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Mu-Conotoxin Provide feedback
Mu-conotoxins are peptide inhibitors of voltage-sensitive sodium channels .
Nielsen KJ, Watson M, Adams DJ, Hammarstrom AK, Gage PW, Hill JM, Craik DJ, Thomas L, Adams D, Alewood PF, Lewis RJ; , J Biol Chem 2002;277:27247-27255.: Solution structure of mu-conotoxin PIIIA, a preferential inhibitor of persistent tetrodotoxin-sensitive sodium channels. PUBMED:12006587 EPMC:12006587
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR008036
This entry represents Mu-type conotoxins. Cone snail toxins, conotoxins, are small peptides with disulphide connectivity, that target ion-channels or G-protein coupled receptors. Based on the number and pattern of disulphide bonds and biological activities, conotoxins can be classified into several families [PUBMED:11478951]. Omega, delta and kappa families of conotoxins have a knottin or inhibitor cystine knot scaffold. The knottin scaffold is a very special disulphide through disulphide knot, in which the III-VI disulphide bond crosses the macrocycle formed by two other disulphide bonds (I-IV and II-V) and the interconnecting backbone segments, where I-VI indicates the six cysteine residues starting from the N terminus.
The disulphide bonding network as well as specific amino acids in inter-cysteine loops provide specificity of conotoxin [PUBMED:10988292]. The cysteine arrangement is the same for omega, delta and kappa families, but omega conotoxins are calcium channel blockers, whereas delta conotoxins delay the inactivation of sodium channels and kappa conotoxins are potassium channel blockers [PUBMED:11478951]. Mu conotoxins have two types of cysteine arrangement, but the knottin scaffold is not observed. Conotoxin gm9a, a putative 27-residue polypeptide encoded by Conus gloriamaris, has been shown to adopt an inhibitory cystine knot motif constrained by three disulphide bonds [PUBMED:12006587, PUBMED:12193600].Mu conotoxins target the voltage-gated sodium channels, preferential skeletal muscle [PUBMED:11478951], and are useful probes for investigating voltage-dependent sodium channels of excitable tissues [PUBMED:2410412]. Alpha conotoxins have two types of cysteine arrangement [PUBMED:1390774] and are competitive nicotinic acetylcholine receptor antagonists.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Cellular component||extracellular region (GO:0005576)|
|Molecular function||sodium channel inhibitor activity (GO:0019871)|
|Biological process||pathogenesis (GO:0009405)|
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This clan contains a set of related small protein toxins and what appears to be the functionally distinct Albumin I domain. All members of this clan have a knottin-like fold. Additional information about this clan may be found from .
The clan contains the following 19 members:Agouti Albumin_I Conotoxin Mu-conotoxin Omega-toxin Tachystatin_B Toxin_11 Toxin_12 Toxin_16 Toxin_18 Toxin_21 Toxin_22 Toxin_23 Toxin_24 Toxin_27 Toxin_30 Toxin_7 Toxin_9 UPF0506
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Curation and family details
|Seed source:||Pfam-B_34209 (release 7.8)|
|Number in seed:||4|
|Number in full:||7|
|Average length of the domain:||21.60 aa|
|Average identity of full alignment:||60 %|
|Average coverage of the sequence by the domain:||58.75 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||7|
|Download:||download the raw HMM for this family|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Mu-conotoxin domain has been found. There are 6 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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