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Conserved domains on  [gi|21706696|gb|AAH33902|]
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Calsyntenin 1 [Homo sapiens]

Protein Classification

Graphical summary

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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) ...
 556-909 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: 697.29  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21706696   556 DLQVLEDSGRGVQIQAHRSQLVLTLEGEDLGELDKAMQHISYLNSRQFPTPGIRRLKITSTIKCFNEATCISVPPVDGYV 635
Cdd:pfam19699   1 DLQDPENSGSGVKVHFNPSQSVLTLEGDDIESLNKAMQHVSYVNSRQFPTPGVRRLKLTTSVKCFNEESCISIPDVEGYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21706696   636 MVLQPEEPKISLSGVHHFARAASEFESSEGVFLFPELRIISTITREVEPEGDGAEDPTVQESLVSEEIVHDLDTCEVTVE 715
Cdd:pfam19699  81 MVLQPEEPKISLSGIDHFARPASEFESPEGVPLFPELRIVSTITREVESEGDGEDDPTVQESLVSEEIVHNLDGCEVTVL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21706696   716 GEELNHEQESLEVDMARLQQKGIEVSSSELGMTFTGVDTMASYEEVLHLLRYRNWHARSLLDRKFKLICSELNGRYISNE 795
Cdd:pfam19699 161 GEELNPEQESLEVDMALLQQRGLEISSSTLGITITGVESMASYEEVLHLIRYRNWNTESLFERKFKLSCSELNGRYASNE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21706696   796 FKVEVNVIHTANPMEHANHMAAQPQFVHPEHRSFVDLSGHNLANPHPFAVVHSTATVVIVVCVSSLVFMIILGVFRIRAA 875
Cdd:pfam19699 241 FKVEVNVLHTANPVEHPNHMAAQPQFVHPVHHAFPDLSGHNLANPHPSSVVPSAATVVIVVCVSFLVFMIILGVFRIRSA 320

                         330       340       350
                  ....*....|....*....|....*....|....
gi 21706696   876 HRRTMRDQDTGKENEMDWDDSALTITVNPMETYE 909
Cdd:pfam19699 321 HQRGMRDQEGGKENEMDWDDSALTITVNPMETYE 354
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 41-149 3.42e-12

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: 63.49  E-value: 3.42e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21706696  41 TYHGIVTEND--NTVLLDppLIALDKDAPLrfAGEIcGFKIHGQNvPFDAVVVDKSTGEgvIRSKEKLDCELQKDYSFTI 118
Cdd:cd11304   1 SYEVSVPENAppGTVVLT--VSATDPDSGE--NGEV-TYSIVSGN-EDGLFSIDPSTGE--ITTAKPLDREEQSSYTLTV 72

                        90       100       110
                ....*....|....*....|....*....|.
gi 21706696 119 QAYDCGKGPdgtnvkKSHKATVHIQVNDVNE 149
Cdd:cd11304  73 TATDGGGPP------LSSTATVTITVLDVND 97
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 158-248 3.80e-11

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: 60.40  E-value: 3.80e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21706696 158 SYKATVIEGKQYDS-ILRVEAVDADcSPQFSQIcSYEIITPDV--PFTVDKD-GYIKNTEKLNYGKEHQYKLTVTAYDCG 233
Cdd:cd11304   1 SYEVSVPENAPPGTvVLTVSATDPD-SGENGEV-TYSIVSGNEdgLFSIDPStGEITTAKPLDREEQSSYTLTVTATDGG 78

