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Conserved domains on  [gi|1039759210|ref|XP_017171265|]
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potassium voltage-gated channel subfamily KQT member 2 isoform X27 [Mus musculus]

Protein Classification

potassium voltage-gated channel subfamily KQT member 2( domain architecture ID 10926107)

potassium voltage-gated channel subfamily KQT member 2 (KCNQ2) associates with KCNQ3 to form a potassium channel with essentially identical properties to the channel underlying the native M-current, a slowly activating and deactivating potassium conductance which plays a critical role in determining the subthreshold electrical excitability of neurons as well as the responsiveness to synaptic inputs

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
KCNQ_channel super family cl04130
KCNQ voltage-gated potassium channel; This family matches to the C-terminal tail of KCNQ type ...
17-270 4.38e-108

KCNQ voltage-gated potassium channel; This family matches to the C-terminal tail of KCNQ type potassium channels.


The actual alignment was detected with superfamily member pfam03520:

Pssm-ID: 460954  Cd Length: 190  Bit Score: 319.01  E-value: 4.38e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759210  17 SPSADQSLDDSPSKVPKSWSFGDRSRTRQAFRIKGAASRQNSEEASLPGEDIVEDnKSCNCEFVTEDLTPGLKVSIRAVC 96
Cdd:pfam03520   1 SPSAEDSIEASPSKVQKSWSFNDRTRFRTSLRLKGSASRQSSEEASGPGEEVAED-KGCHCDFLVEDLIPALKTVIRAVR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759210  97 VMRFLVSKRKFKESLRPYDVMDVIEQYSAGHLDMLSRIKSLQSrqeplpvqsgheqgppgqnqawhkghqglgdRIDMIV 176
Cdd:pfam03520  80 IMKFLVAKRKFKETLRPYDVKDVIEQYSAGHLDMLCRIKSLQT-------------------------------RVDQIV 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759210 177 GPPPPSTPRHKKypTKGPtapsrespqysprvdqivgrgptitdkdrtKGPAETELPEDPSMMGRLGKVEKQVLSMEKKL 256
Cdd:pfam03520 129 GRGPPPTDKKKR--EKGP------------------------------KVPAEGDLVEDLSMMGRVVKVEKQVQSIEKKL 176
                         250
                  ....*....|....
gi 1039759210 257 DFLVSIYTQRMGIP 270
Cdd:pfam03520 177 DFLLDIYSQCLRKG 190
KCNQC3-Ank-G_bd pfam11956
Ankyrin-G binding motif of KCNQ2-3; Interactions with ankyrin-G are crucial to the ...
384-484 1.74e-53

Ankyrin-G binding motif of KCNQ2-3; Interactions with ankyrin-G are crucial to the localization of voltage-gated sodium channels (VGSCs) at the axon initial segment and for neurons to initiate action potentials. This conserved 9-amino acid motif ((V/A)P(I/L)AXXE(S/D)D) is required for ankyrin-G binding and functions to localize sodium channels to a variety of 'excitable' membrane domains both inside and outside of the nervous system. This motif has also been identified in the potassium channel 6TM proteins KCNQ2 and KCNQ3, that correspond to the M channels that exert a crucial influence over neuronal excitability. KCNQ2/KCNQ3 channels are preferentially localized to the surface of axons both at the axonal initial segment and more distally, and this axonal initial segment targeting of surface KCNQ channels is mediated by these ankyrin-G binding motifs of KCNQ2 and KCNQ3. KCNQ3 is a major determinant of M channel localization to the AIS, rather than KCNQ2. Phylogenetic analysis reveals that anchor motifs evolved sequentially in chordates (NaV channel) and jawed vertebrates (KCNQ2/3).


