KCNC1_RAT
ID KCNC1_RAT Reviewed; 585 AA.
AC P25122;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Potassium voltage-gated channel subfamily C member 1;
DE AltName: Full=NGK2;
DE AltName: Full=RAW2;
DE AltName: Full=Voltage-gated potassium channel subunit Kv3.1;
DE AltName: Full=Voltage-gated potassium channel subunit Kv4;
GN Name=Kcnc1;
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=2023941; DOI=10.1073/pnas.88.9.3932;
RA Luneau C.J., Williams J.B., Marshall J., Levitan E.S., Oliva C.,
RA Smith J.S., Antanavage J., Folander K., Stein R.B., Swanson R.,
RA Kaczmarek L.K., Buhrow S.A.;
RT "Alternative splicing contributes to K+ channel diversity in the mammalian
RT central nervous system.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:3932-3936(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
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).
RN [3]
RP FUNCTION, SUBUNIT, INTERACTION WITH KCNC2, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=10482766; DOI=10.1152/jn.1999.82.3.1512;
RA Hernandez-Pineda R., Chow A., Amarillo Y., Moreno H., Saganich M.,
RA Vega-Saenz de Miera E.C., Hernandez-Cruz A., Rudy B.;
RT "Kv3.1-Kv3.2 channels underlie a high-voltage-activating component of the
RT delayed rectifier K+ current in projecting neurons from the globus
RT pallidus.";
RL J. Neurophysiol. 82:1512-1528(1999).
RN [4]
RP SUBUNIT, INTERACTION WITH KCNC2; KCNE1 AND KCNE2, FUNCTION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=14679187; DOI=10.1074/jbc.m310501200;
RA Lewis A., McCrossan Z.A., Abbott G.W.;
RT "MinK, MiRP1, and MiRP2 diversify Kv3.1 and Kv3.2 potassium channel
RT gating.";
RL J. Biol. Chem. 279:7884-7892(2004).
RN [5]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=20857303; DOI=10.1007/s00418-010-0742-6;
RA Puente N., Mendizabal-Zubiaga J., Elezgarai I., Reguero L., Buceta I.,
RA Grandes P.;
RT "Precise localization of the voltage-gated potassium channel subunits
RT Kv3.1b and Kv3.3 revealed in the molecular layer of the rat cerebellar
RT cortex by a pre-embedding immunogold method.";
RL Histochem. Cell Biol. 134:403-409(2010).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44; SER-130; SER-142; SER-158
RP AND SER-160, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [7]
RP SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-220 AND ASN-229, AND MUTAGENESIS
RP OF ASN-220 AND ASN-229.
RX PubMed=24161696; DOI=10.1016/j.bbagen.2013.10.025;
RA Hall M.K., Weidner D.A., Bernetski C.J., Schwalbe R.A.;
RT "N-Linked glycan site occupancy impacts the distribution of a potassium
RT channel in the cell body and outgrowths of neuronal-derived cells.";
RL Biochim. Biophys. Acta 1840:595-604(2014).
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 (PubMed:10482766,
CC PubMed:14679187). Can form functional homotetrameric channels and
CC heterotetrameric channels that contain variable proportions of KCNC2,
CC and possibly other family members as well (PubMed:10482766,
CC PubMed:14679187). Contributes to fire sustained trains of very brief
CC action potentials at high frequency in pallidal neurons
CC (PubMed:10482766). {ECO:0000269|PubMed:10482766,
CC ECO:0000269|PubMed:14679187}.
CC -!- SUBUNIT: Heteromultimer with KCNG3, KCNG4 and KCNV2 (By similarity).
CC Heteromultimer with KCNC2 (PubMed:10482766, PubMed:14679187).