                        90
                ....*....|....*
gi 21706696 234 KKRATEDVLVKISIK 248
Cdd:cd11304  79 GPPLSSTATVTITVL 93
 
Name Accession Description Interval E-value
CLSTN_C pfam19699
Calsyntenin C-terminal; This is the cytoplasmic C-terminal domain of clasyntenin (CLSTN) ...
 556-909 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: 697.29  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21706696   556 DLQVLEDSGRGVQIQAHRSQLVLTLEGEDLGELDKAMQHISYLNSRQFPTPGIRRLKITSTIKCFNEATCISVPPVDGYV 635
Cdd:pfam19699   1 DLQDPENSGSGVKVHFNPSQSVLTLEGDDIESLNKAMQHVSYVNSRQFPTPGVRRLKLTTSVKCFNEESCISIPDVEGYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21706696   636 MVLQPEEPKISLSGVHHFARAASEFESSEGVFLFPELRIISTITREVEPEGDGAEDPTVQESLVSEEIVHDLDTCEVTVE 715
Cdd:pfam19699  81 MVLQPEEPKISLSGIDHFARPASEFESPEGVPLFPELRIVSTITREVESEGDGEDDPTVQESLVSEEIVHNLDGCEVTVL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21706696   716 GEELNHEQESLEVDMARLQQKGIEVSSSELGMTFTGVDTMASYEEVLHLLRYRNWHARSLLDRKFKLICSELNGRYISNE 795
Cdd:pfam19699 161 GEELNPEQESLEVDMALLQQRGLEISSSTLGITITGVESMASYEEVLHLIRYRNWNTESLFERKFKLSCSELNGRYASNE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21706696   796 FKVEVNVIHTANPMEHANHMAAQPQFVHPEHRSFVDLSGHNLANPHPFAVVHSTATVVIVVCVSSLVFMIILGVFRIRAA 875
Cdd:pfam19699 241 FKVEVNVLHTANPVEHPNHMAAQPQFVHPVHHAFPDLSGHNLANPHPSSVVPSAATVVIVVCVSFLVFMIILGVFRIRSA 320

                         330       340       350
                  ....*....|....*....|....*....|....
gi 21706696   876 HRRTMRDQDTGKENEMDWDDSALTITVNPMETYE 909
Cdd:pfam19699 321 HQRGMRDQEGGKENEMDWDDSALTITVNPMETYE 354
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 41-149 3.42e-12

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: 63.49  E-value: 3.42e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21706696  41 TYHGIVTEND--NTVLLDppLIALDKDAPLrfAGEIcGFKIHGQNvPFDAVVVDKSTGEgvIRSKEKLDCELQKDYSFTI 118
Cdd:cd11304   1 SYEVSVPENAppGTVVLT--VSATDPDSGE--NGEV-TYSIVSGN-EDGLFSIDPSTGE--ITTAKPLDREEQSSYTLTV 72

                        90       100       110
                ....*....|....*....|....*....|.
gi 21706696 119 QAYDCGKGPdgtnvkKSHKATVHIQVNDVNE 149
Cdd:cd11304  73 TATDGGGPP------LSSTATVTITVLDVND 97
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 158-248 3.80e-11

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: 60.40  E-value: 3.80e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21706696 158 SYKATVIEGKQYDS-ILRVEAVDADcSPQFSQIcSYEIITPDV--PFTVDKD-GYIKNTEKLNYGKEHQYKLTVTAYDCG 233
Cdd:cd11304   1 SYEVSVPENAPPGTvVLTVSATDPD-SGENGEV-TYSIVSGNEdgLFSIDPStGEITTAKPLDREEQSSYTLTVTATDGG 78

                        90
                ....*....|....*
gi 21706696 234 KKRATEDVLVKISIK 248
Cdd:cd11304  79 GPPLSSTATVTITVL 93
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
 61-152 1.56e-09

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: 55.43  E-value: 1.56e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21706696     61 ALDKDAPLRfaGEIcGFKIHGQNvPFDAVVVDKSTGegVIRSKEKLDCELQKDYSFTIQAYDCGKGPDGTNvkkshkATV 140
Cdd:smart00112   2 ATDADSGEN--GKV-TYSILSGN-DDGLFSIDPETG--EITTTKPLDREEQPEYTLTVEATDGGGPPLSST------ATV 69

                           90
                   ....*....|..
gi 21706696    141 HIQVNDVNEYAP 152
Cdd:smart00112  70 TITVLDVNDNAP 81
Cadherin pfam00028
Cadherin domain;
159-247 1.30e-07

