P26231 (CTNA1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Catenin alpha-1

Alternative name(s):
102 kDa cadherin-associated protein
Alpha E-catenin
CAP102

Gene names

Name:	Ctnna1
Synonyms:	Catna1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	906 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.7
Subunit structure	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. Ref.4 Ref.7 Ref.14 Ref.17
Subcellular location	Cytoplasm › cytoskeleton. Cell junction › adherens junction. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell junction. Note: Found at cell-cell boundaries and probably at cell-matrix boundaries.
Tissue specificity	Expressed ubiquitously in normal tissues.
Post-translational modification	Sumoylated By similarity.
Sequence similarities	Belongs to the vinculin/alpha-catenin family.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Cell junction Cell membrane Cytoplasm Cytoskeleton Membrane
PTM	Acetylation Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	aging Inferred from electronic annotation. Source: Compara apical junction assembly Inferred from mutant phenotype PubMed 16543460. Source: MGI axon regeneration Inferred from electronic annotation. Source: Compara cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW cellular response to indole-3-methanol Inferred from electronic annotation. Source: Compara establishment or maintenance of cell polarity Inferred from mutant phenotype PubMed 16543460. Source: MGI gap junction assembly Inferred from electronic annotation. Source: Compara male gonad development Inferred from electronic annotation. Source: Compara negative regulation of apoptotic process Inferred from mutant phenotype PubMed 16543460. Source: MGI negative regulation of neuroblast proliferation Inferred from mutant phenotype PubMed 16543460. Source: MGI odontogenesis of dentin-containing tooth Inferred from electronic annotation. Source: Compara ovarian follicle development Inferred from electronic annotation. Source: Compara positive regulation of smoothened signaling pathway Inferred from genetic interaction PubMed 16543460. Source: MGI protein heterooligomerization Inferred from electronic annotation. Source: Compara response to estrogen stimulus Inferred from electronic annotation. Source: Compara
Cellular_component	acrosomal vesicle Inferred from electronic annotation. Source: Compara actin cytoskeleton Inferred from electronic annotation. Source: InterPro catenin complex Inferred from electronic annotation. Source: Compara intercalated disc Inferred from direct assay PubMed 17535849. Source: MGI lamellipodium Inferred from direct assay PubMed 14657280. Source: MGI plasma membrane Inferred from direct assay PubMed 16510873. Source: MGI zonula adherens Inferred from direct assay PubMed 11025210. Source: MGI
Molecular_function	actin filament binding Inferred from direct assay PubMed 11795944. Source: MGI structural molecule activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CTNNB1	P35222	2	EBI-647895,EBI-491549	From a different organism.
Ctnnb1	Q02248	2	EBI-647895,EBI-397872

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 906

905

Catenin alpha-1

PRO_0000064262

Regions

Region

2 – 228

227

Involved in homodimerization By similarity

Region

97 – 148

52

Interaction with JUP and CTNNB1 By similarity

Region

325 – 394

70

Interaction with alpha-actinin By similarity

Amino acid modifications

Modified residue

2

1

N-acetylthreonine By similarity

Modified residue

634

1

Phosphothreonine By similarity

Modified residue

641

1

Phosphoserine Ref.5 Ref.9 Ref.10 Ref.12 Ref.13 Ref.15

Modified residue

645

1

Phosphothreonine By similarity

Modified residue

652

1

Phosphoserine Ref.8 Ref.12

Modified residue

654

1

Phosphothreonine Ref.5 Ref.11

Modified residue

655

1

Phosphoserine Ref.8 Ref.11

Modified residue

658

1

Phosphothreonine Ref.5 Ref.11

Secondary structure

1

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906

Helix Strand Turn

Details...

