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Conserved domains on  [gi|1937288970|ref|XP_037819933|]
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armadillo segment polarity protein isoform X3 [Lucilia sericata]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CTNNAbd_CTNNB1-like super family cl45904
alpha-catenin binding domain found in catenin beta-1 (CTNNB1), catenin gamma (CTNNG) and ...
85-159 1.24e-47

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.


The actual alignment was detected with superfamily member cd21726:

Pssm-ID: 459249  Cd Length: 75  Bit Score: 162.58  E-value: 1.24e-47
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1937288970  85 EQVDDMNSQLSQTRSQRIRAAMFPETLEEGIEIPSTQFDPQQPTAVQRLAEPSQMLKHAVVNLINYQDDAELATR 159
Cdd:cd21726     1 EQVDEMNQQLNQTRSQRVRAAMFPETLEEGVQIPSTQFDPQQPTAVQRLAEPSQMLKHAVVNLINYQDDADLATR 75
Arm pfam00514
Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form ...
361-398 2.25e-06

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.


:

Pssm-ID: 425727 [Multi-domain]  Cd Length: 41  Bit Score: 44.75  E-value: 2.25e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1937288970 361 NKPAIVDAGGMQALAMHLGNPSPRLVQNCLWTLRNLSD 398
Cdd:pfam00514   4 NKQAVIEAGAVPPLVRLLSSPDEEVQEEAAWALSNLAA 41
Arm pfam00514
Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form ...
597-636 1.33e-05

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.


:

Pssm-ID: 425727 [Multi-domain]  Cd Length: 41  Bit Score: 42.44  E-value: 1.33e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1937288970 597 SHNRALIRQQSVIPIFVRLLFNEIENIQRVAAGVLCELAA 636
Cdd:pfam00514   2 PENKQAVIEAGAVPPLVRLLSSPDEEVQEEAAWALSNLAA 41
Adaptin_N super family cl37648
Adaptin N terminal region; This family consists of the N terminal region of various alpha, ...
150-304 1.50e-05

Adaptin N terminal region; This family consists of the N terminal region of various alpha, beta and gamma subunits of the AP-1, AP-2 and AP-3 adaptor protein complexes. The adaptor protein (AP) complexes are involved in the formation of clathrin-coated pits and vesicles. The N-terminal region of the various adaptor proteins (APs) is constant by comparison to the C-terminal which is variable within members of the AP-2 family; and it has been proposed that this constant region interacts with another uniform component of the coated vesicles.


The actual alignment was detected with superfamily member pfam01602:

Pssm-ID: 396262 [Multi-domain]  Cd Length: 523  Bit Score: 48.39  E-value: 1.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937288970 150 YQDDAELATRAIPELIKLLNDEDQVVVSQAAMMVHQLSKKEasrHAIMN-SPQMVAALVRAISNSNDLESTKaAVGTLHN 228
Cdd:pfam01602 142 YRKSPDLVRDFVPELKELLSDKDPGVQSAAVALLYEICKND---RLYLKlLPLLFRRLCNLLGVLNPWLQVK-ILRLLTR 217
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1937288970 229 LSHHRQGLLAIFksggIPALVKLLSSPVESVLFYAITTLHNLLLHQDGSKMAVrlagglQKMVTLL--QRNNVKFLAI 304
Cdd:pfam01602 218 LAPLDPLLPKEL----LEDLLNLLQNSNNAVLYETANTIVHLAPAPELIVLAV------NALGRLLssPDENLRYVAL 285
Arm pfam00514
Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form ...
439-481 2.85e-03

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.


:

Pssm-ID: 425727 [Multi-domain]  Cd Length: 41  Bit Score: 35.89  E-value: 2.85e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1937288970 439 NQRNKATVCQVGGVDALVRTIINagDREEITEPAVCALRHLTT 481
Cdd:pfam00514   1 SPENKQAVIEAGAVPPLVRLLSS--PDEEVQEEAAWALSNLAA 41
 
Name Accession Description Interval E-value
CTNNAbd_dArm cd21726
alpha-catenin binding domain found in Drosophila melanogaster armadillo segment polarity ...
85-159 1.24e-47

alpha-catenin binding domain found in Drosophila melanogaster armadillo segment polarity protein (dArm) and similar proteins; dArm is a Drosophila catenin that plays a role during central nervous system development. It can associate with alpha-catenin. The neural isoform of dArm 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-terminus of dArm, which shows high sequence similarity with alpha-catenin binding domain of catenin beta-1 (CTNNB1).


