alpha-catenin binding domain found in catenin beta-1 (CTNNB1) and similar proteins; CTNNB1, also called beta-catenin, is a key downstream component of the canonical Wnt signaling pathway. In the absence of Wnt, it forms a complex with AXIN1, AXIN2, APC, CSNK1A1 and GSK3B that promotes phosphorylation on N-terminal Ser and Thr residues, and ubiquitination of CTNNB1 via BTRC and its subsequent degradation by the proteasome. In the presence of Wnt ligand, CTNNB1 is not ubiquitinated and accumulates in the nucleus, where it acts as a coactivator for transcription factors of the TCF/LEF family, leading to activation of Wnt responsive genes. CTNNB1 is involved in the regulation of cell adhesion as a component of an E-cadherin:catenin adhesion complex. It acts as a negative regulator of centrosome cohesion. It is involved in the CDK2/PTPN6/CTNNB1/CEACAM1 pathway of insulin internalization. It blocks anoikis of malignant kidney and intestinal epithelial cells and promotes their anchorage-independent growth by down-regulating DAPK2. It disrupts PML function and PML-NB formation by inhibiting RANBP2-mediated sumoylation of PML. This model corresponds to a small region at the C-terminus of CTNNB1, which is responsible for alpha-catenin binding.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1069363047  77 QVADIDGQYAMTRAQRVRAAMFPETLDEGMQIPSTQFDSAHPTNVQRLAEPSQMLKHAVVNLINYQDDAELATR 150
Cdd:cd21724     1 QVADIDGQYAMTRAQRVRAAMFPETLDEGMQIPSTQFDAAHPTNVQRLAEPSQMLKHAVVNLINYQDDAELATR 74

Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form super-helix of helices that is proposed to mediate interaction of beta-catenin with its ligands. CAUTION: This family does not contain all known armadillo repeats.

                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1069363047 584 HNRIVIRGLNTIPLFVQLLYSPIENIQRVAAGVLCELA 621
Cdd:pfam00514   3 ENKQAVIEAGAVPPLVRLLSSPDEEVQEEAAWALSNLA 40

cellulose synthase-interactive protein; Provisional

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069363047  215 GTLHNLSHHREGLL-AIFKSGGIPALVKMLGSPVDSVLFYAITTLHNLLLHQEGAKMAVRLAGGLQKMVALLNKTNVKFL 293
Cdd:PLN03200   169 GALRNLCGSTDGFWsATLEAGGVDILVKLLSSGNSDAQANAASLLARLMMAFESSISKVLDAGAVKQLLKLLGQGNEVSV 248

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069363047  294 -AITTDCLQILAYGNQESKLIILASGGPQALVNIMRTYSYEKLLWTTSRVLKVLSVCSSnkpAIVeAGGMQALGLHLTDS 372
Cdd:PLN03200   249 rAEAAGALEALSSQSKEAKQAIADAGGIPALINATVAPSKEFMQGEFAQALQENAMGAL---ANI-CGGMSALILYLGEL 324

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069363047  373 SQ--RLVQNCLWTLRNLSDAATKQEGMEG---------LLGTLVQLLGSDDINVV---TCAA-------GILSNLTCNNY 431
Cdd:PLN03200   325 SEspRSPAPIADTLGALAYALMVFDSSAEstrafdptvIEQILVKLLKPRDTKLVqerIIEAlaslygnAYLSRKLNHAE 404

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069363047  432 KNKMMVC----QVGGI-EALVRTVL----------RA-GDREDI--------------TEPAICALRHLTSRHQEAEMAQ 481
Cdd:PLN03200   405 AKKVLVGlitmATADVqEELIRALSslccgkgglwEAlGGREGVqllisllglsseqqQEYAVALLAILTDEVDESKWAI 484

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069363047  482 NAVRlhyGLPVVVKLLHPPSHwpliKA---TVGLIRNlaLCpaNH-----APLREQGAIPRLVQLLVRAHQDTQR----- 548
Cdd:PLN03200   485 TAAG---GIPPLVQLLETGSQ----KAkedSATVLWN--LC--CHsedirACVESAGAVPALLWLLKNGGPKGQEiaakt 553

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069363047  549 -----RTSMGGTQQQfVEGVRMEEIVEGCTGAL----HILARDIHNRIVIRGL---NTIPLFVQLLYSPIENIQRVAAGV 616
Cdd:PLN03200   554 ltklvRTADAATISQ-LTALLLGDLPESKVHVLdvlgHVLSVASLEDLVREGSaanDALRTLIQLLSSSKEETQEKAASV 632

