CTNB1_DANRE
ID CTNB1_DANRE Reviewed; 780 AA.
AC F1QGH7; A0A0N4SUA5; Q7ZU14; Q90424;
DT 13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Catenin beta-1;
DE AltName: Full=Beta-catenin;
GN Name=ctnnb1 {ECO:0000312|ZFIN:ZDB-GENE-980526-362};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=8562427; DOI=10.1016/0925-4773(95)00442-4;
RA Kelly G.M., Erezyilmaz D.F., Moon R.T.;
RT "Induction of a secondary embryonic axis in zebrafish occurs following the
RT overexpression of beta-catenin.";
RL Mech. Dev. 53:261-273(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=25371059; DOI=10.1038/ncomms6368;
RA Lu F.I., Sun Y.H., Wei C.Y., Thisse C., Thisse B.;
RT "Tissue-specific derepression of TCF/LEF controls the activity of the
RT Wnt/beta-catenin pathway.";
RL Nat. Commun. 5:5368-5368(2014).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=30467143; DOI=10.1126/science.aat1045;
RA Yan L., Chen J., Zhu X., Sun J., Wu X., Shen W., Zhang W., Tao Q., Meng A.;
RT "Maternal Huluwa dictates the embryonic body axis through beta-catenin in
RT vertebrates.";
RL Science 362:0-0(2018).
RN [6] {ECO:0007744|PDB:2Z6G}
RP X-RAY CRYSTALLOGRAPHY (3.40 ANGSTROMS).
RX PubMed=18334222; DOI=10.1016/j.str.2007.12.021;
RA Xing Y., Takemaru K., Liu J., Berndt J.D., Zheng J.J., Moon R.T., Xu W.;
RT "Crystal structure of a full-length beta-catenin.";
RL Structure 16:478-487(2008).
CC -!- FUNCTION: Key downstream component of the canonical Wnt signaling
CC pathway (By similarity). In the absence of Wnt, forms a complex with
CC axin1, axin2, apc, csnk1a1 and gsk3b that promotes phosphorylation on
CC N-terminal Ser and Thr residues and ubiquitination of ctnnb1 and its
CC subsequent degradation by the proteasome (By similarity). In the
CC presence of Wnt ligand, ctnnb1 is not ubiquitinated and accumulates in
CC the nucleus, where it acts as a coactivator for transcription factors
CC of the TCF/LEF family, leading to activate Wnt responsive genes (By
CC similarity). Plays a key role in dorsoventral patterning: in
CC prospective ventral blastomeres, its down-regulation by axin1 and axin2
CC leads to inhibit the Wnt signaling pathway, while in prospective dorsal
CC blastomeres, degradation of axin results in stabilization and nuclear
CC translocation of ctnnb1 (PubMed:8562427, PubMed:30467143).
CC {ECO:0000250|UniProtKB:P35222, ECO:0000250|UniProtKB:Q02248,
CC ECO:0000269|PubMed:30467143, ECO:0000269|PubMed:8562427}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P35222}. Nucleus
CC {ECO:0000269|PubMed:25371059, ECO:0000269|PubMed:30467143}. Cell
CC membrane {ECO:0000269|PubMed:25371059, ECO:0000269|PubMed:30467143}.
CC Note=Cytoplasmic when it is unstabilized (high level of
CC phosphorylation). Translocates to the nucleus when it is stabilized
CC (low level of phosphorylation). The majority of beta-catenin is
CC localized to the cell membrane. {ECO:0000250|UniProtKB:B6V8E6,
CC ECO:0000250|UniProtKB:P35222}.
CC -!- DEVELOPMENTAL STAGE: Expressed maternally and is widely distributed in
CC the early embryo (PubMed:8562427). Expressed in the posterior ventral
CC and lateral mesodermal, and ectodermal cells during gastrulation
CC (PubMed:25371059). {ECO:0000269|PubMed:25371059,
CC ECO:0000269|PubMed:8562427}.
