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Conserved domains on  [gi|28573789|ref|NP_788363|]
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dystroglycan, isoform D [Drosophila melanogaster]

Protein Classification

cadherin repeat domain-containing protein( domain architecture ID 10344465)

cadherin repeat domain-containing protein similar to Homo sapiens desmoglein-2, which is involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion; cadherins are are calcium-dependent cell adhesion proteins that preferentially interact with themselves in connecting cells

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DAG1 super family cl12309
Dystroglycan (Dystrophin-associated glycoprotein 1); Dystroglycan is one of the ...
 989-1262 5.51e-139

Dystroglycan (Dystrophin-associated glycoprotein 1); Dystroglycan is one of the dystrophin-associated glycoproteins, which is encoded by a 5.5 kb transcript in human. The protein product is cleaved into two non-covalently associated subunits, [alpha] (N-terminal) and [beta] (C-terminal). In skeletal muscle the dystroglycan complex works as a transmembrane linkage between the extracellular matrix and the cytoskeleton. [alpha]-dystroglycan is extracellular and binds to merosin ([alpha]-2 laminin) in the basement membrane, while [beta]-dystroglycan is a transmembrane protein and binds to dystrophin, which is a large rod-like cytoskeletal protein, absent in Duchenne muscular dystrophy patients. Dystrophin binds to intracellular actin cables. In this way, the dystroglycan complex, which links the extracellular matrix to the intracellular actin cables, is thought to provide structural integrity in muscle tissues. The dystroglycan complex is also known to serve as an agrin receptor in muscle, where it may regulate agrin-induced acetylcholine receptor clustering at the neuromuscular junction. There is also evidence which suggests the function of dystroglycan as a part of the signal transduction pathway because it is shown that Grb2, a mediator of the Ras-related signal pathway, can interact with the cytoplasmic domain of dystroglycan. In general, aberrant expression of dystrophin-associated protein complex underlies the pathogenesis of Duchenne muscular dystrophy, Becker muscular dystrophy and severe childhood autosomal recessive muscular dystrophy. Interestingly, no genetic disease has been described for either [alpha]- or [beta]-dystroglycan. Dystroglycan is widely distributed in non-muscle tissues as well as in muscle tissues. During epithelial morphogenesis of kidney, the dystroglycan complex is shown to act as a receptor for the basement membrane. Dystroglycan expression in mouse brain and neural retina has also been reported. However, the physiological role of dystroglycan in non-muscle tissues has remained unclear.


The actual alignment was detected with superfamily member pfam05454:

Pssm-ID: 461655  Cd Length: 290  Bit Score: 424.41  E-value: 5.51e-139
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573789    989 FFFKAYLSIKHERFNADLQRK--FVERVAKLNGDPTTGQIQIRSITthhdSDGTIVNFYNTTLyrKHNSCREKEVAMTRS 1066
Cdd:pfam05454    1 VFFKAKFSGDHERVNNDIHKKilLVKKLAFAFGDRNSSTITLRSIT----KGSIIVEWTNNTL--PHEPCPKEQVAGLSK 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573789   1067 VYLNSDLSLREAAKRALGPELNLTNFSVVPFSICHHTENIDTNQLDYIPSR------PEEPTHKSSFGEDYMITFVWPIV 1140
Cdd:pfam05454   75 KILDSDGSPREAFKNALEPEFKLTNISVVGSGSCRHTEFIPTNQLDYIPSRtpptgtPDRPTEKSSEDDVYLHTVIPAVV 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573789   1141 IIVAMLVAASIIACCLHwcRQRSGKMELgdeEERKSFRAKGIPVIFQDEYEE-KPEIGNKSPVILKDEKPPLLPPSYNTS 1219
Cdd:pfam05454  155 VAAILLIAGIIAMICYR--KKRKGKLTL---EDQATFIKKGVPIIFADELDDsKPPPSSSMPLILKEEKPPLPPPEYPNQ 229

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28573789   1220 NM------------------NGDNDVDDYVPPPSVVVGGREVRGKSPATPSYRKPPPYVSP 1262
Cdd:pfam05454  230 NVpettplnqdllgeytplrDEDPNAPPYQPPPPFTAPMEGKGSRPKNMTPYRSPPPYVPP 290
alpha_DG_C super family cl16905
C-terminal domain of alpha dystroglycan; Dystroglycan is a glycoprotein widely distributed in ...
 60-190 1.98e-39

