Descriptions

Alpha-catenin acts as a mechanosensor in adherens junction formation by facilitating the recruitment of vinculin to adherens junctions in the actomyosin-derived tension-dependent manner. Alpha-catenin consists of three major domains with distinct functionalities: an N-terminal (N) domain participates in beta-catenin binding and homodimerization; a modulatory (M) domain interacts with several actin-binding proteins, including vinculin; and a C-terminal (C) domain directly and/or indirectly binds to F-actin. In catenin alpha-1 (Ctnna1, αE-catenin), the vinculin-binding site (VBS) is autoinhibited by occluding the vinculin-binding hydrophobic surfaces within the MI helical bundle. The MIII region inhibits the interaction between the VBS and vinculin. In the high-tension state, Ctnna1 adopts the "open" conformation that disrupts the inhibitory role of MIII region, releasing the MI bundle and unfurling the vinculin-binding site.

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

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

Description
EC Number
Subcellular Localization
  • Cytoplasm, cytoskeleton
  • Cell junction, adherens junction
  • Cell membrane ; Peripheral membrane protein ; Cytoplasmic side
  • Cell junction
  • Found only at cell-cell boundaries
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

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