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 -!- SEQUENCE CAUTION:
CC Sequence=CABZ01038334; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; U41081; AAC59732.1; -; mRNA.
DR EMBL; CABZ01038334; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC047815; AAH47815.1; -; mRNA.
DR RefSeq; NP_571134.2; NM_131059.2.
DR PDB; 2Z6G; X-ray; 3.40 A; A=1-780.
DR PDBsum; 2Z6G; -.
DR AlphaFoldDB; F1QGH7; -.
DR SMR; F1QGH7; -.
DR STRING; 7955.ENSDARP00000032935; -.
DR PaxDb; F1QGH7; -.
DR PRIDE; F1QGH7; -.
DR Ensembl; ENSDART00000038495; ENSDARP00000032935; ENSDARG00000014571.
DR GeneID; 30265; -.
DR KEGG; dre:30265; -.
DR CTD; 1499; -.
DR ZFIN; ZDB-GENE-980526-362; ctnnb1.
DR eggNOG; KOG4203; Eukaryota.
DR GeneTree; ENSGT00940000155471; -.
DR HOGENOM; CLU_008757_1_1_1; -.
DR InParanoid; F1QGH7; -.
DR OrthoDB; 321213at2759; -.
DR PhylomeDB; F1QGH7; -.
DR TreeFam; TF317997; -.
DR Reactome; R-DRE-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-DRE-196299; Beta-catenin phosphorylation cascade.
DR Reactome; R-DRE-201681; TCF dependent signaling in response to WNT.
DR Reactome; R-DRE-201722; Formation of the beta-catenin:TCF transactivating complex.
DR Reactome; R-DRE-3134973; LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production.
DR Reactome; R-DRE-351906; Apoptotic cleavage of cell adhesion proteins.
DR Reactome; R-DRE-3769402; Deactivation of the beta-catenin transactivating complex.
DR Reactome; R-DRE-4086398; Ca2+ pathway.
DR Reactome; R-DRE-418990; Adherens junctions interactions.
DR Reactome; R-DRE-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-DRE-525793; Myogenesis.
DR Reactome; R-DRE-5626467; RHO GTPases activate IQGAPs.
DR Reactome; R-DRE-8853884; Transcriptional Regulation by VENTX.
DR Reactome; R-DRE-8951430; RUNX3 regulates WNT signaling.
DR PRO; PR:F1QGH7; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 16.
DR Bgee; ENSDARG00000014571; Expressed in tail bud paraxial mesoderm and 44 other tissues.
DR GO; GO:0005912; C:adherens junction; IDA:ZFIN.
DR GO; GO:0016342; C:catenin complex; IDA:ZFIN.
DR GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0014704; C:intercalated disc; IDA:ZFIN.
DR GO; GO:0016020; C:membrane; IDA:ZFIN.
DR GO; GO:0005902; C:microvillus; IDA:ZFIN.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005915; C:zonula adherens; IDA:ZFIN.
DR GO; GO:0045294; F:alpha-catenin binding; IBA:GO_Central.
DR GO; GO:0045296; F:cadherin binding; IDA:ZFIN.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IBA:GO_Central.
DR GO; GO:0019903; F:protein phosphatase binding; IBA:GO_Central.
DR GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IC:ZFIN.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0060026; P:convergent extension; IGI:ZFIN.
DR GO; GO:0048262; P:determination of dorsal/ventral asymmetry; IDA:ZFIN.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; IGI:ZFIN.
DR GO; GO:0007398; P:ectoderm development; IGI:ZFIN.
DR GO; GO:0000578; P:embryonic axis specification; IMP:ZFIN.
DR GO; GO:0003094; P:glomerular filtration; IMP:ZFIN.
DR GO; GO:0001889; P:liver development; IGI:ZFIN.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:2000055; P:positive regulation of Wnt signaling pathway involved in dorsal/ventral axis specification; IDA:UniProtKB.
DR DisProt; DP02584; -.
DR Gene3D; 1.25.10.10; -; 1.
