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Database: UniProt
Entry: KCNC1_MOUSE
LinkDB: KCNC1_MOUSE
Original site: KCNC1_MOUSE 
ID   KCNC1_MOUSE             Reviewed;         511 AA.
AC   P15388; E9PVV3;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   27-SEP-2017, entry version 161.
DE   RecName: Full=Potassium voltage-gated channel subfamily C member 1;
DE   AltName: Full=NGK2 {ECO:0000303|PubMed:2599109};
DE   AltName: Full=Voltage-gated potassium channel subunit Kv3.1;
DE   AltName: Full=Voltage-gated potassium channel subunit Kv4;
GN   Name=Kcnc1 {ECO:0000312|MGI:MGI:96667};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=2599109; DOI=10.1016/0014-5793(89)81488-7;
RA   Yokoyama S., Imoto K., Kawamura T., Higashida H., Iwabe N., Miyata T.,
RA   Numa S.;
RT   "Potassium channels from NG108-15 neuroblastoma-glioma hybrid cells.
RT   Primary structure and functional expression from cDNAs.";
RL   FEBS Lett. 259:37-42(1989).
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.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=1400413;
RA   Grissmer S., Ghanshani S., Dethlefs B., McPherson J.D., Wasmuth J.J.,
RA   Gutman G.A., Cahalan M.D., Chandy K.G.;
RT   "The Shaw-related potassium channel gene, Kv3.1, on human chromosome
RT   11, encodes the type l K+ channel in T cells.";
RL   J. Biol. Chem. 267:20971-20979(1992).
RN   [4]
RP   DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX   PubMed=9037088; DOI=10.1073/pnas.94.4.1533;
RA   Ho C.S., Grange R.W., Joho R.H.;
RT   "Pleiotropic effects of a disrupted K+ channel gene: reduced body
RT   weight, impaired motor skill and muscle contraction, but no
RT   seizures.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:1533-1538(1997).
RN   [5]
RP   DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX   PubMed=11517255;
RA   Espinosa F., McMahon A., Chan E., Wang S., Ho C.S., Heintz N.,
RA   Joho R.H.;
RT   "Alcohol hypersensitivity, increased locomotion, and spontaneous
RT   myoclonus in mice lacking the potassium channels Kv3.1 and Kv3.3.";
RL   J. Neurosci. 21:6657-6665(2001).
RN   [6]
RP   DISRUPTION PHENOTYPE, AND TISSUE 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.,
RA   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   [7]
RP   DISRUPTION PHENOTYPE.
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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160; SER-474 AND
RP   THR-483, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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
RT   expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Voltage-gated potassium channel that plays an important
CC       role in the rapid repolarization of fast-firing brain neurons. The
CC       channel opens in response to the voltage difference across the
CC       membrane, forming a potassium-selective channel through which
CC       potassium ions pass in accordance with their electrochemical
CC       gradient (PubMed:2599109, PubMed:1400413). Can form functional
CC       homotetrameric channels and heterotetrameric channels that contain
CC       variable proportions of KCNC2, and possibly other family members
CC       as well. Contributes to fire sustained trains of very brief action
CC       potentials at high frequency in pallidal neurons.
CC       {ECO:0000250|UniProtKB:P25122, ECO:0000269|PubMed:1400413,
CC       ECO:0000269|PubMed:2599109}.
CC   -!- SUBUNIT: Heteromultimer with KCNG3, KCNG4 and KCNV2 (By
CC       similarity). Heteromultimer with KCNC2 (By similarity).
CC       Heterotetramer with KCNC3 (By similarity). Interacts with the
CC       ancillary subunits KCNE1 and KCNE2; the interaction modulates
CC       channel activity (By similarity). {ECO:0000250,
CC       ECO:0000250|UniProtKB:P48547}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1400413,
CC       ECO:0000269|PubMed:2599109}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=KV3.1;
CC         IsoId=P15388-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P15388-3; Sequence=VSP_058604;
CC         Note=No experimental confirmation available. Gene prediction
CC         based on EST data.;
CC   -!- TISSUE SPECIFICITY: Detected in cerebellum (PubMed:11517255,
CC       PubMed:15217387). Detected in brain (at protein level)
CC       (PubMed:9037088). Detected in brain (PubMed:9037088).
