CTNB1_XENLA
ID CTNB1_XENLA Reviewed; 781 AA.
AC P26233;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Catenin beta-1;
DE AltName: Full=Beta-catenin;
GN Name=ctnnb1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Brain;
RX PubMed=1962194; DOI=10.1126/science.1962194;
RA McCrea P.D., Turck C.W., Gumbiner B.M.;
RT "A homolog of the armadillo protein in Drosophila (plakoglobin) associated
RT with E-cadherin.";
RL Science 254:1359-1361(1991).
RN [2]
RP INTERACTION WITH CDH3.
RX PubMed=17052462; DOI=10.1016/j.molcel.2006.09.001;
RA Sampietro J., Dahlberg C.L., Cho U.S., Hinds T.R., Kimelman D., Xu W.;
RT "Crystal structure of a beta-catenin/BCL9/Tcf4 complex.";
RL Mol. Cell 24:293-300(2006).
RN [3]
RP INTERACTION WITH CUSTOS, AND SUBCELLULAR LOCATION.
RX PubMed=25157132; DOI=10.1073/pnas.1414437111;
RA Komiya Y., Mandrekar N., Sato A., Dawid I.B., Habas R.;
RT "Custos controls beta-catenin to regulate head development during
RT vertebrate embryogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:13099-13104(2014).
CC -!- FUNCTION: Key downstream component of the canonical Wnt signaling
CC pathway. In the absence of Wnt, forms a complex with axin1, axin2, apc,
CC csnk1a1 and gsk3b that promotes phosphorylation on N-terminal Ser and
CC Thr residues and ubiquitination of ctnnb1 and its subsequent
CC degradation by the proteasome. In the presence of Wnt ligand, ctnnb1 is
CC not ubiquitinated and accumulates in the nucleus, where it acts as a
CC coactivator for transcription factors of the TCF/LEF family, leading to
CC activate Wnt responsive genes (By similarity). Plays a key role in
CC dorsoventral patterning: in prospective ventral blastomeres, its down-
CC regulation by axin1 and axin2 leads to inhibit the Wnt signaling
CC pathway, while in prospective dorsal blastomeres, degradation of axin
CC results in stabilization and nuclear translocation of ctnnb1 (By
CC similarity). {ECO:0000250|UniProtKB:F1QGH7,
CC ECO:0000250|UniProtKB:P35222, ECO:0000250|UniProtKB:Q02248}.
CC -!- SUBUNIT: Interacts with EP-Cadherin/CDH3 (PubMed:17052462). Interacts
CC with custos; the interaction is positively regulated by Wnt stimulation
CC (PubMed:25157132). {ECO:0000269|PubMed:17052462,
CC ECO:0000269|PubMed:25157132}.
CC -!- INTERACTION:
CC P26233; A0SNQ7: tshz3.L; NbExp=3; IntAct=EBI-7373758, EBI-7373787;
CC P26233; Q61473: Sox17; Xeno; NbExp=3; IntAct=EBI-7373758, EBI-9106822;
CC P26233; P15884: TCF4; Xeno; NbExp=2; IntAct=EBI-7373758, EBI-533224;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P35222}. Nucleus
CC {ECO:0000269|PubMed:25157132}. Cell membrane
CC {ECO:0000250|UniProtKB:F1QGH7}. Note=Cytoplasmic when it is
CC unstabilized (high level of phosphorylation). Translocates to the
CC nucleus when it is stabilized (low level of phosphorylation). The
CC majority of beta-catenin is localized to the cell membrane (By
CC similarity). Reduced nuclear localization seen in the presence of
CC custos (PubMed:25157132). {ECO:0000250|UniProtKB:B6V8E6,
CC ECO:0000250|UniProtKB:P35222, ECO:0000269|PubMed:25157132}.
CC -!- PTM: Phosphorylation by gsk3b promotes ubiquitination and subsequent
CC degradation by the proteasome. {ECO:0000250|UniProtKB:P35222}.
CC -!- PTM: Ubiquitinated when phosphorylated by gsk3b, leading to its
CC degradation. {ECO:0000250|UniProtKB:P35222}.
CC -!- SIMILARITY: Belongs to the beta-catenin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M77013; AAA49670.1; -; mRNA.
DR PIR; S35099; S35099.
DR AlphaFoldDB; P26233; -.
DR SMR; P26233; -.
