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Database: UniProt
Entry: U6CUG1_NEOVI
LinkDB: U6CUG1_NEOVI
Original site: U6CUG1_NEOVI 
ID   U6CUG1_NEOVI            Unreviewed;       781 AA.
AC   U6CUG1;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=Catenin beta-1 {ECO:0000256|ARBA:ARBA00039590};
DE   AltName: Full=Beta-catenin {ECO:0000256|ARBA:ARBA00042006};
GN   Name=CTNB1 {ECO:0000313|EMBL:CCP73253.1};
OS   Neovison vison (American mink) (Mustela vison).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Mustelinae; Neogale.
OX   NCBI_TaxID=452646 {ECO:0000313|EMBL:CCP73253.1};
RN   [1] {ECO:0000313|EMBL:CCP73253.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Pool of brain {ECO:0000313|EMBL:CCP73253.1};
RA   Anistoroaei R., Christensen K.;
RT   "An American mink transcriptome.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSNVIP00000031759.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cell junction, adherens junction
CC       {ECO:0000256|ARBA:ARBA00004536}. Cell membrane
CC       {ECO:0000256|ARBA:ARBA00004236}. Cytoplasm
CC       {ECO:0000256|ARBA:ARBA00004496}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004370}. Nucleus
CC       {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the beta-catenin family.
CC       {ECO:0000256|ARBA:ARBA00005462}.
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DR   EMBL; HAAF01001427; CCP73253.1; -; mRNA.
DR   SMR; U6CUG1; -.
DR   Ensembl; ENSNVIT00000036798.1; ENSNVIP00000031759.1; ENSNVIG00000024433.1.
DR   GeneTree; ENSGT00940000155471; -.
DR   OrthoDB; 50711at2759; -.
DR   Proteomes; UP000694425; Unplaced.
DR   GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
DR   GO; GO:0030877; C:beta-catenin destruction complex; IEA:Ensembl.
DR   GO; GO:0070369; C:beta-catenin-TCF7L2 complex; IEA:Ensembl.
DR   GO; GO:0016342; C:catenin complex; IEA:Ensembl.
DR   GO; GO:0005938; C:cell cortex; IEA:Ensembl.
DR   GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0000791; C:euchromatin; IEA:Ensembl.
DR   GO; GO:0016328; C:lateral plasma membrane; IEA:Ensembl.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR   GO; GO:0045294; F:alpha-catenin binding; IEA:Ensembl.
DR   GO; GO:0045296; F:cadherin binding; IEA:Ensembl.
DR   GO; GO:0070411; F:I-SMAD binding; IEA:Ensembl.
DR   GO; GO:0019900; F:kinase binding; IEA:Ensembl.
DR   GO; GO:0030331; F:nuclear estrogen receptor binding; IEA:Ensembl.
DR   GO; GO:0005102; F:signaling receptor binding; IEA:Ensembl.
DR   GO; GO:0003713; F:transcription coactivator activity; IEA:Ensembl.
DR   GO; GO:0001222; F:transcription corepressor binding; IEA:Ensembl.
DR   GO; GO:0044325; F:transmembrane transporter binding; IEA:Ensembl.
DR   GO; GO:0034333; P:adherens junction assembly; IEA:Ensembl.
DR   GO; GO:0001569; P:branching involved in blood vessel morphogenesis; IEA:Ensembl.
DR   GO; GO:0060070; P:canonical Wnt signaling pathway; IEA:Ensembl.
DR   GO; GO:0098609; P:cell-cell adhesion; IEA:Ensembl.
DR   GO; GO:0071363; P:cellular response to growth factor stimulus; IEA:Ensembl.
DR   GO; GO:0071681; P:cellular response to indole-3-methanol; IEA:Ensembl.
DR   GO; GO:0061154; P:endothelial tube morphogenesis; IEA:Ensembl.
DR   GO; GO:0072497; P:mesenchymal stem cell differentiation; IEA:Ensembl.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; IEA:Ensembl.
DR   GO; GO:0033234; P:negative regulation of protein sumoylation; IEA:Ensembl.
DR   GO; GO:1990138; P:neuron projection extension; IEA:Ensembl.
DR   GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl.
DR   GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IEA:Ensembl.
