CTNA1_BOVIN
ID CTNA1_BOVIN Reviewed; 906 AA.
AC Q3MHM6;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=Catenin alpha-1;
GN Name=CTNNA1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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 only at cell-
CC cell boundaries.
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; BC105180; AAI05181.1; -; mRNA.
DR RefSeq; NP_001030443.1; NM_001035366.1.
DR AlphaFoldDB; Q3MHM6; -.
DR SMR; Q3MHM6; -.
DR STRING; 9913.ENSBTAP00000018863; -.
DR PaxDb; Q3MHM6; -.
DR PeptideAtlas; Q3MHM6; -.
DR PRIDE; Q3MHM6; -.
DR GeneID; 526848; -.
DR KEGG; bta:526848; -.
DR CTD; 1495; -.
DR eggNOG; KOG3681; Eukaryota.
DR InParanoid; Q3MHM6; -.
DR OrthoDB; 953344at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:InterPro.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0016342; C:catenin complex; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:InterPro.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0008013; F:beta-catenin binding; IBA:GO_Central.
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:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
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 2: Evidence at transcript level;
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..906
FT /note="Catenin alpha-1"
FT /id="PRO_0000248837"
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 325..394
FT /note="Interaction with alpha-actinin"
FT /evidence="ECO:0000250"
FT REGION 864..894
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 864..884
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 295
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35221"
FT MOD_RES 297
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35221"
FT MOD_RES 634
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P35221"
FT MOD_RES 641
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35221"
FT MOD_RES 645
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P35221"
FT MOD_RES 652
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35221"
FT MOD_RES 655
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35221"
FT MOD_RES 658
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P35221"
FT MOD_RES 851
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 797
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P35221"
SQ SEQUENCE 906 AA; 100133 MW; 71D0F32C05C4BB13 CRC64;
MTAVHTGNIN FKWDPKSLEI RTLAVERLLE PLVTQVTTLV NTNSKGPSNK KRGRSKKAHV
LAASVEQATE NFLEKGDKIA KESQFLKEEL VAAVEDVRKQ CDLMKSAAGE FADDPCSSVK
RGNMVRAARA LLSAVTRLLI LADMADVYKL LVQLKLVEDG ILKLRNAGTE QDLGIQYKAL
KPEVDKLNIM AAKRQQELKD VGHRDQMAAA RGILQKNVPI LYTASQACLQ HPDVAAYKAN
RDLIYKQLQQ AVTGISNAAQ ATASDDASQH PGAGGGELAY ALNNFDKQII VDPLSFSEER
FRPSLEERLE SIISGAALMA DSSCTRDDRR ERIVAECNAV RQALQDLLSE YMGNAGRKER
SDALNSAIDK MTKKTRDLRR QLRKAVMDHV SDSFLETNVP LLVLVEAAKN GNEKEVKEYA
QVFREHANKL IEVANLACSI SNNEEGVKLV RMSASQLEAL CPQVINAALA LAAKPQSKLA
QENMDLFKEQ WEKQVRVLTD AVDDITSIDD FLAVSENHIL EDVNKCVIAL QEKDVDGLDR
TAGAIRGRAA RVIHVVTSEM DNYEPGVYTE KVLEATKLLS NTVMPRFTEQ VEAAVEALSS
DPAQPMDENE FIDASRLVYD GIRDIRKAVL MIRTPEELDD SDFETEDFDV RSRTSVQTED
DQLIAGQSAR AIMAQLPQEQ KAKIAEQVAS FQEEKSKLDA EVSKWDDSGN DIIVLAKQMC
MIMMEMTDFT RGKGPLKNTS DVISAAKKIA EAGSRMDKLG RTIADHCPDS ACKQDLLAYL
QRIALYCHQL NICSKVKAEV QNLGGELVVS GVDSAMSLIQ AAKNLMNAVV QTVKASYVAS
TKYQKSQGMA SLNLPAVSWK MKAPEKKPLV KREKQDETQT KIKRASQKKH VNPVQALSEF
KAMDSI
