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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

  1. actin filament binding Source: MGI
  2. beta-catenin binding Source: MGI
  3. cadherin binding Source: MGI
  4. gamma-catenin binding Source: MGI
  5. poly(A) RNA binding Source: MGI
  6. structural molecule activity Source: InterPro
  7. vinculin binding Source: MGI

GO - Biological processi

  1. actin filament organization Source: InterPro
  2. aging Source: Ensembl
  3. apical junction assembly Source: MGI
  4. axon regeneration Source: Ensembl
  5. cellular protein localization Source: MGI
  6. cellular response to indole-3-methanol Source: MGI
  7. epithelial cell-cell adhesion Source: MGI
  8. establishment or maintenance of cell polarity Source: MGI
  9. gap junction assembly Source: Ensembl
  10. male gonad development Source: Ensembl
  11. negative regulation of apoptotic process Source: MGI
  12. negative regulation of cell motility Source: MGI
  13. negative regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: MGI
  14. negative regulation of integrin-mediated signaling pathway Source: MGI
  15. negative regulation of neuroblast proliferation Source: MGI
  16. odontogenesis of dentin-containing tooth Source: Ensembl
  17. ovarian follicle development Source: Ensembl
  18. positive regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: MGI
  19. positive regulation of smoothened signaling pathway Source: MGI
  20. protein heterooligomerization Source: Ensembl
  21. regulation of cell proliferation Source: MGI
  22. response to estrogen Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiREACT_304595. CDO in myogenesis.
REACT_308832. Adherens junctions interactions.
REACT_321965. VEGFR2 mediated vascular permeability.

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
ProteomesiUP000000589 Componenti: Chromosome 18

Organism-specific databases

MGIiMGI:88274. Ctnna1.

Subcellular locationi

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.

GO - Cellular componenti

  1. acrosomal vesicle Source: Ensembl
  2. actin cytoskeleton Source: InterPro
  3. adherens junction Source: MGI
  4. catenin complex Source: MGI
  5. cell-cell adherens junction Source: MGI
  6. cell-cell junction Source: MGI
  7. cytosol Source: InterPro
  8. focal adhesion Source: MGI
  9. intercalated disc Source: MGI
  10. lamellipodium Source: MGI
  11. plasma membrane Source: MGI
  12. zonula adherens Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 906905Catenin alpha-1PRO_0000064262Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonineBy similarity
Modified residuei264 – 2641PhosphoserineBy similarity
Modified residuei295 – 2951PhosphoserineBy similarity
Modified residuei297 – 2971PhosphoserineBy similarity
Modified residuei634 – 6341PhosphothreonineBy similarity
Modified residuei641 – 6411Phosphoserine2 Publications
Modified residuei645 – 6451PhosphothreonineBy similarity
Modified residuei652 – 6521PhosphoserineBy similarity
Modified residuei851 – 8511PhosphoserineBy similarity

Post-translational modificationi

Sumoylated.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP26231.
PaxDbiP26231.
PRIDEiP26231.

PTM databases

PhosphoSiteiP26231.

Expressioni

Tissue specificityi

Expressed ubiquitously in normal tissues.

Gene expression databases

BgeeiP26231.
CleanExiMM_CTNNA1.
ExpressionAtlasiP26231. baseline and differential.
GenevestigatoriP26231.

Interactioni

Subunit structurei

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.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.

Protein-protein interaction databases

BioGridi198510. 8 interactions.
DIPiDIP-35299N.
IntActiP26231. 14 interactions.
MINTiMINT-138480.

Structurei

Secondary structure

1
906
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi59 – 8224Combined sources
Beta strandi84 – 863Combined sources
Helixi87 – 11327Combined sources
Helixi118 – 16548Combined sources
Helixi170 – 19526Combined sources
Helixi201 – 23030Combined sources
Helixi235 – 25925Combined sources
Helixi305 – 31511Combined sources
Helixi328 – 35225Combined sources
Helixi392 – 3965Combined sources
Helixi399 – 40911Combined sources
Helixi413 – 44028Combined sources
Helixi444 – 47330Combined sources
Helixi478 – 50629Combined sources
Helixi508 – 53124Combined sources
Helixi535 – 56026Combined sources
Helixi567 – 58115Combined sources
Helixi583 – 59816Combined sources
Helixi608 – 62922Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 19-878.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP26231.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 228227Involved in homodimerizationBy similarityAdd
BLAST
Regioni97 – 14852Interaction with JUP and CTNNB1By similarityAdd
BLAST
Regioni325 – 39470Interaction with alpha-actininBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the vinculin/alpha-catenin family.Curated

Phylogenomic databases

eggNOGiNOG240050.
HOGENOMiHOG000280724.
HOVERGENiHBG000069.
InParanoidiP26231.
KOiK05691.
OMAiWERQVRV.
OrthoDBiEOG7HQN7B.
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:April 30, 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.
UniGeneiMm.18962.

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.
UniGeneiMm.18962.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 19-878.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198510. 8 interactions.
DIPiDIP-35299N.
IntActiP26231. 14 interactions.
MINTiMINT-138480.

PTM databases

PhosphoSiteiP26231.

Proteomic databases

MaxQBiP26231.
PaxDbiP26231.
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

eggNOGiNOG240050.
HOGENOMiHOG000280724.
HOVERGENiHBG000069.
InParanoidiP26231.
KOiK05691.
OMAiWERQVRV.
OrthoDBiEOG7HQN7B.
PhylomeDBiP26231.
TreeFamiTF313686.

Enzyme and pathway databases

ReactomeiREACT_304595. CDO in myogenesis.
REACT_308832. Adherens junctions interactions.
REACT_321965. VEGFR2 mediated vascular permeability.

Miscellaneous databases

ChiTaRSiCtnna1. mouse.
EvolutionaryTraceiP26231.
NextBioi281096.
PROiP26231.
SOURCEiSearch...

Gene expression databases

BgeeiP26231.
CleanExiMM_CTNNA1.
ExpressionAtlasiP26231. baseline and differential.
GenevestigatoriP26231.

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...

Publicationsi

« Hide 'large scale' publications
  1. 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(1990) [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(2003) [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(1993) [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(2004) [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(2004) [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(2007) [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(2007) [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(2008) [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(1999) [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(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 385-651, INTERACTION WITH MLLT4 AND F-ACTIN.

Entry informationi

Entry nameiCTNA1_MOUSE
AccessioniPrimary (citable) accession number: P26231
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 30, 1992
Last sequence update: April 30, 1992
Last modified: March 31, 2015
This is version 153 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

External Data

Dasty 3

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 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.