CC Heterotetramer with KCNC3 (By similarity). Interacts with the ancillary
CC subunits KCNE1 and KCNE2; the interaction modulates channel activity
CC (PubMed:14679187). {ECO:0000250, ECO:0000250|UniProtKB:P48547,
CC ECO:0000269|PubMed:10482766, ECO:0000269|PubMed:14679187}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10482766,
CC ECO:0000269|PubMed:14679187, ECO:0000269|PubMed:24161696}; Multi-pass
CC membrane protein {ECO:0000255}. Cell projection, axon
CC {ECO:0000269|PubMed:20857303}. Presynaptic cell membrane
CC {ECO:0000269|PubMed:20857303}. Note=Localizes in parallel fiber
CC membranes, distributed on the perisynaptic and extrasynaptic membranes
CC away from the active zones. {ECO:0000269|PubMed:20857303}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P25122-1; Sequence=Displayed;
CC Name=2; Synonyms=Short;
CC IsoId=P25122-2; Sequence=VSP_001016, VSP_001017;
CC -!- TISSUE SPECIFICITY: Expressed in brain (PubMed:1378392). Expressed in
CC globus pallidal neurons of the basal ganglia (at protein level)
CC (PubMed:10482766). Detected on Purkinje cells in the cerebellum
CC molecular layer (at protein level) (PubMed:20857303).
CC {ECO:0000269|PubMed:10482766, ECO:0000269|PubMed:1378392,
CC ECO:0000269|PubMed:20857303}.
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 tail may be important in modulation of channel activity
CC and/or targeting of the channel to specific subcellular compartments.
CC {ECO:0000305}.
CC -!- PTM: N-glycosylated; contains sialylated glycans.
CC {ECO:0000269|PubMed:24161696}.
CC -!- SIMILARITY: Belongs to the potassium channel family. C (Shaw) (TC
CC 1.A.1.2) subfamily. Kv3.1/KCNC1 sub-subfamily. {ECO:0000305}.
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DR EMBL; M68880; AAA41501.1; -; mRNA.
DR EMBL; X62840; CAA44644.1; -; mRNA.
DR PIR; A39395; A39395.
DR RefSeq; NP_036988.1; NM_012856.1. [P25122-1]
DR AlphaFoldDB; P25122; -.
DR SMR; P25122; -.
DR BioGRID; 247366; 1.
DR STRING; 10116.ENSRNOP00000015260; -.
DR BindingDB; P25122; -.
DR ChEMBL; CHEMBL2321617; -.
DR DrugCentral; P25122; -.
DR GuidetoPHARMACOLOGY; 548; -.
DR GlyGen; P25122; 2 sites.
DR iPTMnet; P25122; -.
DR PhosphoSitePlus; P25122; -.
DR PaxDb; P25122; -.
DR PRIDE; P25122; -.
DR ABCD; P25122; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000089488; ENSRNOP00000074146; ENSRNOG00000055401. [P25122-1]
DR GeneID; 25327; -.
DR KEGG; rno:25327; -.
DR UCSC; RGD:2955; rat. [P25122-1]
DR CTD; 3746; -.
DR RGD; 2955; Kcnc1.
DR eggNOG; KOG3713; Eukaryota.
DR GeneTree; ENSGT00940000156912; -.
DR HOGENOM; CLU_011722_4_3_1; -.
DR InParanoid; P25122; -.
DR OMA; MGQGDDS; -.
DR OrthoDB; 818306at2759; -.
DR PhylomeDB; P25122; -.
DR Reactome; R-RNO-1296072; Voltage gated Potassium channels.
DR PRO; PR:P25122; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000055401; Expressed in cerebellum and 7 other tissues.
DR Genevisible; P25122; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030673; C:axolemma; ISO:RGD.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
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; ISO: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:0016020; C:membrane; IDA:RGD.
DR GO; GO:0032589; C:neuron projection membrane; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0032809; C:neuronal cell body membrane; IDA:UniProtKB.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IDA:UniProtKB.
DR GO; GO:0005251; F:delayed rectifier potassium channel activity; IDA:UniProtKB.
DR GO; GO:0019894; F:kinesin binding; ISO:RGD.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:UniProtKB.
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:0007420; P:brain development; IEP:RGD.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0021549; P:cerebellum development; IEP:RGD.
DR GO; GO:0021759; P:globus pallidus development; IEP:RGD.
