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Protein

Catenin alpha-1

Gene

Ctnna1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

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
  • protein heterooligomerization Source: Ensembl
  • regulation of cell proliferation Source: MGI
  • response to estrogen Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Cell 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 18

Organism-specific databases

MGIiMGI:88274. Ctnna1.

Subcellular locationi

GO - Cellular componenti

  • acrosomal vesicle Source: Ensembl
  • actin cytoskeleton Source: InterPro
  • adherens junction Source: MGI
  • catenin complex Source: MGI
  • cell-cell adherens junction Source: MGI
  • cell-cell junction Source: MGI
  • cell junction Source: MGI
  • cytosol Source: InterPro
  • flotillin complex Source: UniProtKB
  • focal adhesion Source: MGI
  • Golgi apparatus Source: MGI
  • intercalated disc Source: MGI
  • intracellular membrane-bounded organelle Source: MGI
  • lamellipodium Source: MGI
  • plasma membrane Source: MGI
  • zonula adherens Source: MGI
Complete GO annotation...

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

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
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
Modified residuei851PhosphoserineBy similarity1

Post-translational modificationi

Sumoylated.By similarity

Keywords - PTMi

Acetylation, 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. 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. Interacts with vinculin/VCL (By similarity).By similarity5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CTNNB1P352222EBI-647895,EBI-491549From a different organism.
Ctnnb1Q022482EBI-647895,EBI-397872
Mllt4O358892EBI-647895,EBI-6654073From a different organism.

GO - Molecular functioni

Protein-protein interaction databases

BioGridi198510. 11 interactors.
DIPiDIP-35299N.
IntActiP26231. 14 interactors.
MINTiMINT-138480.
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[»]
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.
OMAiWERQVRV.
OrthoDBiEOG091G01KR.
PhylomeDBiP26231.
TreeFamiTF313686.

Family and domain databases

InterProiIPR001033. Alpha_catenin.
IPR030047. CTNNA1.
IPR006077. Vinculin/catenin.
IPR000633. Vinculin_CS.
[Graphical view]
PANTHERiPTHR18914. PTHR18914. 1 hit.
PTHR18914:SF24. PTHR18914:SF24. 1 hit.
PfamiPF01044. Vinculin. 2 hits.
[Graphical view]
PRINTSiPR00805. ALPHACATENIN.
SUPFAMiSSF47220. SSF47220. 4 hits.
PROSITEiPS00663. VINCULIN_1. 1 hit.
[Graphical view]

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.

Cross-referencesi

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.

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[»]
ProteinModelPortaliP26231.
SMRiP26231.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198510. 11 interactors.
DIPiDIP-35299N.
IntActiP26231. 14 interactors.
MINTiMINT-138480.
STRINGi10090.ENSMUSP00000049007.

PTM databases

iPTMnetiP26231.
PhosphoSitePlusiP26231.
SwissPalmiP26231.

Proteomic databases

EPDiP26231.
PaxDbiP26231.
PeptideAtlasiP26231.
PRIDEiP26231.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi1495.
MGIiMGI:88274. Ctnna1.

Phylogenomic databases

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

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.

Miscellaneous databases

ChiTaRSiCtnna1. mouse.
EvolutionaryTraceiP26231.
PROiP26231.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000037815.
CleanExiMM_CTNNA1.
ExpressionAtlasiP26231. baseline and differential.
GenevisibleiP26231. MM.

Family and domain databases

InterProiIPR001033. Alpha_catenin.
IPR030047. CTNNA1.
IPR006077. Vinculin/catenin.
IPR000633. Vinculin_CS.
[Graphical view]
PANTHERiPTHR18914. PTHR18914. 1 hit.
PTHR18914:SF24. PTHR18914:SF24. 1 hit.
PfamiPF01044. Vinculin. 2 hits.
[Graphical view]
PRINTSiPR00805. ALPHACATENIN.
SUPFAMiSSF47220. SSF47220. 4 hits.
PROSITEiPS00663. VINCULIN_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCTNA1_MOUSE
AccessioniPrimary (citable) accession number: P26231
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: November 2, 2016
This is version 168 of the entry and version 1 of the sequence. [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

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.