Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P26231

- CTNA1_MOUSE

UniProt

P26231 - CTNA1_MOUSE

Protein

Catenin alpha-1

Gene

Ctnna1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 1 (01 May 1992)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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. protein binding Source: IntAct
    3. structural molecule activity Source: InterPro

    GO - Biological processi

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

    Keywords - Biological processi

    Cell adhesion

    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: 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: Ensembl
    5. cell-cell adherens junction Source: MGI
    6. intercalated disc Source: MGI
    7. lamellipodium Source: MGI
    8. plasma membrane Source: MGI
    9. zonula adherens Source: MGI

    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 residuei634 – 6341PhosphothreonineBy similarity
    Modified residuei641 – 6411Phosphoserine2 Publications
    Modified residuei645 – 6451PhosphothreonineBy similarity
    Modified residuei652 – 6521PhosphoserineBy 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

    ArrayExpressiP26231.
    BgeeiP26231.
    CleanExiMM_CTNNA1.
    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 – 8224
    Beta strandi84 – 863
    Helixi87 – 11327
    Helixi118 – 16548
    Helixi170 – 19526
    Helixi201 – 23030
    Helixi235 – 25925
    Helixi305 – 31511
    Helixi328 – 35225
    Helixi392 – 3965
    Helixi399 – 40911
    Helixi413 – 44028
    Helixi444 – 47330
    Helixi478 – 50629
    Helixi508 – 53124
    Helixi535 – 56026
    Helixi567 – 58115
    Helixi583 – 59816
    Helixi608 – 62922

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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 22-878.
    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.
    IPR006077. Vinculin/catenin.
    IPR000633. Vinculin_CS.
    [Graphical view]
    PANTHERiPTHR18914. PTHR18914. 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

    MTAVHAGNIN FKWDPKSLEI RTLAVERLLE PLVTQVTTLV NTNSKGPSNK    50
    KRGRSKKAHV LAASVEQATE NFLEKGDKIA KESQFLKEEL VVAVEDVRKQ 100
    GDLMKSAAGE FADDPCSSVK RGNMVRAARA LLSAVTRLLI LADMADVYKL 150
    LVQLKVVEDG ILKLRNAGNE QDLGIQYKAL KPEVDKLNIM AAKRQQELKD 200
    VGNRDQMAAA RGILQKNVPI LYTASQACLQ HPDVAAYKAN RDLIYKQLQQ 250
    AVTGISNAAQ ATASDDAAQH QGGSGGELAY ALNNFDKQII VDPLSFSEER 300
    FRPSLEERLE SIISGAALMA DSSCTRDDRR ERIVAECNAV RQALQDLLSE 350
    YMGNAGRKER SDALNSAIDK MTKKTRDLRR QLRKAVMDHV SDSFLETNVP 400
    LLVLIEAAKN GNEKEVKEYA QVFREHANKL IEVANLACSI SNNEEGVKLV 450
    RMSASQLEAL CPQVINAALA LAAKPQSKLA QENMDLFKEQ WEKQVRVLTD 500
    AVDDITSIDD FLAVSENHIL EDVNKCVIAL QEKDVDGLDR TAGAIRGRAA 550
    RVIHVVTSEM DNYEPGVYTE KVLEATKLLS NTVMPRFTEQ VEAAVEALSS 600
    DPAQPMDENE FIDASRLVYD GIRDIRKAVL MIRTPEELDD SDFETEDFDV 650
    RSRTSVQTED DQLIAGQSAR AIMAQLPQEQ KAKIAEQVAS FQEEKSKLDA 700
    EVSKWDDSGN DIIVLAKQMC MIMMEMTDFT RGKGPLKNTS DVISAAKKIA 750
    EAGSRMDKLG RTIADHCPDS ACKQDLLAYL QRIALYCHQL NICSKVKAEV 800
    QNLGGELVVS GVDSAMSLIQ AAKNLMNAVV QTVKASYVAS TKYQKSQGMA 850
    SLNLPAVSWK MKAPEKKPLV KREKQDETQT KIKRASQKKH VNPVQALSEF 900
    KAMDSI 906
    Length:906
    Mass (Da):100,106
    Last modified:May 1, 1992 - v1
    Checksum:i3ED1EC50925DBBB5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X59990 mRNA. Translation: CAA42607.1 .
    D90362 mRNA. Translation: BAA14376.1 .
    BC048163 mRNA. Translation: AAH48163.1 .
    CCDSi CCDS29139.1.
    PIRi A39529.
    RefSeqi NP_033948.1. NM_009818.1.
    UniGenei Mm.18962.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DOV X-ray 3.00 A 82-262 [» ]
    1DOW X-ray 1.80 A 57-261 [» ]
    1L7C X-ray 2.50 A/B/C 385-651 [» ]
    4E17 X-ray 2.30 B 321-356 [» ]
    4E18 X-ray 2.40 B 302-356 [» ]
    4K1N X-ray 6.50 A/B 1-906 [» ]
    ProteinModelPortali P26231.
    SMRi P26231. Positions 22-878.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198510. 8 interactions.
    DIPi DIP-35299N.
    IntActi P26231. 14 interactions.
    MINTi MINT-138480.

    PTM databases

    PhosphoSitei P26231.

    Proteomic databases

    MaxQBi P26231.
    PaxDbi P26231.
    PRIDEi P26231.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000042345 ; ENSMUSP00000049007 ; ENSMUSG00000037815 .
    GeneIDi 12385.
    KEGGi mmu:12385.
    UCSCi uc008ely.1. mouse.

    Organism-specific databases

    CTDi 1495.
    MGIi MGI:88274. Ctnna1.

    Phylogenomic databases

    eggNOGi NOG240050.
    HOGENOMi HOG000280724.
    HOVERGENi HBG000069.
    InParanoidi P26231.
    KOi K05691.
    OMAi WERQVRV.
    OrthoDBi EOG7HQN7B.
    PhylomeDBi P26231.
    TreeFami TF313686.

    Miscellaneous databases

    ChiTaRSi CTNNA1. mouse.
    EvolutionaryTracei P26231.
    NextBioi 281096.
    PROi P26231.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P26231.
    Bgeei P26231.
    CleanExi MM_CTNNA1.
    Genevestigatori P26231.

    Family and domain databases

    InterProi IPR001033. Alpha_catenin.
    IPR006077. Vinculin/catenin.
    IPR000633. Vinculin_CS.
    [Graphical view ]
    PANTHERi PTHR18914. PTHR18914. 1 hit.
    Pfami PF01044. Vinculin. 2 hits.
    [Graphical view ]
    PRINTSi PR00805. ALPHACATENIN.
    SUPFAMi SSF47220. SSF47220. 4 hits.
    PROSITEi PS00663. VINCULIN_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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(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.

    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: October 1, 2014
    This is version 147 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