KCNC3_RAT
ID KCNC3_RAT Reviewed; 889 AA.
AC Q01956;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Potassium voltage-gated channel subfamily C member 3;
DE AltName: Full=KSHIIID {ECO:0000303|PubMed:1381835};
DE AltName: Full=Voltage-gated potassium channel subunit Kv3.3 {ECO:0000303|PubMed:20857303};
GN Name=Kcnc3;
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] (ISOFORMS KSHIIID.1 AND KSHIIID.2), FUNCTION,
RP AND SUBCELLULAR LOCATION.
RC TISSUE=Brain;
RX PubMed=1381835; DOI=10.1098/rspb.1992.0036;
RA de Miera E.V.-S., Moreno H., Fruhling D., Kentros C., Rudy B.;
RT "Cloning of ShIII (Shaw-like) cDNAs encoding a novel high-voltage-
RT activating, TEA-sensitive, type-A K+ channel.";
RL Proc. R. Soc. B 248:9-18(1992).
RN [2]
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).
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:1381835). It plays a
CC role in the regulation of the frequency, shape and duration of action
CC potentials in Purkinje cells. Required for normal survival of
CC cerebellar neurons, probably via its role in regulating the duration
CC and frequency of action potentials that in turn regulate the activity
CC of voltage-gated Ca(2+) channels and cellular Ca(2+) homeostasis.
CC Required for normal motor function (By similarity). 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 (By similarity).
CC {ECO:0000250|UniProtKB:Q14003, ECO:0000250|UniProtKB:Q63959,
CC ECO:0000269|PubMed:1381835}.
CC -!- SUBUNIT: Homotetramer. Heterotetramer with KCNC1. Interacts (via C-
CC terminus) with HAX1. Identified in a complex with ACTR3, a subunit of
CC the Arp2/3 complex; this interaction is indirect and depends on the
CC presence of HAX1. {ECO:0000250|UniProtKB:Q14003}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1381835};
CC Multi-pass membrane protein {ECO:0000255}. Presynaptic cell membrane
CC {ECO:0000269|PubMed:20857303}; Multi-pass membrane protein
CC {ECO:0000255}. Perikaryon {ECO:0000250|UniProtKB:Q63959}. Cell
CC projection, axon {ECO:0000250|UniProtKB:Q63959}. Cell projection,
CC dendrite {ECO:0000250|UniProtKB:Q63959}. Cell projection, dendritic
CC spine membrane {ECO:0000269|PubMed:20857303}; 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 (PubMed:20857303). Detected at
CC presynaptic calices of Held (By similarity). Colocalizes with the
CC cortical actin cytoskeleton and the Arp2/3 complex (By similarity).
CC {ECO:0000250|UniProtKB:Q14003, ECO:0000250|UniProtKB:Q63959,
CC ECO:0000269|PubMed:20857303}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=KSHIIID.1;
CC IsoId=Q01956-1; Sequence=Displayed;
CC Name=KSHIIID.2;
CC IsoId=Q01956-2; Sequence=VSP_001022, VSP_001023;
CC -!- TISSUE SPECIFICITY: Detected on Purkinje cells in the cerebellum
CC molecular layer (at protein level). {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 cytoplasmic N-terminus mediates N-type inactivation.
CC {ECO:0000250|UniProtKB:Q14003}.
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:0000250|UniProtKB:Q14003}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q14003}.
CC -!- SIMILARITY: Belongs to the potassium channel family. C (Shaw) (TC
CC 1.A.1.2) subfamily. Kv3.3/KCNC3 sub-subfamily. {ECO:0000305}.
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DR EMBL; M84210; AAA73182.1; -; mRNA.
DR EMBL; M84211; AAA41470.1; -; mRNA.
DR AlphaFoldDB; Q01956; -.
DR SMR; Q01956; -.
DR STRING; 10116.ENSRNOP00000027062; -.
DR GuidetoPHARMACOLOGY; 550; -.
DR GlyGen; Q01956; 1 site.
DR PaxDb; Q01956; -.
DR PRIDE; Q01956; -.
DR ABCD; Q01956; 1 sequenced antibody.
DR UCSC; RGD:621358; rat. [Q01956-1]
DR RGD; 621358; Kcnc3.
DR eggNOG; KOG3713; Eukaryota.
DR InParanoid; Q01956; -.
DR PhylomeDB; Q01956; -.
DR Reactome; R-RNO-1296072; Voltage gated Potassium channels.
DR PRO; PR:Q01956; -.
DR Proteomes; UP000002494; Unplaced.
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:0043679; C:axon terminus; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0032591; C:dendritic spine membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
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:0032809; C:neuronal cell body membrane; ISO:RGD.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
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; 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; IPR005404; K_chnl_volt-dep_Kv3.3.
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; 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 Alternative splicing; Cell membrane; Cell projection; Cytoplasm;
KW Cytoskeleton; Glycoprotein; Ion channel; Ion transport; Membrane;
KW Methylation; Phosphoprotein; Postsynaptic cell membrane; Potassium;
KW Potassium channel; Potassium transport; Reference proteome; Synapse;
KW Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..889
FT /note="Potassium voltage-gated channel subfamily C member
FT 3"
FT /id="PRO_0000054057"
FT TOPO_DOM 1..291
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
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..889
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..80
FT /note="Important for normal N-type inactivation"
FT /evidence="ECO:0000250|UniProtKB:Q14003"
FT REGION 10..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 691..834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 852..889
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 504..509
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT COMPBIAS 23..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 COMPBIAS 757..780
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 626
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q63959"
FT MOD_RES 697
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63959"
FT MOD_RES 702
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63959"
FT MOD_RES 759
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q63959"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 662..679
FT /note="NDLGVLEEGDPRPNGDPA -> EAGARTGGVGRPGGWGSG (in isoform
FT KSHIIID.2)"
FT /evidence="ECO:0000303|PubMed:1381835"
FT /id="VSP_001022"
FT VAR_SEQ 680..889
FT /note="Missing (in isoform KSHIIID.2)"
FT /evidence="ECO:0000303|PubMed:1381835"
FT /id="VSP_001023"
SQ SEQUENCE 889 AA; 94393 MW; 51424C047B4FC367 CRC64;
MLSSVCVWSF SGRQGTRKQH SQPAPTPQPP ESSPPPLLPP PQQQCAQPGT AASPAGAPLS
CGPGGRRAEP CSGLPAVAMG RHGGGGGDSG KIVINVGGVR HETYRSTLRT LPGTRLAGLT
EPEAAARFDY DPGTDEFFFD RHPGVFAYVL NYYRTGKLHC PADVCGPLFE EELGFWGIDE
TDVEACCWMT YRQHRDAEEA LDSFEAPDSS GNANANAGGA HDAGLDDEAG AGGGGLDGAG
GELKRLCFQD AGGGAGGPAG GPGGAGGTWW 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
ITPPSMGVTV AGAYPPGPHT HPGLLRGGAG GLGIMGLPPL PAPGEPCPLA QEEVIETNRA
GNDLGVLEEG DPRPNGDPAA AALAHEDCPA IDQPAMSPED KSPITPGSRG RYSRDRACFL
VTDYAPSPDG SIRKATGAPP LPPHAGVSQA PPASCPTSTP TQQPGYPPSG RAPSPPQATP
EAPAIFDVWL PPFHRSHQPP GKHQRGGRHP GVSPSPQQRA CVGEPPSASH PQSLTLCISV
PSSCHRLRPR ETLGFPLSLP PRLATGNGGR ECPRDPGLPF PSRHSSPAV