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 50.38  E-value: 1.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21706696   159 YKATVIEGKQYDS-ILRVEAVDADCSPQfSQIcSYEIITPDVP--FTVDKD-GYIKNTEKLNYGKEHQYKLTVTAYDCGK 234
Cdd:pfam00028   1 YSASVPENAPVGTeVLTVTATDPDLGPN-GRI-FYSILGGGPGgnFRIDPDtGDISTTKPLDRESIGEYELTVEATDSGG 78

                          90
                  ....*....|...
gi 21706696   235 KRATEDVLVKISI 247
Cdd:pfam00028  79 PPLSSTATVTITV 91
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
 177-248 1.96e-07

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: 49.27  E-value: 1.96e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21706696    177 AVDADcSPQFSQIcSYEIITPDV--PFTVDKD-GYIKNTEKLNYGKEHQYKLTVTAYDCGKKRATEDVLVKISIK 248
Cdd:smart00112   2 ATDAD-SGENGKV-TYSILSGNDdgLFSIDPEtGEITTTKPLDREEQPEYTLTVEATDGGGPPLSSTATVTITVL 74
Cadherin pfam00028
Cadherin domain;
42-144 3.23e-04

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 40.75  E-value: 3.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21706696    42 YHGIVTEN--DNTVLLdpPLIALDKDAPLRfaGEIcGFKIHGQNvPFDAVVVDKSTGEgvIRSKEKLDCELQKDYSFTIQ 119
Cdd:pfam00028   1 YSASVPENapVGTEVL--TVTATDPDLGPN--GRI-FYSILGGG-PGGNFRIDPDTGD--ISTTKPLDRESIGEYELTVE 72

                          90       100
                  ....*....|....*....|....*
gi 21706696   120 AYDCGKGPdgtnvkKSHKATVHIQV 144
Cdd:pfam00028  73 ATDSGGPP------LSSTATVTITV 91
 
Name Accession Description Interval E-value
CLSTN_C pfam19699
Calsyntenin C-terminal; This is the cytoplasmic C-terminal domain of clasyntenin (CLSTN) ...
 556-909 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: 697.29  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21706696   556 DLQVLEDSGRGVQIQAHRSQLVLTLEGEDLGELDKAMQHISYLNSRQFPTPGIRRLKITSTIKCFNEATCISVPPVDGYV 635
Cdd:pfam19699   1 DLQDPENSGSGVKVHFNPSQSVLTLEGDDIESLNKAMQHVSYVNSRQFPTPGVRRLKLTTSVKCFNEESCISIPDVEGYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21706696   636 MVLQPEEPKISLSGVHHFARAASEFESSEGVFLFPELRIISTITREVEPEGDGAEDPTVQESLVSEEIVHDLDTCEVTVE 715
Cdd:pfam19699  81 MVLQPEEPKISLSGIDHFARPASEFESPEGVPLFPELRIVSTITREVESEGDGEDDPTVQESLVSEEIVHNLDGCEVTVL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21706696   716 GEELNHEQESLEVDMARLQQKGIEVSSSELGMTFTGVDTMASYEEVLHLLRYRNWHARSLLDRKFKLICSELNGRYISNE 795
Cdd:pfam19699 161 GEELNPEQESLEVDMALLQQRGLEISSSTLGITITGVESMASYEEVLHLIRYRNWNTESLFERKFKLSCSELNGRYASNE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21706696   796 FKVEVNVIHTANPMEHANHMAAQPQFVHPEHRSFVDLSGHNLANPHPFAVVHSTATVVIVVCVSSLVFMIILGVFRIRAA 875
Cdd:pfam19699 241 FKVEVNVLHTANPVEHPNHMAAQPQFVHPVHHAFPDLSGHNLANPHPSSVVPSAATVVIVVCVSFLVFMIILGVFRIRSA 320

                         330       340       350
                  ....*....|....*....|....*....|....
gi 21706696   876 HRRTMRDQDTGKENEMDWDDSALTITVNPMETYE 909
Cdd:pfam19699 321 HQRGMRDQEGGKENEMDWDDSALTITVNPMETYE 354
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 41-149 3.42e-12

