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Protein

Catenin alpha-1

Gene

CTNNA1

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Names & Taxonomyi

Protein namesi
Recommended name:
Catenin alpha-1
Gene namesi
Name:CTNNA1
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
Proteomesi
  • UP000001811 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 907906Catenin alpha-1PRO_0000248838Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonineBy similarity
Modified residuei264 – 2641PhosphoserineBy similarity
Modified residuei268 – 2681PhosphoserineBy similarity
Modified residuei296 – 2961PhosphoserineBy similarity
Modified residuei298 – 2981PhosphoserineBy similarity
Modified residuei635 – 6351PhosphothreonineBy similarity
Modified residuei642 – 6421PhosphoserineBy similarity
Modified residuei646 – 6461PhosphothreonineBy similarity
Modified residuei653 – 6531PhosphoserineBy similarity
Modified residuei656 – 6561PhosphoserineBy similarity
Modified residuei659 – 6591PhosphothreonineBy similarity
Modified residuei852 – 8521PhosphoserineBy similarity

Post-translational modificationi

Sumoylated.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

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. Interacts with LIMA1 (By similarity).By similarity

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000006694.

Structurei

3D structure databases

ProteinModelPortaliQ59I72.
SMRiQ59I72. Positions 57-261, 378-632.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 228227Involved in homodimerizationBy similarityAdd
BLAST
Regioni97 – 14852Interaction with JUP and CTNNB1By similarityAdd
BLAST
Regioni326 – 39570Interaction with alpha-actininBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the vinculin/alpha-catenin family.Curated

Phylogenomic databases

eggNOGiKOG3681. Eukaryota.
ENOG410XSRU. LUCA.
HOGENOMiHOG000280724.
HOVERGENiHBG000069.
InParanoidiQ59I72.
KOiK05691.

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.

Q59I72-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTAVHAGNIN FKWDPKSLEI RTLAVERLLE PLVTQVTTLV NTNSKGPSNK
60 70 80 90 100
KRGRSKKAHV LAASVEQATE NFLDKGDKIA KESQFLKEEL VAAVEDVRKQ
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
VGHRDQMAAA RGILQKNVPI LYTASQACLQ HPDVAAYKAN RDLIYKQLQQ
260 270 280 290 300
AVNGISNAAQ ATTSDDASQH PGGSGGGELA YALNDFDKQI IVDPLSFSEE
310 320 330 340 350
RFRPSLEERL ESIISGAALM ADSSCTRDDR RERIVAECNA VRQALQDLLS
360 370 380 390 400
EYMGNAGRKE RSDALNSAID KMTKKTRDLR RQLRKAVMDH VSDSFLETNV
410 420 430 440 450
PLLVLIEAAK NGNEKEVKEY AQVFREHANK LIEVANLACS ISNNEEGVKL
460 470 480 490 500
VRMSASQLEA LCPQVINAAL ALAAKPQSKL AQENMDLFKE QWEKQVRVLT
510 520 530 540 550
DAVDDITSID DFLAVSENHI LEDVNKCVIA LQEKDVDGLD RTAGAIRGRA
560 570 580 590 600
ARVIHVVTSE MDNYEPGVYT EKVLEATKLL SNTVMPRFTE QVEAAVEALS
610 620 630 640 650
SDPAQPMDEN EFIDASRLVY DGIRDIRKAV LMIRTPEELD DSDFETEDFD
660 670 680 690 700
VRSRTSVQTE DDQLIAGQSA RAIMAQLPQE QKAKIAEQVA SFQEEKSKLD
710 720 730 740 750
AEVSKWDDSG NDIIVLAKQM CMIMMEMTDF TRGKGPLKNT SDVISAAKKI
760 770 780 790 800
AEAGSRMDKL GRTIADHCPD SACKQDLLAY LQRIALYCHQ LNICSKVKAE
810 820 830 840 850
VQNLGGELVV SGVDSAMSLI QAAKNLMNAV VQTVKASYVA STKYQKSQGM
860 870 880 890 900
ASLNLPAVSW KMKAPEKKPL VKREKQDETQ TKIKRASQKK HVNPVQALSE

FKAMDSI
Length:907
Mass (Da):100,173
Last modified:April 26, 2005 - v1
Checksum:i5F9B98B23CF36275
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB193105 Genomic DNA. Translation: BAD91666.1.
RefSeqiNP_001164613.1. NM_001171142.1.
UniGeneiOcu.1707.

Genome annotation databases

GeneIDi100328952.
KEGGiocu:100328952.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB193105 Genomic DNA. Translation: BAD91666.1.
RefSeqiNP_001164613.1. NM_001171142.1.
UniGeneiOcu.1707.

3D structure databases

ProteinModelPortaliQ59I72.
SMRiQ59I72. Positions 57-261, 378-632.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000006694.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100328952.
KEGGiocu:100328952.

Organism-specific databases

CTDi1495.

Phylogenomic databases

eggNOGiKOG3681. Eukaryota.
ENOG410XSRU. LUCA.
HOGENOMiHOG000280724.
HOVERGENiHBG000069.
InParanoidiQ59I72.
KOiK05691.

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

  1. "Regulation of beta-catenin signaling and maintenance of chondrocyte differentiation by ubiquitin-independent proteasomal degradation of alpha-catenin."
    Hwang S.-G., Yu S.-S., Ryu J.-H., Jeon H.-B., Yoo Y.-J., Eom S.-H., Chun J.-S.
    J. Biol. Chem. 280:12758-12765(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Articular cartilage.

Entry informationi

Entry nameiCTNA1_RABIT
AccessioniPrimary (citable) accession number: Q59I72
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: April 26, 2005
Last modified: December 9, 2015
This is version 70 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

Complete proteome, Reference proteome

Documents

  1. 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.