CC       {ECO:0000269|PubMed:11517255, ECO:0000269|PubMed:15217387,
CC       ECO:0000269|PubMed:9037088}.
CC   -!- DOMAIN: The segment S4 is probably the voltage-sensor and is
CC       characterized by a series of positively charged amino acids at
CC       every third position. {ECO:0000305}.
CC   -!- DOMAIN: The tail may be important in modulation of channel
CC       activity and/or targeting of the channel to specific subcellular
CC       compartments. {ECO:0000305}.
CC   -!- PTM: N-glycosylated; contains sialylated glycans.
CC       {ECO:0000250|UniProtKB:P25122}.
CC   -!- DISRUPTION PHENOTYPE: Mutant mice are born at the expected
CC       Mendelian rate. They are viable and fertile, but have lower body
CC       weight than wild-type. They have normal spontaneous locomotor
CC       activity, but impaired motor skills (PubMed:9037088). Mice lacking
CC       both Kcnc3 and Kcnc1 are born at the expected Mendelian rate, but
CC       the pups do not thrive and all die about 26 days after birth when
CC       kept together with other littermates. Their failure to thrive may
CC       be due to motor problems; mutant pups survive when fed separately,
CC       but 45 days after birth their body weight is only 50 to 60 % of
CC       that of wild-type (PubMed:11517255). They appear uncoordinated and
CC       display severe ataxia, myoclonus and spontaneous whole-body muscle
CC       jerks, but display no obvious alterations in brain morphology
CC       (PubMed:11517255, PubMed:15217387, PubMed:16923152). Mutant mice
CC       are also much more sensitive to ethanol and fall sideways at
CC       ethanol concentrations that have no effect on wild-type mice
CC       (PubMed:11517255). They display increased locomotor and
CC       exploratory activity (PubMed:11517255, PubMed:15217387). Mice
CC       lacking Kcnc1 show reduced response to tremorogenic agent
CC       harmaline; mice lacking both Kcnc3 and Kcnc1 are resistant to the
CC       tremorogenic agent harmaline (PubMed:15217387).
CC       {ECO:0000269|PubMed:11517255, ECO:0000269|PubMed:15217387,
CC       ECO:0000269|PubMed:16923152}.
CC   -!- SIMILARITY: Belongs to the potassium channel family. C (Shaw) (TC
CC       1.A.1.2) subfamily. Kv3.1/KCNC1 sub-subfamily. {ECO:0000305}.
DR   EMBL; Y07521; CAA68814.1; -; mRNA.
DR   EMBL; AC020786; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC090652; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS21278.1; -. [P15388-1]
DR   CCDS; CCDS52252.1; -. [P15388-3]
DR   PIR; S07095; S07095.
DR   RefSeq; NP_032447.1; NM_008421.3. [P15388-1]
DR   UniGene; Mm.249386; -.
DR   ProteinModelPortal; P15388; -.
DR   SMR; P15388; -.
DR   BioGrid; 200887; 3.
DR   STRING; 10090.ENSMUSP00000124938; -.
DR   GuidetoPHARMACOLOGY; 548; -.
DR   iPTMnet; P15388; -.
DR   PhosphoSitePlus; P15388; -.
DR   PaxDb; P15388; -.
DR   PeptideAtlas; P15388; -.
DR   PRIDE; P15388; -.
DR   Ensembl; ENSMUST00000025202; ENSMUSP00000025202; ENSMUSG00000058975. [P15388-1]
DR   Ensembl; ENSMUST00000160433; ENSMUSP00000124938; ENSMUSG00000058975. [P15388-3]
DR   GeneID; 16502; -.
DR   KEGG; mmu:16502; -.
DR   UCSC; uc009gyo.2; mouse. [P15388-1]
DR   CTD; 3746; -.
DR   MGI; MGI:96667; Kcnc1.
DR   eggNOG; KOG3713; Eukaryota.
DR   eggNOG; COG1226; LUCA.
DR   GeneTree; ENSGT00760000118846; -.
DR   HOGENOM; HOG000231012; -.
DR   HOVERGEN; HBG105862; -.
DR   InParanoid; P15388; -.
DR   KO; K04887; -.
DR   OMA; SGGFWRR; -.
