CTND1_MOUSE
ID CTND1_MOUSE Reviewed; 938 AA.
AC P30999; Q3TSU9; Q80XQ4; Q8CHF8;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Catenin delta-1;
DE AltName: Full=Cadherin-associated Src substrate;
DE Short=CAS;
DE AltName: Full=p120 catenin;
DE Short=p120(ctn);
DE AltName: Full=p120(cas);
GN Name=Ctnnd1; Synonyms=Catns, Kiaa0384;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=SWR/J;
RX PubMed=1334250;
RA Reynolds A.B., Herbert L., Cleveland J.L., Berg S.T., Gaut J.R.;
RT "p120, a novel substrate of protein tyrosine kinase receptors and of p60v-
RT src, is related to cadherin-binding factors beta-catenin, plakoglobin and
RT armadillo.";
RL Oncogene 7:2439-2445(1992).
RN [2]
RP SEQUENCE REVISION.
RA Reynolds A.B.;
RL Submitted (DEC-1992) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=12465718; DOI=10.1093/dnares/9.5.179;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: I.
RT The complete nucleotide sequences of 100 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 9:179-188(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP INTERACTION WITH ZBTB33.
RX PubMed=10207085; DOI=10.1128/mcb.19.5.3614;
RA Daniel J.M., Reynolds A.B.;
RT "The catenin p120(ctn) interacts with Kaiso, a novel BTB/POZ domain zinc
RT finger transcription factor.";
RL Mol. Cell. Biol. 19:3614-3623(1999).
RN [7]
RP INTERACTION WITH ZBTB33.
RX PubMed=12087177; DOI=10.1093/nar/gkf398;
RA Daniel J.M., Spring C.M., Crawford H.C., Reynolds A.B., Baig A.;
RT "The p120(ctn)-binding partner Kaiso is a bi-modal DNA-binding protein that
RT recognizes both a sequence-specific consensus and methylated CpG
RT dinucleotides.";
RL Nucleic Acids Res. 30:2911-2919(2002).
RN [8]
RP FUNCTION, NUCLEAR LOCALIZATION SIGNAL, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF 622-LYS-LYS-623.
RX PubMed=15138284; DOI=10.1242/jcs.01101;
RA Kelly K.F., Spring C.M., Otchere A.A., Daniel J.M.;
RT "NLS-dependent nuclear localization of p120ctn is necessary to relieve
RT Kaiso-mediated transcriptional repression.";
RL J. Cell Sci. 117:2675-2686(2004).
RN [9]
RP ERRATUM OF PUBMED:15138284.
RA Kelly K.F., Spring C.M., Otchere A.A., Daniel J.M.;
RL J. Cell Sci. 117:3405-3405(2004).
RN [10]
RP INTERACTION WITH GNA12 AND GNA13.
RX PubMed=15240885; DOI=10.1073/pnas.0401366101;
RA Krakstad B.F., Ardawatia V.V., Aragay A.M.;
RT "A role for Galpha12/Galpha13 in p120ctn regulation.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:10314-10319(2004).
RN [11]
RP FUNCTION.
RX PubMed=15817151; DOI=10.1016/j.yexcr.2005.01.007;
RA Spring C.M., Kelly K.F., O'Kelly I., Graham M., Crawford H.C., Daniel J.M.;
RT "The catenin p120ctn inhibits Kaiso-mediated transcriptional repression of
RT the beta-catenin/TCF target gene matrilysin.";
RL Exp. Cell Res. 305:253-265(2005).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-217; TYR-221 AND TYR-280, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-904, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [14]
RP INTERACTION WITH GLIS2, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17344476; DOI=10.1091/mbc.e06-10-0941;
RA Hosking C.R., Ulloa F., Hogan C., Ferber E.C., Figueroa A., Gevaert K.,
RA Birchmeier W., Briscoe J., Fujita Y.;
RT "The transcriptional repressor Glis2 is a novel binding partner for p120
RT catenin.";
RL Mol. Biol. Cell 18:1918-1927(2007).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230; SER-252; SER-288;
RP SER-349; SER-847; SER-857; TYR-865 AND SER-899, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [17]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=19267394; DOI=10.1002/humu.20981;
RA Roth W., Reuter U., Wohlenberg C., Bruckner-Tuderman L., Magin T.M.;
RT "Cytokines as genetic modifiers in K5-/- mice and in human epidermolysis
RT bullosa simplex.";
RL Hum. Mutat. 30:832-841(2009).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-228; TYR-257; SER-349;
RP SER-352 AND TYR-904, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; THR-59; SER-225; SER-230;
RP SER-252; SER-269; SER-288; TYR-291; SER-300; THR-304; SER-320; SER-349;
RP SER-352; SER-713; SER-847; SER-857; SER-864; TYR-865; SER-868; THR-869;
RP SER-899 AND SER-920, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [21]
RP DEVELOPMENTAL STAGE.