C-terminal domain of alpha dystroglycan; Dystroglycan is a glycoprotein widely distributed in skeletal muscle and other tissues; the pre-protein is cleaved into two subunits (alpha and beta) that form a complex which links the extracellular matrix to the cytoskeleton. This C-terminal domain of the alpha-subunit appears to contact neighboring cadherin-like repeats of alpha dystroglycan, and may also be involved in interactions with other components of the dystrophin-dystroglycan-complex (DGC). DGC has been shown to interact with extracellular matrix components such as laminin, perlecan and m-agrin, suggesting that the complex may play various different roles depending on the extracellular ligand.


The actual alignment was detected with superfamily member cd11305:

Pssm-ID: 473046  Cd Length: 124  Bit Score: 142.47  E-value: 1.98e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573789   60 SCQNTPSEIVLSLLLKKHdWSELTATKRAHVQAKLAKFFAIPKEFISLDSVSKRELRSMHklAMRKGGKGNKNIetlNRR 139
Cdd:cd11305    1 VCPNGEPVTVLTVILDAD-LSKLTPKQRVHLLNKLAKFLGLPLDAFKLLPVSNNGLFDMS--ALMAGPGNVKKA---NEA 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 28573789  140 LGRASFMIGCGPSYfvMGEPIAKQIAHQMKDGTIGALTEENFGLWFIWRKE 190
Cdd:cd11305   75 GTLLSWQVGCGGDL--NHLPLVSQLEEQAKDGTLAEVLGLPVIGWHVANKK 123
Dystroglycan_repeat cd11303
Cadherin-like repeat domain of alpha dystroglycan; Dystroglycan is a glycoprotein widely ...
 885-986 3.14e-24

Cadherin-like repeat domain of alpha dystroglycan; Dystroglycan is a glycoprotein widely distributed in skeletal muscle and other tissues; the pre-protein is cleaved into two subunits (alpha and beta) that form a complex which links the extracellular matrix to the cytoskeleton. Cadherin-like dystroglycan repeats are present in the extracellular alpha-dystroglycan subunit, which binds to the alpha-2-laminin G-domain in the basement membrane as part of the dystrophin-dystroglycan-complex (DGC). DGC has been shown to interact with other etxtracellular matrix components as well, such as perlecan and m-agrin, suggesting that the complex may play various different roles depending on the extracellular ligand.


:

Pssm-ID: 206636 [Multi-domain]  Cd Length: 99  Bit Score: 98.20  E-value: 3.14e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573789  885 MPRNQVDRVNASLGQLLVYKVPADTFYDANDN-QLTLTLKTrdhlelSPRHWLQFDSKNEEFYGIPKSGDIGSEEYLLVA 963
Cdd:cd11303    1 SPLWGIPDLVAVVGRLFTYKIPPDTFSGNGDTyQVSEAGKD------DLPSWLQFDSSSRTLYGLPLSDDVGVHYISVTA 74

                         90       100
                 ....*....|....*....|....*
gi 28573789  964 EDSG--GLSAHDALVVVVSPAPKRD 986
Cdd:cd11303   75 EDKGsaGSQASDVFSIDVHPEPHPE 99
Dystroglycan_repeat cd11303
Cadherin-like repeat domain of alpha dystroglycan; Dystroglycan is a glycoprotein widely ...
 654-758 2.09e-23

Cadherin-like repeat domain of alpha dystroglycan; Dystroglycan is a glycoprotein widely distributed in skeletal muscle and other tissues; the pre-protein is cleaved into two subunits (alpha and beta) that form a complex which links the extracellular matrix to the cytoskeleton. Cadherin-like dystroglycan repeats are present in the extracellular alpha-dystroglycan subunit, which binds to the alpha-2-laminin G-domain in the basement membrane as part of the dystrophin-dystroglycan-complex (DGC). DGC has been shown to interact with other etxtracellular matrix components as well, such as perlecan and m-agrin, suggesting that the complex may play various different roles depending on the extracellular ligand.


:

Pssm-ID: 206636 [Multi-domain]  Cd Length: 99  Bit Score: 95.89  E-value: 2.09e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573789  654 IIKTRLQKLAVTSGKAFTFHVLPETFYDAEDqgNLRLALTDKDGhelkANSWLQFNADKRELYGLPLDDTVSRWQYRLSA 733
Cdd:cd11303    1 SPLWGIPDLVAVVGRLFTYKIPPDTFSGNGD--TYQVSEAGKDD----LPSWLQFDSSSRTLYGLPLSDDVGVHYISVTA 74

                         90       100
                 ....*....|....*....|....*
gi 28573789  734 TDSGNASVTETVEISVQQHRAVRTI 758
Cdd:cd11303   75 EDKGSAGSQASDVFSIDVHPEPHPE 99
 
Name Accession Description Interval E-value
DAG1 pfam05454
Dystroglycan (Dystrophin-associated glycoprotein 1); Dystroglycan is one of the ...
 989-1262 5.51e-139

Dystroglycan (Dystrophin-associated glycoprotein 1); Dystroglycan is one of the dystrophin-associated glycoproteins, which is encoded by a 5.5 kb transcript in human. The protein product is cleaved into two non-covalently associated subunits, [alpha] (N-terminal) and [beta] (C-terminal). In skeletal muscle the dystroglycan complex works as a transmembrane linkage between the extracellular matrix and the cytoskeleton. [alpha]-dystroglycan is extracellular and binds to merosin ([alpha]-2 laminin) in the basement membrane, while [beta]-dystroglycan is a transmembrane protein and binds to dystrophin, which is a large rod-like cytoskeletal protein, absent in Duchenne muscular dystrophy patients. Dystrophin binds to intracellular actin cables. In this way, the dystroglycan complex, which links the extracellular matrix to the intracellular actin cables, is thought to provide structural integrity in muscle tissues. The dystroglycan complex is also known to serve as an agrin receptor in muscle, where it may regulate agrin-induced acetylcholine receptor clustering at the neuromuscular junction. There is also evidence which suggests the function of dystroglycan as a part of the signal transduction pathway because it is shown that Grb2, a mediator of the Ras-related signal pathway, can interact with the cytoplasmic domain of dystroglycan. In general, aberrant expression of dystrophin-associated protein complex underlies the pathogenesis of Duchenne muscular dystrophy, Becker muscular dystrophy and severe childhood autosomal recessive muscular dystrophy. Interestingly, no genetic disease has been described for either [alpha]- or [beta]-dystroglycan. Dystroglycan is widely distributed in non-muscle tissues as well as in muscle tissues. During epithelial morphogenesis of kidney, the dystroglycan complex is shown to act as a receptor for the basement membrane. Dystroglycan expression in mouse brain and neural retina has also been reported. However, the physiological role of dystroglycan in non-muscle tissues has remained unclear.


Pssm-ID: 461655  Cd Length: 290  Bit Score: 424.41  E-value: 5.51e-139
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573789    989 FFFKAYLSIKHERFNADLQRK--FVERVAKLNGDPTTGQIQIRSITthhdSDGTIVNFYNTTLyrKHNSCREKEVAMTRS 1066
Cdd:pfam05454    1 VFFKAKFSGDHERVNNDIHKKilLVKKLAFAFGDRNSSTITLRSIT----KGSIIVEWTNNTL--PHEPCPKEQVAGLSK 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573789   1067 VYLNSDLSLREAAKRALGPELNLTNFSVVPFSICHHTENIDTNQLDYIPSR------PEEPTHKSSFGEDYMITFVWPIV 1140
Cdd:pfam05454   75 KILDSDGSPREAFKNALEPEFKLTNISVVGSGSCRHTEFIPTNQLDYIPSRtpptgtPDRPTEKSSEDDVYLHTVIPAVV 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573789   1141 IIVAMLVAASIIACCLHwcRQRSGKMELgdeEERKSFRAKGIPVIFQDEYEE-KPEIGNKSPVILKDEKPPLLPPSYNTS 1219
Cdd:pfam05454  155 VAAILLIAGIIAMICYR--KKRKGKLTL---EDQATFIKKGVPIIFADELDDsKPPPSSSMPLILKEEKPPLPPPEYPNQ 229

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28573789   1220 NM------------------NGDNDVDDYVPPPSVVVGGREVRGKSPATPSYRKPPPYVSP 1262
Cdd:pfam05454  230 NVpettplnqdllgeytplrDEDPNAPPYQPPPPFTAPMEGKGSRPKNMTPYRSPPPYVPP 290
alpha_DG_C cd11305
C-terminal domain of alpha dystroglycan; Dystroglycan is a glycoprotein widely distributed in ...
 60-190 1.98e-39

C-terminal domain of alpha dystroglycan; Dystroglycan is a glycoprotein widely distributed in skeletal muscle and other tissues; the pre-protein is cleaved into two subunits (alpha and beta) that form a complex which links the extracellular matrix to the cytoskeleton. This C-terminal domain of the alpha-subunit appears to contact neighboring cadherin-like repeats of alpha dystroglycan, and may also be involved in interactions with other components of the dystrophin-dystroglycan-complex (DGC). DGC has been shown to interact with extracellular matrix components such as laminin, perlecan and m-agrin, suggesting that the complex may play various different roles depending on the extracellular ligand.


Pssm-ID: 206765  Cd Length: 124  Bit Score: 142.47  E-value: 1.98e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573789   60 SCQNTPSEIVLSLLLKKHdWSELTATKRAHVQAKLAKFFAIPKEFISLDSVSKRELRSMHklAMRKGGKGNKNIetlNRR 139
Cdd:cd11305    1 VCPNGEPVTVLTVILDAD-LSKLTPKQRVHLLNKLAKFLGLPLDAFKLLPVSNNGLFDMS--ALMAGPGNVKKA---NEA 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 28573789  140 LGRASFMIGCGPSYfvMGEPIAKQIAHQMKDGTIGALTEENFGLWFIWRKE 190
Cdd:cd11305   75 GTLLSWQVGCGGDL--NHLPLVSQLEEQAKDGTLAEVLGLPVIGWHVANKK 123
Dystroglycan_repeat cd11303
Cadherin-like repeat domain of alpha dystroglycan; Dystroglycan is a glycoprotein widely ...
 885-986 3.14e-24

Cadherin-like repeat domain of alpha dystroglycan; Dystroglycan is a glycoprotein widely distributed in skeletal muscle and other tissues; the pre-protein is cleaved into two subunits (alpha and beta) that form a complex which links the extracellular matrix to the cytoskeleton. Cadherin-like dystroglycan repeats are present in the extracellular alpha-dystroglycan subunit, which binds to the alpha-2-laminin G-domain in the basement membrane as part of the dystrophin-dystroglycan-complex (DGC). DGC has been shown to interact with other etxtracellular matrix components as well, such as perlecan and m-agrin, suggesting that the complex may play various different roles depending on the extracellular ligand.


Pssm-ID: 206636 [Multi-domain]  Cd Length: 99  Bit Score: 98.20  E-value: 3.14e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573789  885 MPRNQVDRVNASLGQLLVYKVPADTFYDANDN-QLTLTLKTrdhlelSPRHWLQFDSKNEEFYGIPKSGDIGSEEYLLVA 963
Cdd:cd11303    1 SPLWGIPDLVAVVGRLFTYKIPPDTFSGNGDTyQVSEAGKD------DLPSWLQFDSSSRTLYGLPLSDDVGVHYISVTA 74

                         90       100
                 ....*....|....*....|....*
gi 28573789  964 EDSG--GLSAHDALVVVVSPAPKRD 986
Cdd:cd11303   75 EDKGsaGSQASDVFSIDVHPEPHPE 99
Dystroglycan_repeat cd11303
Cadherin-like repeat domain of alpha dystroglycan; Dystroglycan is a glycoprotein widely ...
 654-758 2.09e-23

Cadherin-like repeat domain of alpha dystroglycan; Dystroglycan is a glycoprotein widely distributed in skeletal muscle and other tissues; the pre-protein is cleaved into two subunits (alpha and beta) that form a complex which links the extracellular matrix to the cytoskeleton. Cadherin-like dystroglycan repeats are present in the extracellular alpha-dystroglycan subunit, which binds to the alpha-2-laminin G-domain in the basement membrane as part of the dystrophin-dystroglycan-complex (DGC). DGC has been shown to interact with other etxtracellular matrix components as well, such as perlecan and m-agrin, suggesting that the complex may play various different roles depending on the extracellular ligand.


Pssm-ID: 206636 [Multi-domain]  Cd Length: 99  Bit Score: 95.89  E-value: 2.09e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573789  654 IIKTRLQKLAVTSGKAFTFHVLPETFYDAEDqgNLRLALTDKDGhelkANSWLQFNADKRELYGLPLDDTVSRWQYRLSA 733
Cdd:cd11303    1 SPLWGIPDLVAVVGRLFTYKIPPDTFSGNGD--TYQVSEAGKDD----LPSWLQFDSSSRTLYGLPLSDDVGVHYISVTA 74

                         90       100
                 ....*....|....*....|....*
gi 28573789  734 TDSGNASVTETVEISVQQHRAVRTI 758
Cdd:cd11303   75 EDKGSAGSQASDVFSIDVHPEPHPE 99
CADG smart00736
Dystroglycan-type cadherin-like domains; Cadherin-homologous domains present in metazoan ...
 657-752 3.66e-21

Dystroglycan-type cadherin-like domains; Cadherin-homologous domains present in metazoan dystroglycans and alpha/epsilon sarcoglycans, yeast Axl2p and in a very large protein from magnetotactic bacteria. Likely to bind calcium ions.


Pssm-ID: 214795 [Multi-domain]  Cd Length: 97  Bit Score: 89.32  E-value: 3.66e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573789     657 TRLQKLAVTSGKAFTFHVLPETFYDAeDQGNLRLALTDKDGHELKanSWLQFNADKRELYGLPLDDTVSRWQYRLSATDS 736
Cdd:smart00736    2 NAIGDQTATEGESFSYTIPSSTFTDA-DGDTLTYSATLSDGSALP--SWLSFDSDTGTLSGTPTNSDVGSLSLKVTATDS 78

                            90
                    ....*....|....*.
gi 28573789     737 GNASVTETVEISVQQH 752
Cdd:smart00736   79 SGASASDTFTITVVNT 94
CADG smart00736
Dystroglycan-type cadherin-like domains; Cadherin-homologous domains present in metazoan ...
 888-983 4.80e-21

Dystroglycan-type cadherin-like domains; Cadherin-homologous domains present in metazoan dystroglycans and alpha/epsilon sarcoglycans, yeast Axl2p and in a very large protein from magnetotactic bacteria. Likely to bind calcium ions.


Pssm-ID: 214795 [Multi-domain]  Cd Length: 97  Bit Score: 88.94  E-value: 4.80e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573789     888 NQVDRVNASLGQLLVYKVPADTFYDANDNQLTLTLKTRDHLELspRHWLQFDSKNEEFYGIPKSGDIGSEEYLLVAEDSG 967
Cdd:smart00736    2 NAIGDQTATEGESFSYTIPSSTFTDADGDTLTYSATLSDGSAL--PSWLSFDSDTGTLSGTPTNSDVGSLSLKVTATDSS 79

                            90
                    ....*....|....*.
gi 28573789     968 GLSAHDALVVVVSPAP 983
Cdd:smart00736   80 GASASDTFTITVVNTN 95
He_PIG pfam05345
Putative Ig domain; This alignment represents the conserved core region of ~90 residue repeat ...
 653-749 2.64e-04

Putative Ig domain; This alignment represents the conserved core region of ~90 residue repeat found in several haemagglutinins and other cell surface proteins. Sequence similarities to (pfam02494) and (pfam00801) suggest an Ig-like fold (personal obs:C. Yeats). So this family may be similar in function to the (pfam02639) and (pfam02638) domains. This domain is also found in the WisP family of proteins of Tropheryma whipplei.


Pssm-ID: 398814 [Multi-domain]  Cd Length: 95  Bit Score: 41.30  E-value: 2.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573789    653 PIIKTRLQKLAVTSGKAFTFHVLPETFYDAEDQGNLRLALTDKDGHelkANSWLQFNADKRELYGLPLDDTVSRWQYRLS 732
Cdd:pfam05345    1 PPVVTSPADQTATVGTPYSFTLSASGGSDPYGGSTVTYSTTATGGA---LPSGLTLNSSTGTISGTPTSVQPGTYTFTVT 77

                           90
                   ....*....|....*..
gi 28573789    733 ATDSGNASVTETVEISV 749
Cdd:pfam05345   78 ATDSSGLSSSTTFTLTV 94
 
Name Accession Description Interval E-value
DAG1 pfam05454
Dystroglycan (Dystrophin-associated glycoprotein 1); Dystroglycan is one of the ...
 989-1262 5.51e-139

Dystroglycan (Dystrophin-associated glycoprotein 1); Dystroglycan is one of the dystrophin-associated glycoproteins, which is encoded by a 5.5 kb transcript in human. The protein product is cleaved into two non-covalently associated subunits, [alpha] (N-terminal) and [beta] (C-terminal). In skeletal muscle the dystroglycan complex works as a transmembrane linkage between the extracellular matrix and the cytoskeleton. [alpha]-dystroglycan is extracellular and binds to merosin ([alpha]-2 laminin) in the basement membrane, while [beta]-dystroglycan is a transmembrane protein and binds to dystrophin, which is a large rod-like cytoskeletal protein, absent in Duchenne muscular dystrophy patients. Dystrophin binds to intracellular actin cables. In this way, the dystroglycan complex, which links the extracellular matrix to the intracellular actin cables, is thought to provide structural integrity in muscle tissues. The dystroglycan complex is also known to serve as an agrin receptor in muscle, where it may regulate agrin-induced acetylcholine receptor clustering at the neuromuscular junction. There is also evidence which suggests the function of dystroglycan as a part of the signal transduction pathway because it is shown that Grb2, a mediator of the Ras-related signal pathway, can interact with the cytoplasmic domain of dystroglycan. In general, aberrant expression of dystrophin-associated protein complex underlies the pathogenesis of Duchenne muscular dystrophy, Becker muscular dystrophy and severe childhood autosomal recessive muscular dystrophy. Interestingly, no genetic disease has been described for either [alpha]- or [beta]-dystroglycan. Dystroglycan is widely distributed in non-muscle tissues as well as in muscle tissues. During epithelial morphogenesis of kidney, the dystroglycan complex is shown to act as a receptor for the basement membrane. Dystroglycan expression in mouse brain and neural retina has also been reported. However, the physiological role of dystroglycan in non-muscle tissues has remained unclear.


Pssm-ID: 461655  Cd Length: 290  Bit Score: 424.41  E-value: 5.51e-139
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573789    989 FFFKAYLSIKHERFNADLQRK--FVERVAKLNGDPTTGQIQIRSITthhdSDGTIVNFYNTTLyrKHNSCREKEVAMTRS 1066
Cdd:pfam05454    1 VFFKAKFSGDHERVNNDIHKKilLVKKLAFAFGDRNSSTITLRSIT----KGSIIVEWTNNTL--PHEPCPKEQVAGLSK 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573789   1067 VYLNSDLSLREAAKRALGPELNLTNFSVVPFSICHHTENIDTNQLDYIPSR------PEEPTHKSSFGEDYMITFVWPIV 1140
Cdd:pfam05454   75 KILDSDGSPREAFKNALEPEFKLTNISVVGSGSCRHTEFIPTNQLDYIPSRtpptgtPDRPTEKSSEDDVYLHTVIPAVV 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573789   1141 IIVAMLVAASIIACCLHwcRQRSGKMELgdeEERKSFRAKGIPVIFQDEYEE-KPEIGNKSPVILKDEKPPLLPPSYNTS 1219
Cdd:pfam05454  155 VAAILLIAGIIAMICYR--KKRKGKLTL---EDQATFIKKGVPIIFADELDDsKPPPSSSMPLILKEEKPPLPPPEYPNQ 229

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28573789   1220 NM------------------NGDNDVDDYVPPPSVVVGGREVRGKSPATPSYRKPPPYVSP 1262
Cdd:pfam05454  230 NVpettplnqdllgeytplrDEDPNAPPYQPPPPFTAPMEGKGSRPKNMTPYRSPPPYVPP 290
alpha_DG_C cd11305
C-terminal domain of alpha dystroglycan; Dystroglycan is a glycoprotein widely distributed in ...
 60-190 1.98e-39

C-terminal domain of alpha dystroglycan; Dystroglycan is a glycoprotein widely distributed in skeletal muscle and other tissues; the pre-protein is cleaved into two subunits (alpha and beta) that form a complex which links the extracellular matrix to the cytoskeleton. This C-terminal domain of the alpha-subunit appears to contact neighboring cadherin-like repeats of alpha dystroglycan, and may also be involved in interactions with other components of the dystrophin-dystroglycan-complex (DGC). DGC has been shown to interact with extracellular matrix components such as laminin, perlecan and m-agrin, suggesting that the complex may play various different roles depending on the extracellular ligand.


Pssm-ID: 206765  Cd Length: 124  Bit Score: 142.47  E-value: 1.98e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573789   60 SCQNTPSEIVLSLLLKKHdWSELTATKRAHVQAKLAKFFAIPKEFISLDSVSKRELRSMHklAMRKGGKGNKNIetlNRR 139
Cdd:cd11305    1 VCPNGEPVTVLTVILDAD-LSKLTPKQRVHLLNKLAKFLGLPLDAFKLLPVSNNGLFDMS--ALMAGPGNVKKA---NEA 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 28573789  140 LGRASFMIGCGPSYfvMGEPIAKQIAHQMKDGTIGALTEENFGLWFIWRKE 190
Cdd:cd11305   75 GTLLSWQVGCGGDL--NHLPLVSQLEEQAKDGTLAEVLGLPVIGWHVANKK 123
Dystroglycan_repeat cd11303
Cadherin-like repeat domain of alpha dystroglycan; Dystroglycan is a glycoprotein widely ...
 885-986 3.14e-24

Cadherin-like repeat domain of alpha dystroglycan; Dystroglycan is a glycoprotein widely distributed in skeletal muscle and other tissues; the pre-protein is cleaved into two subunits (alpha and beta) that form a complex which links the extracellular matrix to the cytoskeleton. Cadherin-like dystroglycan repeats are present in the extracellular alpha-dystroglycan subunit, which binds to the alpha-2-laminin G-domain in the basement membrane as part of the dystrophin-dystroglycan-complex (DGC). DGC has been shown to interact with other etxtracellular matrix components as well, such as perlecan and m-agrin, suggesting that the complex may play various different roles depending on the extracellular ligand.


Pssm-ID: 206636 [Multi-domain]  Cd Length: 99  Bit Score: 98.20  E-value: 3.14e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573789  885 MPRNQVDRVNASLGQLLVYKVPADTFYDANDN-QLTLTLKTrdhlelSPRHWLQFDSKNEEFYGIPKSGDIGSEEYLLVA 963
Cdd:cd11303    1 SPLWGIPDLVAVVGRLFTYKIPPDTFSGNGDTyQVSEAGKD------DLPSWLQFDSSSRTLYGLPLSDDVGVHYISVTA 74

                         90       100
                 ....*....|....*....|....*
gi 28573789  964 EDSG--GLSAHDALVVVVSPAPKRD 986
Cdd:cd11303   75 EDKGsaGSQASDVFSIDVHPEPHPE 99
Dystroglycan_repeat cd11303
Cadherin-like repeat domain of alpha dystroglycan; Dystroglycan is a glycoprotein widely ...
 654-758 2.09e-23

Cadherin-like repeat domain of alpha dystroglycan; Dystroglycan is a glycoprotein widely distributed in skeletal muscle and other tissues; the pre-protein is cleaved into two subunits (alpha and beta) that form a complex which links the extracellular matrix to the cytoskeleton. Cadherin-like dystroglycan repeats are present in the extracellular alpha-dystroglycan subunit, which binds to the alpha-2-laminin G-domain in the basement membrane as part of the dystrophin-dystroglycan-complex (DGC). DGC has been shown to interact with other etxtracellular matrix components as well, such as perlecan and m-agrin, suggesting that the complex may play various different roles depending on the extracellular ligand.


