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Conserved domains on  [gi|1831508489|ref|NP_001368642|]
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Protein inscuteable homologue C-terminal domain-containing protein [Caenorhabditis elegans]

Protein Classification

INSC_LBD superfamily-containing protein( domain architecture ID 1908151)

INSC_LBD superfamily-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
INSC_LBD super family cl41917
LGN-binding domain (LBD) of protein Inscuteable (INSC) and similar proteins; Inscuteable (INSC) ...
 367-662 1.34e-14

LGN-binding domain (LBD) of protein Inscuteable (INSC) and similar proteins; Inscuteable (INSC) functions as an adapter protein linking the Par polarity complex (composed of Par3, Par6 and protein kinase C iota) to the Gpsm1/Gpsm2 complex, and is involved in cell polarity and spindle orientation during mitosis. Par3 interacts with INSC which binds directly to Pins (partner of Insc, homolog of vertebrate LGN/Gpsm2 and AGS3/Gpsm1). Pins then associates with the heterotrimeric G proteins and NuMA, which interacts directly with the cell spindle to control the orientation of the spindle and the division plane of mitotic cells. INSC may regulate cell proliferation and differentiation in the developing nervous system, may play a role in the asymmetric division of fibroblasts, and may also participate in the process of stratification of the squamous epithelium. This model corresponds to the Leu-Gly-Asn Repeat-Enriched Protein (LGN)-binding domain (LBD) of INSC. It interacts with the tetratricopeptide repeat (TPR) motifs of LGN, also called G-protein-signaling modulator 2 (Gpsm2).


The actual alignment was detected with superfamily member pfam19427:

Pssm-ID: 477865  Cd Length: 394  Bit Score: 76.49  E-value: 1.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508489 367 TEMARLkmnVQELQKNRDKGIIDM--------NNMTNFFAILLRKSIESVLLVFVRIIsknlcESNGKDRLTPICLEHLI 438
Cdd:pfam19427   7 TELTKI---FQKLEKNRWQRVHSTavrlnchvRSMISEYSSFARNSSEEMQQILVRQI-----ESSDNIYTIESAISSLF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508489 439 HICLFGDELCIEAIQKGCISSVIRIMKNDQPQENTLRfLLRTLAVLCGVSKGALALLTQGGL----DLVIDrllSISSSI 514
Cdd:pfam19427  79 SLTQEGAQLCSIIAKEGGVVALFKICRQDCFRCLYPH-ALRTLASICCVEEGINQLEKVDGIlclaDILTD---ETHSEA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508489 515 CSVEAAGILTQLTNPQSAFIR-----LNHVEPIISRLLDLIDQCKSGDSLLLATAALNNVTLQNPNGVDIMYRNNSIRRL 589
Cdd:pfam19427 155 TRAEAAAVVAQITSPHLPFTQhlssfLENMEDIVTALIKLCQEASSGEVFLLASAALANITFFDTMACEMLLQLNAMKIL 234

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1831508489 590 ISA-YNRENCATVFVQEQIVTAFSRLAA-RHLDHQMVDQNAIPVLLEFL----SLTHPIHADYCRRIRYKAAVCIGTLA 662
Cdd:pfam19427 235 LEAcTDKQRVDTPYSRDQVVTILANMSVlEQCASDIIQENGIELLMEMLsekpSSGSPAEVAACERVQQKAAVTLARLS 313
 
Name Accession Description Interval E-value
Insc_C pfam19427
Protein inscuteable C-terminal; This entry represents the C-terminal region of protein ...
 367-662 1.34e-14

Protein inscuteable C-terminal; This entry represents the C-terminal region of protein Inscuteable (Insc) containing four putative armadillo repeats and the conserved extreme C-terminal tetrapeptide Glu-Ser-Phe-Val which is in agreement with the class I PDZ-binding motif X-Ser/Thr-X-/ (X and /are unspecified and hydrophobic residues, respectively). Insc functions as an adaptor protein that binds simultaneously with Partner of Insc (Pins, consisting of alpha subunit (Ga) of heterotrimeric G proteins and its guanine nucleotide dissociation inhibitor) and Par3 (PDZ-containing proteins) to regulate their apical localization in neuroblasts, which is required for the correct execution of the asymmetric division.


