P30997
SS
Gene name |
CTNNA2 |
Protein name |
Catenin alpha-2 |
Names |
Alpha N-catenin , Neural alpha-catenin |
Species |
Gallus gallus (Chicken) |
KEGG Pathway |
gga:396035 |
EC number |
|
Protein Class |
|
Descriptions
Catenin alpha-3 (Ctnna3, αT-catenin) functions as a crucial molecular bridge, connecting cadherin proteins to the actin cytoskeleton and ensuring the integrity of cell-cell adhesion. In contrast to Ctnna1, the αT-catenin N-terminus is required to maintain the middle (M)-region autoinhibition and modulate vinculin binding. The steric, nonspecific interactions between the αT-catenin N-terminus and M-region promote MI folding and M-region autoinhibition. Actin binding relieves the autoinhibition, which is tension-dependent.
Autoinhibitory domains (AIDs)
Target domain |
262-630 (Middle region) |
Relief mechanism |
Others |
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
- Heier JA et al. (2021) "Distinct intramolecular interactions regulate autoinhibition of vinculin binding in αT-catenin and αE-catenin", The Journal of biological chemistry, 296, 100582
- Ishiyama N et al. (2013) "An autoinhibited structure of α-catenin and its implications for vinculin recruitment to adherens junctions", The Journal of biological chemistry, 288, 15913-25
- Hirano Y et al. (2018) "The force-sensing device region of α-catenin is an intrinsically disordered segment in the absence of intramolecular stabilization of the autoinhibitory form", Genes to cells : devoted to molecular & cellular mechanisms, 23, 370-385
- Choi HJ et al. (2012) "αE-catenin is an autoinhibited molecule that coactivates vinculin", Proceedings of the National Academy of Sciences of the United States of America, 109, 8576-81
- Rangarajan ES et al. (2023) "Distinct inter-domain interactions of dimeric versus monomeric α-catenin link cell junctions to filaments", Communications biology, 6, 276
- Barrick S et al. (2018) "Salt bridges gate α-catenin activation at intercellular junctions", Molecular biology of the cell, 29, 111-122
- Li J et al. (2015) "Structural Determinants of the Mechanical Stability of α-Catenin", The Journal of biological chemistry, 290, 18890-903
Autoinhibited structure
Activated structure
1 structures for P30997
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P30997-F1 | Predicted | AlphaFoldDB |
No variants for P30997
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P30997 | |||||
2 associated diseases with P30997
[MIM: 614893]: Immunodeficiency 32A (IMD32A)
An immunologic disorder characterized by abnormal peripheral blood myeloid phenotype with a marked loss of CD11C-positive/CD1C dendritic cells, resulting in selective susceptibility to mycobacterial infections. {ECO:0000269|PubMed:21524210}. Note=The disease is caused by variants affecting the gene represented in this entry.
[MIM: 226990]: Immunodeficiency 32B (IMD32B)
An autosomal recessive primary immunodeficiency characterized by monocyte and dendritic cell deficiency, myeloproliferation, and susceptibility to severe opportunistic infections, including disseminated BCG infection and oral candidiasis. {ECO:0000269|PubMed:21524210, ECO:0000269|PubMed:25122610}. Note=The disease is caused by variants affecting the gene represented in this entry.
Without disease ID
- An immunologic disorder characterized by abnormal peripheral blood myeloid phenotype with a marked loss of CD11C-positive/CD1C dendritic cells, resulting in selective susceptibility to mycobacterial infections. {ECO:0000269|PubMed:21524210}. Note=The disease is caused by variants affecting the gene represented in this entry.
- An autosomal recessive primary immunodeficiency characterized by monocyte and dendritic cell deficiency, myeloproliferation, and susceptibility to severe opportunistic infections, including disseminated BCG infection and oral candidiasis. {ECO:0000269|PubMed:21524210, ECO:0000269|PubMed:25122610}. Note=The disease is caused by variants affecting the gene represented in this entry.