DR IDEAL; IID50014; -.
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 3D-structure; Activator; Cell membrane; Cytoplasm; Membrane; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation; Wnt signaling pathway.
FT CHAIN 1..780
FT /note="Catenin beta-1"
FT /id="PRO_0000446374"
FT REPEAT 140..179
FT /note="ARM 1"
FT /evidence="ECO:0000255"
FT REPEAT 224..263
FT /note="ARM 2"
FT /evidence="ECO:0000255"
FT REPEAT 266..305
FT /note="ARM 3"
FT /evidence="ECO:0000255"
FT REPEAT 350..389
FT /note="ARM 4"
FT /evidence="ECO:0000255"
FT REPEAT 399..430
FT /note="ARM 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00259"
FT REPEAT 431..472
FT /note="ARM 6"
FT /evidence="ECO:0000255"
FT REPEAT 478..518
FT /note="ARM 7"
FT /evidence="ECO:0000255"
FT REPEAT 520..561
FT /note="ARM 8"
FT /evidence="ECO:0000255"
FT REPEAT 583..622
FT /note="ARM 9"
FT /evidence="ECO:0000255"
FT REPEAT 624..663
FT /note="ARM 10"
FT /evidence="ECO:0000255"
FT REGION 34..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 735..770
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"
FT CONFLICT 241
FT /note="K -> N (in Ref. 1; AAC59732)"
FT /evidence="ECO:0000305"
FT CONFLICT 242
FT /note="M -> V (in Ref. 3; AAH47815)"
FT /evidence="ECO:0000305"
FT CONFLICT 253
FT /note="Y -> H (in Ref. 1; AAC59732)"
FT /evidence="ECO:0000305"
FT CONFLICT 446
FT /note="L -> P (in Ref. 3; AAH47815)"
FT /evidence="ECO:0000305"
FT CONFLICT 571
FT /note="G -> A (in Ref. 1; AAC59732)"
FT /evidence="ECO:0000305"
FT HELIX 130..160
FT /evidence="ECO:0007829|PDB:2Z6G"
FT HELIX 164..178
FT /evidence="ECO:0007829|PDB:2Z6G"
FT HELIX 181..187
FT /evidence="ECO:0007829|PDB:2Z6G"
FT HELIX 191..203
FT /evidence="ECO:0007829|PDB:2Z6G"
FT HELIX 207..221
FT /evidence="ECO:0007829|PDB:2Z6G"
FT HELIX 224..232
FT /evidence="ECO:0007829|PDB:2Z6G"
FT HELIX 235..242
FT /evidence="ECO:0007829|PDB:2Z6G"
FT HELIX 248..264
FT /evidence="ECO:0007829|PDB:2Z6G"
FT HELIX 268..274
FT /evidence="ECO:0007829|PDB:2Z6G"
FT HELIX 277..283
FT /evidence="ECO:0007829|PDB:2Z6G"
FT HELIX 284..286
FT /evidence="ECO:0007829|PDB:2Z6G"
FT HELIX 290..304
FT /evidence="ECO:0007829|PDB:2Z6G"
FT HELIX 308..315
FT /evidence="ECO:0007829|PDB:2Z6G"
FT TURN 316..318
FT /evidence="ECO:0007829|PDB:2Z6G"
FT HELIX 319..327
FT /evidence="ECO:0007829|PDB:2Z6G"
FT HELIX 333..347