Pssm-ID: 466076  Cd Length: 394  Bit Score: 76.49  E-value: 1.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508489 367 TEMARLkmnVQELQKNRDKGIIDM--------NNMTNFFAILLRKSIESVLLVFVRIIsknlcESNGKDRLTPICLEHLI 438
Cdd:pfam19427   7 TELTKI---FQKLEKNRWQRVHSTavrlnchvRSMISEYSSFARNSSEEMQQILVRQI-----ESSDNIYTIESAISSLF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508489 439 HICLFGDELCIEAIQKGCISSVIRIMKNDQPQENTLRfLLRTLAVLCGVSKGALALLTQGGL----DLVIDrllSISSSI 514
Cdd:pfam19427  79 SLTQEGAQLCSIIAKEGGVVALFKICRQDCFRCLYPH-ALRTLASICCVEEGINQLEKVDGIlclaDILTD---ETHSEA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508489 515 CSVEAAGILTQLTNPQSAFIR-----LNHVEPIISRLLDLIDQCKSGDSLLLATAALNNVTLQNPNGVDIMYRNNSIRRL 589
Cdd:pfam19427 155 TRAEAAAVVAQITSPHLPFTQhlssfLENMEDIVTALIKLCQEASSGEVFLLASAALANITFFDTMACEMLLQLNAMKIL 234

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1831508489 590 ISA-YNRENCATVFVQEQIVTAFSRLAA-RHLDHQMVDQNAIPVLLEFL----SLTHPIHADYCRRIRYKAAVCIGTLA 662
Cdd:pfam19427 235 LEAcTDKQRVDTPYSRDQVVTILANMSVlEQCASDIIQENGIELLMEMLsekpSSGSPAEVAACERVQQKAAVTLARLS 313
INSC_LBD cd21966
LGN-binding domain (LBD) of protein Inscuteable (INSC) and similar proteins; Inscuteable (INSC) ...
 379-549 2.82e-05

LGN-binding domain (LBD) of protein Inscuteable (INSC) and similar proteins; Inscuteable (INSC) functions as an adapter protein linking the Par polarity complex (composed of Par3, Par6 and protein kinase C iota) to the Gpsm1/Gpsm2 complex, and is involved in cell polarity and spindle orientation during mitosis. Par3 interacts with INSC which binds directly to Pins (partner of Insc, homolog of vertebrate LGN/Gpsm2 and AGS3/Gpsm1). Pins then associates with the heterotrimeric G proteins and NuMA, which interacts directly with the cell spindle to control the orientation of the spindle and the division plane of mitotic cells. INSC may regulate cell proliferation and differentiation in the developing nervous system, may play a role in the asymmetric division of fibroblasts, and may also participate in the process of stratification of the squamous epithelium. This model corresponds to the Leu-Gly-Asn Repeat-Enriched Protein (LGN)-binding domain (LBD) of INSC. It interacts with the tetratricopeptide repeat (TPR) motifs of LGN, also called G-protein-signaling modulator 2 (Gpsm2).


Pssm-ID: 439320 [Multi-domain]  Cd Length: 300  Bit Score: 46.48  E-value: 2.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508489 379 LQKNRDKGIIDMNNMTNFFAILLRKSIESVLLVFVRIISKNLCESNGKDRLTpicleHLIHICLFGDELCIEAIQKGCIS 458
Cdd:cd21966   130 SKPNLEELLKLLTTLGQSFSKLVDLLLLKELQILVDSLEEPTSELSLRAALS-----ALTSLGLEGPHLCRLIAKEGGVR 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508489 459 SVIRI-MKNDQPQENTLrfLLRTLAVLCGVSKGALALLTQGGLDLVID-RLLSISSSICSVEAAGILTQLTNPqsaFIRL 536
Cdd:cd21966   205 ALLIVcRDCKSSSVRAL--ALRALATVCCVPEAIRQFEKAGGIEILSDiLTDESRSEPERSEAAGVLAQITSP---WIDD 279

                         170       180
                  ....*....|....*....|.
gi 1831508489 537 NH--------VEPIISRLLDL 549
Cdd:cd21966   280 NHhlsgliehMEDLVKALTRL 300
 
Name Accession Description Interval E-value
Insc_C pfam19427
Protein inscuteable C-terminal; This entry represents the C-terminal region of protein ...
 367-662 1.34e-14

Protein inscuteable C-terminal; This entry represents the C-terminal region of protein Inscuteable (Insc) containing four putative armadillo repeats and the conserved extreme C-terminal tetrapeptide Glu-Ser-Phe-Val which is in agreement with the class I PDZ-binding motif X-Ser/Thr-X-/ (X and /are unspecified and hydrophobic residues, respectively). Insc functions as an adaptor protein that binds simultaneously with Partner of Insc (Pins, consisting of alpha subunit (Ga) of heterotrimeric G proteins and its guanine nucleotide dissociation inhibitor) and Par3 (PDZ-containing proteins) to regulate their apical localization in neuroblasts, which is required for the correct execution of the asymmetric division.


