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0  structures 37  species 0  interactions 127  sequences 9  architectures

Family: KCNQC3-Ank-G_bd (PF11956)

Summary: Ankyrin-G binding motif of KCNQ2-3

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This is the Wikipedia entry entitled "Ankyrin-G binding motif of KCNQ2-3". More...

Ankyrin-G binding motif of KCNQ2-3 Edit Wikipedia article

Ankyrin-G binding motif of KCNQ2-3
Identifiers
Symbol KCNQC3-Ank-G_bd
Pfam PF11956
InterPro IPR020969

In molecular biology, the ankyrin-G binding motif of KCNQ2-3 is a protein motif found in the potassium channels KCNQ2 and KCNQ3.

Interactions with ankyrin-G (ankyrin-3) are crucial to the localisation 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 localise sodium channels to a variety of 'excitable' membrane domains both inside and outside of the nervous system.[1] This motif has also been identified in the potassium channel 6TM proteins KCNQ2 and KCNQ3 [2] that correspond to the M channels that exert a crucial influence over neuronal excitability. KCNQ2/KCNQ3 channels are preferentially localised 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.[3] KCNQ3 is a major determinant of M channel localisation to the AIS, rather than KCNQ2.[4] Phylogenetic analysis reveals that anchor motifs evolved sequentially in chordates (NaV channel) and jawed vertebrates (KCNQ2/3).[5]

References[edit]

  1. ^ Lemaillet G, Walker B, Lambert S (July 2003). "Identification of a conserved ankyrin-binding motif in the family of sodium channel alpha subunits". J. Biol. Chem. 278 (30): 27333–9. doi:10.1074/jbc.M303327200. PMID 12716895. 
  2. ^ Pan Z, Kao T, Horvath Z, Lemos J, Sul JY, Cranstoun SD, Bennett V, Scherer SS, Cooper EC (March 2006). "A common ankyrin-G-based mechanism retains KCNQ and NaV channels at electrically active domains of the axon". J. Neurosci. 26 (10): 2599–613. doi:10.1523/JNEUROSCI.4314-05.2006. PMID 16525039. 
  3. ^ Chung HJ, Jan YN, Jan LY (June 2006). "Polarized axonal surface expression of neuronal KCNQ channels is mediated by multiple signals in the KCNQ2 and KCNQ3 C-terminal domains". Proc. Natl. Acad. Sci. U.S.A. 103 (23): 8870–5. doi:10.1073/pnas.0603376103. PMC 1472242. PMID 16735477. 
  4. ^ Rasmussen HB, Frøkjaer-Jensen C, Jensen CS, Jensen HS, Jørgensen NK, Misonou H, Trimmer JS, Olesen SP, Schmitt N (March 2007). "Requirement of subunit co-assembly and ankyrin-G for M-channel localization at the axon initial segment". J. Cell. Sci. 120 (Pt 6): 953–63. doi:10.1242/jcs.03396. PMID 17311847. 
  5. ^ Hill AS, Nishino A, Nakajo K, Zhang G, Fineman JR, Selzer ME, Okamura Y, Cooper EC (December 2008). "Ion channel clustering at the axon initial segment and node of Ranvier evolved sequentially in early chordates". PLoS Genet. 4 (12): e1000317. doi:10.1371/journal.pgen.1000317. PMC 2597720. PMID 19112491. 

This article incorporates text from the public domain Pfam and InterPro IPR020969

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Ankyrin-G binding motif of KCNQ2-3 Provide feedback

Interactions with ankyrin-G are crucial to the localisation 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 localise sodium channels to a variety of 'excitable' membrane domains both inside and outside of the nervous system [1]. This motif has also been identified in the potassium channel 6TM proteins KCNQ2 and KCNQ3 [2] that correspond to the M channels that exert a crucial influence over neuronal excitability. KCNQ2/KCNQ3 channels are preferentially localised 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 [3]. KCNQ3 is a major determinant of M channel localisation to the AIS, rather than KCNQ2 [4]. Phylogenetic analysis reveals that anchor motifs evolved sequentially in chordates (NaV channel) and jawed vertebrates (KCNQ2/3) [5].

Literature references

  1. Lemaillet G, Walker B, Lambert S;, J Biol Chem. 2003;278:27333-27339.: Identification of a conserved ankyrin-binding motif in the family of sodium channel alpha subunits. PUBMED:12716895 EPMC:12716895

  2. Pan Z, Kao T, Horvath Z, Lemos J, Sul JY, Cranstoun SD, Bennett V, Scherer SS, Cooper EC;, J Neurosci. 2006;26:2599-2613.: A common ankyrin-G-based mechanism retains KCNQ and NaV channels at electrically active domains of the axon. PUBMED:16525039 EPMC:16525039

  3. Chung HJ, Jan YN, Jan LY;, Proc Natl Acad Sci U S A. 2006;103:8870-8875.: Polarized axonal surface expression of neuronal KCNQ channels is mediated by multiple signals in the KCNQ2 and KCNQ3 C-terminal domains. PUBMED:16735477 EPMC:16735477

  4. Rasmussen HB, Frokjaer-Jensen C, Jensen CS, Jensen HS, Jorgensen NK, Misonou H, Trimmer JS, Olesen SP, Schmitt N;, J Cell Sci. 2007;120:953-963.: Requirement of subunit co-assembly and ankyrin-G for M-channel localization at the axon initial segment. PUBMED:17311847 EPMC:17311847

  5. Hill AS, Nishino A, Nakajo K, Zhang G, Fineman JR, Selzer ME, Okamura Y, Cooper EC;, PLoS Genet. 2008;4:e1000317.: Ion channel clustering at the axon initial segment and node of Ranvier evolved sequentially in early chordates. PUBMED:19112491 EPMC:19112491


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR020969

Interactions with ankyrin-G are crucial to the localisation 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 localise sodium channels to a variety of 'excitable' membrane domains both inside and outside of the nervous system [PUBMED:12716895]. This motif has also been identified in the potassium channel 6TM proteins KCNQ2 and KCNQ3 [PUBMED:16525039] that correspond to the M channels that exert a crucial influence over neuronal excitability. KCNQ2/KCNQ3 channels are preferentially localised 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 [PUBMED:16735477]. KCNQ3 is a major determinant of M channel localisation to the AIS, rather than KCNQ2 [PUBMED:17311847]. Phylogenetic analysis reveals that anchor motifs evolved sequentially in chordates (NaV channel) and jawed vertebrates (KCNQ2/3) [PUBMED:19112491].

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(4)
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Representative proteomes NCBI
(111)
Meta
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RP15
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RP35
(6)
RP55
(19)
RP75
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Seed source: Pfam-B_10256 (release 23.0)
Previous IDs: none
Type: Motif
Author: Cooper E, Coggill P
Number in seed: 4
Number in full: 127
Average length of the domain: 100.90 aa
Average identity of full alignment: 62 %
Average coverage of the sequence by the domain: 12.78 %

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HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 20.5 20.5
Trusted cut-off 24.0 67.0
Noise cut-off 18.6 18.4
Model length: 102
Family (HMM) version: 3
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