P35220
Gene name |
alpha-Cat (CG17947) |
Protein name |
Catenin alpha |
Names |
|
Species |
Drosophila melanogaster (Fruit fly) |
KEGG Pathway |
dme:Dmel_CG17947 |
EC number |
|
Protein Class |
|

Descriptions
Autoinhibitory domains (AIDs)
Target domain |
308-355 (vinculin-binding site within the MI region) |
Relief mechanism |
Others |
Assay |
|
Target domain |
268-634 (Middle region) |
Relief mechanism |
Others |
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

1 structures for P35220
Entry ID | Method | Resolution | Chain | Position | Source |
---|---|---|---|---|---|
AF-P35220-F1 | Predicted | AlphaFoldDB |
No variants for P35220
Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
---|---|---|---|---|---|
No variants for P35220 |
No associated diseases with P35220
1 regional properties for P35220
Type | Name | Position | InterPro Accession |
---|---|---|---|
conserved_site | Vinculin, conserved site | 183 - 203 | IPR000633 |
Functions
5 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. |
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. |
plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
5 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. |
identical protein binding | Binding to an identical protein or proteins. |
structural molecule activity | The action of a molecule that contributes to the structural integrity of a complex. |
7 GO annotations of biological process
Name | Definition |
---|---|
adherens junction assembly | The aggregation, arrangement and bonding together of a set of components to form an adherens junction. An adherens junction is a cell-cell junction composed of the epithelial cadherin-catenin complex at which the cytoplasmic face of the plasma membrane is attached to actin filaments. |
adherens junction organization | A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of an adherens junction. An adherens junction is a cell-cell junction composed of the epithelial cadherin-catenin complex at which the cytoplasmic face of the plasma membrane is attached to actin filaments. |
apical constriction | The actin-mediated process that results in the contraction of the apical end of a polarized columnar epithelial cell. |
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. |
dorsal closure, amnioserosa morphology change | The changes that occur during dorsal closure of the shape and structure of the amnioserosa, an epithelium that occupies the dorsal side of the embryo. |
head morphogenesis | The process in which the anatomical structures of the head are generated and organized. The head is the anterior-most division of the body. |
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 |
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 |
P26231 | Ctnna1 | Catenin alpha-1 | Mus musculus (Mouse) | EV |
Q64727 | Vcl | Vinculin | Mus musculus (Mouse) | SS |
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 |
MLKPDKMGTL | TDFGQIALKW | DPKNLEIRTM | SVEKTLEPLV | LQVTTLVNTK | GPSKKKKGKS |
70 | 80 | 90 | 100 | 110 | 120 |
KRASALVAAV | EKATENFIQK | GEQIAYENPD | ITQEMLTAVD | EVKKTGDAMS | IAAREFSEDP |
130 | 140 | 150 | 160 | 170 | 180 |
CSSLKRGNMV | RAARNLLSAV | TRLLILADMV | DVHLLLKSLH | IVEDDLNKLK | NASSQDELMD |
190 | 200 | 210 | 220 | 230 | 240 |
NMRQFGRNAG | ELIKQAAKRQ | QELKDPQLRD | DLAAARAMLK | KHSTMLLTAS | KVYVRHPELD |
250 | 260 | 270 | 280 | 290 | 300 |
LAKVNRDFIL | KQVCDAVNTI | SDVAQGKSSQ | PTDIYSGAGE | LAAALDDFDE | GIVMDPMTYS |
310 | 320 | 330 | 340 | 350 | 360 |
EKRSRQLLEE | RLESIISAAA | LMADADCTRD | ERRERIVAEC | NAVRQALQDL | LSEYMSNMSQ |
370 | 380 | 390 | 400 | 410 | 420 |
KDNSPGLSRA | IDQMCRKTRD | LRRQLRKAVV | DHVSDSFLET | TTPLLDLIEA | AKSGNEKKVR |
430 | 440 | 450 | 460 | 470 | 480 |
EKSEIFTKHA | EKLVEVANLV | CSMSNNEDGV | KMVRYAAAQI | ESLCPQVINA | ASILTVRPNS |
490 | 500 | 510 | 520 | 530 | 540 |
KVAQENMTTY | RQAWEVQVRI | LTEAVDDITT | IDDFLAVSEN | HILEDVNKCV | MALQVGDARD |
550 | 560 | 570 | 580 | 590 | 600 |
LRATAGAIQG | RSSRVCNVVE | AEMDNYEPCI | YTKRVLEAVK | VLRDQVMMKF | DQRVGAAVGA |
610 | 620 | 630 | 640 | 650 | 660 |
LSNNSNKDVD | ENDFIDASRL | VYDGVREIRR | AVLMNRSSED | LDTDTEFEPV | EDLTLETRSR |
670 | 680 | 690 | 700 | 710 | 720 |
SSAHTGDQTV | DEYPDISGIC | TAREAMRKMT | EEDKQKIAQQ | VELFRREKLT | FDSEVAKWDD |
730 | 740 | 750 | 760 | 770 | 780 |
TGNDIIFLAK | HMCMIMMEMT | DFTRGRGPLK | TTMDVINAAK | KISEAGTKLD | KLTREIAEQC |
790 | 800 | 810 | 820 | 830 | 840 |
PESSTKKDLL | AYLQRIALYC | HQIQITSKVK | ADVQNISGEL | IVSGLDSATS | LIQAAKNLMN |
850 | 860 | 870 | 880 | 890 | 900 |
AVVLTVKYSY | VASTKYTRQG | TVSSPIVVWK | MKAPEKKPLV | RPEKPEEVRA | KVRKGSQKKV |
910 | |||||
QNPIHALSEF | QSPADAV |