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Protein

Catenin alpha-1

Gene

Ctnna1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Molecular functioni

  • actin filament binding Source: MGI
  • beta-catenin binding Source: MGI
  • cadherin binding Source: MGI
  • gamma-catenin binding Source: MGI
  • identical protein binding Source: IntAct
  • protein heterodimerization activity Source: MGI
  • structural molecule activity Source: InterPro
  • vinculin binding Source: MGI

GO - Biological processi

  • actin filament organization Source: InterPro
  • aging Source: Ensembl
  • apical junction assembly Source: MGI
  • axon regeneration Source: Ensembl
  • cellular protein localization Source: MGI
  • cellular response to indole-3-methanol Source: MGI
  • epithelial cell-cell adhesion Source: MGI
  • establishment or maintenance of cell polarity Source: MGI
  • gap junction assembly Source: Ensembl
  • male gonad development Source: Ensembl
  • negative regulation of apoptotic process Source: MGI
  • negative regulation of cell motility Source: MGI
  • negative regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: MGI
  • negative regulation of integrin-mediated signaling pathway Source: MGI
  • negative regulation of neuroblast proliferation Source: MGI
  • odontogenesis of dentin-containing tooth Source: Ensembl
  • ovarian follicle development Source: Ensembl
  • positive regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: MGI
  • positive regulation of smoothened signaling pathway Source: MGI
  • regulation of cell proliferation Source: MGI
  • response to estrogen Source: Ensembl

Keywordsi

Biological processCell adhesion

Enzyme and pathway databases

ReactomeiR-MMU-375170 CDO in myogenesis
R-MMU-418990 Adherens junctions interactions
R-MMU-5218920 VEGFR2 mediated vascular permeability
R-MMU-5626467 RHO GTPases activate IQGAPs

Names & Taxonomyi

Protein namesi
Recommended name:
Catenin alpha-1
Alternative name(s):
102 kDa cadherin-associated protein
Alpha E-catenin
CAP102
Gene namesi
Name:Ctnna1
Synonyms:Catna1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 18

Organism-specific databases

MGIiMGI:88274 Ctnna1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi436L → P: Mice bearing this mutation exhibit several retinal pigment epithelium (RPE) anomalies, including pigmentary abnormalities, focal thickening, elevated lesions, and decreased light-activated responses. Mutant animals show dysmorphology in the form of RPE cell shedding and accumulation of large multinucleated RPE cells. 1 Publication1
Mutagenesisi641 – 658SDFET…TSVQT → ADFETEDFDVRARAAVQA: No effect on cell aggregation or E-cadherin/catenin complex assembly. Decreases strength of cell-cell adhesion. 1 PublicationAdd BLAST18
Mutagenesisi641 – 658SDFET…TSVQT → EDFETEDFDVREREEVQE: No effect on cell aggregation or E-cadherin/catenin complex assembly. Increases strength of cell-cell adhesion. 1 PublicationAdd BLAST18
Mutagenesisi641S → A: No effect on cell aggregation or E-cadherin/catenin complex assembly. Decreases strength of cell-cell adhesion. 1 Publication1
Mutagenesisi641S → E: No effect on cell aggregation or E-cadherin/catenin complex assembly. Increases strength of cell-cell adhesion. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000642622 – 906Catenin alpha-1Add BLAST905

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylthreonineBy similarity1
Cross-linki57Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei264PhosphoserineBy similarity1
Modified residuei295PhosphoserineBy similarity1
Modified residuei297PhosphoserineBy similarity1
Modified residuei634PhosphothreonineCombined sources1
Modified residuei641PhosphoserineCombined sources1
Modified residuei645PhosphothreonineCombined sources1
Modified residuei652PhosphoserineCombined sources1
Modified residuei655PhosphoserineCombined sources1
Modified residuei658PhosphothreonineCombined sources1
Cross-linki797Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei851PhosphoserineBy similarity1

Post-translational modificationi

Sumoylated.By similarity
Phosphorylation seems to contribute to the strength of cell-cell adhesion rather than to the basic capacity for cell-cell adhesion.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP26231
PaxDbiP26231
PeptideAtlasiP26231
PRIDEiP26231

PTM databases

iPTMnetiP26231
PhosphoSitePlusiP26231
SwissPalmiP26231

Expressioni

Tissue specificityi

Expressed ubiquitously in normal tissues.

Gene expression databases

BgeeiENSMUSG00000037815
CleanExiMM_CTNNA1
ExpressionAtlasiP26231 baseline and differential
GenevisibleiP26231 MM

Interactioni

Subunit structurei

Monomer and homodimer; the monomer preferentially binds to CTNNB1 and the homodimer to actin. Binds AFDN and F-actin (PubMed:11907041). 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. Alternatively, the CTNNA1-containing complex may be linked to F-actin by other proteins such as LIMA1 (PubMed:18093941). Interacts with LIMA1 (PubMed:18093941). Interacts with ARHGAP21 and with AJUBA (By similarity). Interacts with vinculin/VCL (By similarity).By similarity7 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • actin filament binding Source: MGI
  • beta-catenin binding Source: MGI
  • cadherin binding Source: MGI
  • gamma-catenin binding Source: MGI
  • identical protein binding Source: IntAct
  • protein heterodimerization activity Source: MGI
  • vinculin binding Source: MGI

Protein-protein interaction databases

BioGridi198510, 15 interactors
CORUMiP26231
DIPiDIP-35299N
IntActiP26231, 19 interactors
MINTiP26231
STRINGi10090.ENSMUSP00000049007

