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P26231 (CTNA1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 146. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Catenin alpha-1
Alternative name(s):
102 kDa cadherin-associated protein
Alpha E-catenin
CAP102
Gene names
Name:Ctnna1
Synonyms:Catna1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length906 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. May play a crucial role in cell differentiation. Ref.6

Subunit structure

Monomer and homodimer; the monomer preferentially binds to CTNNB1 and the homodimer to actin. Binds MLLT4 and F-actin. 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. The stable association of CTNNA1 is controversial as CTNNA1 was shown not to bind to F-actin when assembled in the complex. Alternatively, the CTNNA1-containing complex may be linked to F-actin by other proteins such as LIMA1. Interacts with ARHGAP21 and with AJUBA By similarity. Interacts with LIMA1. Ref.4 Ref.6 Ref.8 Ref.11

Subcellular location

Cytoplasmcytoskeleton. Cell junctionadherens 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.

Post-translational modification

Sumoylated By similarity.

Sequence similarities

Belongs to the vinculin/alpha-catenin family.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentCell junction
Cell membrane
Cytoplasm
Cytoskeleton
Membrane
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processaging

Inferred from electronic annotation. Source: Ensembl

apical junction assembly

Inferred from mutant phenotype PubMed 16543460PubMed 22411810. Source: MGI

axon regeneration

Inferred from electronic annotation. Source: Ensembl

cellular protein localization

Inferred from mutant phenotype PubMed 22411810. Source: MGI

cellular response to indole-3-methanol

Inferred from electronic annotation. Source: Ensembl

epithelial cell-cell adhesion

Inferred from mutant phenotype PubMed 22411810. Source: MGI

establishment or maintenance of cell polarity

Inferred from mutant phenotype PubMed 16543460. Source: MGI

gap junction assembly

Inferred from electronic annotation. Source: Ensembl

male gonad development

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Inferred from mutant phenotype PubMed 16543460. Source: MGI

negative regulation of cell motility

Inferred from mutant phenotype PubMed 22411810. Source: MGI

negative regulation of extrinsic apoptotic signaling pathway in absence of ligand

Inferred from mutant phenotype PubMed 22411810. Source: MGI

negative regulation of integrin-mediated signaling pathway

Inferred from mutant phenotype PubMed 22411810. Source: MGI

negative regulation of neuroblast proliferation

Inferred from mutant phenotype PubMed 16543460. Source: MGI

odontogenesis of dentin-containing tooth

Inferred from electronic annotation. Source: Ensembl

ovarian follicle development

Inferred from electronic annotation. Source: Ensembl

positive regulation of extrinsic apoptotic signaling pathway in absence of ligand

Inferred from mutant phenotype PubMed 22411810. Source: MGI

positive regulation of smoothened signaling pathway

Inferred from genetic interaction PubMed 16543460. Source: MGI

protein heterooligomerization

Inferred from electronic annotation. Source: Ensembl

regulation of cell proliferation

Inferred from genetic interaction PubMed 17989230. Source: MGI

response to estrogen

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentacrosomal vesicle

Inferred from electronic annotation. Source: Ensembl

actin cytoskeleton

Inferred from electronic annotation. Source: InterPro

adherens junction

Inferred from direct assay PubMed 12695331. Source: MGI

catenin complex

Inferred from electronic annotation. Source: Ensembl

cell-cell adherens junction

Inferred from direct assay PubMed 15775979PubMed 16510873. Source: MGI

intercalated disc

Inferred from direct assay PubMed 17535849. Source: MGI

lamellipodium

Inferred from direct assay PubMed 14657280. Source: MGI

plasma membrane

Inferred from direct assay PubMed 16510873. Source: MGI

zonula adherens

Inferred from direct assay PubMed 11025210. Source: MGI

   Molecular_functionactin filament binding

Inferred from direct assay PubMed 11795944. Source: MGI

protein binding

Inferred from physical interaction Ref.10PubMed 10974003PubMed 9264463. Source: IntAct

structural molecule activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CTNNB1P352222EBI-647895,EBI-491549From a different organism.
Ctnnb1Q022482EBI-647895,EBI-397872
Mllt4O358892EBI-647895,EBI-6654073From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 906905Catenin alpha-1
PRO_0000064262

