KCNC3_MOUSE
ID KCNC3_MOUSE Reviewed; 769 AA.
AC Q63959; D3YZV2; E9Q5E5; Q62088;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 07-OCT-2020, sequence version 3.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Potassium voltage-gated channel subfamily C member 3;
DE AltName: Full=KSHIIID;
DE AltName: Full=Voltage-gated potassium channel subunit Kv3.3;
GN Name=Kcnc3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=8301351; DOI=10.1523/jneurosci.14-02-00511.1994;
RA Goldman-Wohl D.S., Chan E., Baird D., Heintz N.;
RT "Kv3.3b: a novel Shaw type potassium channel expressed in terminally
RT differentiated cerebellar Purkinje cells and deep cerebellar nuclei.";
RL J. Neurosci. 14:511-522(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-660.
RC STRAIN=AKR/J;
RX PubMed=1740329; DOI=10.1016/0888-7543(92)90365-y;
RA Ghanshani S., Pak M., McPherson J.D., Strong M., Dethlefs B., Wasmuth J.J.,
RA Salkoff L.A., Gutman G.A., Chandy G.K.;
RT "Genomic organization, nucleotide sequence, and cellular distribution of a
RT Shaw-related potassium channel gene, Kv3.3, and mapping of Kv3.3 and Kv3.4
RT to human chromosomes 19 and 1.";
RL Genomics 12:190-196(1992).
RN [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=11517255; DOI=10.1523/jneurosci.21-17-06657.2001;
RA Espinosa F., McMahon A., Chan E., Wang S., Ho C.S., Heintz N., Joho R.H.;
RT "Alcohol hypersensitivity, increased locomotion, and spontaneous myoclonus
RT in mice lacking the potassium channels Kv3.1 and Kv3.3.";
RL J. Neurosci. 21:6657-6665(2001).
RN [5]
RP DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=15217387; DOI=10.1111/j.0953-816x.2004.03385.x;
RA McMahon A., Fowler S.C., Perney T.M., Akemann W., Knoepfel T., Joho R.H.;
RT "Allele-dependent changes of olivocerebellar circuit properties in the
RT absence of the voltage-gated potassium channels Kv3.1 and Kv3.3.";
RL Eur. J. Neurosci. 19:3317-3327(2004).
RN [6]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=16923152; DOI=10.1111/j.1601-183x.2005.00184.x;
RA Joho R.H., Street C., Matsushita S., Knoepfel T.;
RT "Behavioral motor dysfunction in Kv3-type potassium channel-deficient
RT mice.";
RL Genes Brain Behav. 5:472-482(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND TISSUE SPECIFICITY.
RX PubMed=18539595; DOI=10.1074/jbc.m801663200;
RA Desai R., Kronengold J., Mei J., Forman S.A., Kaczmarek L.K.;
RT "Protein kinase C modulates inactivation of Kv3.3 channels.";
RL J. Biol. Chem. 283:22283-22294(2008).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=18448641; DOI=10.1523/jneurosci.5486-07.2008;
RA Hurlock E.C., McMahon A., Joho R.H.;
RT "Purkinje-cell-restricted restoration of Kv3.3 function restores complex
RT spikes and rescues motor coordination in Kcnc3 mutants.";
RL J. Neurosci. 28:4640-4648(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-687; SER-692; SER-731;
RP SER-734; SER-742; THR-750 AND SER-754, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-424.
RX PubMed=24218544; DOI=10.1113/jphysiol.2013.264309;
RA Irie T., Matsuzaki Y., Sekino Y., Hirai H.;
RT "Kv3.3 channels harbouring a mutation of spinocerebellar ataxia type 13
RT alter excitability and induce cell death in cultured cerebellar Purkinje
RT cells.";
RL J. Physiol. (Lond.) 592:229-247(2014).
RN [12]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-626, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF GLY-593,
RP AND INTERACTION WITH HAX1.