DR   OrthoDB; EOG091G0EJL; -.
DR   PhylomeDB; P15388; -.
DR   TreeFam; TF352511; -.
DR   Reactome; R-MMU-1296072; Voltage gated Potassium channels.
DR   PRO; PR:P15388; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   Bgee; ENSMUSG00000058975; -.
DR   ExpressionAtlas; P15388; baseline and differential.
DR   Genevisible; P15388; MM.
DR   GO; GO:0030673; C:axolemma; IDA:MGI.
DR   GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR   GO; GO:0032590; C:dendrite membrane; IDA:MGI.
DR   GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR   GO; GO:0032809; C:neuronal cell body membrane; IDA:MGI.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; ISS:UniProtKB.
DR   GO; GO:0005251; F:delayed rectifier potassium channel activity; ISS:UniProtKB.
DR   GO; GO:0044325; F:ion channel binding; IPI:UniProtKB.
DR   GO; GO:0019894; F:kinesin binding; IDA:MGI.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IBA:GO_Central.
DR   GO; GO:0035690; P:cellular response to drug; IEA:Ensembl.
DR   GO; GO:0021549; P:cerebellum development; IEA:Ensembl.
DR   GO; GO:0021759; P:globus pallidus development; IEA:Ensembl.
DR   GO; GO:1903818; P:positive regulation of voltage-gated potassium channel activity; IEA:Ensembl.
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:0014075; P:response to amine; IEA:Ensembl.
DR   GO; GO:0010996; P:response to auditory stimulus; IEA:Ensembl.
DR   GO; GO:0071774; P:response to fibroblast growth factor; IEA:Ensembl.
DR   GO; GO:0009642; P:response to light intensity; IEA:Ensembl.
DR   GO; GO:1990089; P:response to nerve growth factor; IEA:Ensembl.
DR   GO; GO:0035864; P:response to potassium ion; IEA:Ensembl.
DR   GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
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.
DR   InterPro; IPR003131; T1-type_BTB.
DR   InterPro; IPR028325; VG_K_chnl.
DR   PANTHER; PTHR11537; PTHR11537; 1.
DR   Pfam; PF02214; BTB_2; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   PRINTS; PR00169; KCHANNEL.
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; Complete proteome; Glycoprotein;
KW   Ion channel; Ion transport; Membrane; Phosphoprotein; Potassium;
KW   Potassium channel; Potassium transport; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN         1    511       Potassium voltage-gated channel subfamily
FT                                C member 1.
FT                                /FTId=PRO_0000054052.
FT   TOPO_DOM      1    190       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    191    209       Helical; Name=Segment S1. {ECO:0000255}.
FT   TRANSMEM    248    267       Helical; Name=Segment S2. {ECO:0000255}.
FT   TOPO_DOM    268    276       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    277    295       Helical; Name=Segment S3. {ECO:0000255}.
FT   TRANSMEM    309    331       Helical; Voltage-sensor; Name=Segment S4.
FT                                {ECO:0000255}.
FT   TOPO_DOM    332    344       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    345    366       Helical; Name=Segment S5. {ECO:0000255}.
FT   TRANSMEM    415    436       Helical; Name=Segment S6. {ECO:0000255}.
FT   TOPO_DOM    437    511       Cytoplasmic. {ECO:0000255}.
FT   MOTIF       400    405       Selectivity filter. {ECO:0000250}.
FT   MOD_RES      44     44       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P25122}.
FT   MOD_RES     130    130       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P25122}.
FT   MOD_RES     142    142       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P25122}.
FT   MOD_RES     158    158       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P25122}.
FT   MOD_RES     160    160       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     474    474       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     483    483       Phosphothreonine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   CARBOHYD    220    220       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    229    229       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   VAR_SEQ     502    511       GRKPLRGMSI -> DSKLNGEVAKAALANEDCPHIDQALTP
FT                                DEGLPFTRSGTRERYGPCFLLSTGEYACPPGGGMRKDLCKE
FT                                SPVIAKYMPTEAVRVT (in isoform 2).
FT                                /FTId=VSP_058604.
SQ   SEQUENCE   511 AA;  57928 MW;  50A939E8F7120F37 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 AGRKPLRGMS I
//
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