Regions

Region2 – 228227Involved in homodimerization By similarity
Region97 – 14852Interaction with JUP and CTNNB1 By similarity
Region325 – 39470Interaction with alpha-actinin By similarity

Amino acid modifications

Modified residue21N-acetylthreonine By similarity
Modified residue6341Phosphothreonine By similarity
Modified residue6411Phosphoserine Ref.7 Ref.9
Modified residue6451Phosphothreonine By similarity
Modified residue6521Phosphoserine By similarity

Secondary structure

...................................... 906
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P26231 [UniParc].

Last modified May 1, 1992. Version 1.
Checksum: 3ED1EC50925DBBB5

FASTA906100,106
        10         20         30         40         50         60 
MTAVHAGNIN FKWDPKSLEI RTLAVERLLE PLVTQVTTLV NTNSKGPSNK KRGRSKKAHV 

        70         80         90        100        110        120 
LAASVEQATE NFLEKGDKIA KESQFLKEEL VVAVEDVRKQ GDLMKSAAGE FADDPCSSVK 

       130        140        150        160        170        180 
RGNMVRAARA LLSAVTRLLI LADMADVYKL LVQLKVVEDG ILKLRNAGNE QDLGIQYKAL 

       190        200        210        220        230        240 
KPEVDKLNIM AAKRQQELKD VGNRDQMAAA RGILQKNVPI LYTASQACLQ HPDVAAYKAN 

       250        260        270        280        290        300 
RDLIYKQLQQ AVTGISNAAQ ATASDDAAQH QGGSGGELAY ALNNFDKQII VDPLSFSEER 

       310        320        330        340        350        360 
FRPSLEERLE SIISGAALMA DSSCTRDDRR ERIVAECNAV RQALQDLLSE YMGNAGRKER 

       370        380        390        400        410        420 
SDALNSAIDK MTKKTRDLRR QLRKAVMDHV SDSFLETNVP LLVLIEAAKN GNEKEVKEYA 

       430        440        450        460        470        480 
QVFREHANKL IEVANLACSI SNNEEGVKLV RMSASQLEAL CPQVINAALA LAAKPQSKLA 

       490        500        510        520        530        540 
QENMDLFKEQ WEKQVRVLTD AVDDITSIDD FLAVSENHIL EDVNKCVIAL QEKDVDGLDR 

       550        560        570        580        590        600 
TAGAIRGRAA RVIHVVTSEM DNYEPGVYTE KVLEATKLLS NTVMPRFTEQ VEAAVEALSS 

       610        620        630        640        650        660 
DPAQPMDENE FIDASRLVYD GIRDIRKAVL MIRTPEELDD SDFETEDFDV RSRTSVQTED 

       670        680        690        700        710        720 
DQLIAGQSAR AIMAQLPQEQ KAKIAEQVAS FQEEKSKLDA EVSKWDDSGN DIIVLAKQMC 

       730        740        750        760        770        780 
MIMMEMTDFT RGKGPLKNTS DVISAAKKIA EAGSRMDKLG RTIADHCPDS ACKQDLLAYL 

       790        800        810        820        830        840 
QRIALYCHQL NICSKVKAEV QNLGGELVVS GVDSAMSLIQ AAKNLMNAVV QTVKASYVAS 

       850        860        870        880        890        900 
TKYQKSQGMA SLNLPAVSWK MKAPEKKPLV KREKQDETQT KIKRASQKKH VNPVQALSEF 