5 regional properties for P30997
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Ras-associating domain | 779 - 866 | IPR000159 |
| domain | Ras-like guanine nucleotide exchange factor, N-terminal | 111 - 239 | IPR000651 |
| domain | Ras guanine-nucleotide exchange factors catalytic domain | 363 - 630 | IPR001895 |
| domain | Ral guanine nucleotide dissociation stimulator, RA domain | 779 - 864 | IPR015758 |
| conserved_site | Ras guanine-nucleotide exchange factor, conserved site | 545 - 575 | IPR019804 |
Functions
8 GO annotations of cellular component
| Name | Definition |
|---|---|
| actin cytoskeleton | The part of the cytoskeleton (the internal framework of a cell) composed of actin and associated proteins. Includes actin cytoskeleton-associated complexes. |
| 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. |
| axon | The long process of a neuron that conducts nerve impulses, usually away from the cell body to the terminals and varicosities, which are sites of storage and release of neurotransmitter. |
| catenin complex | Complex of peripheral cytoplasmic proteins (alpha-, beta- and gamma-catenin) that interact with the cytoplasmic region of uvomorulin/E-cadherin to connect it to the actin cytoskeleton. |
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| 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. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
4 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. |
| beta-catenin binding | Binding to a catenin beta subunit. |
| cadherin binding | Binding to cadherin, a type I membrane protein involved in cell adhesion. |
| structural molecule activity | The action of a molecule that contributes to the structural integrity of a complex. |
10 GO annotations of biological process
| Name | Definition |
|---|---|
| axonogenesis | De novo generation of a long process of a neuron, including the terminal branched region. Refers to the morphogenesis or creation of shape or form of the developing axon, which carries efferent (outgoing) action potentials from the cell body towards target cells. |
| brain morphogenesis | The process in which the anatomical structures of the brain are generated and organized. The brain is one of the two components of the central nervous system and is the center of thought and emotion. It is responsible for the coordination and control of bodily activities and the interpretation of information from the senses (sight, hearing, smell, etc.). |
| cell migration | The controlled self-propelled movement of a cell from one site to a destination guided by molecular cues. |
| cell-cell adhesion | The attachment of one cell to another cell via adhesion molecules. |
| dendrite morphogenesis | The process in which the anatomical structures of a dendrite are generated and organized. |
| epithelial cell differentiation | The process in which a relatively unspecialized cell acquires specialized features of an epithelial cell, any of the cells making up an epithelium. |
| neural crest cell migration | The characteristic movement of cells from the dorsal ridge of the neural tube to a variety of locations in a vertebrate embryo. |
| protein localization | Any process in which a protein is transported to, or maintained in, a specific location. |
