CTNA1_RABIT
ID CTNA1_RABIT Reviewed; 907 AA.
AC Q59I72;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Catenin alpha-1;
GN Name=CTNNA1;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Articular cartilage;
RX PubMed=15695815; DOI=10.1074/jbc.m413367200;
RA Hwang S.-G., Yu S.-S., Ryu J.-H., Jeon H.-B., Yoo Y.-J., Eom S.-H.,
RA Chun J.-S.;
RT "Regulation of beta-catenin signaling and maintenance of chondrocyte
RT differentiation by ubiquitin-independent proteasomal degradation of alpha-
RT catenin.";
RL J. Biol. Chem. 280:12758-12765(2005).
CC -!- FUNCTION: Associates with the cytoplasmic domain of a variety of
CC cadherins. The association of catenins to cadherins produces a complex
CC which is linked to the actin filament network, and which seems to be of
CC primary importance for cadherins cell-adhesion properties. Can
CC associate with both E- and N-cadherins. Originally believed to be a
CC stable component of E-cadherin/catenin adhesion complexes and to
CC mediate the linkage of cadherins to the actin cytoskeleton at adherens
CC junctions. In contrast, cortical actin was found to be much more
CC dynamic than E-cadherin/catenin complexes and CTNNA1 was shown not to
CC bind to F-actin when assembled in the complex suggesting a different
CC linkage between actin and adherens junctions components. The
CC homodimeric form may regulate actin filament assembly and inhibit actin
CC branching by competing with the Arp2/3 complex for binding to actin
CC filaments. Involved in the regulation of WWTR1/TAZ, YAP1 and TGFB1-
CC dependent SMAD2 and SMAD3 nuclear accumulation (By similarity). May
CC play a crucial role in cell differentiation (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:P26231}.
CC -!- SUBUNIT: Monomer and homodimer; the monomer preferentially binds to
CC CTNNB1 and the homodimer to actin (By similarity). Component of an
CC cadherin:catenin adhesion complex composed of at least of CDH26, beta-
CC catenin/CTNNB1, alpha-catenin/CTNNA1 and p120 catenin/CTNND1 (By
CC similarity). Possible component of an E-cadherin/ catenin adhesion
CC complex together with E-cadherin/CDH1 and beta-catenin/CTNNB1 or gamma-
CC catenin/JUP; the complex is located to adherens junctions (By
CC similarity). The stable association of CTNNA1 is controversial as
CC CTNNA1 was shown not to bind to F-actin when assembled in the complex
CC (By similarity). Alternatively, the CTNNA1-containing complex may be
CC linked to F-actin by other proteins such as LIMA1 (By similarity).
CC Binds AFDN and F-actin (By similarity). Interacts with ARHGAP21 (By
CC similarity). Interacts with AJUBA (By similarity). Interacts with LIMA1
CC (By similarity). Interacts with vinculin/VCL (By similarity).
CC {ECO:0000250|UniProtKB:P26231, ECO:0000250|UniProtKB:P35221}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell
CC junction, adherens junction {ECO:0000250}. Cell membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}. Cell junction {ECO:0000250}. Note=Found at cell-cell
CC boundaries and probably at cell-matrix boundaries. {ECO:0000250}.
CC -!- PTM: Sumoylated. {ECO:0000250|UniProtKB:P35221}.
CC -!- PTM: Phosphorylation seems to contribute to the strength of cell-cell
CC adhesion rather than to the basic capacity for cell-cell adhesion.
CC {ECO:0000250|UniProtKB:P26231}.
CC -!- SIMILARITY: Belongs to the vinculin/alpha-catenin family.
CC {ECO:0000305}.
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DR EMBL; AB193105; BAD91666.1; -; Genomic_DNA.
DR RefSeq; NP_001164613.1; NM_001171142.1.
DR AlphaFoldDB; Q59I72; -.
DR SMR; Q59I72; -.
DR CORUM; Q59I72; -.
DR STRING; 9986.ENSOCUP00000006694; -.
DR PRIDE; Q59I72; -.
DR GeneID; 100328952; -.
DR KEGG; ocu:100328952; -.
DR CTD; 1495; -.
DR eggNOG; KOG3681; Eukaryota.
DR InParanoid; Q59I72; -.
DR OrthoDB; 953344at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:InterPro.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR GO; GO:0008013; F:beta-catenin binding; IEA:InterPro.
