| Identification |
|---|
| HMDB Protein ID
| HMDBP10841 |
| Secondary Accession Numbers
| |
| Name
| Potassium voltage-gated channel subfamily KQT member 3 |
| Synonyms
|
- KQT-like 3
- Potassium channel subunit alpha KvLQT3
- Voltage-gated potassium channel subunit Kv7.3
|
| Gene Name
| KCNQ3 |
| Protein Type
| Unknown |
| Biological Properties |
|---|
| General Function
| Involved in potassium channel activity |
| Specific Function
| Probably important in the regulation of neuronal excitability. Associates with KCNQ2 or KCNQ5 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 |
| Pathways
|
Not Available
|
| Reactions
| Not Available |
| GO Classification
|
| Component |
| membrane |
| cell part |
| ion channel complex |
| cation channel complex |
| potassium channel complex |
| voltage-gated potassium channel complex |
| macromolecular complex |
| protein complex |
| Function |
| transmembrane transporter activity |
| substrate-specific transmembrane transporter activity |
| ion transmembrane transporter activity |
| transporter activity |
| ion channel activity |
| cation channel activity |
| potassium channel activity |
| voltage-gated potassium channel activity |
| Process |
| establishment of localization |
| transport |
| transmembrane transport |
| monovalent inorganic cation transport |
| potassium ion transport |
| ion transport |
| cation transport |
|
| Cellular Location
|
- Membrane
- Multi-pass membrane protein
|
| Gene Properties |
|---|
| Chromosome Location
| Chromosome:8 |
| Locus
| 8q24 |
| SNPs
| KCNQ3 |
| Gene Sequence
|
>2619 bp
ATGGGGCTCAAGGCGCGCAGGGCGGCGGGGGCGGCTGGCGGCGGCGGCGACGGGGGCGGC
GGAGGCGGCGGGGCGGCTAACCCAGCCGGAGGGGACGCGGCGGCGGCCGGCGACGAGGAG
CGGAAAGTGGGGCTGGCGCCCGGCGACGTGGAGCAAGTCACCTTGGCGCTCGGGGCCGGA
GCCGACAAAGACGGGACCCTGCTGCTGGAGGGCGGCGGCCGCGACGAGGGGCAGCGGAGG
ACCCCGCAGGGCATCGGGCTCCTGGCCAAGACCCCGCTGAGCCGCCCAGTCAAGAGAAAC
AACGCCAAGTACCGGCGCATCCAAACTTTGATCTACGACGCCCTGGAGAGACCGCGGGGC
TGGGCGCTGCTTTACCACGCGTTGGTGTTCCTGATTGTCCTGGGGTGCTTGATTCTGGCT
GTCCTGACCACATTCAAGGAGTATGAGACTGTCTCGGGAGACTGGCTTCTGTTACTGGAG
ACATTTGCTATTTTCATCTTTGGAGCCGAGTTTGCTTTGAGGATCTGGGCTGCTGGATGT
TGCTGCCGATACAAAGGCTGGCGGGGCCGACTGAAGTTTGCCAGGAAGCCCCTGTGCATG
TTGGACATCTTTGTGCTGATTGCCTCTGTGCCAGTGGTTGCTGTGGGAAACCAAGGCAAT
GTTCTGGCCACCTCCCTGCGAAGCCTGCGCTTCCTGCAGATCCTGCGCATGCTGCGGATG
GACCGGAGAGGTGGCACCTGGAAGCTTCTGGGCTCAGCCATCTGTGCCCACAGCAAAGAA
CTCATCACGGCCTGGTACATCGGTTTCCTGACACTCATCCTTTCTTCATTTCTTGTCTAC
CTGGTTGAGAAAGACGTCCCAGAGGTGGATGCACAAGGAGAGGAGATGAAAGAGGAGTTT
GAGACCTATGCAGATGCCCTGTGGTGGGGCCTGATCACACTGGCCACCATTGGCTATGGA
GACAAGACACCCAAAACGTGGGAAGGCCGTCTGATTGCCGCCACCTTTTCCTTAATTGGC
GTCTCCTTTTTTGCCCTTCCAGCGGGCATCCTGGGGTCCGGGCTGGCCCTCAAGGTGCAG
GAGCAACACCGTCAGAAGCACTTTGAGAAAAGGAGGAAGCCAGCTGCTGAGCTCATTCAG
GCTGCCTGGAGGTATTATGCTACCAACCCCAACAGGATTGACCTGGTGGCGACATGGAGA
TTTTATGAATCAGTCGTCTCTTTTCCTTTCTTCAGGAAAGAACAGCTGGAGGCAGCATCC
AGCCAAAAGCTGGGTCTCTTGGATCGGGTTCGCCTTTCTAATCCTCGTGGTAGCAATACT
AAAGGAAAGCTATTTACCCCTCTGAATGTAGATGCCATAGAAGAAAGTCCTTCTAAAGAA
CCAAAGCCTGTTGGCTTAAACAATAAAGAGCGTTTCCGCACGGCCTTCCGCATGAAAGCC