Structurei

Secondary structure

1906
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi59 – 82Combined sources24
Beta strandi84 – 86Combined sources3
Helixi87 – 113Combined sources27
Helixi118 – 165Combined sources48
Helixi170 – 195Combined sources26
Helixi201 – 230Combined sources30
Helixi235 – 259Combined sources25
Helixi305 – 315Combined sources11
Helixi328 – 352Combined sources25
Helixi392 – 396Combined sources5
Helixi399 – 409Combined sources11
Helixi413 – 440Combined sources28
Helixi444 – 473Combined sources30
Helixi478 – 506Combined sources29
Helixi508 – 531Combined sources24
Helixi535 – 560Combined sources26
Helixi567 – 581Combined sources15
Helixi583 – 598Combined sources16
Helixi608 – 629Combined sources22

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5Y04X-ray2.85B276-375[»]
ProteinModelPortaliP26231
SMRiP26231
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP26231

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 228Involved in homodimerizationBy similarityAdd BLAST227
Regioni97 – 148Interaction with JUP and CTNNB1By similarityAdd BLAST52
Regioni325 – 394Interaction with alpha-actininBy similarityAdd BLAST70

Sequence similaritiesi

Belongs to the vinculin/alpha-catenin family.Curated

Phylogenomic databases

eggNOGiKOG3681 Eukaryota
ENOG410XSRU LUCA
GeneTreeiENSGT00550000074411
HOGENOMiHOG000280724
HOVERGENiHBG000069
InParanoidiP26231
KOiK05691
OMAiVLQRNIP
OrthoDBiEOG091G01KR
PhylomeDBiP26231
TreeFamiTF313686

Family and domain databases

InterProiView protein in InterPro
IPR036723 Alpha-catenin/vinculin-like_sf
IPR001033 Alpha_catenin
IPR030047 CTNNA1
IPR006077 Vinculin/catenin
IPR000633 Vinculin_CS
PANTHERiPTHR18914 PTHR18914, 1 hit
PTHR18914:SF24 PTHR18914:SF24, 1 hit
PfamiView protein in Pfam
PF01044 Vinculin, 2 hits
PRINTSiPR00805 ALPHACATENIN
SUPFAMiSSF47220 SSF47220, 4 hits
PROSITEiView protein in PROSITE
PS00663 VINCULIN_1, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P26231-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTAVHAGNIN FKWDPKSLEI RTLAVERLLE PLVTQVTTLV NTNSKGPSNK
60 70 80 90 100
KRGRSKKAHV LAASVEQATE NFLEKGDKIA KESQFLKEEL VVAVEDVRKQ
110 120 130 140 150
GDLMKSAAGE FADDPCSSVK RGNMVRAARA LLSAVTRLLI LADMADVYKL
160 170 180 190 200
LVQLKVVEDG ILKLRNAGNE QDLGIQYKAL KPEVDKLNIM AAKRQQELKD
210 220 230 240 250
VGNRDQMAAA RGILQKNVPI LYTASQACLQ HPDVAAYKAN RDLIYKQLQQ
260 270 280 290 300
AVTGISNAAQ ATASDDAAQH QGGSGGELAY ALNNFDKQII VDPLSFSEER
310 320 330 340 350
FRPSLEERLE SIISGAALMA DSSCTRDDRR ERIVAECNAV RQALQDLLSE
360 370 380 390 400
YMGNAGRKER SDALNSAIDK MTKKTRDLRR QLRKAVMDHV SDSFLETNVP
410 420 430 440 450
LLVLIEAAKN GNEKEVKEYA QVFREHANKL IEVANLACSI SNNEEGVKLV
460 470 480 490 500
RMSASQLEAL CPQVINAALA LAAKPQSKLA QENMDLFKEQ WEKQVRVLTD
510 520 530 540 550
AVDDITSIDD FLAVSENHIL EDVNKCVIAL QEKDVDGLDR TAGAIRGRAA
560 570 580 590 600
RVIHVVTSEM DNYEPGVYTE KVLEATKLLS NTVMPRFTEQ VEAAVEALSS
610 620 630 640 650
DPAQPMDENE FIDASRLVYD GIRDIRKAVL MIRTPEELDD SDFETEDFDV
660 670 680 690 700
RSRTSVQTED DQLIAGQSAR AIMAQLPQEQ KAKIAEQVAS FQEEKSKLDA
710 720 730 740 750
EVSKWDDSGN DIIVLAKQMC MIMMEMTDFT RGKGPLKNTS DVISAAKKIA
760 770 780 790 800
EAGSRMDKLG RTIADHCPDS ACKQDLLAYL QRIALYCHQL NICSKVKAEV
810 820 830 840 850
QNLGGELVVS GVDSAMSLIQ AAKNLMNAVV QTVKASYVAS TKYQKSQGMA
860 870 880 890 900
SLNLPAVSWK MKAPEKKPLV KREKQDETQT KIKRASQKKH VNPVQALSEF

KAMDSI
Length:906
Mass (Da):100,106
Last modified:May 1, 1992 - v1
Checksum:i3ED1EC50925DBBB5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59990 mRNA Translation: CAA42607.1
D90362 mRNA Translation: BAA14376.1
BC048163 mRNA Translation: AAH48163.1
CCDSiCCDS29139.1
PIRiA39529
RefSeqiNP_033948.1, NM_009818.1
XP_011245120.1, XM_011246818.2
UniGeneiMm.18962
Mm.384762

Genome annotation databases

EnsembliENSMUST00000042345; ENSMUSP00000049007; ENSMUSG00000037815
GeneIDi12385
KEGGimmu:12385
UCSCiuc008ely.1 mouse

Similar proteinsi

Entry informationi

Entry nameiCTNA1_MOUSE
AccessioniPrimary (citable) accession number: P26231
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: May 23, 2018
This is version 180 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

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