DR GO; GO:0045296; F:cadherin binding; IEA:InterPro.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0007015; P:actin filament organization; IEA:InterPro.
DR GO; GO:0090136; P:epithelial cell-cell adhesion; IEA:InterPro.
DR GO; GO:1900181; P:negative regulation of protein localization to nucleus; ISS:UniProtKB.
DR InterPro; IPR036723; Alpha-catenin/vinculin-like_sf.
DR InterPro; IPR001033; Alpha_catenin.
DR InterPro; IPR030047; CTNNA1/CTNNA3.
DR InterPro; IPR006077; Vinculin/catenin.
DR InterPro; IPR000633; Vinculin_CS.
DR PANTHER; PTHR18914:SF24; PTHR18914:SF24; 1.
DR Pfam; PF01044; Vinculin; 2.
DR PRINTS; PR00805; ALPHACATENIN.
DR SUPFAM; SSF47220; SSF47220; 4.
DR PROSITE; PS00663; VINCULIN_1; 1.
PE 3: Inferred from homology;
KW Acetylation; Cell adhesion; Cell junction; Cell membrane; Cytoplasm;
KW Cytoskeleton; Isopeptide bond; Membrane; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P35221"
FT CHAIN 2..907
FT /note="Catenin alpha-1"
FT /id="PRO_0000248838"
FT REGION 2..228
FT /note="Involved in homodimerization"
FT /evidence="ECO:0000250"
FT REGION 97..148
FT /note="Interaction with JUP and CTNNB1"
FT /evidence="ECO:0000250"
FT REGION 326..395
FT /note="Interaction with alpha-actinin"
FT /evidence="ECO:0000250"
FT REGION 865..895
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 865..885
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000250|UniProtKB:P35221"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35221"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35221"
FT MOD_RES 296
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35221"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35221"
FT MOD_RES 635
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P35221"
FT MOD_RES 642
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35221"
FT MOD_RES 646
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P35221"
FT MOD_RES 653
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35221"
FT MOD_RES 656
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35221"
FT MOD_RES 659
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P35221"
FT MOD_RES 852
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35221"
FT CROSSLNK 57
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P35221"
FT CROSSLNK 798
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P35221"
SQ SEQUENCE 907 AA; 100173 MW; 5F9B98B23CF36275 CRC64;
MTAVHAGNIN FKWDPKSLEI RTLAVERLLE PLVTQVTTLV NTNSKGPSNK KRGRSKKAHV
LAASVEQATE NFLDKGDKIA KESQFLKEEL VAAVEDVRKQ GDLMKSAAGE FADDPCSSVK
RGNMVRAARA LLSAVTRLLI LADMADVYKL LVQLKVVEDG ILKLRNAGNE QDLGIQYKAL
KPEVDKLNIM AAKRQQELKD VGHRDQMAAA RGILQKNVPI LYTASQACLQ HPDVAAYKAN
RDLIYKQLQQ AVNGISNAAQ ATTSDDASQH PGGSGGGELA YALNDFDKQI IVDPLSFSEE
RFRPSLEERL ESIISGAALM ADSSCTRDDR RERIVAECNA VRQALQDLLS EYMGNAGRKE
RSDALNSAID KMTKKTRDLR RQLRKAVMDH VSDSFLETNV PLLVLIEAAK NGNEKEVKEY
AQVFREHANK LIEVANLACS ISNNEEGVKL VRMSASQLEA LCPQVINAAL ALAAKPQSKL
AQENMDLFKE QWEKQVRVLT DAVDDITSID DFLAVSENHI LEDVNKCVIA LQEKDVDGLD
RTAGAIRGRA ARVIHVVTSE MDNYEPGVYT EKVLEATKLL SNTVMPRFTE QVEAAVEALS
SDPAQPMDEN EFIDASRLVY DGIRDIRKAV LMIRTPEELD DSDFETEDFD VRSRTSVQTE
DDQLIAGQSA RAIMAQLPQE QKAKIAEQVA SFQEEKSKLD AEVSKWDDSG NDIIVLAKQM
CMIMMEMTDF TRGKGPLKNT SDVISAAKKI AEAGSRMDKL GRTIADHCPD SACKQDLLAY
LQRIALYCHQ LNICSKVKAE VQNLGGELVV SGVDSAMSLI QAAKNLMNAV VQTVKASYVA
STKYQKSQGM ASLNLPAVSW KMKAPEKKPL VKREKQDETQ TKIKRASQKK HVNPVQALSE
FKAMDSI
