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Conserved domains on  [gi|1034660215|ref|XP_016868889|]
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potassium voltage-gated channel subfamily KQT member 3 isoform X1 [Homo sapiens]

Protein Classification

potassium voltage-gated channel subfamily KQT member 2( domain architecture ID 11999096)

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 pfam03520
KCNQ voltage-gated potassium channel; This family matches to the C-terminal tail of KCNQ type ...
 372-576 1.88e-112

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: 339.81  E-value: 1.88e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034660215 372 TPLNVDAIEESPSKEPKPVGLNNKERFRTAFRMKAYAFWQSSEDA-GTGDPMAEDRGYGNDFPIEDMIPTLKAAIRAVRI 450
Cdd:pfam03520   1 SPSAEDSIEASPSKVQKSWSFNDRTRFRTSLRLKGSASRQSSEEAsGPGEEVAEDKGCHCDFLVEDLIPALKTVIRAVRI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034660215 451 LQFRLYKKKFKETLRPYDVKDVIEQYSAGHLDMLSRIKYLQTRIDMIFTPGPPSTPKHKKsQKGSAFTfpsqqsprnepy 530
Cdd:pfam03520  81 MKFLVAKRKFKETLRPYDVKDVIEQYSAGHLDMLCRIKSLQTRVDQIVGRGPPPTDKKKR-EKGPKVP------------ 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1034660215 531 varPSTSEIEDQSMMGKFVKVERQVQDMGKKLDFLVDMHMQHMERL 576
Cdd:pfam03520 148 ---AEGDLVEDLSMMGRVVKVEKQVQSIEKKLDFLLDIYSQCLRKG 190
KCNQC3-Ank-G_bd pfam11956
Ankyrin-G binding motif of KCNQ2-3; Interactions with ankyrin-G are crucial to the ...
 696-792 3.47e-52

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: 176.51  E-value: 3.47e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034660215 696 YSDRISPRQRRSITRDSDTPLSLMSVNHEELERSPSGFSISQDRDDYVFG----PNGGSSWMREKRYLAEGETDTDTDPF 771
Cdd:pfam11956   1 LQDLSGGRGRTTALRDSDTPLSILSVNHEELERSPSGFSISQSRENLDFLnngcAAGVAPWTRVRPYLAEGETDTDTDPF 80

                          90       100
                  ....*....|....*....|.
gi 1034660215 772 TPSGSMPLSSTGDGISDSVWT 792
Cdd:pfam11956  81 TPSGPPPLSSTGEGFGDMGWS 101
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 56-289 1.60e-36

Ion transport protein; This family contains sodium, potassium and calcium ion channels. This family is 6 transmembrane helices in which the last two helices flank a loop which determines ion selectivity. In some sub-families (e.g. Na channels) the domain is repeated four times, whereas in others (e.g. K channels) the protein forms as a tetramer in the membrane.


:

Pssm-ID: 459842 [Multi-domain]  Cd Length: 238  Bit Score: 137.78  E-value: 1.60e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034660215  56 FLIVLGCLILAVLTTFkEYETVSGDWLLLLETFAIFIFGAEFALRIWAAGCCCRYkgwrgrlkfARKPLCMLDIFVLIAS 135
Cdd:pfam00520  10 LLILLNTIFLALETYF-QPEEPLTTVLEILDYVFTGIFTLEMLLKIIAAGFKKRY---------FRSPWNILDFVVVLPS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034660215 136 VpvVAVGNQGNVLATSLRSLRFLQILRMLRMDRRGGTWKLLGSAICAHSKELITAWYIGFLTLILSSFLVYLVEKDVPEV 215
Cdd:pfam00520  80 L--ISLVLSSVGSLSGLRVLRLLRLLRLLRLIRRLEGLRTLVNSLIRSLKSLGNLLLLLLLFLFIFAIIGYQLFGGKLKT 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034660215 216 DAQGEEMKEEFETYADALWWGLITLATIGYGDKTPKTWEGR-------LIAATFSLIGVSFFALPAGILGSGLALKVQEQ 288
Cdd:pfam00520 158 WENPDNGRTNFDNFPNAFLWLFQTMTTEGWGDIMYDTIDGKgefwayiYFVSFIILGGFLLLNLFIAVIIDNFQELTERT 237