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: 63.49  E-value: 3.42e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21706696  41 TYHGIVTEND--NTVLLDppLIALDKDAPLrfAGEIcGFKIHGQNvPFDAVVVDKSTGEgvIRSKEKLDCELQKDYSFTI 118
Cdd:cd11304   1 SYEVSVPENAppGTVVLT--VSATDPDSGE--NGEV-TYSIVSGN-EDGLFSIDPSTGE--ITTAKPLDREEQSSYTLTV 72

                        90       100       110
                ....*....|....*....|....*....|.
gi 21706696 119 QAYDCGKGPdgtnvkKSHKATVHIQVNDVNE 149
Cdd:cd11304  73 TATDGGGPP------LSSTATVTITVLDVND 97
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 158-248 3.80e-11

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: 60.40  E-value: 3.80e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21706696 158 SYKATVIEGKQYDS-ILRVEAVDADcSPQFSQIcSYEIITPDV--PFTVDKD-GYIKNTEKLNYGKEHQYKLTVTAYDCG 233
Cdd:cd11304   1 SYEVSVPENAPPGTvVLTVSATDPD-SGENGEV-TYSIVSGNEdgLFSIDPStGEITTAKPLDREEQSSYTLTVTATDGG 78

                        90
                ....*....|....*
gi 21706696 234 KKRATEDVLVKISIK 248
Cdd:cd11304  79 GPPLSSTATVTITVL 93
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
 61-152 1.56e-09

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: 55.43  E-value: 1.56e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21706696     61 ALDKDAPLRfaGEIcGFKIHGQNvPFDAVVVDKSTGegVIRSKEKLDCELQKDYSFTIQAYDCGKGPDGTNvkkshkATV 140
Cdd:smart00112   2 ATDADSGEN--GKV-TYSILSGN-DDGLFSIDPETG--EITTTKPLDREEQPEYTLTVEATDGGGPPLSST------ATV 69

                           90
                   ....*....|..
gi 21706696    141 HIQVNDVNEYAP 152
Cdd:smart00112  70 TITVLDVNDNAP 81
Cadherin pfam00028
Cadherin domain;
159-247 1.30e-07

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 50.38  E-value: 1.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21706696   159 YKATVIEGKQYDS-ILRVEAVDADCSPQfSQIcSYEIITPDVP--FTVDKD-GYIKNTEKLNYGKEHQYKLTVTAYDCGK 234
Cdd:pfam00028   1 YSASVPENAPVGTeVLTVTATDPDLGPN-GRI-FYSILGGGPGgnFRIDPDtGDISTTKPLDRESIGEYELTVEATDSGG 78

                          90
                  ....*....|...
gi 21706696   235 KRATEDVLVKISI 247
Cdd:pfam00028  79 PPLSSTATVTITV 91
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
 177-248 1.96e-07

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: 49.27  E-value: 1.96e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21706696    177 AVDADcSPQFSQIcSYEIITPDV--PFTVDKD-GYIKNTEKLNYGKEHQYKLTVTAYDCGKKRATEDVLVKISIK 248
Cdd:smart00112   2 ATDAD-SGENGKV-TYSILSGNDdgLFSIDPEtGEITTTKPLDREEQPEYTLTVEATDGGGPPLSSTATVTITVL 74
Cadherin pfam00028
Cadherin domain;
42-144 3.23e-04

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 40.75  E-value: 3.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21706696    42 YHGIVTEN--DNTVLLdpPLIALDKDAPLRfaGEIcGFKIHGQNvPFDAVVVDKSTGEgvIRSKEKLDCELQKDYSFTIQ 119
Cdd:pfam00028   1 YSASVPENapVGTEVL--TVTATDPDLGPN--GRI-FYSILGGG-PGGNFRIDPDTGD--ISTTKPLDRESIGEYELTVE 72

                          90       100
                  ....*....|....*....|....*
gi 21706696   120 AYDCGKGPdgtnvkKSHKATVHIQV 144
Cdd:pfam00028  73 ATDSGGPP------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.
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