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 02-DEC-2020, entry version 184. 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 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 [18] 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 [19] 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). 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:0000250|UniProtKB:O60716}. 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}. Note=Interaction with GLIS2 promotes CC nuclear translocation (PubMed:17344476). Detected at cell-cell contacts CC (By similarity). NANOS1 induces its translocation from sites of cell- CC cell contact to the cytoplasm (By similarity). CDH1 enhances cell CC membrane localization (By 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 -!- 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 SMR; P30999; -. DR BioGRID; 198513; 33. DR CORUM; P30999; -. DR DIP; DIP-31972N; -. DR IntAct; P30999; 23. DR MINT; P30999; -. DR STRING; 10090.ENSMUSP00000141166; -. DR GlyConnect; 2420; 5 N-Linked glycans (1 site). [P30999-2] DR GlyGen; P30999; 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 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 eggNOG; KOG1048; Eukaryota. DR GeneTree; ENSGT00940000156045; -. DR HOGENOM; CLU_009111_1_0_1; -. DR InParanoid; P30999; -. 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; 0 hits in 12 CRISPR screens. DR ChiTaRS; Ctnnd1; mouse. DR PRO; PR:P30999; -. DR Proteomes; UP000000589; Chromosome 2. DR RNAct; P30999; protein. DR Bgee; ENSMUSG00000034101; Expressed in undifferentiated genital tubercle and 74 other tissues. DR ExpressionAtlas; P30999; baseline and differential. DR Genevisible; P30999; MM. DR GO; GO:0005912; C:adherens junction; IDA:MGI. 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:MGI. 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: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: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 COILED 10..46 FT /evidence="ECO:0000255" 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:0000244|PubMed:21183079" FT MOD_RES 59 FT /note="Phosphothreonine" FT /evidence="ECO:0000244|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:0000244|PubMed:15592455" FT MOD_RES 221 FT /note="Phosphotyrosine" FT /evidence="ECO:0000244|PubMed:15592455" FT MOD_RES 225 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:21183079" FT MOD_RES 228 FT /note="Phosphotyrosine" FT /evidence="ECO:0000244|PubMed:19131326" FT MOD_RES 230 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:17242355, FT ECO:0000244|PubMed:21183079" FT MOD_RES 252 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:17242355, FT ECO:0000244|PubMed:21183079" FT MOD_RES 257 FT /note="Phosphotyrosine" FT /evidence="ECO:0000244|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:0000244|PubMed:21183079" FT MOD_RES 280 FT /note="Phosphotyrosine" FT /evidence="ECO:0000244|PubMed:15592455" FT MOD_RES 288 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:17242355, FT ECO:0000244|PubMed:21183079" FT MOD_RES 291 FT /note="Phosphotyrosine" FT /evidence="ECO:0000244|PubMed:21183079" FT MOD_RES 300 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:21183079" FT MOD_RES 304 FT /note="Phosphothreonine" FT /evidence="ECO:0000244|PubMed:21183079" FT MOD_RES 320 FT /note="Phosphoserine" FT /evidence="ECO:0000244|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:0000244|PubMed:17242355, FT ECO:0000244|PubMed:18630941, ECO:0000244|PubMed:19131326, FT ECO:0000244|PubMed:21183079" FT MOD_RES 352 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:19131326, FT ECO:0000244|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:0000244|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:0000244|PubMed:17242355, FT ECO:0000244|PubMed:21183079" FT MOD_RES 857 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:17242355, FT ECO:0000244|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:0000244|PubMed:21183079" FT MOD_RES 865 FT /note="Phosphotyrosine" FT /evidence="ECO:0000244|PubMed:17242355, FT ECO:0000244|PubMed:21183079" FT MOD_RES 868 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:21183079" FT MOD_RES 869 FT /note="Phosphothreonine" FT /evidence="ECO:0000244|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:0000244|PubMed:17242355, FT ECO:0000244|PubMed:21183079" FT MOD_RES 904 FT /note="Phosphotyrosine" FT /evidence="ECO:0000244|PubMed:17947660, FT ECO:0000244|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:0000244|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 //