:

Pssm-ID: 463411  Cd Length: 101  Bit Score: 174.97  E-value: 1.74e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759210 384 LEGTPACRPSEAALRDSDTSISIPSVDHEELERSFSGFSISQSKENLDALG-SCYAAVAPCAKVRPYIAEGESDTDSDLC 462
Cdd:pfam11956   1 LQDLSGGRGRTTALRDSDTPLSILSVNHEELERSPSGFSISQSRENLDFLNnGCAAGVAPWTRVRPYLAEGETDTDTDPF 80
                          90       100
                  ....*....|....*....|..
gi 1039759210 463 TPCGPPPRSATGEGpFGDVAWA 484
Cdd:pfam11956  81 TPSGPPPLSSTGEG-FGDMGWS 101
KCNQ2_u3 pfam16642
Unstructured region on Potassium channel subunit alpha KvLQT2; KCNQ2_u3 is a region of ...
284-372 1.56e-34

Unstructured region on Potassium channel subunit alpha KvLQT2; KCNQ2_u3 is a region of natively unstructured sequence on potassium voltage-gated channel subfamily KQT member 2 proteins from higher eukaryotes. It lies between families KCNQ_channel, pfam03520, and KCNQC3-Ank_bd, pfam11956. The function is not known.


:

Pssm-ID: 465213  Cd Length: 98  Bit Score: 124.98  E-value: 1.56e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759210 284 EPAPPYHSPEDSRDHADKHGCIIKIVRSTSSTGQRNYAAPPAIPPAQCP--PSTSWQQS-------HQRHGTSPVGDHGS 354
Cdd:pfam16642   1 DPAPPYHSPEDSREHKDKNGCITKIIRSTSSMGQKNFSAPPAPAVPHSHcpPSTSWQQQlqhpygrSMSHGSSPVGDPGS 80
                          90
                  ....*....|....*...
gi 1039759210 355 LVRIPPPPAHERSLSAYG 372
Cdd:pfam16642  81 LVRIPPPPAHERSLSAYS 98
 
Name Accession Description Interval E-value
KCNQ_channel pfam03520
KCNQ voltage-gated potassium channel; This family matches to the C-terminal tail of KCNQ type ...
17-270 4.38e-108

KCNQ voltage-gated potassium channel; This family matches to the C-terminal tail of KCNQ type potassium channels.


Pssm-ID: 460954  Cd Length: 190  Bit Score: 319.01  E-value: 4.38e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759210  17 SPSADQSLDDSPSKVPKSWSFGDRSRTRQAFRIKGAASRQNSEEASLPGEDIVEDnKSCNCEFVTEDLTPGLKVSIRAVC 96
Cdd:pfam03520   1 SPSAEDSIEASPSKVQKSWSFNDRTRFRTSLRLKGSASRQSSEEASGPGEEVAED-KGCHCDFLVEDLIPALKTVIRAVR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759210  97 VMRFLVSKRKFKESLRPYDVMDVIEQYSAGHLDMLSRIKSLQSrqeplpvqsgheqgppgqnqawhkghqglgdRIDMIV 176
Cdd:pfam03520  80 IMKFLVAKRKFKETLRPYDVKDVIEQYSAGHLDMLCRIKSLQT-------------------------------RVDQIV 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759210 177 GPPPPSTPRHKKypTKGPtapsrespqysprvdqivgrgptitdkdrtKGPAETELPEDPSMMGRLGKVEKQVLSMEKKL 256
Cdd:pfam03520 129 GRGPPPTDKKKR--EKGP------------------------------KVPAEGDLVEDLSMMGRVVKVEKQVQSIEKKL 176
                         250
                  ....*....|....
gi 1039759210 257 DFLVSIYTQRMGIP 270
Cdd:pfam03520 177 DFLLDIYSQCLRKG 190
KCNQC3-Ank-G_bd pfam11956
Ankyrin-G binding motif of KCNQ2-3; Interactions with ankyrin-G are crucial to the ...
384-484 1.74e-53