                  .
gi 1034660215 289 H 289
Cdd:pfam00520 238 E 238
 
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 ...
 372-576 1.88e-112

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: 339.81  E-value: 1.88e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034660215 372 TPLNVDAIEESPSKEPKPVGLNNKERFRTAFRMKAYAFWQSSEDA-GTGDPMAEDRGYGNDFPIEDMIPTLKAAIRAVRI 450
Cdd:pfam03520   1 SPSAEDSIEASPSKVQKSWSFNDRTRFRTSLRLKGSASRQSSEEAsGPGEEVAEDKGCHCDFLVEDLIPALKTVIRAVRI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034660215 451 LQFRLYKKKFKETLRPYDVKDVIEQYSAGHLDMLSRIKYLQTRIDMIFTPGPPSTPKHKKsQKGSAFTfpsqqsprnepy 530
Cdd:pfam03520  81 MKFLVAKRKFKETLRPYDVKDVIEQYSAGHLDMLCRIKSLQTRVDQIVGRGPPPTDKKKR-EKGPKVP------------ 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1034660215 531 varPSTSEIEDQSMMGKFVKVERQVQDMGKKLDFLVDMHMQHMERL 576
Cdd:pfam03520 148 ---AEGDLVEDLSMMGRVVKVEKQVQSIEKKLDFLLDIYSQCLRKG 190
KCNQC3-Ank-G_bd pfam11956
Ankyrin-G binding motif of KCNQ2-3; Interactions with ankyrin-G are crucial to the ...
 696-792 3.47e-52

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: 176.51  E-value: 3.47e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034660215 696 YSDRISPRQRRSITRDSDTPLSLMSVNHEELERSPSGFSISQDRDDYVFG----PNGGSSWMREKRYLAEGETDTDTDPF 771
Cdd:pfam11956   1 LQDLSGGRGRTTALRDSDTPLSILSVNHEELERSPSGFSISQSRENLDFLnngcAAGVAPWTRVRPYLAEGETDTDTDPF 80

                          90       100
                  ....*....|....*....|.
gi 1034660215 772 TPSGSMPLSSTGDGISDSVWT 792
Cdd:pfam11956  81 TPSGPPPLSSTGEGFGDMGWS 101
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 56-289 1.60e-36

Ion transport protein; This family contains sodium, potassium and calcium ion channels. This family is 6 transmembrane helices in which the last two helices flank a loop which determines ion selectivity. In some sub-families (e.g. Na channels) the domain is repeated four times, whereas in others (e.g. K channels) the protein forms as a tetramer in the membrane.


Pssm-ID: 459842 [Multi-domain]  Cd Length: 238  Bit Score: 137.78  E-value: 1.60e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034660215  56 FLIVLGCLILAVLTTFkEYETVSGDWLLLLETFAIFIFGAEFALRIWAAGCCCRYkgwrgrlkfARKPLCMLDIFVLIAS 135
Cdd:pfam00520  10 LLILLNTIFLALETYF-QPEEPLTTVLEILDYVFTGIFTLEMLLKIIAAGFKKRY---------FRSPWNILDFVVVLPS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034660215 136 VpvVAVGNQGNVLATSLRSLRFLQILRMLRMDRRGGTWKLLGSAICAHSKELITAWYIGFLTLILSSFLVYLVEKDVPEV 215
Cdd:pfam00520  80 L--ISLVLSSVGSLSGLRVLRLLRLLRLLRLIRRLEGLRTLVNSLIRSLKSLGNLLLLLLLFLFIFAIIGYQLFGGKLKT 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034660215 216 DAQGEEMKEEFETYADALWWGLITLATIGYGDKTPKTWEGR-------LIAATFSLIGVSFFALPAGILGSGLALKVQEQ 288
Cdd:pfam00520 158 WENPDNGRTNFDNFPNAFLWLFQTMTTEGWGDIMYDTIDGKgefwayiYFVSFIILGGFLLLNLFIAVIIDNFQELTERT 237


                  .
gi 1034660215 289 H 289
Cdd:pfam00520 238 E 238
PRK10537 PRK10537
voltage-gated potassium channel protein;
193-271 1.89e-03

voltage-gated potassium channel protein;


Pssm-ID: 236711 [Multi-domain]  Cd Length: 393  Bit Score: 41.55  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034660215 193 IGFLTLILSSFL--VYLvekdvpevdaqGEEMKEEFETYADALWWGLITLATIGYGDKTPKTWEGRLIAATFSLIGVSFF 270
Cdd:PRK10537  142 ISITSLLFYSTFgaLYL-----------GDGFSPPIESLSTAFYFSIVTMSTVGYGDIVPVSESARLFTISVIILGITVF 210