Pssm-ID: 466076  Cd Length: 394  Bit Score: 76.49  E-value: 1.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508489 367 TEMARLkmnVQELQKNRDKGIIDM--------NNMTNFFAILLRKSIESVLLVFVRIIsknlcESNGKDRLTPICLEHLI 438
Cdd:pfam19427   7 TELTKI---FQKLEKNRWQRVHSTavrlnchvRSMISEYSSFARNSSEEMQQILVRQI-----ESSDNIYTIESAISSLF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508489 439 HICLFGDELCIEAIQKGCISSVIRIMKNDQPQENTLRfLLRTLAVLCGVSKGALALLTQGGL----DLVIDrllSISSSI 514
Cdd:pfam19427  79 SLTQEGAQLCSIIAKEGGVVALFKICRQDCFRCLYPH-ALRTLASICCVEEGINQLEKVDGIlclaDILTD---ETHSEA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508489 515 CSVEAAGILTQLTNPQSAFIR-----LNHVEPIISRLLDLIDQCKSGDSLLLATAALNNVTLQNPNGVDIMYRNNSIRRL 589
Cdd:pfam19427 155 TRAEAAAVVAQITSPHLPFTQhlssfLENMEDIVTALIKLCQEASSGEVFLLASAALANITFFDTMACEMLLQLNAMKIL 234

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1831508489 590 ISA-YNRENCATVFVQEQIVTAFSRLAA-RHLDHQMVDQNAIPVLLEFL----SLTHPIHADYCRRIRYKAAVCIGTLA 662
Cdd:pfam19427 235 LEAcTDKQRVDTPYSRDQVVTILANMSVlEQCASDIIQENGIELLMEMLsekpSSGSPAEVAACERVQQKAAVTLARLS 313
INSC_LBD cd21966
LGN-binding domain (LBD) of protein Inscuteable (INSC) and similar proteins; Inscuteable (INSC) ...
 379-549 2.82e-05

LGN-binding domain (LBD) of protein Inscuteable (INSC) and similar proteins; Inscuteable (INSC) functions as an adapter protein linking the Par polarity complex (composed of Par3, Par6 and protein kinase C iota) to the Gpsm1/Gpsm2 complex, and is involved in cell polarity and spindle orientation during mitosis. Par3 interacts with INSC which binds directly to Pins (partner of Insc, homolog of vertebrate LGN/Gpsm2 and AGS3/Gpsm1). Pins then associates with the heterotrimeric G proteins and NuMA, which interacts directly with the cell spindle to control the orientation of the spindle and the division plane of mitotic cells. INSC may regulate cell proliferation and differentiation in the developing nervous system, may play a role in the asymmetric division of fibroblasts, and may also participate in the process of stratification of the squamous epithelium. This model corresponds to the Leu-Gly-Asn Repeat-Enriched Protein (LGN)-binding domain (LBD) of INSC. It interacts with the tetratricopeptide repeat (TPR) motifs of LGN, also called G-protein-signaling modulator 2 (Gpsm2).


Pssm-ID: 439320 [Multi-domain]  Cd Length: 300  Bit Score: 46.48  E-value: 2.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508489 379 LQKNRDKGIIDMNNMTNFFAILLRKSIESVLLVFVRIISKNLCESNGKDRLTpicleHLIHICLFGDELCIEAIQKGCIS 458
Cdd:cd21966   130 SKPNLEELLKLLTTLGQSFSKLVDLLLLKELQILVDSLEEPTSELSLRAALS-----ALTSLGLEGPHLCRLIAKEGGVR 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508489 459 SVIRI-MKNDQPQENTLrfLLRTLAVLCGVSKGALALLTQGGLDLVID-RLLSISSSICSVEAAGILTQLTNPqsaFIRL 536
Cdd:cd21966   205 ALLIVcRDCKSSSVRAL--ALRALATVCCVPEAIRQFEKAGGIEILSDiLTDESRSEPERSEAAGVLAQITSP---WIDD 279

                         170       180
                  ....*....|....*....|.
gi 1831508489 537 NH--------VEPIISRLLDL 549
Cdd:cd21966   280 NHhlsgliehMEDLVKALTRL 300
 
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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