CTND1_XENLA
ID CTND1_XENLA Reviewed; 859 AA.
AC Q8AXM9; Q8AXN0;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Catenin delta-1;
DE AltName: Full=Xp120(ctn);
DE AltName: Full=p120 catenin;
DE Short=p120(ctn);
GN Name=ctnnd1;
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] (ISOFORMS 1 AND 2), FUNCTION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=15292404; DOI=10.1242/jcs.01298;
RA Ciesiolka M., Delvaeye M., Van Imschoot G., Verschuere V., McCrea P.,
RA van Roy F., Vleminckx K.;
RT "p120 catenin is required for morphogenetic movements involved in the
RT formation of the eyes and the craniofacial skeleton in Xenopus.";
RL J. Cell Sci. 117:4325-4339(2004).
RN [2]
RP FUNCTION, INTERACTION WITH C-CADHERIN, AND DEVELOPMENTAL STAGE.
RX PubMed=10068468; DOI=10.1006/dbio.1998.9158;
RA Paulson A.F., Fang X., Ji H., Reynolds A.B., McCrea P.D.;
RT "Misexpression of the catenin p120(ctn)1A perturbs Xenopus gastrulation but
RT does not elicit Wnt-directed axis specification.";
RL Dev. Biol. 207:350-363(1999).
RN [3]
RP INTERACTION WITH ZBTB33.
RX PubMed=11751886; DOI=10.1074/jbc.m109508200;
RA Kim S.-W., Fang X., Ji H., Paulson A.F., Daniel J.M., Ciesiolka M.,
RA van Roy F., McCrea P.D.;
RT "Isolation and characterization of XKaiso, a transcriptional repressor that
RT associates with the catenin Xp120(ctn) in Xenopus laevis.";
RL J. Biol. Chem. 277:8202-8208(2002).
RN [4]
RP FUNCTION.
RX PubMed=15067024; DOI=10.1083/jcb.200307109;
RA Fang X., Ji H., Kim S.-W., Park J.-I., Vaught T.G., Anastasiadis P.Z.,
RA Ciesiolka M., McCrea P.D.;
RT "Vertebrate development requires ARVCF and p120 catenins and their
RT interplay with RhoA and Rac.";
RL J. Cell Biol. 165:87-98(2004).
RN [5]
RP FUNCTION.
RX PubMed=15543138; DOI=10.1038/ncb1191;
RA Kim S.-W., Park J.-I., Spring C.M., Sater A.K., Ji H., Otchere A.A.,
RA Daniel J.M., McCrea P.D.;
RT "Non-canonical Wnt signals are modulated by the Kaiso transcriptional
RT repressor and p120-catenin.";
RL Nat. Cell Biol. 6:1212-1220(2004).
RN [6]
RP FUNCTION.
RX PubMed=15935774; DOI=10.1016/j.devcel.2005.04.010;
RA Park J.-I., Kim S.-W., Lyons J.P., Ji H., Nguyen T.T., Cho K., Barton M.C.,
RA Deroo T., Vleminckx K., Moon R.T., McCrea P.D.;
RT "Kaiso/p120-catenin and TCF/beta-catenin complexes coordinately regulate
RT canonical Wnt gene targets.";
RL Dev. Cell 8:843-854(2005).
CC -!- FUNCTION: Key regulator of cell-cell adhesion that associates with and
CC regulates the cell adhesion properties of both C-, E- and N-cadherins,
CC being critical for their surface stability. Beside cell-cell adhesion,
CC regulates gene transcription through several transcription factors
CC including ZBTB33/Kaiso2 and GLIS2, and the activity of Rho family
CC GTPases and downstream cytoskeletal dynamics. Implicated both in cell
CC transformation by SRC and in ligand-induced receptor signaling through
CC the EGF, PDGF, CSF-1 and ERBB2 receptors. Required for gastrulation,
CC axial elongation and development of the craniofacial skeleton and eye.
CC {ECO:0000269|PubMed:10068468, ECO:0000269|PubMed:15067024,
CC ECO:0000269|PubMed:15292404, ECO:0000269|PubMed:15543138,
CC ECO:0000269|PubMed:15935774}.
CC -!- SUBUNIT: Interacts with C-cadherin and with zbtb33.
CC {ECO:0000269|PubMed:10068468, ECO:0000269|PubMed:11751886}.
CC -!- INTERACTION:
CC Q8AXM9; Q8JJ48: dact1-a; NbExp=6; IntAct=EBI-6260685, EBI-6259065;
CC Q8AXM9; P51142: dvl2; NbExp=2; IntAct=EBI-6260685, EBI-6257503;
CC Q8AXM9; Q8UVQ4: zbtb33; NbExp=2; IntAct=EBI-6260685, EBI-6261609;
CC -!- SUBCELLULAR LOCATION: Cell junction, adherens junction
CC {ECO:0000250|UniProtKB:O60716}. Cytoplasm
CC {ECO:0000250|UniProtKB:O60716}. Nucleus {ECO:0000250|UniProtKB:O60716}.
CC Cell membrane {ECO:0000250|UniProtKB:O60716}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8AXM9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8AXM9-2; Sequence=VSP_016649;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:15292404}.
CC -!- DEVELOPMENTAL STAGE: Expressed maternally and throughout early
CC embryogenesis. Highly expressed in tissues participating in prominent
CC morphogenetic movements. Enriched in the animal hemisphere in early
CC gastrula and the anterior region in late neurula. Expressed in the head
CC region in the tailbud stage, particularly the optic vesicle, ear
CC vesicle, olfactory placode and branchial arches. Expression is also
CC weakly elevated in the somites, notochord and pronephros.
CC {ECO:0000269|PubMed:10068468, ECO:0000269|PubMed:15292404}.
CC -!- DOMAIN: ARM repeats 1 to 5 mediate interaction with cadherins.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the beta-catenin family. {ECO:0000305}.
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DR EMBL; AF150743; AAO13693.1; -; mRNA.
DR EMBL; AF150744; AAO13694.1; -; mRNA.
DR RefSeq; NP_001082468.1; NM_001088999.2. [Q8AXM9-1]
DR AlphaFoldDB; Q8AXM9; -.
DR SMR; Q8AXM9; -.
DR IntAct; Q8AXM9; 3.
DR MaxQB; Q8AXM9; -.
DR GeneID; 398490; -.
DR KEGG; xla:398490; -.
DR CTD; 398490; -.
DR Xenbase; XB-GENE-919837; ctnnd1.L.
DR OrthoDB; 233858at2759; -.
DR Proteomes; UP000186698; Chromosome 7L.
DR Bgee; 398490; Expressed in egg cell and 19 other tissues.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005911; C:cell-cell junction; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045296; F:cadherin binding; IEA:InterPro.
DR GO; GO:0098609; P:cell-cell adhesion; IEA:InterPro.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR028439; Catenin_d1.
DR InterPro; IPR028435; Plakophilin/d_Catenin.
DR PANTHER; PTHR10372; PTHR10372; 1.
DR PANTHER; PTHR10372:SF6; PTHR10372:SF6; 1.
DR Pfam; PF00514; Arm; 2.
DR SMART; SM00185; ARM; 6.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50176; ARM_REPEAT; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Cell junction; Cell membrane;
KW Coiled coil; Cytoplasm; Developmental protein; Membrane; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Wnt signaling pathway.
FT CHAIN 1..859
FT /note="Catenin delta-1"
FT /id="PRO_0000064298"
FT REPEAT 279..317
FT /note="ARM 1"
FT REPEAT 320..359
FT /note="ARM 2"
FT REPEAT 363..401
FT /note="ARM 3"
FT REPEAT 402..446
FT /note="ARM 4"
FT REPEAT 464..503
FT /note="ARM 5"
FT REPEAT 513..552
FT /note="ARM 6"
FT REPEAT 574..614
FT /note="ARM 7"
FT REPEAT 621..660
FT /note="ARM 8"
FT REPEAT 661..700
FT /note="ARM 9"
FT REPEAT 701..746
FT /note="ARM 10"
FT REGION 226..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 15..44
FT /evidence="ECO:0000255"
FT COMPBIAS 240..254
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..74
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15292404"
FT /id="VSP_016649"
SQ SEQUENCE 859 AA; 94561 MW; 7FE6744BCECF8C41 CRC64;
MDEPESESPA SILASVRAQE AQFELLSRAL EEERRHVTAQ LDRVWVTPQE PPLANGSLTR
RQQDGLPFLY TPTRMEAHSV HADERYVIDD SSYKSCTLTD ESRCSEIPIQ TVVGYSQTLD
RPYREAAGSG GAYTTVPRNY HFRGPGVDST MPLISQSPHP GYSSLSRPNQ RYRSVDPFRG
PGYGPQPQVR GGGLGGSQSD LLSGRIYGSE DAYGLEDDRR SLGGFIDGPD YATTGRRGAN
GGDPRRRLRS YEDPLSDHFG SIPTSGSLSS LGPAPLTLAP NSGPWRHPEL PEVLAMLSYT
LDAVRLNAAA YLQHLSYRNE DVKREVCRLR GIPPLISLLE DPRAPIRLAA CGALKNLSYG
PARENKMAVK NCDGVPALAR LLRRRGEGIE GRELAECVTG TLWNLSSLDS VKMELVDQAL
YTLTQEILVP HSGWQQDGGM QDRVEGKPRH VEWEPALVNT TGCLRNISSE RSEARRKMRE
CEGLVDSVVH ILRSEVSHGL VDSKLLENVV CLLRNISYHV HREIPHAEKY MESPQNASAE
TQNPSCFGVR RGKGKKASEE AVDTVDFPKQ TMPAQGYDLL FQPEIVRLYI SLVKSSHTPA
VLEASAGAIQ NLCAGNWVYG RCIRAAVRQE KGLSSLADHL THESERVVRA ICGALRNLCG
DNRNRELIGK HALNSLVARL SSSSAQSSAL SEDTNVCVIN TIHEVISGNL EAAKRLRESQ
GIERLVLINK GGGRSEREIR AAGFCLQTIW GYKELRRPLE KDGWKKSDFQ VSTAATSSVQ
GYDDSTLPLI DRNLKNEKKS VNADIPLNDF IADQFTHNGD SSNRLPTRSD ELSELDPLKE
CSVSAGGSLN LGDAEDQRV