Ankyrin-G binding motif of KCNQ2-3; Interactions with ankyrin-G are crucial to the localization of voltage-gated sodium channels (VGSCs) at the axon initial segment and for neurons to initiate action potentials. This conserved 9-amino acid motif ((V/A)P(I/L)AXXE(S/D)D) is required for ankyrin-G binding and functions to localize sodium channels to a variety of 'excitable' membrane domains both inside and outside of the nervous system. This motif has also been identified in the potassium channel 6TM proteins KCNQ2 and KCNQ3, that correspond to the M channels that exert a crucial influence over neuronal excitability. KCNQ2/KCNQ3 channels are preferentially localized to the surface of axons both at the axonal initial segment and more distally, and this axonal initial segment targeting of surface KCNQ channels is mediated by these ankyrin-G binding motifs of KCNQ2 and KCNQ3. KCNQ3 is a major determinant of M channel localization to the AIS, rather than KCNQ2. Phylogenetic analysis reveals that anchor motifs evolved sequentially in chordates (NaV channel) and jawed vertebrates (KCNQ2/3).


Pssm-ID: 463411  Cd Length: 101  Bit Score: 174.97  E-value: 1.74e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759210 384 LEGTPACRPSEAALRDSDTSISIPSVDHEELERSFSGFSISQSKENLDALG-SCYAAVAPCAKVRPYIAEGESDTDSDLC 462
Cdd:pfam11956   1 LQDLSGGRGRTTALRDSDTPLSILSVNHEELERSPSGFSISQSRENLDFLNnGCAAGVAPWTRVRPYLAEGETDTDTDPF 80
                          90       100
                  ....*....|....*....|..
gi 1039759210 463 TPCGPPPRSATGEGpFGDVAWA 484
Cdd:pfam11956  81 TPSGPPPLSSTGEG-FGDMGWS 101
KCNQ2_u3 pfam16642
Unstructured region on Potassium channel subunit alpha KvLQT2; KCNQ2_u3 is a region of ...
284-372 1.56e-34

Unstructured region on Potassium channel subunit alpha KvLQT2; KCNQ2_u3 is a region of natively unstructured sequence on potassium voltage-gated channel subfamily KQT member 2 proteins from higher eukaryotes. It lies between families KCNQ_channel, pfam03520, and KCNQC3-Ank_bd, pfam11956. The function is not known.


Pssm-ID: 465213  Cd Length: 98  Bit Score: 124.98  E-value: 1.56e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759210 284 EPAPPYHSPEDSRDHADKHGCIIKIVRSTSSTGQRNYAAPPAIPPAQCP--PSTSWQQS-------HQRHGTSPVGDHGS 354
Cdd:pfam16642   1 DPAPPYHSPEDSREHKDKNGCITKIIRSTSSMGQKNFSAPPAPAVPHSHcpPSTSWQQQlqhpygrSMSHGSSPVGDPGS 80
                          90
                  ....*....|....*...
gi 1039759210 355 LVRIPPPPAHERSLSAYG 372
Cdd:pfam16642  81 LVRIPPPPAHERSLSAYS 98
 
Name Accession Description Interval E-value
KCNQ_channel pfam03520
KCNQ voltage-gated potassium channel; This family matches to the C-terminal tail of KCNQ type ...
17-270 4.38e-108

KCNQ voltage-gated potassium channel; This family matches to the C-terminal tail of KCNQ type potassium channels.