Pssm-ID: 439243  Cd Length: 75  Bit Score: 162.58  E-value: 1.24e-47
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1937288970  85 EQVDDMNSQLSQTRSQRIRAAMFPETLEEGIEIPSTQFDPQQPTAVQRLAEPSQMLKHAVVNLINYQDDAELATR 159
Cdd:cd21726     1 EQVDEMNQQLNQTRSQRVRAAMFPETLEEGVQIPSTQFDPQQPTAVQRLAEPSQMLKHAVVNLINYQDDADLATR 75
Arm pfam00514
Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form ...
361-398 2.25e-06

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.


Pssm-ID: 425727 [Multi-domain]  Cd Length: 41  Bit Score: 44.75  E-value: 2.25e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1937288970 361 NKPAIVDAGGMQALAMHLGNPSPRLVQNCLWTLRNLSD 398
Cdd:pfam00514   4 NKQAVIEAGAVPPLVRLLSSPDEEVQEEAAWALSNLAA 41
ARM smart00185
Armadillo/beta-catenin-like repeats; Approx. 40 amino acid repeat. Tandem repeats form ...
358-398 3.29e-06

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.


Pssm-ID: 214547 [Multi-domain]  Cd Length: 41  Bit Score: 44.34  E-value: 3.29e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1937288970  358 CSSNKPAIVDAGGMQALAMHLGNPSPRLVQNCLWTLRNLSD 398
Cdd:smart00185   1 DDENKQAVVDAGGLPALVELLKSEDEEVVKEAAWALSNLSS 41
Arm pfam00514
Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form ...
597-636 1.33e-05

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.


Pssm-ID: 425727 [Multi-domain]  Cd Length: 41  Bit Score: 42.44  E-value: 1.33e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1937288970 597 SHNRALIRQQSVIPIFVRLLFNEIENIQRVAAGVLCELAA 636
Cdd:pfam00514   2 PENKQAVIEAGAVPPLVRLLSSPDEEVQEEAAWALSNLAA 41
Adaptin_N pfam01602
Adaptin N terminal region; This family consists of the N terminal region of various alpha, ...
150-304 1.50e-05

Adaptin N terminal region; This family consists of the N terminal region of various alpha, beta and gamma subunits of the AP-1, AP-2 and AP-3 adaptor protein complexes. The adaptor protein (AP) complexes are involved in the formation of clathrin-coated pits and vesicles. The N-terminal region of the various adaptor proteins (APs) is constant by comparison to the C-terminal which is variable within members of the AP-2 family; and it has been proposed that this constant region interacts with another uniform component of the coated vesicles.


Pssm-ID: 396262 [Multi-domain]  Cd Length: 523  Bit Score: 48.39  E-value: 1.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937288970 150 YQDDAELATRAIPELIKLLNDEDQVVVSQAAMMVHQLSKKEasrHAIMN-SPQMVAALVRAISNSNDLESTKaAVGTLHN 228
Cdd:pfam01602 142 YRKSPDLVRDFVPELKELLSDKDPGVQSAAVALLYEICKND---RLYLKlLPLLFRRLCNLLGVLNPWLQVK-ILRLLTR 217
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1937288970 229 LSHHRQGLLAIFksggIPALVKLLSSPVESVLFYAITTLHNLLLHQDGSKMAVrlagglQKMVTLL--QRNNVKFLAI 304
Cdd:pfam01602 218 LAPLDPLLPKEL----LEDLLNLLQNSNNAVLYETANTIVHLAPAPELIVLAV------NALGRLLssPDENLRYVAL 285
ARM smart00185
Armadillo/beta-catenin-like repeats; Approx. 40 amino acid repeat. Tandem repeats form ...
238-270 2.56e-05

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.


