UniProt functional annotation for P26231



	UniProt functional annotation for P26231

UniProt code: P26231.

Organism: Mus musculus (Mouse).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus.

Function: Associates with the cytoplasmic domain of a variety of cadherins. The association of catenins to cadherins produces a complex which is linked to the actin filament network, and which seems to be of primary importance for cadherins cell-adhesion properties. Can associate with both E- and N-cadherins. Originally believed to be a stable component of E-cadherin/catenin adhesion complexes and to mediate the linkage of cadherins to the actin cytoskeleton at adherens junctions. In contrast, cortical actin was found to be much more dynamic than E-cadherin/catenin complexes and CTNNA1 was shown not to bind to F-actin when assembled in the complex suggesting a different linkage between actin and adherens junctions components. The homodimeric form may regulate actin filament assembly and inhibit actin branching by competing with the Arp2/3 complex for binding to actin filaments. Involved in the regulation of WWTR1/TAZ, YAP1 and TGFB1- dependent SMAD2 and SMAD3 nuclear accumulation (PubMed:21145499). May play a crucial role in cell differentiation. {ECO:0000269|PubMed:16325583, ECO:0000269|PubMed:21145499}.

Subunit: Monomer and homodimer; the monomer preferentially binds to CTNNB1 and the homodimer to actin (PubMed:16325583). Component of an cadherin:catenin adhesion complex composed of at least of CDH26, beta- catenin/CTNNB1, alpha-catenin/CTNNA1 and p120 catenin/CTNND1 (By similarity). Possible component of an E-cadherin/ catenin adhesion complex together with E-cadherin/CDH1 and beta-catenin/CTNNB1 or gamma- catenin/JUP; the complex is located to adherens junctions (PubMed:7982500, PubMed:16325582, PubMed:16325583, PubMed:18093941, PubMed:25653389, PubMed:10882138). The stable association of CTNNA1 is controversial as CTNNA1 was shown not to bind to F-actin when assembled in the complex (PubMed:16325582, PubMed:18093941). Alternatively, the CTNNA1-containing complex may be linked to F-actin by other proteins such as LIMA1 (PubMed:18093941). Binds AFDN and F-actin (PubMed:11907041). Interacts with LIMA1 (By similarity) (PubMed:18093941). Interacts with ARHGAP21 (By similarity). Interacts with AJUBA (By similarity). Interacts with vinculin/VCL (By similarity). {ECO:0000250|UniProtKB:P35221, ECO:0000269|PubMed:10882138, ECO:0000269|PubMed:11907041, ECO:0000269|PubMed:16325582, ECO:0000269|PubMed:16325583, ECO:0000269|PubMed:18093941, ECO:0000269|PubMed:25653389, ECO:0000269|PubMed:7982500}.

Subcellular location: Cytoplasm, cytoskeleton. Cell junction, adherens junction. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell junction. Note=Found at cell-cell boundaries and probably at cell- matrix boundaries.

Tissue specificity: Expressed ubiquitously in normal tissues.

Ptm: Sumoylated. {ECO:0000250|UniProtKB:P35221}.

Ptm: Phosphorylation seems to contribute to the strength of cell-cell adhesion rather than to the basic capacity for cell-cell adhesion. {ECO:0000305|PubMed:25653389}.

Similarity: Belongs to the vinculin/alpha-catenin family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Mus musculus (Mouse).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus.



Function:		Associates with the cytoplasmic domain of a variety of cadherins. The association of catenins to cadherins produces a complex which is linked to the actin filament network, and which seems to be of primary importance for cadherins cell-adhesion properties. Can associate with both E- and N-cadherins. Originally believed to be a stable component of E-cadherin/catenin adhesion complexes and to mediate the linkage of cadherins to the actin cytoskeleton at adherens junctions. In contrast, cortical actin was found to be much more dynamic than E-cadherin/catenin complexes and CTNNA1 was shown not to bind to F-actin when assembled in the complex suggesting a different linkage between actin and adherens junctions components. The homodimeric form may regulate actin filament assembly and inhibit actin branching by competing with the Arp2/3 complex for binding to actin filaments. Involved in the regulation of WWTR1/TAZ, YAP1 and TGFB1- dependent SMAD2 and SMAD3 nuclear accumulation (PubMed:21145499). May play a crucial role in cell differentiation. {ECO:0000269\|PubMed:16325583, ECO:0000269\|PubMed:21145499}.


Subunit:		Monomer and homodimer; the monomer preferentially binds to CTNNB1 and the homodimer to actin (PubMed:16325583). Component of an cadherin:catenin adhesion complex composed of at least of CDH26, beta- catenin/CTNNB1, alpha-catenin/CTNNA1 and p120 catenin/CTNND1 (By similarity). Possible component of an E-cadherin/ catenin adhesion complex together with E-cadherin/CDH1 and beta-catenin/CTNNB1 or gamma- catenin/JUP; the complex is located to adherens junctions (PubMed:7982500, PubMed:16325582, PubMed:16325583, PubMed:18093941, PubMed:25653389, PubMed:10882138). The stable association of CTNNA1 is controversial as CTNNA1 was shown not to bind to F-actin when assembled in the complex (PubMed:16325582, PubMed:18093941). Alternatively, the CTNNA1-containing complex may be linked to F-actin by other proteins such as LIMA1 (PubMed:18093941). Binds AFDN and F-actin (PubMed:11907041). Interacts with LIMA1 (By similarity) (PubMed:18093941). Interacts with ARHGAP21 (By similarity). Interacts with AJUBA (By similarity). Interacts with vinculin/VCL (By similarity). {ECO:0000250\|UniProtKB:P35221, ECO:0000269\|PubMed:10882138, ECO:0000269\|PubMed:11907041, ECO:0000269\|PubMed:16325582, ECO:0000269\|PubMed:16325583, ECO:0000269\|PubMed:18093941, ECO:0000269\|PubMed:25653389, ECO:0000269\|PubMed:7982500}.
Subcellular location:		Cytoplasm, cytoskeleton. Cell junction, adherens junction. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell junction. Note=Found at cell-cell boundaries and probably at cell- matrix boundaries.
Tissue specificity:		Expressed ubiquitously in normal tissues.
Ptm:		Sumoylated. {ECO:0000250\|UniProtKB:P35221}.
Ptm:		Phosphorylation seems to contribute to the strength of cell-cell adhesion rather than to the basic capacity for cell-cell adhesion. {ECO:0000305\|PubMed:25653389}.
Similarity:		Belongs to the vinculin/alpha-catenin family. {ECO:0000305}.