Pssm-ID: 460954  Cd Length: 190  Bit Score: 319.01  E-value: 4.38e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759210  17 SPSADQSLDDSPSKVPKSWSFGDRSRTRQAFRIKGAASRQNSEEASLPGEDIVEDnKSCNCEFVTEDLTPGLKVSIRAVC 96
Cdd:pfam03520   1 SPSAEDSIEASPSKVQKSWSFNDRTRFRTSLRLKGSASRQSSEEASGPGEEVAED-KGCHCDFLVEDLIPALKTVIRAVR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759210  97 VMRFLVSKRKFKESLRPYDVMDVIEQYSAGHLDMLSRIKSLQSrqeplpvqsgheqgppgqnqawhkghqglgdRIDMIV 176
Cdd:pfam03520  80 IMKFLVAKRKFKETLRPYDVKDVIEQYSAGHLDMLCRIKSLQT-------------------------------RVDQIV 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759210 177 GPPPPSTPRHKKypTKGPtapsrespqysprvdqivgrgptitdkdrtKGPAETELPEDPSMMGRLGKVEKQVLSMEKKL 256
Cdd:pfam03520 129 GRGPPPTDKKKR--EKGP------------------------------KVPAEGDLVEDLSMMGRVVKVEKQVQSIEKKL 176
                         250
                  ....*....|....
gi 1039759210 257 DFLVSIYTQRMGIP 270
Cdd:pfam03520 177 DFLLDIYSQCLRKG 190
KCNQC3-Ank-G_bd pfam11956
Ankyrin-G binding motif of KCNQ2-3; Interactions with ankyrin-G are crucial to the ...
384-484 1.74e-53

Ankyrin-G binding motif of KCNQ2-3; Interactions with ankyrin-G are crucial to the localization of voltage-gated sodium channels (VGSCs) at the axon initial segment and for neurons to initiate action potentials. This conserved 9-amino acid motif ((V/A)P(I/L)AXXE(S/D)D) is required for ankyrin-G binding and functions to localize sodium channels to a variety of 'excitable' membrane domains both inside and outside of the nervous system. This motif has also been identified in the potassium channel 6TM proteins KCNQ2 and KCNQ3, that correspond to the M channels that exert a crucial influence over neuronal excitability. KCNQ2/KCNQ3 channels are preferentially localized to the surface of axons both at the axonal initial segment and more distally, and this axonal initial segment targeting of surface KCNQ channels is mediated by these ankyrin-G binding motifs of KCNQ2 and KCNQ3. KCNQ3 is a major determinant of M channel localization to the AIS, rather than KCNQ2. Phylogenetic analysis reveals that anchor motifs evolved sequentially in chordates (NaV channel) and jawed vertebrates (KCNQ2/3).


Pssm-ID: 463411  Cd Length: 101  Bit Score: 174.97  E-value: 1.74e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759210 384 LEGTPACRPSEAALRDSDTSISIPSVDHEELERSFSGFSISQSKENLDALG-SCYAAVAPCAKVRPYIAEGESDTDSDLC 462
Cdd:pfam11956   1 LQDLSGGRGRTTALRDSDTPLSILSVNHEELERSPSGFSISQSRENLDFLNnGCAAGVAPWTRVRPYLAEGETDTDTDPF 80
                          90       100
                  ....*....|....*....|..
gi 1039759210 463 TPCGPPPRSATGEGpFGDVAWA 484
Cdd:pfam11956  81 TPSGPPPLSSTGEG-FGDMGWS 101
KCNQ2_u3 pfam16642
Unstructured region on Potassium channel subunit alpha KvLQT2; KCNQ2_u3 is a region of ...
284-372 1.56e-34

Unstructured region on Potassium channel subunit alpha KvLQT2; KCNQ2_u3 is a region of natively unstructured sequence on potassium voltage-gated channel subfamily KQT member 2 proteins from higher eukaryotes. It lies between families KCNQ_channel, pfam03520, and KCNQC3-Ank_bd, pfam11956. The function is not known.


Pssm-ID: 465213  Cd Length: 98  Bit Score: 124.98  E-value: 1.56e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759210 284 EPAPPYHSPEDSRDHADKHGCIIKIVRSTSSTGQRNYAAPPAIPPAQCP--PSTSWQQS-------HQRHGTSPVGDHGS 354
Cdd:pfam16642   1 DPAPPYHSPEDSREHKDKNGCITKIIRSTSSMGQKNFSAPPAPAVPHSHcpPSTSWQQQlqhpygrSMSHGSSPVGDPGS 80
                          90
                  ....*....|....*...
gi 1039759210 355 LVRIPPPPAHERSLSAYG 372
Cdd:pfam16642  81 LVRIPPPPAHERSLSAYS 98
 
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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