Helix

59 – 82

24

Beta strand

84 – 86

3

Helix

87 – 113

27

Helix

118 – 165

48

Helix

170 – 195

26

Helix

201 – 230

30

Helix

235 – 259

25

Helix

305 – 315

11

Helix

328 – 352

25

Helix

392 – 396

5

Helix

399 – 409

11

Helix

413 – 440

28

Helix

444 – 473

30

Helix

478 – 506

29

Helix

508 – 531

24

Helix

535 – 560

26

Helix

567 – 581

15

Helix

583 – 598

16

Helix

608 – 629

22

Sequences

	Sequence		Length	Mass (Da)
	P26231 [UniParc]. Last modified May 1, 1992. Version 1. Checksum: 3ED1EC50925DBBB5	FASTA	906	100,106
	10 20 30 40 50 60 MTAVHAGNIN FKWDPKSLEI RTLAVERLLE PLVTQVTTLV NTNSKGPSNK KRGRSKKAHV 70 80 90 100 110 120 LAASVEQATE NFLEKGDKIA KESQFLKEEL VVAVEDVRKQ GDLMKSAAGE FADDPCSSVK 130 140 150 160 170 180 RGNMVRAARA LLSAVTRLLI LADMADVYKL LVQLKVVEDG ILKLRNAGNE QDLGIQYKAL 190 200 210 220 230 240 KPEVDKLNIM AAKRQQELKD VGNRDQMAAA RGILQKNVPI LYTASQACLQ HPDVAAYKAN 250 260 270 280 290 300 RDLIYKQLQQ AVTGISNAAQ ATASDDAAQH QGGSGGELAY ALNNFDKQII VDPLSFSEER 310 320 330 340 350 360 FRPSLEERLE SIISGAALMA DSSCTRDDRR ERIVAECNAV RQALQDLLSE YMGNAGRKER 370 380 390 400 410 420 SDALNSAIDK MTKKTRDLRR QLRKAVMDHV SDSFLETNVP LLVLIEAAKN GNEKEVKEYA 430 440 450 460 470 480 QVFREHANKL IEVANLACSI SNNEEGVKLV RMSASQLEAL CPQVINAALA LAAKPQSKLA 490 500 510 520 530 540 QENMDLFKEQ WEKQVRVLTD AVDDITSIDD FLAVSENHIL EDVNKCVIAL QEKDVDGLDR 550 560 570 580 590 600 TAGAIRGRAA RVIHVVTSEM DNYEPGVYTE KVLEATKLLS NTVMPRFTEQ VEAAVEALSS 610 620 630 640 650 660 DPAQPMDENE FIDASRLVYD GIRDIRKAVL MIRTPEELDD SDFETEDFDV RSRTSVQTED 670 680 690 700 710 720 DQLIAGQSAR AIMAQLPQEQ KAKIAEQVAS FQEEKSKLDA EVSKWDDSGN DIIVLAKQMC 730 740 750 760 770 780 MIMMEMTDFT RGKGPLKNTS DVISAAKKIA EAGSRMDKLG RTIADHCPDS ACKQDLLAYL 790 800 810 820 830 840 QRIALYCHQL NICSKVKAEV QNLGGELVVS GVDSAMSLIQ AAKNLMNAVV QTVKASYVAS 850 860 870 880 890 900 TKYQKSQGMA SLNLPAVSWK MKAPEKKPLV KREKQDETQT KIKRASQKKH VNPVQALSEF KAMDSI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The uvomorulin-anchorage protein alpha catenin is a vinculin homologue." Herrenknecht K., Ozawa M., Eckerskorn C., Lottspeich F., Lenter M., Kemler R. Proc. Natl. Acad. Sci. U.S.A. 88:9156-9160(1991) [PubMed] [Europe PMC] [Abstract] 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]	"Phosphoproteomic analysis of the developing mouse brain." Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P. Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641; THR-654 AND THR-658, MASS SPECTROMETRY. Tissue: Embryonic brain.
[6]	"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.
[7]	"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.
[8]	"Proteomic analysis of in vivo phosphorylated synaptic proteins." Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I., Blackstock W.P., Choudhary J.S., Grant S.G. J. Biol. Chem. 280:5972-5982(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-652 AND SER-655, MASS SPECTROMETRY. Tissue: Forebrain.
[9]	"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry." Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R. J. Proteome Res. 6:250-262(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, MASS SPECTROMETRY. Tissue: Liver.
[10]	"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations." Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M. Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, MASS SPECTROMETRY. Tissue: Brain cortex.
[11]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-654; SER-655 AND THR-658, MASS SPECTROMETRY. Tissue: Liver.
[12]	"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 AND SER-652, MASS SPECTROMETRY. Tissue: Liver.
[13]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, MASS SPECTROMETRY. Tissue: Melanoma.
[14]	"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.
[15]	"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, MASS SPECTROMETRY. Tissue: Embryonic fibroblast.
[16]	"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.
[17]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X59990 mRNA. Translation: CAA42607.1.
D90362 mRNA. Translation: BAA14376.1.
BC048163 mRNA. Translation: AAH48163.1.

IPI

IPI00112963.

PIR

A39529.

RefSeq

NP_033948.1. NM_009818.1.

UniGene

Mm.18962.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P26231.

SMR

P26231. Positions 22-878.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-35299N.

IntAct

P26231. 10 interactions.

MINT

MINT-138480.

PTM databases

PhosphoSite

P26231.

Proteomic databases

PaxDb

P26231.

PRIDE

P26231.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000042345; ENSMUSP00000049007; ENSMUSG00000037815.

GeneID

12385.

KEGG

mmu:12385.

UCSC

uc008ely.1. mouse.

Organism-specific databases

CTD

1495.

MGI

MGI:88274. Ctnna1.

Phylogenomic databases

eggNOG

NOG240050.

HOGENOM

HOG000280724.

HOVERGEN

HBG000069.

InParanoid

P26231.

KO

K05691.

OMA

VHTGNIN.

OrthoDB

EOG49W2G4.

Enzyme and pathway databases

Reactome

REACT_93132. Metabolism of proteins.

Gene expression databases

ArrayExpress

P26231.

Bgee

P26231.

CleanEx

MM_CTNNA1.

Genevestigator

P26231.

GermOnline

ENSMUSG00000037815. Mus musculus.

Family and domain databases

InterPro

IPR001033. Alpha_catenin.
IPR006077. Vinculin/catenin.
IPR000633. Vinculin_CS.
[Graphical view]

Pfam

PF01044. Vinculin. 2 hits.
[Graphical view]

PRINTS

PR00805. ALPHACATENIN.

SUPFAM

SSF47220. Vinculin/catenin. 4 hits.

PROSITE

PS00663. VINCULIN_1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

CTNNA1. mouse.

EvolutionaryTrace

P26231.

NextBio

281096.

SOURCE

Search...

Entry information

Entry name

CTNA1_MOUSE

Accession

Primary (citable) accession number: P26231

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	May 1, 1992
Last modified:	May 29, 2013
This is version 134 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program