KCNC4_RAT
ID KCNC4_RAT Reviewed; 625 AA.
AC Q63734;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Potassium voltage-gated channel subfamily C member 4;
DE AltName: Full=Raw3;
DE AltName: Full=Voltage-gated potassium channel subunit Kv3.4;
GN Name=Kcnc4;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1840526; DOI=10.1016/0014-5793(91)80119-n;
RA Schroeter K.H., Ruppersberg J.P., Wunder F., Rettig J., Stocker M.,
RA Pongs O.;
RT "Cloning and functional expression of a TEA-sensitive A-type potassium
RT channel from rat brain.";
RL FEBS Lett. 278:211-216(1991).
RN [2]
RP CHARACTERIZATION.
RX PubMed=1378392; DOI=10.1002/j.1460-2075.1992.tb05312.x;
RA Rettig J., Wunder F., Stocker M., Lichtinghagen R., Mastiaux F., Beckh S.,
RA Kues W., Pedarzani P., Schroeter K.H., Ruppersberg J.P., Veh R., Pongs O.;
RT "Characterization of a Shaw-related potassium channel family in rat
RT brain.";
RL EMBO J. 11:2473-2486(1992).
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.
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.
CC -!- DOMAIN: The tail may be important in modulation of channel activity
CC and/or targeting of the channel to specific subcellular compartments.
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; X62841; CAA44645.1; -; mRNA.
DR PIR; S13919; S13919.
DR RefSeq; NP_001116248.1; NM_001122776.1.
DR AlphaFoldDB; Q63734; -.
DR SMR; Q63734; -.
DR BioGRID; 599395; 1.
DR STRING; 10116.ENSRNOP00000065398; -.
DR DrugCentral; Q63734; -.
DR GuidetoPHARMACOLOGY; 551; -.
DR GlyGen; Q63734; 2 sites.
DR PhosphoSitePlus; Q63734; -.
DR PaxDb; Q63734; -.
DR PRIDE; Q63734; -.
DR ABCD; Q63734; 1 sequenced antibody.
DR GeneID; 684516; -.
DR KEGG; rno:684516; -.
DR CTD; 3749; -.
DR RGD; 1589169; Kcnc4.
DR eggNOG; KOG3713; Eukaryota.
DR InParanoid; Q63734; -.
DR OrthoDB; 818306at2759; -.
DR PhylomeDB; Q63734; -.
DR Reactome; R-RNO-1296072; Voltage gated Potassium channels.
DR PRO; PR:Q63734; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0043679; C:axon terminus; ISO:RGD.
DR GO; GO:0044305; C:calyx of Held; IDA:SynGO.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0032590; C:dendrite membrane; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0098690; C:glycinergic synapse; IDA:SynGO.
DR GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; IDA:SynGO.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IDA:SynGO.
DR GO; GO:0031594; C:neuromuscular junction; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0032809; C:neuronal cell body membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0098794; C:postsynapse; IDA:RGD.
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; IDA:SynGO.
DR GO; GO:0099508; F:voltage-gated ion channel activity involved in regulation of presynaptic membrane potential; IDA:SynGO.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IBA:GO_Central.
DR GO; GO:0030900; P:forebrain development; IEP:RGD.
DR GO; GO:1904456; P:negative regulation of neuronal action potential; IMP:RGD.
DR GO; GO:1904057; P:negative regulation of sensory perception of pain; IMP:RGD.
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; ISO:RGD.
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 1: Evidence at protein 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..625
FT /note="Potassium voltage-gated channel subfamily C member
FT 4"
FT /id="PRO_0000054060"
FT TOPO_DOM 1..227
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..248
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TRANSMEM 279..299
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 300..313
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 314..334
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TRANSMEM 346..365
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 366..381
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 382..402
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TRANSMEM 453..473
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 474..625
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 65..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 437..442
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 508..526
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..543
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 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 625 AA; 68435 MW; C3A86BC88231FB04 CRC64;
MISSVCVSSY RGRKSGNKPP SKTCLKEEMA KGEASEKIII NVGGTRHETY RSTLRTLPGT
RLAWLADPDG GGRPESDGGG AGSSGSSGGG GGCEFFFDRH PGVFAYVLNY YRTGKLHCPA
DVCGPLFEEE LTFWGIDETD VEPCCWMTYR QHRDAEEALD IFESPDGGGG GAGPGDEAGD
DERELALQRL GPHEGGSGPG AGSGGCRGWQ PRMWALFEDP YSSRAARVVA FASLFFILVS
ITTFCLETHE AFNIDRNVTE IHRVGNITSV RFRREVETEP ILTYIEGVCV MWFTLEFLVR
IVCCPDTLDF VKNLLNIIDF VAILPFYLEV GLSGLSSKAA RDVLGFLRVV RFVRILRIFK
LTRHFVGLRV LGHTLRASTN EFLLLIIFLA LGVLIFATMI YYAERIGARP SDPRGNDHTD
FKNIPIGFWW AVVTMTTLGY GDMYPKTWSG MLVGALCALA GVLTIAMPVP VIVNNFGMYY
SLAMAKQKLP KKRKKHVPRP PQLESPIYCK SEETSPRDST YSDTSPPARE EGMVERKRAD
SKQNGDANAV LSDEEGAGLT QPLASAPTPE ERRALRRSGT RDRNKKAAAC FLLSAGDYAC
ADGSVQKEGS VEPKACVPVS HTCAL