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*...
gi 1069363047  617 LCEL-AQDKEAAEAIEAEGATAPLTELLHSRNEGVATYAA---AVLFR 660
Cdd:PLN03200   633 LADIfSSRQDLCESLATDEIINPCIKLLTNNTEAVATQSAralAALSR 680

alpha-catenin binding domain found in catenin beta-1 (CTNNB1) and similar proteins; CTNNB1, also called beta-catenin, is a key downstream component of the canonical Wnt signaling pathway. In the absence of Wnt, it forms a complex with AXIN1, AXIN2, APC, CSNK1A1 and GSK3B that promotes phosphorylation on N-terminal Ser and Thr residues, and ubiquitination of CTNNB1 via BTRC and its subsequent degradation by the proteasome. In the presence of Wnt ligand, CTNNB1 is not ubiquitinated and accumulates in the nucleus, where it acts as a coactivator for transcription factors of the TCF/LEF family, leading to activation of Wnt responsive genes. CTNNB1 is involved in the regulation of cell adhesion as a component of an E-cadherin:catenin adhesion complex. It acts as a negative regulator of centrosome cohesion. It is involved in the CDK2/PTPN6/CTNNB1/CEACAM1 pathway of insulin internalization. It blocks anoikis of malignant kidney and intestinal epithelial cells and promotes their anchorage-independent growth by down-regulating DAPK2. It disrupts PML function and PML-NB formation by inhibiting RANBP2-mediated sumoylation of PML. This model corresponds to a small region at the C-terminus of CTNNB1, which is responsible for alpha-catenin binding.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1069363047  77 QVADIDGQYAMTRAQRVRAAMFPETLDEGMQIPSTQFDSAHPTNVQRLAEPSQMLKHAVVNLINYQDDAELATR 150
Cdd:cd21724     1 QVADIDGQYAMTRAQRVRAAMFPETLDEGMQIPSTQFDAAHPTNVQRLAEPSQMLKHAVVNLINYQDDAELATR 74

Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form super-helix of helices that is proposed to mediate interaction of beta-catenin with its ligands. CAUTION: This family does not contain all known armadillo repeats.

                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1069363047 352 NKPAIVEAGGMQALGLHLTDSSQRLVQNCLWTLRNLSD 389
Cdd:pfam00514   4 NKQAVIEAGAVPPLVRLLSSPDEEVQEEAAWALSNLAA 41

Armadillo/beta-catenin-like repeats; Approx. 40 amino acid repeat. Tandem repeats form superhelix of helices that is proposed to mediate interaction of beta-catenin with its ligands. Involved in transducing the Wingless/Wnt signal. In plakoglobin arm repeats bind alpha-catenin and N-cadherin.

                           10        20        30
                   ....*....|....*....|....*....|...
gi 1069363047  229 AIFKSGGIPALVKMLGSPVDSVLFYAITTLHNL 261
Cdd:smart00185   7 AVVDAGGLPALVELLKSEDEEVVKEAAWALSNL 39

Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form super-helix of helices that is proposed to mediate interaction of beta-catenin with its ligands. CAUTION: This family does not contain all known armadillo repeats.

                          10        20        30
                  ....*....|....*....|....*....|...
gi 1069363047 229 AIFKSGGIPALVKMLGSPVDSVLFYAITTLHNL 261
Cdd:pfam00514   7 AVIEAGAVPPLVRLLSSPDEEVQEEAAWALSNL 39

Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form super-helix of helices that is proposed to mediate interaction of beta-catenin with its ligands. CAUTION: This family does not contain all known armadillo repeats.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1069363047 430 NYKNKMMVCQVGGIEALVRtVLRAGDrEDITEPAICALRHLTS 472
Cdd:pfam00514   1 SPENKQAVIEAGAVPPLVR-LLSSPD-EEVQEEAAWALSNLAA 41