TACGCTTTCTGGCAGAGTTCTGAAGATGCCGGGACAGGTGACCCCATGGCGGAAGACAGG
GGCTATGGGAATGACTTCCCCATCGAAGACATGATCCCCACCCTGAAGGCCGCCATCCGA
GCCGTCAGAATTCTACAATTCCGTCTCTATAAAAAAAAATTCAAGGAGACTTTGAGGCCT
TACGATGTGAAGGATGTGATTGAGCAGTATTCTGCCGGGCATCTCGACATGCTTTCCAGG
ATAAAGTACCTTCAGACGAGAATAGATATGATTTTCACCCCTGGACCTCCCTCCACGCCA
AAACACAAGAAGTCTCAGAAAGGGTCAGCATTCACCTTCCCATCCCAGCAATCTCCCAGG
AATGAACCATATGTAGCCAGACCATCCACATCAGAAATCGAAGACCAAAGCATGATGGGG
AAGTTTGTAAAAGTTGAAAGACAGGTTCAGGACATGGGGAAGAAGCTGGACTTCCTCGTG
GATATGCACATGCAACACATGGAACGGTTGCAGGTGCAGGTCACGGAGTATTACCCAACC
AAGGGCACCTCCTCGCCAGCTGAAGCAGAGAAGAAGGAGGACAACAGGTATTCCGATTTG
AAAACCATCATCTGCAACTATTCTGAGACAGGCCCCCCGGAACCACCCTACAGCTTCCAC
CAGGTGACCATTGACAAAGTCAGCCCCTATGGGTTTTTTGCACATGACCCTGTGAACCTG
CCCCGAGGGGGACCCAGTTCTGGAAAGGTTCAGGCAACTCCTCCTTCCTCAGCAACAACG
TATGTGGAGAGGCCCACGGTCCTGCCTATCTTGACTCTTCTCGACTCCCGAGTGAGCTGC
CACTCCCAGGCTGACCTGCAGGGCCCCTACTCGGACCGAATCTCCCCCCGGCAGAGACGT
AGCATCACGCGAGACAGTGACACACCTCTGTCCCTGATGTCGGTCAACCACGAGGAGCTG
GAGAGGTCTCCAAGTGGCTTCAGCATCTCCCAGGACAGAGATGATTATGTGTTCGGCCCC
AATGGGGGGTCGAGCTGGATGAGGGAGAAGCGGTACCTCGCCGAGGGTGAGACGGACACA
GACACGGACCCCTTCACGCCCAGCGGCTCCATGCCTCTGTCGTCCACAGGGGATGGGATT
TCTGATTCAGTATGGACCCCTTCCAATAAGCCCATTTAA
|
| Protein Properties |
|---|
| Number of Residues
| 872 |
| Molecular Weight
| 96741.5 |
| Theoretical pI
| 9.2 |
| Pfam Domain Function
|
|
| Signals
|
|
|
Transmembrane Regions
|
- 122-142
- 153-173
- 197-217
- 226-247
- 262-282
- 331-351
|
| Protein Sequence
|
>Potassium voltage-gated channel subfamily KQT member 3
MGLKARRAAGAAGGGGDGGGGGGGAANPAGGDAAAAGDEERKVGLAPGDVEQVTLALGAG
ADKDGTLLLEGGGRDEGQRRTPQGIGLLAKTPLSRPVKRNNAKYRRIQTLIYDALERPRG
WALLYHALVFLIVLGCLILAVLTTFKEYETVSGDWLLLLETFAIFIFGAEFALRIWAAGC
CCRYKGWRGRLKFARKPLCMLDIFVLIASVPVVAVGNQGNVLATSLRSLRFLQILRMLRM
DRRGGTWKLLGSAICAHSKELITAWYIGFLTLILSSFLVYLVEKDVPEVDAQGEEMKEEF
ETYADALWWGLITLATIGYGDKTPKTWEGRLIAATFSLIGVSFFALPAGILGSGLALKVQ
EQHRQKHFEKRRKPAAELIQAAWRYYATNPNRIDLVATWRFYESVVSFPFFRKEQLEAAS
SQKLGLLDRVRLSNPRGSNTKGKLFTPLNVDAIEESPSKEPKPVGLNNKERFRTAFRMKA
YAFWQSSEDAGTGDPMAEDRGYGNDFPIEDMIPTLKAAIRAVRILQFRLYKKKFKETLRP
YDVKDVIEQYSAGHLDMLSRIKYLQTRIDMIFTPGPPSTPKHKKSQKGSAFTFPSQQSPR
NEPYVARPSTSEIEDQSMMGKFVKVERQVQDMGKKLDFLVDMHMQHMERLQVQVTEYYPT
KGTSSPAEAEKKEDNRYSDLKTIICNYSETGPPEPPYSFHQVTIDKVSPYGFFAHDPVNL
PRGGPSSGKVQATPPSSATTYVERPTVLPILTLLDSRVSCHSQADLQGPYSDRISPRQRR
SITRDSDTPLSLMSVNHEELERSPSGFSISQDRDDYVFGPNGGSSWMREKRYLAEGETDT
DTDPFTPSGSMPLSSTGDGISDSVWTPSNKPI
|
| External Links |
|---|
| GenBank ID Protein
| 4758630 |
| UniProtKB/Swiss-Prot ID
| O43525 |
| UniProtKB/Swiss-Prot Entry Name
| KCNQ3_HUMAN |
| PDB IDs
|
Not Available |
| GenBank Gene ID
| NM_004519.2 |
| GeneCard ID
| KCNQ3 |
| GenAtlas ID
| KCNQ3 |
| HGNC ID
| HGNC:6297 |
| References |
|---|
| General References
| - Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed:17924679 ]
- Selyanko AA, Hadley JK, Wood IC, Abogadie FC, Jentsch TJ, Brown DA: Inhibition of KCNQ1-4 potassium channels expressed in mammalian cells via M1 muscarinic acetylcholine receptors. J Physiol. 2000 Feb 1;522 Pt 3:349-55. [PubMed:10713961 ]
- Yang WP, Levesque PC, Little WA, Conder ML, Ramakrishnan P, Neubauer MG, Blanar MA: Functional expression of two KvLQT1-related potassium channels responsible for an inherited idiopathic epilepsy. J Biol Chem. 1998 Jul 31;273(31):19419-23. [PubMed:9677360 ]
- Schroeder BC, Kubisch C, Stein V, Jentsch TJ: Moderate loss of function of cyclic-AMP-modulated KCNQ2/KCNQ3 K+ channels causes epilepsy. Nature. 1998 Dec 17;396(6712):687-90. [PubMed:9872318 ]
- Selyanko AA, Hadley JK, Wood IC, Abogadie FC, Delmas P, Buckley NJ, London B, Brown DA: Two types of K(+) channel subunit, Erg1 and KCNQ2/3, contribute to the M-like current in a mammalian neuronal cell. J Neurosci. 1999 Sep 15;19(18):7742-56. [PubMed:10479678 ]
- Tinel N, Diochot S, Lauritzen I, Barhanin J, Lazdunski M, Borsotto M: M-type KCNQ2-KCNQ3 potassium channels are modulated by the KCNE2 subunit. FEBS Lett. 2000 Sep 1;480(2-3):137-41. [PubMed:11034315 ]
- Schwake M, Pusch M, Kharkovets T, Jentsch TJ: Surface expression and single channel properties of KCNQ2/KCNQ3, M-type K+ channels involved in epilepsy. J Biol Chem. 2000 May 5;275(18):13343-8. [PubMed:10788442 ]
- Shapiro MS, Roche JP, Kaftan EJ, Cruzblanca H, Mackie K, Hille B: Reconstitution of muscarinic modulation of the KCNQ2/KCNQ3 K(+) channels that underlie the neuronal M current. J Neurosci. 2000 Mar 1;20(5):1710-21. [PubMed:10684873 ]
- Main MJ, Cryan JE, Dupere JR, Cox B, Clare JJ, Burbidge SA: Modulation of KCNQ2/3 potassium channels by the novel anticonvulsant retigabine. Mol Pharmacol. 2000 Aug;58(2):253-62. [PubMed:10908292 ]
- Wickenden AD, Yu W, Zou A, Jegla T, Wagoner PK: Retigabine, a novel anti-convulsant, enhances activation of KCNQ2/Q3 potassium channels. Mol Pharmacol. 2000 Sep;58(3):591-600. [PubMed:10953053 ]
- Rundfeldt C, Netzer R: The novel anticonvulsant retigabine activates M-currents in Chinese hamster ovary-cells tranfected with human KCNQ2/3 subunits. Neurosci Lett. 2000 Mar 17;282(1-2):73-6. [PubMed:10713399 ]
- Singh NA, Westenskow P, Charlier C, Pappas C, Leslie J, Dillon J, Anderson VE, Sanguinetti MC, Leppert MF: KCNQ2 and KCNQ3 potassium channel genes in benign familial neonatal convulsions: expansion of the functional and mutation spectrum. Brain. 2003 Dec;126(Pt 12):2726-37. Epub 2003 Oct 8. [PubMed:14534157 ]
- Charlier C, Singh NA, Ryan SG, Lewis TB, Reus BE, Leach RJ, Leppert M: A pore mutation in a novel KQT-like potassium channel gene in an idiopathic epilepsy family. Nat Genet. 1998 Jan;18(1):53-5. [PubMed:9425900 ]
- Wickenden AD, Zou A, Wagoner PK, Jegla T: Characterization of KCNQ5/Q3 potassium channels expressed in mammalian cells. Br J Pharmacol. 2001 Jan;132(2):381-4. [PubMed:11159685 ]
- Hirose S, Zenri F, Akiyoshi H, Fukuma G, Iwata H, Inoue T, Yonetani M, Tsutsumi M, Muranaka H, Kurokawa T, Hanai T, Wada K, Kaneko S, Mitsudome A: A novel mutation of KCNQ3 (c.925T-->C) in a Japanese family with benign familial neonatal convulsions. Ann Neurol. 2000 Jun;47(6):822-6. [PubMed:10852552 ]
|