DR   GO; GO:0010909; P:positive regulation of heparan sulfate proteoglycan biosynthetic process; IEA:Ensembl.
DR   GO; GO:0043525; P:positive regulation of neuron apoptotic process; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR   GO; GO:0034394; P:protein localization to cell surface; IEA:Ensembl.
DR   GO; GO:0000209; P:protein polyubiquitination; IEA:Ensembl.
DR   GO; GO:0090279; P:regulation of calcium ion import; IEA:Ensembl.
DR   GO; GO:0030997; P:regulation of centriole-centriole cohesion; IEA:Ensembl.
DR   GO; GO:0070602; P:regulation of centromeric sister chromatid cohesion; IEA:Ensembl.
DR   GO; GO:2000008; P:regulation of protein localization to cell surface; IEA:Ensembl.
DR   GO; GO:0031396; P:regulation of protein ubiquitination; IEA:Ensembl.
DR   GO; GO:0048660; P:regulation of smooth muscle cell proliferation; IEA:Ensembl.
DR   GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR   CDD; cd21724; CTNNAbd_CTNNB1; 1.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000225; Armadillo.
DR   InterPro; IPR013284; Beta-catenin.
DR   PANTHER; PTHR45976; ARMADILLO SEGMENT POLARITY PROTEIN; 1.
DR   PANTHER; PTHR45976:SF4; CATENIN BETA-1; 1.
DR   Pfam; PF00514; Arm; 4.
DR   PRINTS; PR01869; BCATNINFAMLY.
DR   SMART; SM00185; ARM; 12.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   PROSITE; PS50176; ARM_REPEAT; 9.
PE   2: Evidence at transcript level;
KW   Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000694425};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT   REPEAT          151..191
FT                   /note="ARM"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT   REPEAT          193..236
FT                   /note="ARM"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT   REPEAT          235..277
FT                   /note="ARM"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT   REPEAT          277..319
FT                   /note="ARM"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT   REPEAT          319..362
FT                   /note="ARM"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT   REPEAT          400..442
FT                   /note="ARM"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT   REPEAT          442..484
FT                   /note="ARM"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT   REPEAT          489..532
FT                   /note="ARM"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT   REPEAT          594..636
FT                   /note="ARM"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT   REGION          34..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          705..781
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..48
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   781 AA;  85511 MW;  6148652F953F0723 CRC64;
     MATQADLMEL DMAMEPDRKA AVSHWQQQSY LDSGIHSGAT TTAPSLSGKG NPEEEDVDTT
     QVLYEWEQGF SQSFTQEQVA DIDGQYAMTR AQRVRAAMFP ETLDEGMQIP STQFDAAHPT
     NVQRLAEPSQ MLKHAVVNLI NYQDDAELAT RAIPELTKLL NDEDQVVVNK AAVMVHQLSK
     KEASRHAIMR SPQMVSAIVR TMQNTNDVET ARCTAGTLHN LSHHREGLLA IFKSGGIPAL
     VKMLGSPVDS VLFYAITTLH NLLLHQEGAK MAVRLAGGLQ KMVALLNKTN VKFLAITTDC
     LQILAYGNQE SKLIILASGG PQALVNIMRT YTYEKLLWTT SRVLKVLSVC SSNKPAIVEA
     GGMQALGLHL TDPSQRLVQN CLWTLRNLSD AATKQEGMEG LLGTLVQLLG SDDINVVTCA
     AGILSNLTCN NYKNKMMVCQ VGGIEALVRT VLRAGDREDI TEPAICALRH LTSRHQEAEM
     AQNAVRLHYG LPVVVKLLHP PSHWPLIKAT VGLIRNLALC PANHAPLREQ GAIPRLVQLL
     VRAHQDTQRR TSMGGTQQQF VEGVRMEEIV EGCTGALHIL ARDVHNRIVI RGLNTIPLFV
     QLLYSPIENI QRVAAGVLCE LAQDKEAAEA IEAEGATAPL TELLHSRNEG VATYAAAVLF
     RMSEDKPQDY KKRLSVELTS SLFRTEPMAW NETADLGLDI GAQGEPLGYR QDDPSYRSFH
     SGGYGQDALG MDPMMEHEMG GHHPGADYPV DGLPDLGHAQ DLMDGLPPGD SNQLAWFDTD
     L
//
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