RX PubMed=26997484; DOI=10.1016/j.cell.2016.02.009;
RA Zhang Y., Zhang X.F., Fleming M.R., Amiri A., El-Hassar L., Surguchev A.A.,
RA Hyland C., Jenkins D.P., Desai R., Brown M.R., Gazula V.R., Waters M.F.,
RA Large C.H., Horvath T.L., Navaratnam D., Vaccarino F.M., Forscher P.,
RA Kaczmarek L.K.;
RT "Kv3.3 channels bind Hax-1 and Arp2/3 to assemble a stable local actin
RT network that regulates channel gating.";
RL Cell 165:434-448(2016).
CC -!- FUNCTION: Voltage-gated potassium channel that plays an important role
CC in the rapid repolarization of fast-firing brain neurons. The channel
CC opens in response to the voltage difference across the membrane,
CC forming a potassium-selective channel through which potassium ions pass
CC in accordance with their electrochemical gradient. The channel displays
CC rapid activation and inactivation kinetics (PubMed:18539595,
CC PubMed:26997484, PubMed:24218544). It plays a role in the regulation of
CC the frequency, shape and duration of action potentials in Purkinje
CC cells (PubMed:15217387, PubMed:18448641, PubMed:24218544). Required for
CC normal survival of cerebellar neurons, probably via its role in
CC regulating the duration and frequency of action potentials that in turn
CC regulate the activity of voltage-gated Ca(2+) channels and cellular
CC Ca(2+) homeostasis (PubMed:24218544). Required for normal motor
CC function (PubMed:16923152, PubMed:18448641). Plays a role in the
CC reorganization of the cortical actin cytoskeleton and the formation of
CC actin veil structures in neuronal growth cones via its interaction with
CC HAX1 and the Arp2/3 complex (PubMed:26997484).
CC {ECO:0000269|PubMed:15217387, ECO:0000269|PubMed:16923152,
CC ECO:0000269|PubMed:18448641, ECO:0000269|PubMed:18539595,
CC ECO:0000269|PubMed:24218544, ECO:0000269|PubMed:26997484}.
CC -!- SUBUNIT: Homotetramer. Heterotetramer with KCNC1 (By similarity).
CC Interacts (via C-terminus) with HAX1. Identified in a complex with
CC ACTR3, a subunit of the Arp2/3 complex; this interaction is indirect
CC and depends on the presence of HAX1. Interaction with HAX1 modulates
CC channel gating (PubMed:26997484). {ECO:0000250|UniProtKB:Q14003,
CC ECO:0000269|PubMed:26997484}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15217387,
CC ECO:0000269|PubMed:18448641, ECO:0000269|PubMed:18539595,
CC ECO:0000269|PubMed:24218544, ECO:0000269|PubMed:26997484}; Multi-pass
CC membrane protein {ECO:0000255}. Presynaptic cell membrane
CC {ECO:0000269|PubMed:26997484}; Multi-pass membrane protein
CC {ECO:0000255}. Perikaryon {ECO:0000269|PubMed:15217387}. Cell
CC projection, axon {ECO:0000269|PubMed:15217387}. Cell projection,
CC dendrite {ECO:0000269|PubMed:15217387}. Cell projection, dendritic
CC spine membrane {ECO:0000250|UniProtKB:Q01956}; Multi-pass membrane
CC protein {ECO:0000255}. Cytoplasm, cell cortex
CC {ECO:0000250|UniProtKB:Q14003}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q14003}. Note=Detected on Purkinje cell
CC dendritic spines, positioned perisynaptically but also in extrasynaptic
CC positions along the spine membranes (By similarity). Detected at
CC presynaptic calices of Held (PubMed:26997484). Colocalizes with the
CC cortical actin cytoskeleton and the Arp2/3 complex (By similarity).
CC {ECO:0000250|UniProtKB:Q01956, ECO:0000250|UniProtKB:Q14003}.
