Q59I72 (CTNA1_RABIT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Catenin alpha-1

Gene names

Name:

CTNNA1

Organism

Oryctolagus cuniculus (Rabbit) [Complete proteome]

Taxonomic identifier

9986 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

Protein attributes

Sequence length	907 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

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 adherence 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.
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. Interacts with LIMA1 By similarity.
Subcellular location	Cytoplasm › cytoskeleton By similarity. Cell junction › adherens junction By similarity. Cell membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cell junction By similarity. Note: Found at cell-cell boundaries and probably at cell-matrix boundaries By similarity.
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	Complete proteome
Gene Ontology (GO)
Biological process	cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	actin cytoskeleton Inferred from electronic annotation. Source: InterPro cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	structural molecule activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 907	906	Catenin alpha-1		PRO_0000248838
Regions
	Region	2 – 228	227	Involved in homodimerization By similarity
	Region	97 – 148	52	Interaction with JUP and CTNNB1 By similarity
	Region	326 – 395	70	Interaction with alpha-actinin By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylthreonine By similarity
	Modified residue	177	1	Phosphotyrosine By similarity
	Modified residue	186	1	N6-acetyllysine By similarity
	Modified residue	620	1	Phosphotyrosine By similarity
	Modified residue	642	1	Phosphoserine By similarity
	Modified residue	646	1	Phosphothreonine By similarity
	Modified residue	653	1	Phosphoserine By similarity
	Modified residue	655	1	Phosphothreonine By similarity
	Modified residue	656	1	Phosphoserine By similarity
	Modified residue	659	1	Phosphothreonine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q59I72 [UniParc]. Last modified April 26, 2005. Version 1. Checksum: 5F9B98B23CF36275	FASTA	907	100,173
	10 20 30 40 50 60 MTAVHAGNIN FKWDPKSLEI RTLAVERLLE PLVTQVTTLV NTNSKGPSNK KRGRSKKAHV 70 80 90 100 110 120 LAASVEQATE NFLDKGDKIA KESQFLKEEL VAAVEDVRKQ GDLMKSAAGE FADDPCSSVK 130 140 150 160 170 180 RGNMVRAARA LLSAVTRLLI LADMADVYKL LVQLKVVEDG ILKLRNAGNE QDLGIQYKAL 190 200 210 220 230 240 KPEVDKLNIM AAKRQQELKD VGHRDQMAAA RGILQKNVPI LYTASQACLQ HPDVAAYKAN 250 260 270 280 290 300 RDLIYKQLQQ AVNGISNAAQ ATTSDDASQH PGGSGGGELA YALNDFDKQI IVDPLSFSEE 310 320 330 340 350 360 RFRPSLEERL ESIISGAALM ADSSCTRDDR RERIVAECNA VRQALQDLLS EYMGNAGRKE 370 380 390 400 410 420 RSDALNSAID KMTKKTRDLR RQLRKAVMDH VSDSFLETNV PLLVLIEAAK NGNEKEVKEY 430 440 450 460 470 480 AQVFREHANK LIEVANLACS ISNNEEGVKL VRMSASQLEA LCPQVINAAL ALAAKPQSKL 490 500 510 520 530 540 AQENMDLFKE QWEKQVRVLT DAVDDITSID DFLAVSENHI LEDVNKCVIA LQEKDVDGLD 550 560 570 580 590 600 RTAGAIRGRA ARVIHVVTSE MDNYEPGVYT EKVLEATKLL SNTVMPRFTE QVEAAVEALS 610 620 630 640 650 660 SDPAQPMDEN EFIDASRLVY DGIRDIRKAV LMIRTPEELD DSDFETEDFD VRSRTSVQTE 670 680 690 700 710 720 DDQLIAGQSA RAIMAQLPQE QKAKIAEQVA SFQEEKSKLD AEVSKWDDSG NDIIVLAKQM 730 740 750 760 770 780 CMIMMEMTDF TRGKGPLKNT SDVISAAKKI AEAGSRMDKL GRTIADHCPD SACKQDLLAY 790 800 810 820 830 840 LQRIALYCHQ LNICSKVKAE VQNLGGELVV SGVDSAMSLI QAAKNLMNAV VQTVKASYVA 850 860 870 880 890 900 STKYQKSQGM ASLNLPAVSW KMKAPEKKPL VKREKQDETQ TKIKRASQKK HVNPVQALSE FKAMDSI

References

[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: 15695815] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Articular cartilage.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB193105 Genomic DNA. Translation: BAD91666.1.
RefSeq	NP_001164613.1. NM_001171142.1.
UniGene	Ocu.7440.
3D structure databases
HSSP	HSSP built from PDB template 1L7C based on UniProtKB P35221.
ProteinModelPortal	Q59I72.
SMR	Q59I72. Positions 57-261, 378-632.
ModBase	Search...
Protein-protein interaction databases
STRING	Q59I72.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	100328952.
Organism-specific databases
CTD	1495.
Phylogenomic databases
eggNOG	maNOG12937.
GeneTree	ENSGT00550000074411.
HOVERGEN	HBG000069.
OrthoDB	EOG49W2G4.
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...

Entry information

Entry name

CTNA1_RABIT

Accession

Primary (citable) accession number: Q59I72

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 5, 2006
Last sequence update:	April 26, 2005
Last modified:	January 25, 2012
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program