Pssm-ID: 214547 [Multi-domain]  Cd Length: 41  Bit Score: 41.65  E-value: 2.56e-05
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1937288970  238 AIFKSGGIPALVKLLSSPVESVLFYAITTLHNL 270
Cdd:smart00185   7 AVVDAGGLPALVELLKSEDEEVVKEAAWALSNL 39
PLN03200 PLN03200
cellulose synthase-interactive protein; Provisional
161-385 3.85e-05

cellulose synthase-interactive protein; Provisional


Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 47.40  E-value: 3.85e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937288970  161 IPELIKLLNDEDQVVVSQAAMMVHQLSKKEASRHA---IMNSPQMVAALVRAISNSNDLESTKAA--VGTLHNLSHHRQG 235
Cdd:PLN03200   101 IPPLLSLLKSGSAEAQKAAAEAIYAVSSGGLSDHVgskIFSTEGVVPSLWDQLQPGNKQDKVVEGllTGALRNLCGSTDG 180
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937288970  236 LL-AIFKSGGIPALVKLLSSPVESVLFYAITTLHNLLLHQDGSKMAVRLAGGLQKMVTLLQRNNVKFL-AIVTDCLQILA 313
Cdd:PLN03200   181 FWsATLEAGGVDILVKLLSSGNSDAQANAASLLARLMMAFESSISKVLDAGAVKQLLKLLGQGNEVSVrAEAAGALEALS 260
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937288970  314 YGNQESKLIILASGGPNELVRIMRSYDYEKLLWTTSRVLKVLSVCSSnkpAIVdAGGMQALAMHLGN--PSPRL 385
Cdd:PLN03200   261 SQSKEAKQAIADAGGIPALINATVAPSKEFMQGEFAQALQENAMGAL---ANI-CGGMSALILYLGElsESPRS 330
SRP1 COG5064
Karyopherin (importin) alpha [Intracellular trafficking and secretion];
150-439 1.53e-03

Karyopherin (importin) alpha [Intracellular trafficking and secretion];


Pssm-ID: 227396 [Multi-domain]  Cd Length: 526  Bit Score: 41.80  E-value: 1.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937288970 150 YQDDAELATRAIPELIKLLNDED----QVVVSQAAMmvhqlskkeasrhaimnsPQMVAALVraiSNSNDLESTKAAVGT 225
Cdd:COG5064    81 FSDDIEQQLQAVYKFRKLLSKETsppiQPVIDAGVV------------------PRFVEFMD---EIQRDMLQFEAAWAL 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937288970 226 LHNLSHHRQGLLAIFKSGGIPALVKLLSSPVESVLFYAITTLHNLLLHQDGSKMAVRLAGGLQKMVTLLQRN--NVKFLA 303
Cdd:COG5064   140 TNIASGTTQQTKVVVDAGAVPLFIQLLSSTEDDVREQAVWALGNIAGDSEGCRDYVLQCGALEPLLGLLLSSaiHISMLR 219
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937288970 304 IVTDCLQILAYGNQESKLIILASGGPNELVRIMRSYDYEKL---LWTTSRVLKVLSVCSSnkpAIVDAGGMQALAMHLGN 380
Cdd:COG5064   220 NATWTLSNLCRGKNPPPDWSNISQALPILAKLIYSRDPEVLvdaCWAISYLSDGPNEKIQ---AVLDVGIPGRLVELLSH 296
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937288970 381 PSPRLVQNCLWTLRNL---SDAATKVDGMEALLQSLVQVLASTDVNVVTCAAGILSNLTCNN 439
Cdd:COG5064   297 ESAKIQTPALRSVGNIvtgSDDQTQVIINCGALKAFRSLLSSPKENIRKEACWTISNITAGN 358
Arm pfam00514
Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form ...
439-481 2.85e-03

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.


Pssm-ID: 425727 [Multi-domain]  Cd Length: 41  Bit Score: 35.89  E-value: 2.85e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1937288970 439 NQRNKATVCQVGGVDALVRTIINagDREEITEPAVCALRHLTT 481
Cdd:pfam00514   1 SPENKQAVIEAGAVPPLVRLLSS--PDEEVQEEAAWALSNLAA 41
ARM smart00185
Armadillo/beta-catenin-like repeats; Approx. 40 amino acid repeat. Tandem repeats form ...
597-636 3.83e-03

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.