FT /evidence="ECO:0007829|PDB:2Z6G"
FT HELIX 352..358
FT /evidence="ECO:0007829|PDB:2Z6G"
FT HELIX 361..365
FT /evidence="ECO:0007829|PDB:2Z6G"
FT HELIX 366..368
FT /evidence="ECO:0007829|PDB:2Z6G"
FT HELIX 374..388
FT /evidence="ECO:0007829|PDB:2Z6G"
FT HELIX 398..407
FT /evidence="ECO:0007829|PDB:2Z6G"
FT HELIX 413..426
FT /evidence="ECO:0007829|PDB:2Z6G"
FT HELIX 431..438
FT /evidence="ECO:0007829|PDB:2Z6G"
FT TURN 439..441
FT /evidence="ECO:0007829|PDB:2Z6G"
FT HELIX 442..453
FT /evidence="ECO:0007829|PDB:2Z6G"
FT HELIX 457..469
FT /evidence="ECO:0007829|PDB:2Z6G"
FT STRAND 472..474
FT /evidence="ECO:0007829|PDB:2Z6G"
FT HELIX 477..486
FT /evidence="ECO:0007829|PDB:2Z6G"
FT HELIX 490..495
FT /evidence="ECO:0007829|PDB:2Z6G"
FT HELIX 503..517
FT /evidence="ECO:0007829|PDB:2Z6G"
FT HELIX 520..528
FT /evidence="ECO:0007829|PDB:2Z6G"
FT HELIX 531..548
FT /evidence="ECO:0007829|PDB:2Z6G"
FT HELIX 565..579
FT /evidence="ECO:0007829|PDB:2Z6G"
FT HELIX 583..591
FT /evidence="ECO:0007829|PDB:2Z6G"
FT HELIX 595..600
FT /evidence="ECO:0007829|PDB:2Z6G"
FT HELIX 601..603
FT /evidence="ECO:0007829|PDB:2Z6G"
FT HELIX 607..621
FT /evidence="ECO:0007829|PDB:2Z6G"
FT HELIX 624..632
FT /evidence="ECO:0007829|PDB:2Z6G"
FT HELIX 636..641
FT /evidence="ECO:0007829|PDB:2Z6G"
FT HELIX 642..644
FT /evidence="ECO:0007829|PDB:2Z6G"
FT HELIX 648..662
FT /evidence="ECO:0007829|PDB:2Z6G"
FT HELIX 669..680
FT /evidence="ECO:0007829|PDB:2Z6G"
SQ SEQUENCE 780 AA; 85569 MW; D4CBCC6EEBF717F2 CRC64;
MATQSDLMEL EMAMDPDRKA AVSHWQQQSY LDSGIHSGAT TTAPSLSGKG NPEDDDVDNQ
VLYEWEQGFN QSFNQEQVAD IDGQYAMTRA QRVRAAMFPE TLDEGMQIPS TQFDSAHPTN
VQRLAEPSQM LKHAVVNLIN YQDDAELATR AIPELTKLLN DEDQVVVNKA AVMVHQLSKK
EASRHAIMRS PQMVSAIVRT MQNTNDVETA RCTSGTLHNL SHHREGLLAI FKSGGIPALV
KMLGSPVDSV LFYAITTLHN LLLHQEGAKM AVRLAGGLQK MVALLNKTNV KFLAITTDCL
QILAYGNQES KLIILASGGP QALVNIMRTY TYEKLLWTTS RVLKVLSVCS SNKPAIVEAG
GMQALGLHLT DPSQRLVQNC LWTLRNLSDA ATKQEGMEGL LGTLVQLLGS DDINVVTCAA
GILSNLTCNN YKNKMMVCQV GGIEALVRTV LRAGDREDIT EPAICALRHL TSRHQDAEMA
QNAVRLHYGL PVVVKLLHPP SHWPLIKATV GLIRNLALCP ANHAPLREQG AIPRLVQLLV
RAHQDTQRRT SMGGTQQQFV EGVRMEEIVE GCTGALHILA RDIHNRIVIR GLNTIPLFVQ
LLYSPIENIQ RVAAGVLCEL AQDKEAAEAI EAEGATAPLT ELLHSRNEGV ATYAAAVLFR
MSEDKPQDYK KRLSVELTSS LFRTEPMTWN ETGDLGLDIG AQGEPLGYRQ DDPSYRSFHS
GGYGQDAMGM DPMMEHEMAG HHPGPDYPVD GLPDLGHTQD LIDGLPPGDS NQLAWFDTDL