RX PubMed=23001562; DOI=10.1093/hmg/dds398;
RA Alves C.H., Sanz A.S., Park B., Pellissier L.P., Tanimoto N., Beck S.C.,
RA Huber G., Murtaza M., Richard F., Sridevi Gurubaran I., Garcia Garrido M.,
RA Levelt C.N., Rashbass P., Le Bivic A., Seeliger M.W., Wijnholds J.;
RT "Loss of CRB2 in the mouse retina mimics human retinitis pigmentosa due to
RT mutations in the CRB1 gene.";
RL Hum. Mol. Genet. 22:35-50(2013).
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. {ECO:0000250,
CC ECO:0000269|PubMed:15138284, ECO:0000269|PubMed:15817151,
CC ECO:0000269|PubMed:17344476}.
CC -!- SUBUNIT: Belongs to a multiprotein cell-cell adhesion complex that also
CC contains E-cadherin/CDH1, alpha-catenin/CTNNA1, beta-catenin/CTNNB1,
CC and gamma-catenin/JUP. Binds to the C-terminal fragment of PSEN1 and
CC mutually competes for CDH1 (By similarity). Interacts with ZBTB33
CC (PubMed:10207085, PubMed:12087177). Interacts with GLIS2
CC (PubMed:17344476). Interacts with FER (By similarity). Interacts with
CC NANOS1 (via N-terminal region) (By similarity). Interacts (via N-
CC terminus) with GNA12; the interaction regulates CDH1-mediated cell-cell
CC adhesion (PubMed:15240885). Interacts with GNA13 (PubMed:15240885).
CC Component of a cadherin:catenin adhesion complex composed of at least
CC of CDH26, beta-catenin/CTNNB1, alpha-catenin/CTNNA1 and p120
CC catenin/CTNND1 (By similarity). Interacts with CCDC85B (By similarity).
CC Interacts with PLPP3; negatively regulates the PLPP3-mediated
CC stabilization of CTNNB1 (By similarity). {ECO:0000250|UniProtKB:O60716,
CC ECO:0000269|PubMed:10207085, ECO:0000269|PubMed:12087177,
CC ECO:0000269|PubMed:15240885, ECO:0000269|PubMed:17344476}.
CC -!- INTERACTION:
CC P30999; Q60598: Cttn; NbExp=4; IntAct=EBI-529924, EBI-397955;
CC P30999; P35235: Ptpn11; NbExp=3; IntAct=EBI-529924, EBI-397236;
CC P30999; Q8BN78: Zbtb33; NbExp=3; IntAct=EBI-529924, EBI-1216314;
CC -!- SUBCELLULAR LOCATION: Cell junction, adherens junction
CC {ECO:0000269|PubMed:19267394}. Cytoplasm {ECO:0000269|PubMed:15138284,
CC ECO:0000269|PubMed:17344476}. Nucleus {ECO:0000269|PubMed:15138284,
CC ECO:0000269|PubMed:17344476}. Cell membrane
CC {ECO:0000269|PubMed:17344476, ECO:0000269|PubMed:19267394}.
CC Note=Interaction with GLIS2 promotes nuclear translocation
CC (PubMed:17344476). Detected at cell-cell contacts (By similarity).
CC NANOS1 induces its translocation from sites of cell-cell contact to the
CC cytoplasm (By similarity). CDH1 enhances cell membrane localization (By
CC similarity). {ECO:0000250|UniProtKB:O60716,
CC ECO:0000269|PubMed:17344476}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Nucleus
CC {ECO:0000269|PubMed:15138284}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P30999-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P30999-2; Sequence=VSP_030567, VSP_030568;
CC Name=3;
CC IsoId=P30999-3; Sequence=VSP_030568;
CC -!- TISSUE SPECIFICITY: Expressed in basal keratinocytes (at protein
CC level). {ECO:0000269|PubMed:19267394}.
CC -!- DEVELOPMENTAL STAGE: Expressed at the outer limiting membrane of the
CC retina at 18.5 dpc. {ECO:0000269|PubMed:23001562}.