| regulation of synapse structural plasticity | Any process that modulates the frequency, rate or extent of synapse structural plasticity. Synapse structural plasticity is a type of cytoskeletal remodeling; this remodeling is induced by stimuli that can lead to long term potentiation and it can be activity-dependent or -independent. Examples of cytoskeletal changes include the formation of new spines and increase in spine size; this can be accompanied by the insertion of greater numbers of glutamate (or other neurotransmitter) receptors into the post-synaptic membrane. |
| trigeminal ganglion formation | The process that gives rise to the trigeminal ganglion. This process pertains to the initial formation of a structure from unspecified parts. |
16 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q3MHM6 | CTNNA1 | Catenin alpha-1 | Bos taurus (Bovine) | SS |
| P12003 | VCL | Vinculin | Gallus gallus (Chicken) | EV |
| P35220 | alpha-Cat | Catenin alpha | Drosophila melanogaster (Fruit fly) | SS |
| P18206 | VCL | Vinculin | Homo sapiens (Human) | SS |
| P35221 | CTNNA1 | Catenin alpha-1 | Homo sapiens (Human) | EV |
| Q9UI47 | CTNNA3 | Catenin alpha-3 | Homo sapiens (Human) | SS |
| P26232 | CTNNA2 | Catenin alpha-2 | Homo sapiens (Human) | SS |
| Q64727 | Vcl | Vinculin | Mus musculus (Mouse) | SS |
| P26231 | Ctnna1 | Catenin alpha-1 | Mus musculus (Mouse) | EV |
| Q65CL1 | Ctnna3 | Catenin alpha-3 | Mus musculus (Mouse) | EV |
| Q61301 | Ctnna2 | Catenin alpha-2 | Mus musculus (Mouse) | EV |
| P26234 | VCL | Vinculin | Sus scrofa (Pig) | SS |
| P85972 | Vcl | Vinculin | Rattus norvegicus (Rat) | SS |
| P90947 | hmp-1 | Alpha-catenin-like protein hmp-1 | Caenorhabditis elegans | SS |
| A4IGI7 | ctnna2 | Catenin alpha-2 | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) | SS |
| B7ZC77 | Ctnna2 | Catenin alpha-2 | Danio rerio (Zebrafish) (Brachydanio rerio) | SS |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MTSATSPIIL | KWDPKSLEIR | TLTVERLLEP | LVTQVTTLVN | TSNKGPSGKK | KGRSKKAHVL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| AASVEQATQN | FLEKGDQIAK | ESQDLKEELV | AAVEDVRKQG | ETMRIASSEF | ADDPCSSVKR |
| 130 | 140 | 150 | 160 | 170 | 180 |
| GTMVRAARAL | LSAVTRLLIL | ADMADVMRLL | SHLKIVEEAL | EAVKNATNEQ | DLANRFKEFG |
| 190 | 200 | 210 | 220 | 230 | 240 |
| KEMVKLNYVA | ARRQQELKDP | HCRDEMAAAR | GALKKNATML | YTASQAFLRH | PDVAATRANR |
| 250 | 260 | 270 | 280 | 290 | 300 |
| DYVFKQVQEA | IAGISNAAQA | TSPTDENKGH | TGIGELAAAL | NEFDNKIILD | PMTFSEARFR |
| 310 | 320 | 330 | 340 | 350 | 360 |
| PSLEERLESI | ISGAALMADS | SCTRDDRRKR | IVAECKRAVR | QALQDLLSEY | MNNTGRKEKG |
| 370 | 380 | 390 | 400 | 410 | 420 |
| DPLNIAIDKM | TKKTRDLRRQ | LRKAVMDHIS | DSFLETNVPL | LVLIEAAKSG | NEKEVKEYAQ |
| 430 | 440 | 450 | 460 | 470 | 480 |
| VFREHANKLV | EVANLACSIS | NNEEGVKLVR | MAATQIDSLC | PQVINAALTL | AARPQSKVAQ |
| 490 | 500 | 510 | 520 | 530 | 540 |
| DNMDVFKDQW | EKQVRVLTEA | VDDITSVDDF | LSVSENHILE | DVNKCVIALQ | EGDVDTLDRT |
| 550 | 560 | 570 | 580 | 590 | 600 |
| AGAIRGRAAR | VIHIINAEME | NYETGVYTEK | VLEATKLLSE | TVMPRFAEQV | EVAIEALSAN |
| 610 | 620 | 630 | 640 | 650 | 660 |
| VPQPFEENEF | IDASRLVYDG | VRDIRKAVLM | IRTPEELEDD | SDFEQEDYDV | RSRTSVQTED |
| 670 | 680 | 690 | 700 | 710 | 720 |
| DQLIAGQSAR | AIMAQLPQEE | KAKIAEQVEI | FHQEKSKLDA | EVAKWDDSGN | DIIVLAKQMC |
| 730 | 740 | 750 | 760 | 770 | 780 |
| MIMMEMTDFT | RGKGPLKNTS | DVINAAKKIA | EAGSRMDKLA | RAVADQCPDS | ACKQDLLAYL |
| 790 | 800 | 810 | 820 | 830 | 840 |
| QRIALYCHQL | NICSKVKAEV | QNLGGELIVS | GLDSATSLIQ | AAKNLMNAVV | LTVKASYVAS |
| 850 | 860 | 870 | 880 | 890 | 900 |
| TKYQKVYGTA | AVNSPVVSWK | MKAPEKKPLV | KREKPEEYQT | RVRRGSQKKH | ISPVQALSEF |
| KAMDSF |