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

260-626 (Middle region)

Relief mechanism

Others

Assay

Deletion assay

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q65CL1

Entry ID Method Resolution Chain Position Source
AF-Q65CL1-F1 Predicted AlphaFoldDB

45 variants for Q65CL1

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3389097457 10 N>K No EVA
rs3389107742 25 K>T No EVA
rs3401331968 63 E>Q No EVA
rs3400867290 114 Y>C No EVA
rs3401331954 117 K>R* No EVA
rs3400867247 121 V>G No EVA
rs3389103530 137 V>I No EVA
rs3400614975 138 L>I No EVA
rs3401245585 138 L>P No EVA
rs3389078255 223 S>A No EVA
rs3389102534 251 V>A No EVA
rs3389102549 275 S>G No EVA
rs216723148 277 F>I No EVA
rs216723148 277 F>L No EVA
rs1133875150 290 T>S No EVA
rs1132385900 296 V>L No EVA
rs248562796 299 S>L No EVA
rs1135131131 303 R>H No EVA
rs1131789230 307 I>L No EVA
rs1134478589 308 I>F No EVA
rs3389107725 322 D>Y No EVA
rs3389078234 343 L>P No EVA
rs250165314 348 S>R No EVA
rs3389083113 354 E>* No EVA
rs3389078220 361 T>S No EVA
rs1131964311 375 R>K No EVA
rs1133021921 376 Q>H No EVA
rs3389048155 385 I>V No EVA
rs3389102614 415 A>D No EVA
rs3401300809 423 G>C No EVA
rs3401399693 423 G>D No EVA
rs3401239291 426 V>L No EVA
rs3389114771 430 N>Y No EVA
rs3389107698 435 M>I No EVA
rs3412866419 461 N>Y No EVA
rs46078493 535 R>Q No EVA
rs3389091155 536 A>T No EVA
rs3389109742 593 L>V No EVA
rs3401138689 610 S>F No EVA
rs3400873924 611 K>* No EVA
rs3401246884 611 K>M No EVA
rs3400873939 612 K>E No EVA
rs3389113892 638 D>N No EVA
rs3389091071 814 L>S No EVA
rs3389109744 817 A>V No EVA

No associated diseases with Q65CL1

No regional properties for Q65CL1

Type Name Position InterPro Accession
No domain, repeats, and functional sites for Q65CL1

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm, cytoskeleton
  • Cell junction, desmosome
  • Localizes to intercalated disks of cardiomyocytes and in peritubular myoid cells of testis, and colocalizes with CTNNA1 and CTNNA2
  • Colocalizes with PKP2 at intercalated disks in the heart (PubMed:17535849)
PANTHER Family PTHR18914 ALPHA CATENIN
PANTHER Subfamily PTHR18914:SF21 CATENIN ALPHA-3
PANTHER Protein Class non-motor actin binding protein
PANTHER Pathway Category Wnt signaling pathway
alpha-catenin
Cadherin signaling pathway
alpha-catenin

5 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.
cytoskeleton A cellular structure that forms the internal framework of eukaryotic and prokaryotic cells. The cytoskeleton includes intermediate filaments, microfilaments, microtubules, the microtrabecular lattice, and other structures characterized by a polymeric filamentous nature and long-range order within the cell. The various elements of the cytoskeleton not only serve in the maintenance of cellular shape but also have roles in other cellular functions, including cellular movement, cell division, endocytosis, and movement of organelles.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
fascia adherens A cell-cell junction that contains the transmembrane protein N-cadherin, which interacts with identical molecules from neighbouring cells to form a tight mechanical intercellular link; forms a large portion of the intercalated disc, the structure at which myofibrils terminate in cardiomyocytes.
lamellipodium A thin sheetlike process extended by the leading edge of a migrating cell or extending cell process; contains a dense meshwork of actin filaments.

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.