CC -!- DOMAIN: ARM repeats 1 to 5 mediate interaction with cadherins.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated by FER and other protein-tyrosine kinases.
CC Phosphorylated at Ser-288 by PAK5. Dephosphorylated by PTPRJ (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the beta-catenin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC41421.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; Z17804; CAA79078.1; -; mRNA.
DR EMBL; AB093237; BAC41421.1; ALT_INIT; mRNA.
DR EMBL; AK133193; BAE21551.1; -; mRNA.
DR EMBL; AK161790; BAE36576.1; -; mRNA.
DR EMBL; BC043108; AAH43108.1; -; mRNA.
DR EMBL; BC054544; AAH54544.1; -; mRNA.
DR CCDS; CCDS16186.1; -. [P30999-1]
DR CCDS; CCDS50622.1; -. [P30999-2]
DR CCDS; CCDS50623.1; -. [P30999-3]
DR PIR; I48701; S28498.
DR RefSeq; NP_001078917.1; NM_001085448.1. [P30999-3]
DR RefSeq; NP_001078918.1; NM_001085449.1.
DR RefSeq; NP_001078919.1; NM_001085450.1. [P30999-1]
DR RefSeq; NP_001078922.1; NM_001085453.1. [P30999-2]
DR RefSeq; NP_031641.2; NM_007615.4. [P30999-1]
DR RefSeq; XP_006498698.1; XM_006498635.1.
DR RefSeq; XP_017170690.1; XM_017315201.1.
DR RefSeq; XP_017170697.1; XM_017315208.1. [P30999-3]
DR AlphaFoldDB; P30999; -.
DR SMR; P30999; -.
DR BioGRID; 198513; 36.
DR CORUM; P30999; -.
DR DIP; DIP-31972N; -.
DR IntAct; P30999; 20.
DR MINT; P30999; -.
DR STRING; 10090.ENSMUSP00000064518; -.
DR GlyConnect; 2420; 5 N-Linked glycans (1 site). [P30999-2]
DR GlyGen; P30999; 1 site, 5 N-linked glycans (1 site).
DR iPTMnet; P30999; -.
DR PhosphoSitePlus; P30999; -.
DR SwissPalm; P30999; -.
DR CPTAC; non-CPTAC-3781; -.
DR jPOST; P30999; -.
DR MaxQB; P30999; -.
DR PaxDb; P30999; -.
DR PeptideAtlas; P30999; -.
DR PRIDE; P30999; -.
DR ProteomicsDB; 284057; -. [P30999-1]
DR ProteomicsDB; 284058; -. [P30999-2]
DR ProteomicsDB; 284059; -. [P30999-3]
DR DNASU; 12388; -.
DR Ensembl; ENSMUST00000036811; ENSMUSP00000042543; ENSMUSG00000034101. [P30999-3]
DR Ensembl; ENSMUST00000066177; ENSMUSP00000065252; ENSMUSG00000034101. [P30999-2]
DR Ensembl; ENSMUST00000067232; ENSMUSP00000064518; ENSMUSG00000034101. [P30999-1]
DR Ensembl; ENSMUST00000111691; ENSMUSP00000107320; ENSMUSG00000034101. [P30999-1]
DR Ensembl; ENSMUST00000111697; ENSMUSP00000107326; ENSMUSG00000034101. [P30999-3]
DR Ensembl; ENSMUST00000189772; ENSMUSP00000141166; ENSMUSG00000101645. [P30999-1]
DR GeneID; 12388; -.
DR KEGG; mmu:12388; -.
DR UCSC; uc008kio.1; mouse. [P30999-3]
DR UCSC; uc008kip.1; mouse. [P30999-1]
DR UCSC; uc008kit.1; mouse. [P30999-2]
DR CTD; 1500; -.
DR MGI; MGI:105100; Ctnnd1.
DR VEuPathDB; HostDB:ENSMUSG00000034101; -.
DR VEuPathDB; HostDB:ENSMUSG00000101645; -.
DR eggNOG; KOG1048; Eukaryota.
DR GeneTree; ENSGT00940000156045; -.
DR HOGENOM; CLU_009111_1_0_1; -.
DR InParanoid; P30999; -.
DR OMA; GDQMSYP; -.
DR PhylomeDB; P30999; -.
DR TreeFam; TF321877; -.
DR Reactome; R-MMU-418990; Adherens junctions interactions.
