molecules of neurotransmitters into the synaptic cleft. These diffuse across the cleft and transmit the signal to the postsynaptic membrane of the muscle fiber, leading to a change in post-synaptic potential. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| 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. |
| lipid binding | Binding to a lipid. |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| establishment of epithelial cell polarity | The specification and formation of anisotropic intracellular organization of an epithelial cell. |
| presynaptic modulation of chemical synaptic transmission | Any process, acting in the presynapse that results in modulation of chemical synaptic transmission. |
| regulation of ARF protein signal transduction | Any process that modulates the frequency, rate or extent of ARF protein signal transduction. |
| regulation of cell adhesion | Any process that modulates the frequency, rate or extent of attachment of a cell to another cell or to the extracellular matrix. |
15 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q2KI41 | CYTH2 | Cytohesin-2 | Bos taurus (Bovine) | SS |
| Q9UIA0 | CYTH4 | Cytohesin-4 | Homo sapiens (Human) | SS |
| O43739 | CYTH3 | Cytohesin-3 | Homo sapiens (Human) | EV |
| Q99418 | CYTH2 | Cytohesin-2 | Homo sapiens (Human) | SS |
| Q15438 | CYTH1 | Cytohesin-1 | Homo sapiens (Human) | SS |
| Q80YW0 | Cyth4 | Cytohesin-4 | Mus musculus (Mouse) | SS |
| P63034 | Cyth2 | Cytohesin-2 | Mus musculus (Mouse) | SS |
| O08967 | Cyth3 | Cytohesin-3 | Mus musculus (Mouse) | EV |
| Q9QX11 | Cyth1 | Cytohesin-1 | Mus musculus (Mouse) | SS |
| P63035 | Cyth2 | Cytohesin-2 | Rattus norvegicus (Rat) | SS |
| P97696 | Cyth3 | Cytohesin-3 | Rattus norvegicus (Rat) | SS |
| D4A631 | Arfgef1 | Brefeldin A-inhibited guanine nucleotide-exchange protein 1 | Rattus norvegicus (Rat) | PR |
| Q7TSU1 | Arfgef2 | Brefeldin A-inhibited guanine nucleotide-exchange protein 2 | Rattus norvegicus (Rat) | PR |
| Q76M68 | Iqsec3 | IQ motif and SEC7 domain-containing protein 3 | Rattus norvegicus (Rat) | SS |
| A0A0G2JUG7 | Iqsec1 | IQ motif and SEC7 domain-containing protein 1 | Rattus norvegicus (Rat) | SS |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MEDDDSYVPS | DLTAEERQEL | ENIRRRKQEL | LADIQRLKEE | IAEVANEIES | LGSTEERKNM |
| 70 | 80 | 90 | 100 | 110 | 120 |
| QRNKQVAMGR | KKFNMDPKKG | IQFLIENGLL | KNTCEDIAQF | LYKGEGLNKT | AIGDYLGERD |
| 130 | 140 | 150 | 160 | 170 | 180 |
| EFSIQVLHAF | VELHEFTDLN | LVQALRQFLW | SFRLPGEAQK | IDRMMEAFAQ | RYCQCNTGVF |
| 190 | 200 | 210 | 220 | 230 | 240 |
| QSTDTCYVLS | FAIIMLNTSL | HNPNVKDKPT | VERFIAMNRG | INDGGDLPEE | LLRNLYESIK |
| 250 | 260 | 270 | 280 | 290 | 300 |
| NEPFKIPEDD | GNDLTHTFFN | PDREGWLLKL | GGGRVKTWKR | RWFILTDNCL | YYFEYTTDKE |
| 310 | 320 | 330 | 340 | 350 | 360 |
| PRGIIPLENL | SIREVEDSKK | PNCFELYIPD | NKDQVIKACK | TEADGRVVEG | NHTVYRISAP |
| 370 | 380 | 390 | |||
| TPEEKEDWIK | CIKAAISRDP | FYEMLAARKK | KVSSTKRH |