KAMDSI 

« Hide

References

« Hide 'large scale' references
[1]"The uvomorulin-anchorage protein alpha catenin is a vinculin homologue."
Herrenknecht K., Ozawa M., Eckerskorn C., Lottspeich F., Lenter M., Kemler R.
Proc. Natl. Acad. Sci. U.S.A. 88:9156-9160(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Strain: 129/Sv.
[2]"The 102 kd cadherin-associated protein: similarity to vinculin and posttranscriptional regulation of expression."
Nagafuchi A., Takeichi M., Tsukita S.
Cell 65:849-857(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6.
Tissue: Brain.
[4]"Distinct cadherin-catenin complexes in Ca(2+)-dependent cell-cell adhesion."
Butz S., Kemler R.
FEBS Lett. 355:195-200(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN AN E-CADHERIN/CATENIN ADHESION COMPLEX.
[5]"Deconstructing the cadherin-catenin-actin complex."
Yamada S., Pokutta S., Drees F., Weis W.I., Nelson W.J.
Cell 123:889-901(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: RECONSTITUTION OF THE E-CADHERIN/CATENIN ADHESION COMPLEX, LACK OF ACTIN BINDING BY THE E-CADHERIN/CATENIN ADHESION COMPLEX.
[6]"Alpha-catenin is a molecular switch that binds E-cadherin-beta-catenin and regulates actin-filament assembly."
Drees F., Pokutta S., Yamada S., Nelson W.J., Weis W.I.
Cell 123:903-915(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, FUNCTION.
[7]"Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[8]"EPLIN mediates linkage of the cadherin catenin complex to F-actin and stabilizes the circumferential actin belt."
Abe K., Takeichi M.
Proc. Natl. Acad. Sci. U.S.A. 105:13-19(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LIMA1, LACK OF ACTIN BINDING BY THE E-CADHERIN/CATENIN ADHESION COMPLEX.
[9]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
[10]"Structure of the dimerization and beta-catenin-binding region of alpha-catenin."
Pokutta S., Weis W.I.
Mol. Cell 5:533-543(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 57-261 IN COMPLEX WITH CTNNB1.
[11]"Biochemical and structural definition of the l-afadin- and actin-binding sites of alpha-catenin."
Pokutta S., Drees F., Takai Y., Nelson W.J., Weis W.I.
J. Biol. Chem. 277:18868-18874(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 385-651, INTERACTION WITH MLLT4 AND F-ACTIN.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X59990 mRNA. Translation: CAA42607.1.
D90362 mRNA. Translation: BAA14376.1.
BC048163 mRNA. Translation: AAH48163.1.
CCDSCCDS29139.1.
PIRA39529.
RefSeqNP_033948.1. NM_009818.1.
UniGeneMm.18962.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DOVX-ray3.00A82-262[»]
1DOWX-ray1.80A57-261[»]
1L7CX-ray2.50A/B/C385-651[»]
4E17X-ray2.30B321-356[»]
4E18X-ray2.40B302-356[»]
4K1NX-ray6.50A/B1-906[»]
ProteinModelPortalP26231.
SMRP26231. Positions 22-878.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198510. 8 interactions.
DIPDIP-35299N.
IntActP26231. 14 interactions.
MINTMINT-138480.

PTM databases

PhosphoSiteP26231.

Proteomic databases

MaxQBP26231.
PaxDbP26231.
PRIDEP26231.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000042345; ENSMUSP00000049007; ENSMUSG00000037815.
GeneID12385.
KEGGmmu:12385.
UCSCuc008ely.1. mouse.

Organism-specific databases

CTD1495.
MGIMGI:88274. Ctnna1.

Phylogenomic databases

eggNOGNOG240050.
HOGENOMHOG000280724.
HOVERGENHBG000069.
InParanoidP26231.
KOK05691.
OMAWERQVRV.
OrthoDBEOG7HQN7B.
PhylomeDBP26231.
TreeFamTF313686.

Gene expression databases

ArrayExpressP26231.
BgeeP26231.
CleanExMM_CTNNA1.
GenevestigatorP26231.

Family and domain databases

InterProIPR001033. Alpha_catenin.
IPR006077. Vinculin/catenin.
IPR000633. Vinculin_CS.
[Graphical view]
PANTHERPTHR18914. PTHR18914. 1 hit.
PfamPF01044. Vinculin. 2 hits.
[Graphical view]
PRINTSPR00805. ALPHACATENIN.
SUPFAMSSF47220. SSF47220. 4 hits.
PROSITEPS00663. VINCULIN_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCTNNA1. mouse.
EvolutionaryTraceP26231.
NextBio281096.
PROP26231.
SOURCESearch...

Entry information

Entry nameCTNA1_MOUSE
AccessionPrimary (citable) accession number: P26231
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: July 9, 2014
This is version 146 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot