NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|23943822|ref|NP_705728|]
View 

calsyntenin-3 isoform 1 precursor [Mus musculus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
CLSTN_C pfam19699
Calsyntenin C-terminal; This is the cytoplasmic C-terminal domain of clasyntenin (CLSTN) ...
554-913 0e+00

Calsyntenin C-terminal; This is the cytoplasmic C-terminal domain of clasyntenin (CLSTN) proteins 1, 2 and 3 (also known as Alcadein-alpha, gamma and beta). These are postsynaptic Ca2-binding proteins, evolutionarily conserved type I membrane proteins. CLSTN forms a complex with APP and X11-like that stabilizes both APP and CLSTN proteins metabolically. CLSTN strongly associates with kinesin-1 light chains (KLC1) that induce kinesin-1 association with vesicles and functions as a novel cargo in axonal anterograde transport. This domain includes the WD motifs required for KLC1 interaction (although one WD motif is sufficient), and the NP motif.


:

Pssm-ID: 466150  Cd Length: 354  Bit Score: 611.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23943822   554 DYRDFESLGKGMKVHVNPSQSLLTLEGDDVETFNHALQHVAYMNTLRFATPGVRPLRLTTAVKCFSEESCVSIPEVEGYV 633
Cdd:pfam19699   1 DLQDPENSGSGVKVHFNPSQSVLTLEGDDIESLNKAMQHVSYVNSRQFPTPGVRRLKLTTSVKCFNEESCISIPDVEGYV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23943822   634 VVLQPDAPQILLSGTAHFARPAVDFEGPEGVPLFPDLQITCSISHQVEAKADESWQGTVTDTRMSDEIVHNLDGCEISLV 713
Cdd:pfam19699  81 MVLQPEEPKISLSGIDHFARPASEFESPEGVPLFPELRIVSTITREVESEGDGEDDPTVQESLVSEEIVHNLDGCEVTVL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23943822   714 GDDLDPERESLLLDMASLQQRGLELTNTSAYLTIAGVETITVYEEILRQARYQLRHGAALYARKFRLSCSEMNGRYSSNE 793
Cdd:pfam19699 161 GEELNPEQESLEVDMALLQQRGLEISSSTLGITITGVESMASYEEVLHLIRYRNWNTESLFERKFKLSCSELNGRYASNE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23943822   794 FIVEVNVLHSMNRVAHPSHVLSSQQFLHRGHQPPPEMAGHSLASSHRNSMVPSAATLIIVVCVGFLVLMVILGLVRIHSL 873
Cdd:pfam19699 241 FKVEVNVLHTANPVEHPNHMAAQPQFVHPVHHAFPDLSGHNLANPHPSSVVPSAATVVIVVCVSFLVFMIILGVFRIRSA 320
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 23943822   874 HRRVsgtggpSGASTDPKDPDLFWDDSALTIIVNPMESYQ 913
Cdd:pfam19699 321 HQRG------MRDQEGGKENEMDWDDSALTITVNPMETYE 354
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
32-140 5.62e-13

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


:

Pssm-ID: 206637 [Multi-domain]  Cd Length: 98  Bit Score: 65.80  E-value: 5.62e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23943822  32 EYQGIVMEND--NTVLLNppLFALDKDAPLryAGEIcGFRLHgSGVPFEAVILDKATGEglIRAKEPVDCEAQKEHTFTI 109
Cdd:cd11304   1 SYEVSVPENAppGTVVLT--VSATDPDSGE--NGEV-TYSIV-SGNEDGLFSIDPSTGE--ITTAKPLDREEQSSYTLTV 72
                        90       100       110
                ....*....|....*....|....*....|.
gi 23943822 110 QAYDCGEGPdgtntkKSHKATVHVRVNDVNE 140
Cdd:cd11304  73 TATDGGGPP------LSSTATVTITVLDVND 97
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
150-239 7.36e-10

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


:

Pssm-ID: 206637 [Multi-domain]  Cd Length: 98  Bit Score: 56.94  E-value: 7.36e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23943822 150 YRAAVTEG-KLYDRILRVEAIDGDcSPQYSQIcYYEILTPNT--PFLID-NDGNIENTEKLQYSGEKLYKFTVTAYDCGK 225
Cdd:cd11304   2 YEVSVPENaPPGTVVLTVSATDPD-SGENGEV-TYSIVSGNEdgLFSIDpSTGEITTAKPLDREEQSSYTLTVTATDGGG 79
                        90
                ....*....|....
gi 23943822 226 KRAADDAEVEIQVK 239
Cdd:cd11304  80 PPLSSTATVTITVL 93
 
Name Accession Description Interval E-value
CLSTN_C pfam19699
Calsyntenin C-terminal; This is the cytoplasmic C-terminal domain of clasyntenin (CLSTN) ...
554-913 0e+00

Calsyntenin C-terminal; This is the cytoplasmic C-terminal domain of clasyntenin (CLSTN) proteins 1, 2 and 3 (also known as Alcadein-alpha, gamma and beta). These are postsynaptic Ca2-binding proteins, evolutionarily conserved type I membrane proteins. CLSTN forms a complex with APP and X11-like that stabilizes both APP and CLSTN proteins metabolically. CLSTN strongly associates with kinesin-1 light chains (KLC1) that induce kinesin-1 association with vesicles and functions as a novel cargo in axonal anterograde transport. This domain includes the WD motifs required for KLC1 interaction (although one WD motif is sufficient), and the NP motif.


Pssm-ID: 466150  Cd Length: 354  Bit Score: 611.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23943822   554 DYRDFESLGKGMKVHVNPSQSLLTLEGDDVETFNHALQHVAYMNTLRFATPGVRPLRLTTAVKCFSEESCVSIPEVEGYV 633
Cdd:pfam19699   1 DLQDPENSGSGVKVHFNPSQSVLTLEGDDIESLNKAMQHVSYVNSRQFPTPGVRRLKLTTSVKCFNEESCISIPDVEGYV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23943822   634 VVLQPDAPQILLSGTAHFARPAVDFEGPEGVPLFPDLQITCSISHQVEAKADESWQGTVTDTRMSDEIVHNLDGCEISLV 713
Cdd:pfam19699  81 MVLQPEEPKISLSGIDHFARPASEFESPEGVPLFPELRIVSTITREVESEGDGEDDPTVQESLVSEEIVHNLDGCEVTVL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23943822   714 GDDLDPERESLLLDMASLQQRGLELTNTSAYLTIAGVETITVYEEILRQARYQLRHGAALYARKFRLSCSEMNGRYSSNE 793
Cdd:pfam19699 161 GEELNPEQESLEVDMALLQQRGLEISSSTLGITITGVESMASYEEVLHLIRYRNWNTESLFERKFKLSCSELNGRYASNE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23943822   794 FIVEVNVLHSMNRVAHPSHVLSSQQFLHRGHQPPPEMAGHSLASSHRNSMVPSAATLIIVVCVGFLVLMVILGLVRIHSL 873
Cdd:pfam19699 241 FKVEVNVLHTANPVEHPNHMAAQPQFVHPVHHAFPDLSGHNLANPHPSSVVPSAATVVIVVCVSFLVFMIILGVFRIRSA 320
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 23943822   874 HRRVsgtggpSGASTDPKDPDLFWDDSALTIIVNPMESYQ 913
Cdd:pfam19699 321 HQRG------MRDQEGGKENEMDWDDSALTITVNPMETYE 354
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
32-140 5.62e-13

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


Pssm-ID: 206637 [Multi-domain]  Cd Length: 98  Bit Score: 65.80  E-value: 5.62e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23943822  32 EYQGIVMEND--NTVLLNppLFALDKDAPLryAGEIcGFRLHgSGVPFEAVILDKATGEglIRAKEPVDCEAQKEHTFTI 109
Cdd:cd11304   1 SYEVSVPENAppGTVVLT--VSATDPDSGE--NGEV-TYSIV-SGNEDGLFSIDPSTGE--ITTAKPLDREEQSSYTLTV 72
                        90       100       110
                ....*....|....*....|....*....|.
gi 23943822 110 QAYDCGEGPdgtntkKSHKATVHVRVNDVNE 140
Cdd:cd11304  73 TATDGGGPP------LSSTATVTITVLDVND 97
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
52-143 6.48e-10

Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. Cadherin domains occur as repeats in the extracellular regions which are thought to mediate cell-cell contact when bound to calcium.


Pssm-ID: 214520 [Multi-domain]  Cd Length: 81  Bit Score: 56.20  E-value: 6.48e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23943822     52 ALDKDAPLRyaGEIcGFRLHgSGVPFEAVILDKATGEglIRAKEPVDCEAQKEHTFTIQAYDCGEGPDGTNtkkshkATV 131
Cdd:smart00112   2 ATDADSGEN--GKV-TYSIL-SGNDDGLFSIDPETGE--ITTTKPLDREEQPEYTLTVEATDGGGPPLSST------ATV 69
                           90
                   ....*....|..
gi 23943822    132 HVRVNDVNEFAP 143
Cdd:smart00112  70 TITVLDVNDNAP 81
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
150-239 7.36e-10

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


Pssm-ID: 206637 [Multi-domain]  Cd Length: 98  Bit Score: 56.94  E-value: 7.36e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23943822 150 YRAAVTEG-KLYDRILRVEAIDGDcSPQYSQIcYYEILTPNT--PFLID-NDGNIENTEKLQYSGEKLYKFTVTAYDCGK 225
Cdd:cd11304   2 YEVSVPENaPPGTVVLTVSATDPD-SGENGEV-TYSIVSGNEdgLFSIDpSTGEITTAKPLDREEQSSYTLTVTATDGGG 79
                        90
                ....*....|....
gi 23943822 226 KRAADDAEVEIQVK 239
Cdd:cd11304  80 PPLSSTATVTITVL 93
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
168-239 3.56e-05

Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. Cadherin domains occur as repeats in the extracellular regions which are thought to mediate cell-cell contact when bound to calcium.


Pssm-ID: 214520 [Multi-domain]  Cd Length: 81  Bit Score: 43.11  E-value: 3.56e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23943822    168 AIDGDcSPQYSQIcYYEILTPNT--PFLID-NDGNIENTEKLQYSGEKLYKFTVTAYDCGKKRAADDAEVEIQVK 239
Cdd:smart00112   2 ATDAD-SGENGKV-TYSILSGNDdgLFSIDpETGEITTTKPLDREEQPEYTLTVEATDGGGPPLSSTATVTITVL 74
Cadherin pfam00028
Cadherin domain;
150-238 3.34e-04

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 40.36  E-value: 3.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23943822   150 YRAAVTEGKLYD-RILRVEAIDGDCSPQySQIcYYEILTPNTP--FLID-NDGNIENTEKLQYSGEKLYKFTVTAYDCGK 225
Cdd:pfam00028   1 YSASVPENAPVGtEVLTVTATDPDLGPN-GRI-FYSILGGGPGgnFRIDpDTGDISTTKPLDRESIGEYELTVEATDSGG 78
                          90
                  ....*....|...
gi 23943822   226 KRAADDAEVEIQV 238
Cdd:pfam00028  79 PPLSSTATVTITV 91
Cadherin pfam00028
Cadherin domain;
33-135 4.02e-04

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 40.36  E-value: 4.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23943822    33 YQGIVMEN--DNTVLLNppLFALDKDAPL----RYAgeicgFRLHGSGVPFEaviLDKATGEglIRAKEPVDCEAQKEHT 106
Cdd:pfam00028   1 YSASVPENapVGTEVLT--VTATDPDLGPngriFYS-----ILGGGPGGNFR---IDPDTGD--ISTTKPLDRESIGEYE 68
                          90       100
                  ....*....|....*....|....*....
gi 23943822   107 FTIQAYDCGEGPdgtntkKSHKATVHVRV 135
Cdd:pfam00028  69 LTVEATDSGGPP------LSSTATVTITV 91
 
Name Accession Description Interval E-value
CLSTN_C pfam19699
Calsyntenin C-terminal; This is the cytoplasmic C-terminal domain of clasyntenin (CLSTN) ...
554-913 0e+00

Calsyntenin C-terminal; This is the cytoplasmic C-terminal domain of clasyntenin (CLSTN) proteins 1, 2 and 3 (also known as Alcadein-alpha, gamma and beta). These are postsynaptic Ca2-binding proteins, evolutionarily conserved type I membrane proteins. CLSTN forms a complex with APP and X11-like that stabilizes both APP and CLSTN proteins metabolically. CLSTN strongly associates with kinesin-1 light chains (KLC1) that induce kinesin-1 association with vesicles and functions as a novel cargo in axonal anterograde transport. This domain includes the WD motifs required for KLC1 interaction (although one WD motif is sufficient), and the NP motif.


Pssm-ID: 466150  Cd Length: 354  Bit Score: 611.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23943822   554 DYRDFESLGKGMKVHVNPSQSLLTLEGDDVETFNHALQHVAYMNTLRFATPGVRPLRLTTAVKCFSEESCVSIPEVEGYV 633
Cdd:pfam19699   1 DLQDPENSGSGVKVHFNPSQSVLTLEGDDIESLNKAMQHVSYVNSRQFPTPGVRRLKLTTSVKCFNEESCISIPDVEGYV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23943822   634 VVLQPDAPQILLSGTAHFARPAVDFEGPEGVPLFPDLQITCSISHQVEAKADESWQGTVTDTRMSDEIVHNLDGCEISLV 713
Cdd:pfam19699  81 MVLQPEEPKISLSGIDHFARPASEFESPEGVPLFPELRIVSTITREVESEGDGEDDPTVQESLVSEEIVHNLDGCEVTVL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23943822   714 GDDLDPERESLLLDMASLQQRGLELTNTSAYLTIAGVETITVYEEILRQARYQLRHGAALYARKFRLSCSEMNGRYSSNE 793
Cdd:pfam19699 161 GEELNPEQESLEVDMALLQQRGLEISSSTLGITITGVESMASYEEVLHLIRYRNWNTESLFERKFKLSCSELNGRYASNE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23943822   794 FIVEVNVLHSMNRVAHPSHVLSSQQFLHRGHQPPPEMAGHSLASSHRNSMVPSAATLIIVVCVGFLVLMVILGLVRIHSL 873
Cdd:pfam19699 241 FKVEVNVLHTANPVEHPNHMAAQPQFVHPVHHAFPDLSGHNLANPHPSSVVPSAATVVIVVCVSFLVFMIILGVFRIRSA 320
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 23943822   874 HRRVsgtggpSGASTDPKDPDLFWDDSALTIIVNPMESYQ 913
Cdd:pfam19699 321 HQRG------MRDQEGGKENEMDWDDSALTITVNPMETYE 354
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
32-140 5.62e-13

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


Pssm-ID: 206637 [Multi-domain]  Cd Length: 98  Bit Score: 65.80  E-value: 5.62e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23943822  32 EYQGIVMEND--NTVLLNppLFALDKDAPLryAGEIcGFRLHgSGVPFEAVILDKATGEglIRAKEPVDCEAQKEHTFTI 109
Cdd:cd11304   1 SYEVSVPENAppGTVVLT--VSATDPDSGE--NGEV-TYSIV-SGNEDGLFSIDPSTGE--ITTAKPLDREEQSSYTLTV 72
                        90       100       110
                ....*....|....*....|....*....|.
gi 23943822 110 QAYDCGEGPdgtntkKSHKATVHVRVNDVNE 140
Cdd:cd11304  73 TATDGGGPP------LSSTATVTITVLDVND 97
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
52-143 6.48e-10

Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. Cadherin domains occur as repeats in the extracellular regions which are thought to mediate cell-cell contact when bound to calcium.