alpha-catenin binding domain found in catenin beta-1 (CTNNB1) and similar proteins; CTNNB1, also called beta-catenin, is a key downstream component of the canonical Wnt signaling pathway. In the absence of Wnt, it forms a complex with AXIN1, AXIN2, APC, CSNK1A1 and GSK3B that promotes phosphorylation on N-terminal Ser and Thr residues, and ubiquitination of CTNNB1 via BTRC and its subsequent degradation by the proteasome. In the presence of Wnt ligand, CTNNB1 is not ubiquitinated and accumulates in the nucleus, where it acts as a coactivator for transcription factors of the TCF/LEF family, leading to activation of Wnt responsive genes. CTNNB1 is involved in the regulation of cell adhesion as a component of an E-cadherin:catenin adhesion complex. It acts as a negative regulator of centrosome cohesion. It is involved in the CDK2/PTPN6/CTNNB1/CEACAM1 pathway of insulin internalization. It blocks anoikis of malignant kidney and intestinal epithelial cells and promotes their anchorage-independent growth by down-regulating DAPK2. It disrupts PML function and PML-NB formation by inhibiting RANBP2-mediated sumoylation of PML. This model corresponds to a small region at the C-terminus of CTNNB1, which is responsible for alpha-catenin binding.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1069363047  77 QVADIDGQYAMTRAQRVRAAMFPETLDEGMQIPSTQFDSAHPTNVQRLAEPSQMLKHAVVNLINYQDDAELATR 150
Cdd:cd21724     1 QVADIDGQYAMTRAQRVRAAMFPETLDEGMQIPSTQFDAAHPTNVQRLAEPSQMLKHAVVNLINYQDDAELATR 74

alpha-catenin binding domain found in catenin beta-1 (CTNNB1), catenin gamma (CTNNG) and similar proteins; This family includes alpha-catenin binding domain found in catenin beta-1 (CTNNB1), catenin gamma (CTNNG), as well as Drosophila melanogaster armadillo segment polarity protein (dArm). CTNNB1, also called beta-catenin, is a key downstream component of the canonical Wnt signaling pathway. It is involved in the regulation of cell adhesion, as component of an E-cadherin:catenin adhesion complex. It acts as a negative regulator of centrosome cohesion. It is involved in the CDK2/PTPN6/CTNNB1/CEACAM1 pathway of insulin internalization. It blocks anoikis of malignant kidney and intestinal epithelial cells, and promotes their anchorage-independent growth by down-regulating DAPK2. It disrupts PML function and PML-NB formation by inhibiting RANBP2-mediated sumoylation of PML. CTNNG, also called junction plakoglobin (JUP), or desmoplakin III, or desmoplakin-3 (DP3), is a common junctional plaque protein. The membrane-associated plaques are architectural elements in an important strategic position to influence the arrangement and function of both the cytoskeleton and the cells within the tissue. The presence of plakoglobin in both the desmosomes and in the intermediate junctions suggests that it plays a central role in the structure and function of submembranous plaques. CTNNG acts as a substrate for VE-PTP and is required to stimulate VE-cadherin function in endothelial cells. It can replace beta-catenin in E-cadherin/catenin adhesion complexes which are proposed to couple cadherins to the actin cytoskeleton. dArm, which shows high sequence similarity with CTNNB1, is a Drosophila catenin that plays a role during central nervous system development. It can associate with alpha-catenin. Its neural isoform may associate with CadN and participate in the transmission of developmental information. Its cytoplasmic isoform accumulates through Wingless (Wg) signaling; arm function in Wg signal transduction is required early in development for determination of neuroblast fate. Arm and Abl proteins function cooperatively at adherens junctions in both the CNS and epidermis. This model corresponds to a small region at the C-termini of dArm, CTNNB1 and CTNNG; in CTNNB1, this region is responsible for alpha-catenin binding.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069363047  81 IDGQYAMTRAQRVRAAMFPETLDEGMQIPSTQFDSAHPTNVQRLAEPSQMLKHAVVNLINYQDDAELATR 150
Cdd:cd21719     1 LNDQLTQTRAQRVRAAMFPETLDEGEEIPSTQFDPGRSTNVQRLAEPSQLLKTAVVNLINYQDDADLATR 70

Armadillo/beta-catenin-like repeats; Approx. 40 amino acid repeat. Tandem repeats form superhelix of helices that is proposed to mediate interaction of beta-catenin with its ligands. Involved in transducing the Wingless/Wnt signal. In plakoglobin arm repeats bind alpha-catenin and N-cadherin.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1069363047  349 CSSNKPAIVEAGGMQALGLHLTDSSQRLVQNCLWTLRNLSD 389
Cdd:smart00185   1 DDENKQAVVDAGGLPALVELLKSEDEEVVKEAAWALSNLSS 41

Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form super-helix of helices that is proposed to mediate interaction of beta-catenin with its ligands. CAUTION: This family does not contain all known armadillo repeats.