Pssm-ID: 214547 [Multi-domain]  Cd Length: 41  Bit Score: 35.48  E-value: 3.83e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1937288970  597 SHNRALIRQQSVIPIFVRLLFNEIENIQRVAAGVLCELAA 636
Cdd:smart00185   2 DENKQAVVDAGGLPALVELLKSEDEEVVKEAAWALSNLSS 41
 
Name Accession Description Interval E-value
CTNNAbd_dArm cd21726
alpha-catenin binding domain found in Drosophila melanogaster armadillo segment polarity ...
85-159 1.24e-47

alpha-catenin binding domain found in Drosophila melanogaster armadillo segment polarity protein (dArm) and similar proteins; dArm is a Drosophila catenin that plays a role during central nervous system development. It can associate with alpha-catenin. The neural isoform of dArm 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-terminus of dArm, which shows high sequence similarity with alpha-catenin binding domain of catenin beta-1 (CTNNB1).


Pssm-ID: 439243  Cd Length: 75  Bit Score: 162.58  E-value: 1.24e-47
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1937288970  85 EQVDDMNSQLSQTRSQRIRAAMFPETLEEGIEIPSTQFDPQQPTAVQRLAEPSQMLKHAVVNLINYQDDAELATR 159
Cdd:cd21726     1 EQVDEMNQQLNQTRSQRVRAAMFPETLEEGVQIPSTQFDPQQPTAVQRLAEPSQMLKHAVVNLINYQDDADLATR 75
CTNNAbd_CTNNB1-like cd21719
alpha-catenin binding domain found in catenin beta-1 (CTNNB1), catenin gamma (CTNNG) and ...
90-159 8.66e-40

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.


Pssm-ID: 439240  Cd Length: 70  Bit Score: 140.50  E-value: 8.66e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937288970  90 MNSQLSQTRSQRIRAAMFPETLEEGIEIPSTQFDPQQPTAVQRLAEPSQMLKHAVVNLINYQDDAELATR 159
Cdd:cd21719     1 LNDQLTQTRAQRVRAAMFPETLDEGEEIPSTQFDPGRSTNVQRLAEPSQLLKTAVVNLINYQDDADLATR 70
CTNNAbd_CTNNB1 cd21724
alpha-catenin binding domain found in catenin beta-1 (CTNNB1) and similar proteins; CTNNB1, ...
86-159 2.77e-34

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.


Pssm-ID: 439241  Cd Length: 74  Bit Score: 125.37  E-value: 2.77e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937288970  86 QVDDMNSQLSQTRSQRIRAAMFPETLEEGIEIPSTQFDPQQPTAVQRLAEPSQMLKHAVVNLINYQDDAELATR 159
Cdd:cd21724     1 QVADIDGQYAMTRAQRVRAAMFPETLDEGMQIPSTQFDAAHPTNVQRLAEPSQMLKHAVVNLINYQDDAELATR 74
CTNNAbd_CTNNG cd21725
alpha-catenin binding domain found in catenin gamma (CTNNG) and similar proteins; CTNNG, also ...
90-159 1.14e-29

alpha-catenin binding domain found in catenin gamma (CTNNG) and similar proteins; 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. This model corresponds to a small region at the C-terminus of CTNNG, which shows high sequence similarity with alpha-catenin binding domain of catenin beta-1 (CTNNB1).


Pssm-ID: 439242  Cd Length: 70  Bit Score: 111.89  E-value: 1.14e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937288970  90 MNSQLSQTRSQRIRAAMFPETLEEGIEIPSTQFDPQQPTAVQRLAEPSQMLKHAVVNLINYQDDAELATR 159
Cdd:cd21725     1 MESQLTMTRAQRVRAAMFPETVEEGSYLLSTQIEPSQQTNVQKLAEPSQMLKSAIVHLINYQDDAELATR 70
Arm pfam00514
Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form ...
361-398 2.25e-06

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.


Pssm-ID: 425727 [Multi-domain]  Cd Length: 41  Bit Score: 44.75  E-value: 2.25e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1937288970 361 NKPAIVDAGGMQALAMHLGNPSPRLVQNCLWTLRNLSD 398
Cdd:pfam00514   4 NKQAVIEAGAVPPLVRLLSSPDEEVQEEAAWALSNLAA 41
ARM smart00185
Armadillo/beta-catenin-like repeats; Approx. 40 amino acid repeat. Tandem repeats form ...
358-398 3.29e-06

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.