DR GO; GO:0034767; P:positive regulation of ion transmembrane transport; IDA:RGD.
DR GO; GO:1901381; P:positive regulation of potassium ion transmembrane transport; IDA:RGD.
DR GO; GO:1903818; P:positive regulation of voltage-gated potassium channel activity; IDA:RGD.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IDA: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; IMP:RGD.
DR GO; GO:1901379; P:regulation of potassium ion transmembrane transport; IDA:RGD.
DR GO; GO:0014075; P:response to amine; IEP:RGD.
DR GO; GO:0010996; P:response to auditory stimulus; IEP:RGD.
DR GO; GO:0071774; P:response to fibroblast growth factor; IEP:RGD.
DR GO; GO:0009642; P:response to light intensity; IEP:RGD.
DR GO; GO:1990089; P:response to nerve growth factor; IEP:RGD.
DR GO; GO:0035864; P:response to potassium ion; IEP:RGD.
DR GO; GO:0009636; P:response to toxic substance; IEP: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; IPR005403; K_chnl_volt-dep_Kv3.1.
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 PRINTS; PR01581; KV31CHANNEL.
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 Alternative splicing; Cell membrane; Cell projection; Glycoprotein;
KW Ion channel; Ion transport; Membrane; Phosphoprotein; Potassium;
KW Potassium channel; Potassium transport; Reference proteome; Synapse;
KW Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..585
FT /note="Potassium voltage-gated channel subfamily C member
FT 1"
FT /id="PRO_0000054053"
FT TOPO_DOM 1..190
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..209
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TRANSMEM 248..267
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 268..276
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..295
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TRANSMEM 309..331
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 332..344
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 345..366
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TRANSMEM 415..436
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 437..585
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 121..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 400..405
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 158
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 474
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15388"
FT MOD_RES 483
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P15388"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:24161696"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:24161696"
FT VAR_SEQ 502..511
FT /note="DSKLNGEVAK -> GRKPLRGMSI (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_001016"
FT VAR_SEQ 512..585
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_001017"
FT MUTAGEN 220
FT /note="N->Q: Reduces extent of N-glycosylation. Abolishes
FT N-glycosylation; when associated with Q-229."
FT /evidence="ECO:0000269|PubMed:24161696"
FT MUTAGEN 229
FT /note="N->Q: Reduces extent of N-glycosylation. Abolishes
FT N-glycosylation; when associated with Q-220."
FT /evidence="ECO:0000269|PubMed:24161696"
SQ SEQUENCE 585 AA; 65857 MW; DD4E2D32848E2DCF CRC64;
MGQGDESERI VINVGGTRHQ TYRSTLRTLP GTRLAWLAEP DAHSHFDYDP RADEFFFDRH
PGVFAHILNY YRTGKLHCPA DVCGPLYEEE LAFWGIDETD VEPCCWMTYR QHRDAEEALD
SFGGAPLDNS ADDADADGPG DSGDGEDELE MTKRLALSDS PDGRPGGFWR RWQPRIWALF
EDPYSSRYAR YVAFASLFFI LVSITTFCLE THERFNPIVN KTEIENVRNG TQVRYYREAE
TEAFLTYIEG VCVVWFTFEF LMRVVFCPNK VEFIKNSLNI IDFVAILPFY LEVGLSGLSS
KAAKDVLGFL RVVRFVRILR IFKLTRHFVG LRVLGHTLRA STNEFLLLII FLALGVLIFA
TMIYYAERIG AQPNDPSASE HTHFKNIPIG FWWAVVTMTT LGYGDMYPQT WSGMLVGALC
ALAGVLTIAM PVPVIVNNFG MYYSLAMAKQ KLPKKKKKHI PRPPQLGSPN YCKSVVNSPH
HSTQSDTCPL AQEEILEINR ADSKLNGEVA KAALANEDCP HIDQALTPDE GLPFTRSGTR
ERYGPCFLLS TGEYACPPGG GMRKDLCKES PVIAKYMPTE AVRVT