                  .
gi 1034660215 271 A 271
Cdd:PRK10537  211 A 211
 
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 ...
 372-576 1.88e-112

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: 339.81  E-value: 1.88e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034660215 372 TPLNVDAIEESPSKEPKPVGLNNKERFRTAFRMKAYAFWQSSEDA-GTGDPMAEDRGYGNDFPIEDMIPTLKAAIRAVRI 450
Cdd:pfam03520   1 SPSAEDSIEASPSKVQKSWSFNDRTRFRTSLRLKGSASRQSSEEAsGPGEEVAEDKGCHCDFLVEDLIPALKTVIRAVRI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034660215 451 LQFRLYKKKFKETLRPYDVKDVIEQYSAGHLDMLSRIKYLQTRIDMIFTPGPPSTPKHKKsQKGSAFTfpsqqsprnepy 530
Cdd:pfam03520  81 MKFLVAKRKFKETLRPYDVKDVIEQYSAGHLDMLCRIKSLQTRVDQIVGRGPPPTDKKKR-EKGPKVP------------ 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1034660215 531 varPSTSEIEDQSMMGKFVKVERQVQDMGKKLDFLVDMHMQHMERL 576
Cdd:pfam03520 148 ---AEGDLVEDLSMMGRVVKVEKQVQSIEKKLDFLLDIYSQCLRKG 190
KCNQC3-Ank-G_bd pfam11956
Ankyrin-G binding motif of KCNQ2-3; Interactions with ankyrin-G are crucial to the ...
 696-792 3.47e-52

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: 176.51  E-value: 3.47e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034660215 696 YSDRISPRQRRSITRDSDTPLSLMSVNHEELERSPSGFSISQDRDDYVFG----PNGGSSWMREKRYLAEGETDTDTDPF 771
Cdd:pfam11956   1 LQDLSGGRGRTTALRDSDTPLSILSVNHEELERSPSGFSISQSRENLDFLnngcAAGVAPWTRVRPYLAEGETDTDTDPF 80

                          90       100
                  ....*....|....*....|.
gi 1034660215 772 TPSGSMPLSSTGDGISDSVWT 792
Cdd:pfam11956  81 TPSGPPPLSSTGEGFGDMGWS 101
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 56-289 1.60e-36

Ion transport protein; This family contains sodium, potassium and calcium ion channels. This family is 6 transmembrane helices in which the last two helices flank a loop which determines ion selectivity. In some sub-families (e.g. Na channels) the domain is repeated four times, whereas in others (e.g. K channels) the protein forms as a tetramer in the membrane.


Pssm-ID: 459842 [Multi-domain]  Cd Length: 238  Bit Score: 137.78  E-value: 1.60e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034660215  56 FLIVLGCLILAVLTTFkEYETVSGDWLLLLETFAIFIFGAEFALRIWAAGCCCRYkgwrgrlkfARKPLCMLDIFVLIAS 135
Cdd:pfam00520  10 LLILLNTIFLALETYF-QPEEPLTTVLEILDYVFTGIFTLEMLLKIIAAGFKKRY---------FRSPWNILDFVVVLPS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034660215 136 VpvVAVGNQGNVLATSLRSLRFLQILRMLRMDRRGGTWKLLGSAICAHSKELITAWYIGFLTLILSSFLVYLVEKDVPEV 215
Cdd:pfam00520  80 L--ISLVLSSVGSLSGLRVLRLLRLLRLLRLIRRLEGLRTLVNSLIRSLKSLGNLLLLLLLFLFIFAIIGYQLFGGKLKT 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034660215 216 DAQGEEMKEEFETYADALWWGLITLATIGYGDKTPKTWEGR-------LIAATFSLIGVSFFALPAGILGSGLALKVQEQ 288
Cdd:pfam00520 158 WENPDNGRTNFDNFPNAFLWLFQTMTTEGWGDIMYDTIDGKgefwayiYFVSFIILGGFLLLNLFIAVIIDNFQELTERT 237


                  .
gi 1034660215 289 H 289
Cdd:pfam00520 238 E 238
Ion_trans_2 pfam07885
Ion channel; This family includes the two membrane helix type ion channels found in bacteria.
 195-279 1.86e-12

Ion channel; This family includes the two membrane helix type ion channels found in bacteria.


Pssm-ID: 462301 [Multi-domain]  Cd Length: 78  Bit Score: 63.44  E-value: 1.86e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034660215 195 FLTLILSSFLVYLVEKDVPEVDaqgeemkeefetYADALWWGLITLATIGYGDKTPKTWEGRLIAATFSLIGVSFFALPA 274
Cdd:pfam07885   2 VLLLVLIFGTVYYLLEEGWEWS------------FLDALYFSFVTLTTVGYGDIVPLTDAGRLFTIFYILIGIPLFAIFL 69


                  ....*
gi 1034660215 275 GILGS 279
Cdd:pfam07885  70 AVLGR 74
PRK10537 PRK10537
voltage-gated potassium channel protein;
193-271 1.89e-03

voltage-gated potassium channel protein;


Pssm-ID: 236711 [Multi-domain]  Cd Length: 393  Bit Score: 41.55  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034660215 193 IGFLTLILSSFL--VYLvekdvpevdaqGEEMKEEFETYADALWWGLITLATIGYGDKTPKTWEGRLIAATFSLIGVSFF 270
Cdd:PRK10537  142 ISITSLLFYSTFgaLYL-----------GDGFSPPIESLSTAFYFSIVTMSTVGYGDIVPVSESARLFTISVIILGITVF 210


                  .
gi 1034660215 271 A 271
Cdd:PRK10537  211 A 211
 
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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