DR Reactome; R-MMU-5218920; VEGFR2 mediated vascular permeability.
DR BioGRID-ORCS; 12388; 2 hits in 26 CRISPR screens.
DR ChiTaRS; Ctnnd1; mouse.
DR PRO; PR:P30999; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P30999; protein.
DR Bgee; ENSMUSG00000034101; Expressed in embryonic post-anal tail and 81 other tissues.
DR ExpressionAtlas; P30999; baseline and differential.
DR Genevisible; P30999; MM.
DR GO; GO:0005912; C:adherens junction; IDA:UniProtKB.
DR GO; GO:0016327; C:apicolateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0005923; C:bicellular tight junction; IDA:MGI.
DR GO; GO:0016342; C:catenin complex; ISO:MGI.
DR GO; GO:0005911; C:cell-cell junction; IDA:ARUK-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0016600; C:flotillin complex; IDA:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0030426; C:growth cone; ISO:MGI.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; ISO:MGI.
DR GO; GO:0030027; C:lamellipodium; IDA:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0099092; C:postsynaptic density, intracellular component; ISO:MGI.
DR GO; GO:0098831; C:presynaptic active zone cytoplasmic component; ISO:MGI.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:MGI.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0005915; C:zonula adherens; ISO:MGI.
DR GO; GO:0008013; F:beta-catenin binding; ISO:MGI.
DR GO; GO:0045296; F:cadherin binding; ISO:MGI.
DR GO; GO:0050839; F:cell adhesion molecule binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; IPI:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB.
DR GO; GO:1990782; F:protein tyrosine kinase binding; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0007155; P:cell adhesion; IMP:MGI.
DR GO; GO:0098609; P:cell-cell adhesion; IMP:MGI.
DR GO; GO:0044331; P:cell-cell adhesion mediated by cadherin; ISO:MGI.
DR GO; GO:0007043; P:cell-cell junction assembly; IBA:GO_Central.
DR GO; GO:0060690; P:epithelial cell differentiation involved in salivary gland development; IMP:MGI.
DR GO; GO:0072102; P:glomerulus morphogenesis; IMP:MGI.
DR GO; GO:0001822; P:kidney development; IMP:MGI.
DR GO; GO:0001738; P:morphogenesis of a polarized epithelium; IMP:MGI.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISO:MGI.
DR GO; GO:1900086; P:positive regulation of peptidyl-tyrosine autophosphorylation; IGI:MGI.
DR GO; GO:0010954; P:positive regulation of protein processing; IMP:MGI.
DR GO; GO:0050821; P:protein stabilization; ISO:MGI.
DR GO; GO:0099072; P:regulation of postsynaptic membrane neurotransmitter receptor levels; ISO:MGI.
DR GO; GO:0007435; P:salivary gland morphogenesis; IMP:MGI.
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; 3.
DR SMART; SM00185; ARM; 7.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50176; ARM_REPEAT; 3.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell adhesion; Cell junction;
KW Cell membrane; Coiled coil; Cytoplasm; Isopeptide bond; Membrane; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation; Wnt signaling pathway.
FT CHAIN 1..938
FT /note="Catenin delta-1"
FT /id="PRO_0000064297"
FT REPEAT 358..395
FT /note="ARM 1"
FT REPEAT 398..437
FT /note="ARM 2"
FT REPEAT 441..475
FT /note="ARM 3"
FT REPEAT 476..516
FT /note="ARM 4"
FT REPEAT 534..573
FT /note="ARM 5"
FT REPEAT 583..624
FT /note="ARM 6"
FT REPEAT 653..693
FT /note="ARM 7"
FT REPEAT 700..739
FT /note="ARM 8"
FT REPEAT 740..780
FT /note="ARM 9"
FT REPEAT 781..826
FT /note="ARM 10"
FT REGION 1..357
FT /note="Necessary and sufficient for interaction with
FT CCDC85B"
FT /evidence="ECO:0000250|UniProtKB:O60716"
FT REGION 855..938
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 10..46
FT /evidence="ECO:0000255"
FT COMPBIAS 855..872
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 873..888
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 890..910
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 911..925
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 401
FT /note="Essential for interaction with cadherins"
FT /evidence="ECO:0000250|UniProtKB:O60716"
FT SITE 478
FT /note="Essential for interaction with cadherins"
FT /evidence="ECO:0000250|UniProtKB:O60716"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O60716"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60716"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 59
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 112
FT /note="Phosphotyrosine; by FYN"
FT /evidence="ECO:0000250|UniProtKB:O60716"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60716"
FT MOD_RES 217
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT MOD_RES 221
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 228
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 252
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 257
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60716"
FT MOD_RES 269
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 280
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT MOD_RES 288
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 291
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 300
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 304
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60716"
FT MOD_RES 349
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 352
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 617
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60716"
FT MOD_RES 713
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 811
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60716"
FT MOD_RES 847
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 857
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 859
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60716"
FT MOD_RES 861
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60716"
FT MOD_RES 864
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 865
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 868
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 869
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 879
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60716"
FT MOD_RES 899
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 904
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660,
FT ECO:0007744|PubMed:19131326"
FT MOD_RES 906
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O60716"
FT MOD_RES 916
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O60716"
FT MOD_RES 920
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 421
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O60716"
FT CROSSLNK 517
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O60716"
FT CROSSLNK 882
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O60716"
FT VAR_SEQ 626..631
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1334250"
FT /id="VSP_030567"
FT VAR_SEQ 880..900
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:12465718,
FT ECO:0000303|PubMed:1334250, ECO:0000303|PubMed:16141072"
FT /id="VSP_030568"
FT MUTAGEN 622..623
FT /note="KK->AA: Abolishes nuclear localization."
FT /evidence="ECO:0000269|PubMed:15138284"
FT CONFLICT 405
FT /note="R -> A (in Ref. 1; CAA79078)"
FT /evidence="ECO:0000305"
FT CONFLICT 676
FT /note="K -> N (in Ref. 1; CAA79078)"
FT /evidence="ECO:0000305"
FT CONFLICT 715
FT /note="I -> R (in Ref. 1; CAA79078)"
FT /evidence="ECO:0000305"
FT CONFLICT 752
FT /note="I -> R (in Ref. 1; CAA79078)"
FT /evidence="ECO:0000305"
FT MOTIF P30999-2:622..629
FT /note="Nuclear localization signal (NLS)"
FT /evidence="ECO:0000269|PubMed:15138284"
SQ SEQUENCE 938 AA; 104925 MW; 2F13DB7350355832 CRC64;
MDDSEVESTA SILASVKEQE AQFEKLTRAL EEERRHVSAQ LERVRVSPQD ANSLMANGTL
TRRHQNGRFV GDADLERQKF SDLKLNGPQD HNHLLYSTIP RMQEPGQIVE TYTEEDPEGA
MSVVSVETTD DGTTRRTETT VKKVVKTMTT RTVQPVPMGP DGLPVDASAV SNNYIQTLGR
DFRKNGNGGP GPYVGQAGTA TLPRNFHYPP DGYGRHYEDG YPGGSDNYGS LSRVTRIEER
YRPSMEGYRA PSRQDVYGPQ PQVRVGGSSV DLHRFHPEPY GLEDDQRSMG YDDLDYGMMS
DYGTARRTGT PSDPRRRLRS YEDMIGEEVP PDQYYWAPLA QHERGSLASL DSLRKGMPPP
SNWRQPELPE VIAMLGFRLD AVKSNAAAYL QHLCYRNDKV KTDVRKLKGI PILVGLLDHP
KKEVHLGACG ALKNISFGRD QDNKIAIKNC DGVPALVRLL RKARDMDLTE VITGTLWNLS
SHDSIKMEIV DHALHALTDE VIIPHSGWER EPNEDCKPRH IEWESVLTNT AGCLRNVSSE
RSEARRKLRE CDGLVDALIF IVQAEIGQKD SDSKLVENCV CLLRNLSYQV HREIPQAERY
QEALPTVANS TGPHAASCFG AKKGKDEWFS RGKKPTEDPA NDTVDFPKRT SPARGYELLF
QPEVVRIYIS LLKESKTPAI LEASAGAIQN LCAGRWTYGR YIRSALRQEK ALSAIAELLT
SEHERVVKAA SGALRNLAVD ARNKELIGKH AIPNLVKNLP GGQQNSSWNF SEDTVVSILN
TINEVIAENL EAAKKLRETQ GIEKLVLINK SGNRSEKEVR AAALVLQTIW GYKELRKPLE
KEGWKKSDFQ VNLNNASRSQ SSHSYDDSTL PLIDRNQKSD KKPDREEIPM SNMGSNTKSL
DNNYSTLNER GDHNRTLDRS GDLGDMEPLK GAPLMQKI
