Descriptions
Autoinhibitory domains (AIDs)
Target domain |
299-346 (vinculin-binding site within the MI region) |
Relief mechanism |
Others |
Assay |
|
Target domain |
675-865 (F-actin binding domain) |
Relief mechanism |
Partner binding |
Assay |
|
Accessory elements
No accessory elements
References
- 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
- 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
- Yeon JH et al. (2016) "Systems-wide Identification of cis-Regulatory Elements in Proteins", Cell systems, 2, 89-100
- 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

4 structures for P90947
Entry ID | Method | Resolution | Chain | Position | Source |
---|---|---|---|---|---|
5H5M | X-ray | 240 A | A/B | 267-646 | PDB |
5XA5 | X-ray | 160 A | A | 2-275 | PDB |
7UUW | EM | 336 A | G/H/I/K/L/Z | 677-927 | PDB |
AF-P90947-F1 | Predicted | AlphaFoldDB |
No variants for P90947
Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
---|---|---|---|---|---|
No variants for P90947 |
No associated diseases with P90947
4 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. |
apical junction complex | A functional unit located near the cell apex at the points of contact between epithelial cells, which in vertebrates is composed of the tight junction, the zonula adherens, and desmosomes and in some invertebrates, such as Drosophila, is composed of the subapical complex (SAC), the zonula adherens and the septate junction. Functions in the regulation of cell polarity, tissue integrity and intercellular adhesion and permeability. |
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. |
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. |
beta-catenin binding | Binding to a catenin beta subunit. |
cadherin binding | Binding to cadherin, a type I membrane protein involved in cell adhesion. |
8 GO annotations of biological process
Name | Definition |
---|---|
cell migration | The controlled self-propelled movement of a cell from one site to a destination guided by molecular cues. |
cell migration involved in gastrulation | The migration of individual cells within the blastocyst to help establish the multi-layered body plan of the organism (gastrulation). For example, the migration of cells from the surface to the interior of the embryo (ingression). |
cell-cell adhesion | The attachment of one cell to another cell via adhesion molecules. |
cell-cell adhesion mediated by cadherin | The attachment of one cell to another cell via a cadherin, transmembrane proteins having repeating extracellular calcium ion binding domains. |
cortical actin cytoskeleton organization | A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of actin-based cytoskeletal structures in the cell cortex, i.e. just beneath the plasma membrane. |
embryonic body morphogenesis | The process in which the anatomical structures of the embryonic soma are generated and organized. |
regulation of actin cytoskeleton organization | Any process that modulates the frequency, rate or extent of the formation, arrangement of constituent parts, or disassembly of cytoskeletal structures comprising actin filaments and their associated proteins. |
regulation of protein localization | Any process that modulates the frequency, rate or extent of any process in which a protein is transported to, or maintained in, a specific location. |
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 |
P30997 | CTNNA2 | Catenin alpha-2 | Gallus gallus (Chicken) | SS |
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 |
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 |
MPANGNSHAY | FNIDEVRSKN | VLKQITQLIN | EVTNITETFP | LKPGQTTEGL | VATLDAAVAN |
70 | 80 | 90 | 100 | 110 | 120 |
FLQTGSFAIS | KCPIANSDPR | AIDLLHEALG | AVQDTGQVMI | QTGRDFVRDS | TSTNKRAIAT |
130 | 140 | 150 | 160 | 170 | 180 |
NSGRNLLTAV | AKFLILADSI | DVKVIVDKVD | EVRETAHQMI | EADTKIKVDD | LYNLLISQIE |
190 | 200 | 210 | 220 | 230 | 240 |
ELDITVRRRA | IDLVKPNQRD | DLLAARSALR | QTAPLLYTST | RTFVRHPEHE | EARRNRDYTA |
250 | 260 | 270 | 280 | 290 | 300 |
DEMHSALNAL | ESVLNGQQPK | VTFSEYGRIG | DLINEIDTFQ | NRIEIDPAHY | RRGTDRPDLE |
310 | 320 | 330 | 340 | 350 | 360 |
GHCERIVSGS | ASIADAESTR | ENRKQKIVAE | CNNLRQALQE | LLTEYEKSTG | RRDDNDDIPL |
370 | 380 | 390 | 400 | 410 | 420 |
GIAEVHKRTK | DLRRHLRRAI | VDHISDAFLD | TRTPLILLIE | AAKEGHEENT | RYRSKMFQEH |
430 | 440 | 450 | 460 | 470 | 480 |
ANEIVSVARL | SCQLSSDVES | VSVIQHTAAQ | LEKLAPQVAQ | AAILLCHQPT | SKTAQENMET |
490 | 500 | 510 | 520 | 530 | 540 |
YKNAWFDKVR | LLTTALDNIT | TLDDFLAVSE | AHIVEDCERG | IKGITANAST | PDENAANCET |
550 | 560 | 570 | 580 | 590 | 600 |
VDCAAGSIRG | RALRVCDVVD | AEMDFLQNSE | YTETVKQAVR | ILKTQRVDQF | AERASALANR |
610 | 620 | 630 | 640 | 650 | 660 |
QEAHGLTWDP | KTKEEEMNEF | INACTLVHDA | VKDIRHALLM | NRSMNDVDSD | VEYEADGVGA |
670 | 680 | 690 | 700 | 710 | 720 |
ANADANRTIS | EQENQQNLMR | RLPEEEKKKI | QAQIDIFKVT | QTRFEREVAK | WDETGNDIIS |
730 | 740 | 750 | 760 | 770 | 780 |
LANNMCKIMM | SMTEFTRGCG | PLKTTMDVIR | AAQEISLNGS | KLNALARQIG | EESADSQTKK |
790 | 800 | 810 | 820 | 830 | 840 |
DLLAYLSQIT | LYCQQLNICS | KVKADVTQVG | NELVVSALDS | AMSLIQTARN | LLTAVVQTVK |
850 | 860 | 870 | 880 | 890 | 900 |
AAYIASTKFR | RPNANSVRVE | WRMAPPKKQP | LIRPQKNNAI | IRRASERRPL | QPAKVLAEFT |
910 | 920 | ||||
RNEIETGRDS | DDEELDRRHQ | QRINGRL |