7 GO annotations of biological process

Name Definition
actin filament organization A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures comprising actin filaments. Includes processes that control the spatial distribution of actin filaments, such as organizing filaments into meshworks, bundles, or other structures, as by cross-linking.
bundle of His cell-Purkinje myocyte adhesion involved in cell communication The attachment of a bundle of His cell to a Purkinje myocyte via adhesion molecules that results in the cells being juxtaposed so that they can communicate.
cell migration The controlled self-propelled movement of a cell from one site to a destination guided by molecular cues. Cell migration is a central process in the development and maintenance of multicellular organisms.
cell-cell adhesion The attachment of one cell to another cell via adhesion molecules.
epithelial cell-cell adhesion The attachment of an epithelial cell to another epithelial cell via adhesion molecules.
regulation of heart rate by cardiac conduction A cardiac conduction process that modulates the frequency or rate of heart contraction.
regulation of ventricular cardiac muscle cell action potential Any process that modulates the frequency, rate or extent of action potential creation, propagation or termination in a ventricular cardiac muscle cell contributing to the regulation of its contraction. This typically occurs via modulation of the activity or expression of voltage-gated ion channels.

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
P26232 CTNNA2 Catenin alpha-2 Homo sapiens (Human) SS
P35221 CTNNA1 Catenin alpha-1 Homo sapiens (Human) EV
Q9UI47 CTNNA3 Catenin alpha-3 Homo sapiens (Human) SS
Q64727 Vcl Vinculin Mus musculus (Mouse) SS
P26231 Ctnna1 Catenin alpha-1 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
MSAETPITLN MDTQDLQIQT FTVEKLLEPL IIQVTTLVNC PQNPSNRKKG RSKRARVLLA
70 80 90 100 110 120
SVEEATWNLL DKGEMIAKEA TVLKEELAAA LQEVRKESKA LKVSAERFTD DPCYLPKREA
130 140 150 160 170 180
VVQAARALLA AVTRLLVLAD MIDVMCLLQH VSSFQRTFES LKNVSNKSDL QRTYQKLGKE
190 200 210 220 230 240
LESLDYLAFK RQQDLKSPSQ RDEIAGARAT LKENSPLLHS ICSACLEHSD VASLKASKDT
250 260 270 280 290 300
VCEEIQNALD VISNASQGIQ NAPAPPEPQA ATLGSAFDEL ENLIVLNPLT VTEEDVRPSL
310 320 330 340 350 360
EKRLEAIISG AALLADSSCT RDLHRERIIA ECNAIRQALQ DLLTEYMSNT GKTERSNTLN
370 380 390 400 410 420
TAIVNMSKKT RDLRRQLRKA IIDHISDSFL DTTVPLLVLI EAAKNGRVKE IKDYAAIFHE
430 440 450 460 470 480
HTGRLVEVAN LACSMSTNED GIKIVRIAAN HLETLCPQII NAALALASRP KSQVVKNTME
490 500 510 520 530 540
MYKRTWEHYI HVLTEAVDDI TSIDDFLAVS ESHILEDVNK CIIALRDQDA DNLDRAAGAI
550 560 570 580 590 600
RGRAARVAHI VAGEMDSYEP GAYTEGVMRN VNFLTSTVIP EFVTQVNVAL DALSKNSLTA
610 620 630 640 650 660
LDDNQFVDIS KKIYDTIHDI RCSVMMIRTP EELEDVSDLE DDHEVRSHTS IQTEGKTDRA
670 680 690 700 710 720
KMTQLPEAEK EKIAEQVADF KKVKSKLDAE IEIWDDTSND IIVLAKKMCM IMMEMTDFTR
730 740 750 760 770 780
GKGPLKHTTD VIYAAKMISE SGSRMDVLAR QIANQCPDPP CKQDLLAYLE QIKFYSHQLK
790 800 810 820 830 840
ICSQVKAEIQ NLGGELIVSA LDSVTSLIQA AKNLMNAVVQ TVKMSYIAST KIIRIQSSAG
850 860 870 880 890
PRHPVVMWRM KAPAKKPLIK REKPEETWAA VRRGSAKKKI HPVQVMSEFR GRQVY