CC -!- TISSUE SPECIFICITY: Detected on Purkinje cells in the dentate,
CC interposed and medial nucleus in cerebellum (PubMed:15217387,
CC PubMed:18448641). Detected in brainstem (PubMed:18539595). Detected at
CC calyces of Held in the auditory brain stem (at protein level)
CC (PubMed:26997484). Isoform KV3.3B is highly enriched in the brain,
CC particularly in the cerebellum, where its expression is confined to
CC Purkinje cells and deep cerebellar nuclei. Isoform KV3.3A is not
CC expressed in cerebellum. {ECO:0000269|PubMed:15217387,
CC ECO:0000269|PubMed:18448641, ECO:0000269|PubMed:18539595,
CC ECO:0000269|PubMed:26997484, ECO:0000269|PubMed:8301351}.
CC -!- DEVELOPMENTAL STAGE: Expression begins in cerebellar Purkinje cells
CC between postnatal day 8 (P8) and P10 and continues through adulthood.
CC {ECO:0000269|PubMed:8301351}.
CC -!- DOMAIN: The segment S4 is probably the voltage-sensor and is
CC characterized by a series of positively charged amino acids at every
CC third position. {ECO:0000305}.
CC -!- DOMAIN: The cytoplasmic N-terminus mediates N-type inactivation.
CC {ECO:0000269|PubMed:18539595}.
CC -!- DOMAIN: The C-terminal cytoplasmic tail contributes to the regulation
CC of channel inactivation and to the interaction with HAX1 and the Arp2/3
CC complex. {ECO:0000269|PubMed:26997484}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q14003}.
CC -!- DISRUPTION PHENOTYPE: Mice lacking both Kcnc3 and Kcnc1 are born at the
CC expected Mendelian rate, but the pups do not thrive and all die about
CC 26 days after birth when kept together with other littermates. Their
CC failure to thrive may be due to motor problems; mutant pups survive
CC when fed separately, but 45 days after birth their body weight is only
CC 50 to 60 % of that of wild-type (PubMed:11517255). They appear
CC uncoordinated and display severe ataxia, myoclonus and spontaneous
CC whole-body muscle jerks, but display no obvious alterations in brain
CC morphology (PubMed:11517255, PubMed:15217387, PubMed:16923152). Mice
CC lacking only Kcnc3 still display ataxic gait and decreased motor skill,
CC but to a lesser degree than mice lacking both Kcnc3 and Kcnc1
CC (PubMed:16923152, PubMed:18448641). Purkinje cell-specific expression
CC of Kcnc3 restores normal motor skills (PubMed:18448641). Mutant mice
CC are also much more sensitive to ethanol and fall sideways at ethanol
CC concentrations that have no effect on wild-type mice (PubMed:11517255).
CC They display increased locomotor and exploratory activity
CC (PubMed:11517255, PubMed:15217387). Mice lacking Kcnc3 or both Kcnc3
CC and Kcnc1 are resistant to the tremorogenic agent harmaline
CC (PubMed:15217387). {ECO:0000269|PubMed:11517255,
CC ECO:0000269|PubMed:15217387, ECO:0000269|PubMed:16923152,
CC ECO:0000269|PubMed:18448641}.
CC -!- SIMILARITY: Belongs to the potassium channel family. C (Shaw) (TC
CC 1.A.1.2) subfamily. Kv3.3/KCNC3 sub-subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA43209.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA43209.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact. Incorrect C-terminus.; Evidence={ECO:0000305};
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DR EMBL; S69381; AAC60679.1; -; mRNA.
DR EMBL; AC157653; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X60796; CAA43209.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X60797; CAA43209.1; JOINED; Genomic_DNA.
DR CCDS; CCDS39942.1; -.
DR PIR; A42073; A42073.
DR RefSeq; NP_032448.2; NM_008422.2.
DR AlphaFoldDB; Q63959; -.
DR SMR; Q63959; -.
DR STRING; 10090.ENSMUSP00000103539; -.
DR GlyGen; Q63959; 3 sites.
DR iPTMnet; Q63959; -.
DR PhosphoSitePlus; Q63959; -.
DR SwissPalm; Q63959; -.
DR MaxQB; Q63959; -.
DR PaxDb; Q63959; -.
DR PeptideAtlas; Q63959; -.
DR PRIDE; Q63959; -.
DR ProteomicsDB; 263397; -.
DR ProteomicsDB; 353015; -.
DR ABCD; Q63959; 1 sequenced antibody.
DR Antibodypedia; 18827; 305 antibodies from 30 providers.
DR DNASU; 16504; -.
DR Ensembl; ENSMUST00000107907; ENSMUSP00000103540; ENSMUSG00000062785.
DR GeneID; 16504; -.
DR KEGG; mmu:16504; -.
DR CTD; 3748; -.
DR MGI; MGI:96669; Kcnc3.
DR VEuPathDB; HostDB:ENSMUSG00000062785; -.
DR eggNOG; KOG3713; Eukaryota.
DR GeneTree; ENSGT00940000163131; -.
DR InParanoid; Q63959; -.
DR OMA; WMIERTS; -.
DR OrthoDB; 818306at2759; -.
DR Reactome; R-MMU-1296072; Voltage gated Potassium channels.
DR BioGRID-ORCS; 16504; 2 hits in 72 CRISPR screens.
DR PRO; PR:Q63959; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q63959; protein.
DR Bgee; ENSMUSG00000062785; Expressed in cerebellar cortex and 154 other tissues.
DR ExpressionAtlas; Q63959; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030673; C:axolemma; IDA:MGI.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0043679; C:axon terminus; IDA:MGI.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0032590; C:dendrite membrane; IDA:MGI.
DR GO; GO:0032591; C:dendritic spine membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; ISO:MGI.
DR GO; GO:0099056; C:integral component of presynaptic membrane; ISO:MGI.
DR GO; GO:0031594; C:neuromuscular junction; IDA:MGI.
DR GO; GO:0032809; C:neuronal cell body membrane; IDA:MGI.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; ISS:UniProtKB.
DR GO; GO:0005251; F:delayed rectifier potassium channel activity; IBA:GO_Central.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; ISS:UniProtKB.
DR GO; GO:0071805; P:potassium ion transmembrane transport; ISS:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
DR GO; GO:0051262; P:protein tetramerization; ISS:UniProtKB.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0046928; P:regulation of neurotransmitter secretion; IMP:MGI.
DR Gene3D; 1.20.120.350; -; 1.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR003968; K_chnl_volt-dep_Kv.
DR InterPro; IPR003974; K_chnl_volt-dep_Kv3.
DR InterPro; IPR005404; K_chnl_volt-dep_Kv3.3.
DR InterPro; IPR021105; K_chnl_volt-dep_Kv3_ID.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR003131; T1-type_BTB.
DR InterPro; IPR028325; VG_K_chnl.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR11537; PTHR11537; 1.
DR Pfam; PF02214; BTB_2; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF11404; Potassium_chann; 1.
DR PRINTS; PR01582; KV33CHANNEL.
DR PRINTS; PR01491; KVCHANNEL.
DR PRINTS; PR01498; SHAWCHANNEL.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell projection; Cytoplasm; Cytoskeleton; Glycoprotein;
KW Ion channel; Ion transport; Membrane; Methylation; Phosphoprotein;
KW Postsynaptic cell membrane; Potassium; Potassium channel;
KW Potassium transport; Reference proteome; Synapse; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..769
FT /note="Potassium voltage-gated channel subfamily C member
FT 3"
FT /id="PRO_0000054056"
FT TOPO_DOM 1..291
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 292..310
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TRANSMEM 352..371
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 372..380
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 381..399
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TRANSMEM 413..435
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 436..448
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 449..470
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TRANSMEM 519..540
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 541..769
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..80
FT /note="Important for normal N-type inactivation"
FT /evidence="ECO:0000269|PubMed:18539595"
FT REGION 8..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 557..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 679..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 746..769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 504..509
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT COMPBIAS 22..43
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..605
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 626
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 687
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 692
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 731
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 734
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 742
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 750
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 754
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 337
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 484
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 424
FT /note="R->H: Loss of channel activity. Functions as
FT dominant negative mutation that impairs function of wild-
FT type channel subunits. Causes impaired Purkinje cell
FT dendrite growth and premature death of cerebellar Purkinje
FT cells."
FT /evidence="ECO:0000269|PubMed:24218544"
FT MUTAGEN 593
FT /note="G->R: No effect on voltage-dependent channel opening
FT or current amplitude, but decreased rate of inactivation
FT during prolonged depolarization."
FT /evidence="ECO:0000269|PubMed:26997484"
FT CONFLICT 13
FT /note="R -> C (in Ref. 1; AAC60679)"
FT /evidence="ECO:0000305"
FT CONFLICT 51..62
FT /note="AASPAGAPLSCG -> GPSPGVPAFLR (in Ref. 1; AAC60679)"
FT /evidence="ECO:0000305"
FT CONFLICT 257..267
FT /note="GPAGGAGGAGG -> DLPGARAAGA (in Ref. 3; CAA43209)"
FT /evidence="ECO:0000305"
FT CONFLICT 258..259
FT /note="PA -> LP (in Ref. 1; AAC60679)"
FT /evidence="ECO:0000305"
FT CONFLICT 522
FT /note="A -> G (in Ref. 1; AAC60679 and 3; CAA43209)"
FT /evidence="ECO:0000305"
FT CONFLICT 660
FT /note="A -> AV (in Ref. 1; AAC60679)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 769 AA; 81946 MW; E482F3B2216870F5 CRC64;
MLSSVCVWSF RGRQGTGKQQ PQPVPTPQPP ESSPPPLPPP QQQQCSQPGT AASPAGAPLS
CGPGGRRAEP CPGLPAVAMG RHGGGGGDSG KIVINVGGVR HETYRSTLRT LPGTRLAGLT
EPEAAARFDY DPGTDEFFFD RHPGVFAYVL NYYRTGKLHC PADVCGPLFE EELGFWGIDE
TDVEACCWMT YRQHRDAEEA LDSFEAPDSS ANANANAGGA HDAGLDDEAG AGGGGLDGAG
GELKRLCFQD AGGGAGGPAG GAGGAGGTWW RRWQPRVWAL FEDPYSSRAA RYVAFASLFF
ILISITTFCL ETHEGFIHIS NKTVTQASPI PGAPPENITN VEVETEPFLT YVEGVCVVWF
TFEFLMRVTF CPDKVEFLKS SLNIIDCVAI LPFYLEVGLS GLSSKAAKDV LGFLRVVRFV
RILRIFKLTR HFVGLRVLGH TLRASTNEFL LLIIFLALGV LIFATMIYYA ERIGADPDDI
LGSNHTYFKN IPIGFWWAVV TMTTLGYGDM YPKTWSGMLV GALCALAGVL TIAMPVPVIV
NNFGMYYSLA MAKQKLPKKK NKHIPRPPQP GSPNYCKPDP PPPPPPHPHH GSGGISPPPP
ITPPSMGVNV AGAYPPGPHT HPGLLRGGAG GLGIMGLPPL PAPGEPCPLA QEEVIETNRA
DPRPNGDPAA AALAHEDCPA IDQPAMSPED KSPITPGSRG RYSRDRACFL VTDYAPSPDG
SIRKGYEKSR SLSSIVGLSG VSLRLAPLAT PPGSPRATRR APPTLPSIL
