KCNC4_MOUSE
ID KCNC4_MOUSE Reviewed; 628 AA.
AC Q8R1C0;
DT 24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Potassium voltage-gated channel subfamily C member 4;
DE AltName: Full=Voltage-gated potassium channel subunit Kv3.4;
GN Name=Kcnc4;
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 [LARGE SCALE MRNA].
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: This protein mediates the voltage-dependent potassium ion
CC permeability of excitable membranes. Assuming opened or closed
CC conformations in response to the voltage difference across the
CC membrane, the protein forms a potassium-selective channel through which
CC potassium ions may pass in accordance with their electrochemical
CC gradient (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homotetramer (Probable). Heterotetramer of potassium channel
CC proteins (By similarity). {ECO:0000250, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
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:0000250}.
CC -!- DOMAIN: The tail may be important in modulation of channel activity
CC and/or targeting of the channel to specific subcellular compartments.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylation of serine residues in the inactivation gate
CC inhibits rapid channel closure. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the potassium channel family. C (Shaw) (TC
CC 1.A.1.2) subfamily. Kv3.4/KCNC4 sub-subfamily. {ECO:0000305}.
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DR EMBL; BC024837; AAH24837.1; -; mRNA.
DR CCDS; CCDS17738.1; -.
DR RefSeq; NP_666034.1; NM_145922.2.
DR AlphaFoldDB; Q8R1C0; -.
DR SMR; Q8R1C0; -.
DR STRING; 10090.ENSMUSP00000009617; -.
DR GlyGen; Q8R1C0; 2 sites.
DR iPTMnet; Q8R1C0; -.
DR PhosphoSitePlus; Q8R1C0; -.
DR PaxDb; Q8R1C0; -.
DR PRIDE; Q8R1C0; -.
DR ProteomicsDB; 263399; -.
DR ABCD; Q8R1C0; 1 sequenced antibody.
DR Antibodypedia; 3094; 321 antibodies from 31 providers.
DR DNASU; 99738; -.
DR Ensembl; ENSMUST00000009617; ENSMUSP00000009617; ENSMUSG00000027895.
DR GeneID; 99738; -.
DR KEGG; mmu:99738; -.
DR UCSC; uc008qxa.1; mouse.
DR CTD; 3749; -.
DR MGI; MGI:96670; Kcnc4.
DR VEuPathDB; HostDB:ENSMUSG00000027895; -.
DR eggNOG; KOG3713; Eukaryota.
DR GeneTree; ENSGT00940000158860; -.
DR HOGENOM; CLU_011722_4_3_1; -.
DR InParanoid; Q8R1C0; -.
DR OMA; ETICNIW; -.
DR OrthoDB; 818306at2759; -.
DR PhylomeDB; Q8R1C0; -.
DR TreeFam; TF352511; -.
DR Reactome; R-MMU-1296072; Voltage gated Potassium channels.
DR BioGRID-ORCS; 99738; 4 hits in 74 CRISPR screens.
DR PRO; PR:Q8R1C0; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q8R1C0; protein.
DR Bgee; ENSMUSG00000027895; Expressed in olfactory epithelium and 117 other tissues.
DR ExpressionAtlas; Q8R1C0; baseline and differential.
DR Genevisible; Q8R1C0; MM.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0043679; C:axon terminus; IDA:MGI.
DR GO; GO:0044305; C:calyx of Held; ISO:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0032590; C:dendrite membrane; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0098690; C:glycinergic synapse; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; 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:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0032809; C:neuronal cell body membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0098794; C:postsynapse; ISO:MGI.
DR GO; GO:0008021; C:synaptic vesicle; ISO:MGI.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IBA:GO_Central.
DR GO; GO:0005251; F:delayed rectifier potassium channel activity; IBA:GO_Central.
DR GO; GO:1905030; F:voltage-gated ion channel activity involved in regulation of postsynaptic membrane potential; ISO:MGI.
DR GO; GO:0099508; F:voltage-gated ion channel activity involved in regulation of presynaptic membrane potential; ISO:MGI.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IBA:GO_Central.
DR GO; GO:1904456; P:negative regulation of neuronal action potential; ISO:MGI.
DR GO; GO:1904057; P:negative regulation of sensory perception of pain; ISO:MGI.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
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; IPR005405; K_chnl_volt-dep_Kv3.4.
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; PR01583; KV34CHANNEL.
DR PRINTS; PR01491; KVCHANNEL.
DR PRINTS; PR01498; SHAWCHANNEL.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Ion channel; Ion transport; Membrane; Phosphoprotein;
KW Potassium; Potassium channel; Potassium transport; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..628
FT /note="Potassium voltage-gated channel subfamily C member
FT 4"
FT /id="PRO_0000054059"
FT TOPO_DOM 1..230
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 231..251
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TRANSMEM 282..302
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 303..316
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 317..337
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TRANSMEM 349..368
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 369..384
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 385..405
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TRANSMEM 456..476
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 477..628
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..28
FT /note="Inactivation gate"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 62..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 440..445
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..529
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..546
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q03721"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q03721"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q03721"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q03721"
FT CARBOHYD 260
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 628 AA; 68655 MW; E9D7B3EC6A03EBF8 CRC64;
MISSVCVSSY RGRKSGNKPP SKTCLKEEMA KGEASEKIII NVGGTRHETY RSTLRTLPGT
RLAWLADPDG GGRPESDGGG AGSSGSSGGG GGGGGCEFFF DRHPGVFAYV LNYYRTGKLH
CPADVCGPLF EEELTFWGID ETDVEPCCWM TYRQHRDAEE ALDIFESPDG GGGGAGPGDE
AGDDERELAL QRLGPHEGGS GPGAGSGGCR GWQPRMWALF EDPYSSRAAR VVAFASLFFI
LVSITTFCLE THEAFNIDRN VTEIHRVGNI TSVRFRREVE TEPILTYIEG VCVMWFTLEF
LVRIVCCPDT LDFVKNLLNI IDFVAILPFY LEVGLSGLSS KAARDVLGFL RVVRFVRILR
IFKLTRHFVG LRVLGHTLRA STNEFLLLII FLALGVLIFA TMIYYAERIG ARPSDPRGND
HTDFKNIPIG FWWAVVTMTT LGYGDMYPKT WSGMLVGALC ALAGVLTIAM PVPVIVNNFG
MYYSLAMAKQ KLPKKRKKHV PRPPQLESPI YCKSEETSPR DSTYSDTSPP AREEGVVERK
RADSKQNGDA NAVLSDEEGA GLTQPLALAP TPEERRALRR SGTRDRNKKA AACFLLSAGD
YACADGSVRK EGNVEPKACV PVSHTCAL