Pssm-ID: 214547 [Multi-domain]  Cd Length: 41  Bit Score: 44.34  E-value: 3.29e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1937288970  358 CSSNKPAIVDAGGMQALAMHLGNPSPRLVQNCLWTLRNLSD 398
Cdd:smart00185   1 DDENKQAVVDAGGLPALVELLKSEDEEVVKEAAWALSNLSS 41
Arm pfam00514
Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form ...
597-636 1.33e-05

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.


Pssm-ID: 425727 [Multi-domain]  Cd Length: 41  Bit Score: 42.44  E-value: 1.33e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1937288970 597 SHNRALIRQQSVIPIFVRLLFNEIENIQRVAAGVLCELAA 636
Cdd:pfam00514   2 PENKQAVIEAGAVPPLVRLLSSPDEEVQEEAAWALSNLAA 41
Adaptin_N pfam01602
Adaptin N terminal region; This family consists of the N terminal region of various alpha, ...
150-304 1.50e-05

Adaptin N terminal region; This family consists of the N terminal region of various alpha, beta and gamma subunits of the AP-1, AP-2 and AP-3 adaptor protein complexes. The adaptor protein (AP) complexes are involved in the formation of clathrin-coated pits and vesicles. The N-terminal region of the various adaptor proteins (APs) is constant by comparison to the C-terminal which is variable within members of the AP-2 family; and it has been proposed that this constant region interacts with another uniform component of the coated vesicles.


Pssm-ID: 396262 [Multi-domain]  Cd Length: 523  Bit Score: 48.39  E-value: 1.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937288970 150 YQDDAELATRAIPELIKLLNDEDQVVVSQAAMMVHQLSKKEasrHAIMN-SPQMVAALVRAISNSNDLESTKaAVGTLHN 228
Cdd:pfam01602 142 YRKSPDLVRDFVPELKELLSDKDPGVQSAAVALLYEICKND---RLYLKlLPLLFRRLCNLLGVLNPWLQVK-ILRLLTR 217
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1937288970 229 LSHHRQGLLAIFksggIPALVKLLSSPVESVLFYAITTLHNLLLHQDGSKMAVrlagglQKMVTLL--QRNNVKFLAI 304
Cdd:pfam01602 218 LAPLDPLLPKEL----LEDLLNLLQNSNNAVLYETANTIVHLAPAPELIVLAV------NALGRLLssPDENLRYVAL 285
Arm pfam00514
Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form ...
238-270 2.03e-05

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.


Pssm-ID: 425727 [Multi-domain]  Cd Length: 41  Bit Score: 42.06  E-value: 2.03e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1937288970 238 AIFKSGGIPALVKLLSSPVESVLFYAITTLHNL 270
Cdd:pfam00514   7 AVIEAGAVPPLVRLLSSPDEEVQEEAAWALSNL 39
ARM smart00185
Armadillo/beta-catenin-like repeats; Approx. 40 amino acid repeat. Tandem repeats form ...
238-270 2.56e-05

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.


Pssm-ID: 214547 [Multi-domain]  Cd Length: 41  Bit Score: 41.65  E-value: 2.56e-05
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1937288970  238 AIFKSGGIPALVKLLSSPVESVLFYAITTLHNL 270
Cdd:smart00185   7 AVVDAGGLPALVELLKSEDEEVVKEAAWALSNL 39
PLN03200 PLN03200
cellulose synthase-interactive protein; Provisional
161-385 3.85e-05

cellulose synthase-interactive protein; Provisional


Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 47.40  E-value: 3.85e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937288970  161 IPELIKLLNDEDQVVVSQAAMMVHQLSKKEASRHA---IMNSPQMVAALVRAISNSNDLESTKAA--VGTLHNLSHHRQG 235
Cdd:PLN03200   101 IPPLLSLLKSGSAEAQKAAAEAIYAVSSGGLSDHVgskIFSTEGVVPSLWDQLQPGNKQDKVVEGllTGALRNLCGSTDG 180
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937288970  236 LL-AIFKSGGIPALVKLLSSPVESVLFYAITTLHNLLLHQDGSKMAVRLAGGLQKMVTLLQRNNVKFL-AIVTDCLQILA 313
Cdd:PLN03200   181 FWsATLEAGGVDILVKLLSSGNSDAQANAASLLARLMMAFESSISKVLDAGAVKQLLKLLGQGNEVSVrAEAAGALEALS 260
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937288970  314 YGNQESKLIILASGGPNELVRIMRSYDYEKLLWTTSRVLKVLSVCSSnkpAIVdAGGMQALAMHLGN--PSPRL 385
Cdd:PLN03200   261 SQSKEAKQAIADAGGIPALINATVAPSKEFMQGEFAQALQENAMGAL---ANI-CGGMSALILYLGElsESPRS 330
SRP1 COG5064
Karyopherin (importin) alpha [Intracellular trafficking and secretion];
150-439 1.53e-03