Pssm-ID: 214520 [Multi-domain]  Cd Length: 81  Bit Score: 56.20  E-value: 6.48e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23943822     52 ALDKDAPLRyaGEIcGFRLHgSGVPFEAVILDKATGEglIRAKEPVDCEAQKEHTFTIQAYDCGEGPDGTNtkkshkATV 131
Cdd:smart00112   2 ATDADSGEN--GKV-TYSIL-SGNDDGLFSIDPETGE--ITTTKPLDREEQPEYTLTVEATDGGGPPLSST------ATV 69
                           90
                   ....*....|..
gi 23943822    132 HVRVNDVNEFAP 143
Cdd:smart00112  70 TITVLDVNDNAP 81
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
150-239 7.36e-10

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


Pssm-ID: 206637 [Multi-domain]  Cd Length: 98  Bit Score: 56.94  E-value: 7.36e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23943822 150 YRAAVTEG-KLYDRILRVEAIDGDcSPQYSQIcYYEILTPNT--PFLID-NDGNIENTEKLQYSGEKLYKFTVTAYDCGK 225
Cdd:cd11304   2 YEVSVPENaPPGTVVLTVSATDPD-SGENGEV-TYSIVSGNEdgLFSIDpSTGEITTAKPLDREEQSSYTLTVTATDGGG 79
                        90
                ....*....|....
gi 23943822 226 KRAADDAEVEIQVK 239
Cdd:cd11304  80 PPLSSTATVTITVL 93
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
168-239 3.56e-05

Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. Cadherin domains occur as repeats in the extracellular regions which are thought to mediate cell-cell contact when bound to calcium.


Pssm-ID: 214520 [Multi-domain]  Cd Length: 81  Bit Score: 43.11  E-value: 3.56e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23943822    168 AIDGDcSPQYSQIcYYEILTPNT--PFLID-NDGNIENTEKLQYSGEKLYKFTVTAYDCGKKRAADDAEVEIQVK 239
Cdd:smart00112   2 ATDAD-SGENGKV-TYSILSGNDdgLFSIDpETGEITTTKPLDREEQPEYTLTVEATDGGGPPLSSTATVTITVL 74
Cadherin pfam00028
Cadherin domain;
150-238 3.34e-04

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 40.36  E-value: 3.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23943822   150 YRAAVTEGKLYD-RILRVEAIDGDCSPQySQIcYYEILTPNTP--FLID-NDGNIENTEKLQYSGEKLYKFTVTAYDCGK 225
Cdd:pfam00028   1 YSASVPENAPVGtEVLTVTATDPDLGPN-GRI-FYSILGGGPGgnFRIDpDTGDISTTKPLDRESIGEYELTVEATDSGG 78
                          90
                  ....*....|...
gi 23943822   226 KRAADDAEVEIQV 238
Cdd:pfam00028  79 PPLSSTATVTITV 91
Cadherin pfam00028
Cadherin domain;
33-135 4.02e-04

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 40.36  E-value: 4.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23943822    33 YQGIVMEN--DNTVLLNppLFALDKDAPL----RYAgeicgFRLHGSGVPFEaviLDKATGEglIRAKEPVDCEAQKEHT 106
Cdd:pfam00028   1 YSASVPENapVGTEVLT--VTATDPDLGPngriFYS-----ILGGGPGGNFR---IDPDTGD--ISTTKPLDRESIGEYE 68
                          90       100
                  ....*....|....*....|....*....
gi 23943822   107 FTIQAYDCGEGPdgtntkKSHKATVHVRV 135
Cdd:pfam00028  69 LTVEATDSGGPP------LSSTATVTITV 91
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH