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P26231

- CTNA1_MOUSE

UniProt

P26231 - CTNA1_MOUSE

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Protein

Catenin alpha-1

Gene

Ctnna1

Organism
Mus musculus (Mouse)
Status
Reviewed - 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. poly(A) RNA binding Source: Ensembl
  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
Complete GO annotation...

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
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 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

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 – 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 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.
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

        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:
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 19-878.
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

Bgeei P26231.
CleanExi MM_CTNNA1.
ExpressionAtlasi P26231. baseline and differential.
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

« 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(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 29, 2014
This is version 148 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