Karyopherin (importin) alpha [Intracellular trafficking and secretion];


Pssm-ID: 227396 [Multi-domain]  Cd Length: 526  Bit Score: 41.80  E-value: 1.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937288970 150 YQDDAELATRAIPELIKLLNDED----QVVVSQAAMmvhqlskkeasrhaimnsPQMVAALVraiSNSNDLESTKAAVGT 225
Cdd:COG5064    81 FSDDIEQQLQAVYKFRKLLSKETsppiQPVIDAGVV------------------PRFVEFMD---EIQRDMLQFEAAWAL 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937288970 226 LHNLSHHRQGLLAIFKSGGIPALVKLLSSPVESVLFYAITTLHNLLLHQDGSKMAVRLAGGLQKMVTLLQRN--NVKFLA 303
Cdd:COG5064   140 TNIASGTTQQTKVVVDAGAVPLFIQLLSSTEDDVREQAVWALGNIAGDSEGCRDYVLQCGALEPLLGLLLSSaiHISMLR 219
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937288970 304 IVTDCLQILAYGNQESKLIILASGGPNELVRIMRSYDYEKL---LWTTSRVLKVLSVCSSnkpAIVDAGGMQALAMHLGN 380
Cdd:COG5064   220 NATWTLSNLCRGKNPPPDWSNISQALPILAKLIYSRDPEVLvdaCWAISYLSDGPNEKIQ---AVLDVGIPGRLVELLSH 296
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937288970 381 PSPRLVQNCLWTLRNL---SDAATKVDGMEALLQSLVQVLASTDVNVVTCAAGILSNLTCNN 439
Cdd:COG5064   297 ESAKIQTPALRSVGNIvtgSDDQTQVIINCGALKAFRSLLSSPKENIRKEACWTISNITAGN 358
HEAT COG1413
HEAT repeat [General function prediction only];
159-270 1.71e-03

HEAT repeat [General function prediction only];


Pssm-ID: 441023 [Multi-domain]  Cd Length: 137  Bit Score: 39.23  E-value: 1.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937288970 159 RAIPELIKLLNDEDQVVVSQAAMMVHQLskkeasrhaimNSPQMVAALVRAISNSNDlESTKAAVGTLHNLSHHRqglla 238
Cdd:COG1413    16 AAVPALIAALADEDPDVRAAAARALGRL-----------GDPRAVPALLEALKDPDP-EVRAAAAEALGRIGDPE----- 78
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1937288970 239 ifksgGIPALVKLLSSPVESVLFYAITTLHNL 270
Cdd:COG1413    79 -----AVPALIAALKDEDPEVRRAAAEALGRL 105
Arm pfam00514
Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form ...
439-481 2.85e-03

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.


Pssm-ID: 425727 [Multi-domain]  Cd Length: 41  Bit Score: 35.89  E-value: 2.85e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1937288970 439 NQRNKATVCQVGGVDALVRTIINagDREEITEPAVCALRHLTT 481
Cdd:pfam00514   1 SPENKQAVIEAGAVPPLVRLLSS--PDEEVQEEAAWALSNLAA 41
ARM smart00185
Armadillo/beta-catenin-like repeats; Approx. 40 amino acid repeat. Tandem repeats form ...
597-636 3.83e-03

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.


Pssm-ID: 214547 [Multi-domain]  Cd Length: 41  Bit Score: 35.48  E-value: 3.83e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1937288970  597 SHNRALIRQQSVIPIFVRLLFNEIENIQRVAAGVLCELAA 636
Cdd:smart00185   2 DENKQAVVDAGGLPALVELLKSEDEEVVKEAAWALSNLSS 41
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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