DR DIP; DIP-44044N; -.
DR IntAct; P26233; 8.
DR MINT; P26233; -.
DR PRIDE; P26233; -.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0045178; C:basal part of cell; IDA:BHF-UCL.
DR GO; GO:0005911; C:cell-cell junction; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045296; F:cadherin binding; IEA:InterPro.
DR GO; GO:0048738; P:cardiac muscle tissue development; IMP:BHF-UCL.
DR GO; GO:0001502; P:cartilage condensation; IMP:AgBase.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR GO; GO:0002062; P:chondrocyte differentiation; IMP:AgBase.
DR GO; GO:0031076; P:embryonic camera-type eye development; IMP:BHF-UCL.
DR GO; GO:0061037; P:negative regulation of cartilage development; IMP:AgBase.
DR GO; GO:0030336; P:negative regulation of cell migration; IMP:AgBase.
DR GO; GO:0032331; P:negative regulation of chondrocyte differentiation; IMP:AgBase.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IMP:BHF-UCL.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:AgBase.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IMP:AgBase.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:AgBase.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0042060; P:wound healing; IMP:AgBase.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR013284; Beta-catenin.
DR PANTHER; PTHR45976; PTHR45976; 1.
DR Pfam; PF00514; Arm; 4.
DR PRINTS; PR01869; BCATNINFAMLY.
DR SMART; SM00185; ARM; 12.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50176; ARM_REPEAT; 9.
PE 1: Evidence at protein level;
KW Activator; Cell membrane; Cytoplasm; Direct protein sequencing; Membrane;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation; Wnt signaling pathway.
FT CHAIN 1..781
FT /note="Catenin beta-1"
FT /id="PRO_0000064276"
FT REPEAT 141..180
FT /note="ARM 1"
FT REPEAT 225..264
FT /note="ARM 2"
FT REPEAT 267..306
FT /note="ARM 3"
FT REPEAT 351..390
FT /note="ARM 4"
FT REPEAT 391..429
FT /note="ARM 5"
FT REPEAT 432..473
FT /note="ARM 6"
FT REPEAT 479..519
FT /note="ARM 7"
FT REPEAT 521..562
FT /note="ARM 8"
FT REPEAT 584..623
FT /note="ARM 9"
FT REPEAT 625..664
FT /note="ARM 10"
FT REGION 34..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 735..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; 85449 MW; 3ECD27232239F799 CRC64;
MATQADLMEL DMAMEPDRKA AVSHWQQQSY LDSGIHSGAT TTAPSLSGKG NPEDEDVDTN
QVLYEWEQGF SQSFTQDQVA DIDGQYAMTR AQRVRAAMFP ETLDEGMQIP STQFDSAHPT
NVQRLAEPSQ MLKHAVVNLI NYQDDAELAT RAIPELTKLL NDEDQVVVNK AAVMVHQLSK
KEASRHAIMR SPQMVSAIVR TMQNTNDVET ARCTAGTLHN LSHHREGLLA IFKSGGIPAL
VKMLGSPVDS VLFYAITTLH NLLLHQEGAK MAVRLAGGLQ KMVALLNKTN VKFLAITTDC
LQILAYGNQE SKLIILASGG PQALVNIMRT YSYEKLLWTT SRVLKVLSVC SSNKPAIVEA
GGMQALGLHL TDSSQRLVQN CLWTLRNLSD AATKQEGMEG LLGTLVQLLG SDDINVVTCA
AGILSNLTCN NYKNKMMVCQ VGGIEALVRT VLRAGDREDI TEPAICALRH LTSRHQEAEM
AQNAVRLHYG LPVVVKLLHP PSHWPLIKAT VGLIRNLALC PANHAPLREQ GAIPRLVQLL
VRAHQDTQRR TSIGGTQQQF VEGVRMEEIV EGCTGALHIL ARDIHNRIVI RGLNTIPLFV
QLLYSPIENI QRVAAGVLCD VAQDKEAAEA IEAEGATAPL TELLHSRNEG VATYAAAVLF
RMSEDKPQDY KKRLSVELTS SLFRTEPMPW NEAADLGLDI GAQGEPLGYR QDDSSYRSFH
AAGYGQDAMG MDSMMDHDMG GHHPGADYPV DGLPDLSHAQ DLMDGLPPGD SNQLAWFDTD
L