                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1069363047 584 HNRIVIRGLNTIPLFVQLLYSPIENIQRVAAGVLCELA 621
Cdd:pfam00514   3 ENKQAVIEAGAVPPLVRLLSSPDEEVQEEAAWALSNLA 40

cellulose synthase-interactive protein; Provisional

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069363047  215 GTLHNLSHHREGLL-AIFKSGGIPALVKMLGSPVDSVLFYAITTLHNLLLHQEGAKMAVRLAGGLQKMVALLNKTNVKFL 293
Cdd:PLN03200   169 GALRNLCGSTDGFWsATLEAGGVDILVKLLSSGNSDAQANAASLLARLMMAFESSISKVLDAGAVKQLLKLLGQGNEVSV 248

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069363047  294 -AITTDCLQILAYGNQESKLIILASGGPQALVNIMRTYSYEKLLWTTSRVLKVLSVCSSnkpAIVeAGGMQALGLHLTDS 372
Cdd:PLN03200   249 rAEAAGALEALSSQSKEAKQAIADAGGIPALINATVAPSKEFMQGEFAQALQENAMGAL---ANI-CGGMSALILYLGEL 324

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069363047  373 SQ--RLVQNCLWTLRNLSDAATKQEGMEG---------LLGTLVQLLGSDDINVV---TCAA-------GILSNLTCNNY 431
Cdd:PLN03200   325 SEspRSPAPIADTLGALAYALMVFDSSAEstrafdptvIEQILVKLLKPRDTKLVqerIIEAlaslygnAYLSRKLNHAE 404

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069363047  432 KNKMMVC----QVGGI-EALVRTVL----------RA-GDREDI--------------TEPAICALRHLTSRHQEAEMAQ 481
Cdd:PLN03200   405 AKKVLVGlitmATADVqEELIRALSslccgkgglwEAlGGREGVqllisllglsseqqQEYAVALLAILTDEVDESKWAI 484

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069363047  482 NAVRlhyGLPVVVKLLHPPSHwpliKA---TVGLIRNlaLCpaNH-----APLREQGAIPRLVQLLVRAHQDTQR----- 548
Cdd:PLN03200   485 TAAG---GIPPLVQLLETGSQ----KAkedSATVLWN--LC--CHsedirACVESAGAVPALLWLLKNGGPKGQEiaakt 553

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069363047  549 -----RTSMGGTQQQfVEGVRMEEIVEGCTGAL----HILARDIHNRIVIRGL---NTIPLFVQLLYSPIENIQRVAAGV 616
Cdd:PLN03200   554 ltklvRTADAATISQ-LTALLLGDLPESKVHVLdvlgHVLSVASLEDLVREGSaanDALRTLIQLLSSSKEETQEKAASV 632

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*...
gi 1069363047  617 LCEL-AQDKEAAEAIEAEGATAPLTELLHSRNEGVATYAA---AVLFR 660
Cdd:PLN03200   633 LADIfSSRQDLCESLATDEIINPCIKLLTNNTEAVATQSAralAALSR 680

Armadillo/beta-catenin-like repeats; Approx. 40 amino acid repeat. Tandem repeats form superhelix of helices that is proposed to mediate interaction of beta-catenin with its ligands. Involved in transducing the Wingless/Wnt signal. In plakoglobin arm repeats bind alpha-catenin and N-cadherin.

                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1069363047  584 HNRIVIRGLNTIPLFVQLLYSPIENIQRVAAGVLCELAQ 622
Cdd:smart00185   3 ENKQAVVDAGGLPALVELLKSEDEEVVKEAAWALSNLSS 41

Armadillo/beta-catenin-like repeats; Approx. 40 amino acid repeat. Tandem repeats form superhelix of helices that is proposed to mediate interaction of beta-catenin with its ligands. Involved in transducing the Wingless/Wnt signal. In plakoglobin arm repeats bind alpha-catenin and N-cadherin.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1069363047  430 NYKNKMMVCQVGGIEALVRTVLRagDREDITEPAICALRHLTS 472
Cdd:smart00185   1 DDENKQAVVDAGGLPALVELLKS--EDEEVVKEAAWALSNLSS 41