ID F6WBD5_ORNAN Unreviewed; 744 AA.
AC F6WBD5;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 2.
DT 27-MAR-2024, entry version 90.
DE RecName: Full=Catenin beta-1 {ECO:0000256|ARBA:ARBA00039590};
DE AltName: Full=Beta-catenin {ECO:0000256|ARBA:ARBA00042006};
GN Name=CTNNB1 {ECO:0000313|Ensembl:ENSOANP00000010865.3};
OS Ornithorhynchus anatinus (Duckbill platypus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Monotremata; Ornithorhynchidae; Ornithorhynchus.
OX NCBI_TaxID=9258 {ECO:0000313|Ensembl:ENSOANP00000010865.3, ECO:0000313|Proteomes:UP000002279};
RN [1] {ECO:0000313|Ensembl:ENSOANP00000010865.3}
RP IDENTIFICATION.
RC STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000010865.3};
RG Ensembl;
RL Submitted (NOV-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 AlphaFoldDB; F6WBD5; -.
DR STRING; 9258.ENSOANP00000010865; -.
DR Ensembl; ENSOANT00000010867.4; ENSOANP00000010865.3; ENSOANG00000006811.4.
DR eggNOG; KOG4203; Eukaryota.
DR GeneTree; ENSGT00940000155471; -.
DR HOGENOM; CLU_008757_1_1_1; -.
DR InParanoid; F6WBD5; -.
DR OMA; YPKLVYT; -.
DR OrthoDB; 50711at2759; -.
DR TreeFam; TF317997; -.
DR Proteomes; UP000002279; Unplaced.
DR Bgee; ENSOANG00000006811; Expressed in endometrium and 8 other cell types or tissues.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0005938; C:cell cortex; IEA:Ensembl.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0045294; F:alpha-catenin binding; IBA:GO_Central.
DR GO; GO:0045296; F:cadherin binding; IBA:GO_Central.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IBA:GO_Central.
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:0019903; F:protein phosphatase binding; IBA:GO_Central.
DR GO; GO:0005102; F:signaling receptor binding; IEA:Ensembl.
DR GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
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; IBA:GO_Central.
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 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 3: Inferred from homology;
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:UP000002279};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT REPEAT 114..154
FT /note="ARM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT REPEAT 156..199
FT /note="ARM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT REPEAT 198..240
FT /note="ARM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT REPEAT 240..282
FT /note="ARM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT REPEAT 282..325
FT /note="ARM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT REPEAT 363..405
FT /note="ARM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT REPEAT 405..447
FT /note="ARM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT REPEAT 452..495
FT /note="ARM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT REPEAT 557..599
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 670..744
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 744 AA; 81458 MW; B7AAE711BA8F294D CRC64;
MATQADLMEL DMAMEPDRKA AVSHWQQQSY LDSGIHSGAT TTAPSLSGKG NPEEEDVDTT
QVLYEWEQGF SQSFTQEQVA DIDGQYAMTR AQRMLKHAVV NLINYQDDAE LATRAIPELT
KLLNDEDQVV VNKAAVMVHQ LSKKEASRHA IMRSPQMVSA IVRTMQNTND VETARCTAGT
LHNLSHHREG LLAIFKSGGI PALVKMLGSP VDSVLFYAIT TLHNLLLHQE GAKMAVRLAG
GLQKMVALLN KTNVKFLAIT TDCLQILAYG NQESKLIILA SGGPQALVNI MRTYTYEKLL
WTTSRVLKVL SVCSSNKPAI VEAGGMQALG LHLTDPSQRL VQNCLWTLRN LSDAATKQEG
MEGLLGTLVQ LLGSDDINVV TCAAGILSNL TCNNYKNKMM VCQVGGIEAL VRTVLRAGDR
EDITEPAICA LRHLTSRHQE AEMAQNAVRL HYGLPVVVKL LHPPSHWPLI KATVGLIRNL
ALCPANHAPL REQGAIPRLV QLLVRAHQDT QRRTSMGGTQ QQFVEGVRME EIVEGCTGAL
HILARDVHNR IVIRGLNTIP LFVQLLYSPI ENIQRVAAGV LCELAQDKEA AEAIEAEGAT
APLTELLHSR NEGVATYAAA VLFRMSEDKP QDYKKRLSVE LTSSLFRTEP MAWNETADLG
LDIAAQGEPL GYRQDDPSYR SFHSGGYGQD ALGMDPMMEH EMGGHHPGAD YPVDGLPDLG
HAQDLMDGLP PGDSNQLAWF DTDL
//