Pssm-ID: 206636 [Multi-domain]  Cd Length: 99  Bit Score: 95.89  E-value: 2.09e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573789  654 IIKTRLQKLAVTSGKAFTFHVLPETFYDAEDqgNLRLALTDKDGhelkANSWLQFNADKRELYGLPLDDTVSRWQYRLSA 733
Cdd:cd11303    1 SPLWGIPDLVAVVGRLFTYKIPPDTFSGNGD--TYQVSEAGKDD----LPSWLQFDSSSRTLYGLPLSDDVGVHYISVTA 74

                         90       100
                 ....*....|....*....|....*
gi 28573789  734 TDSGNASVTETVEISVQQHRAVRTI 758
Cdd:cd11303   75 EDKGSAGSQASDVFSIDVHPEPHPE 99
CADG smart00736
Dystroglycan-type cadherin-like domains; Cadherin-homologous domains present in metazoan ...
 657-752 3.66e-21

Dystroglycan-type cadherin-like domains; Cadherin-homologous domains present in metazoan dystroglycans and alpha/epsilon sarcoglycans, yeast Axl2p and in a very large protein from magnetotactic bacteria. Likely to bind calcium ions.


Pssm-ID: 214795 [Multi-domain]  Cd Length: 97  Bit Score: 89.32  E-value: 3.66e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573789     657 TRLQKLAVTSGKAFTFHVLPETFYDAeDQGNLRLALTDKDGHELKanSWLQFNADKRELYGLPLDDTVSRWQYRLSATDS 736
Cdd:smart00736    2 NAIGDQTATEGESFSYTIPSSTFTDA-DGDTLTYSATLSDGSALP--SWLSFDSDTGTLSGTPTNSDVGSLSLKVTATDS 78

                            90
                    ....*....|....*.
gi 28573789     737 GNASVTETVEISVQQH 752
Cdd:smart00736   79 SGASASDTFTITVVNT 94
CADG smart00736
Dystroglycan-type cadherin-like domains; Cadherin-homologous domains present in metazoan ...
 888-983 4.80e-21

Dystroglycan-type cadherin-like domains; Cadherin-homologous domains present in metazoan dystroglycans and alpha/epsilon sarcoglycans, yeast Axl2p and in a very large protein from magnetotactic bacteria. Likely to bind calcium ions.


Pssm-ID: 214795 [Multi-domain]  Cd Length: 97  Bit Score: 88.94  E-value: 4.80e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573789     888 NQVDRVNASLGQLLVYKVPADTFYDANDNQLTLTLKTRDHLELspRHWLQFDSKNEEFYGIPKSGDIGSEEYLLVAEDSG 967
Cdd:smart00736    2 NAIGDQTATEGESFSYTIPSSTFTDADGDTLTYSATLSDGSAL--PSWLSFDSDTGTLSGTPTNSDVGSLSLKVTATDSS 79

                            90
                    ....*....|....*.
gi 28573789     968 GLSAHDALVVVVSPAP 983
Cdd:smart00736   80 GASASDTFTITVVNTN 95
He_PIG pfam05345
Putative Ig domain; This alignment represents the conserved core region of ~90 residue repeat ...
 653-749 2.64e-04

Putative Ig domain; This alignment represents the conserved core region of ~90 residue repeat found in several haemagglutinins and other cell surface proteins. Sequence similarities to (pfam02494) and (pfam00801) suggest an Ig-like fold (personal obs:C. Yeats). So this family may be similar in function to the (pfam02639) and (pfam02638) domains. This domain is also found in the WisP family of proteins of Tropheryma whipplei.


Pssm-ID: 398814 [Multi-domain]  Cd Length: 95  Bit Score: 41.30  E-value: 2.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573789    653 PIIKTRLQKLAVTSGKAFTFHVLPETFYDAEDQGNLRLALTDKDGHelkANSWLQFNADKRELYGLPLDDTVSRWQYRLS 732
Cdd:pfam05345    1 PPVVTSPADQTATVGTPYSFTLSASGGSDPYGGSTVTYSTTATGGA---LPSGLTLNSSTGTISGTPTSVQPGTYTFTVT 77

                           90
                   ....*....|....*..
gi 28573789    733 ATDSGNASVTETVEISV 749
Cdd:pfam05345   78 ATDSSGLSSSTTFTLTV 94
 
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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