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

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

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

2 regional properties for P90947

Type Name Position InterPro Accession
domain Homeobox domain 88 - 152 IPR001356
conserved_site Homeobox, conserved site 123 - 146 IPR017970

Functions

Description
EC Number
Subcellular Localization
  • Cell junction, adherens junction
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

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