KCNA3_RAT
ID KCNA3_RAT Reviewed; 525 AA.
AC P15384;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Potassium voltage-gated channel subfamily A member 3;
DE AltName: Full=RCK3;
DE AltName: Full=RGK5;
DE AltName: Full=Voltage-gated potassium channel subunit Kv1.3;
DE AltName: Full=Voltage-gated potassium channel subunit Kv3;
GN Name=Kcna3;
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].
RC TISSUE=Brain;
RX PubMed=2555158; DOI=10.1002/j.1460-2075.1989.tb08483.x;
RA Stuehmer W., Ruppersberg J.P., Schroerter K.H., Sakmann B., Stocker M.,
RA Giese K.P., Perschke A., Baumann A., Pongs O.;
RT "Molecular basis of functional diversity of voltage-gated potassium
RT channels in mammalian brain.";
RL EMBO J. 8:3235-3244(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Brain;
RX PubMed=2361015; DOI=10.1016/0896-6273(90)90146-7;
RA Swanson R., Marshall J., Smith J., Williams J., Boyle M.B., Folander K.,
RA Luneau C.J., Antanavage J., Oliva C., Buhrow S.A., Bennett C., Stein R.B.,
RA Kaczmarek L.M.;
RT "Cloning and expression of cDNA and genomic clones encoding three delayed
RT rectifier potassium channels in rat brain.";
RL Neuron 4:929-939(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Lymphocyte;
RX PubMed=2351830;
RA Douglass J., Osborne P.B., Cai Y.C., Wilkinson M., Christie M.J.,
RA Adelman J.P.;
RT "Characterization and functional expression of a rat genomic DNA clone
RT encoding a lymphocyte potassium channel.";
RL J. Immunol. 144:4841-4850(1990).
RN [4]
RP INTERACTION WITH DLG1; DLG2 AND DLG4.
RX PubMed=7477295; DOI=10.1038/378085a0;
RA Kim E., Niethammer M., Rothschild A., Jan Y.N., Sheng M.;
RT "Clustering of Shaker-type K+ channels by interaction with a family of
RT membrane-associated guanylate kinases.";
RL Nature 378:85-88(1995).
RN [5]
RP GLYCOSYLATION AT ASN-229, LACK OF GLYCOSYLATION AT ASN-228, AND SUBCELLULAR
RP LOCATION.
RX PubMed=22613618; DOI=10.1111/j.1742-4658.2012.08642.x;
RA Zhu J., Yan J., Thornhill W.B.;
RT "N-glycosylation promotes the cell surface expression of Kv1.3 potassium
RT channels.";
RL FEBS J. 279:2632-2644(2012).
CC -!- FUNCTION: Mediates the voltage-dependent potassium ion permeability of
CC excitable membranes. Assuming opened or closed conformations in
CC response to the voltage difference across the membrane, the protein
CC forms a potassium-selective channel through which potassium ions may
CC pass in accordance with their electrochemical gradient.
CC -!- SUBUNIT: Heterotetramer of potassium channel proteins (By similarity).
CC Binds PDZ domains of DLG1, DLG2 and DLG4. {ECO:0000250}.
CC -!- INTERACTION:
CC P15384; P78352: DLG4; Xeno; NbExp=2; IntAct=EBI-631478, EBI-80389;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22613618};
CC Multi-pass membrane protein {ECO:0000269|PubMed:22613618}.
CC -!- DOMAIN: The N-terminus may be important in determining the rate of
CC inactivation of the channel while the tail may play a role in
CC modulation of channel activity and/or targeting of the channel to
CC specific subcellular compartments.
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 -!- PTM: N-glycosylation promotes the cell surface expression.
CC {ECO:0000269|PubMed:22613618}.
CC -!- SIMILARITY: Belongs to the potassium channel family. A (Shaker) (TC
CC 1.A.1.2) subfamily. Kv1.3/KCNA3 sub-subfamily. {ECO:0000305}.
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DR EMBL; X16001; CAA34132.1; -; mRNA.
DR EMBL; M30312; AAA42035.1; -; Genomic_DNA.
DR EMBL; M31744; AAA41500.1; -; Genomic_DNA.
DR PIR; A43531; A43531.
DR RefSeq; NP_062143.3; NM_019270.3.
DR AlphaFoldDB; P15384; -.
DR SMR; P15384; -.
DR BioGRID; 248344; 2.
DR CORUM; P15384; -.
DR IntAct; P15384; 1.
DR STRING; 10116.ENSRNOP00000024372; -.
DR BindingDB; P15384; -.
DR ChEMBL; CHEMBL4248; -.
DR GuidetoPHARMACOLOGY; 540; -.
DR GlyGen; P15384; 1 site.
DR iPTMnet; P15384; -.
DR PhosphoSitePlus; P15384; -.
DR PaxDb; P15384; -.
DR PRIDE; P15384; -.
DR ABCD; P15384; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000092240; ENSRNOP00000075761; ENSRNOG00000062002.
DR Ensembl; ENSRNOT00000108050; ENSRNOP00000096474; ENSRNOG00000062002.
DR GeneID; 29731; -.
DR KEGG; rno:29731; -.
DR UCSC; RGD:2951; rat.
DR CTD; 3738; -.
DR RGD; 2951; Kcna3.
DR eggNOG; KOG1545; Eukaryota.
DR GeneTree; ENSGT00940000160210; -.
DR InParanoid; P15384; -.
DR OMA; GMNSAFK; -.
DR OrthoDB; 695337at2759; -.
DR PhylomeDB; P15384; -.
DR TreeFam; TF313103; -.
DR Reactome; R-RNO-1296072; Voltage gated Potassium channels.
DR PRO; PR:P15384; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000062002; Expressed in thymus and 12 other tissues.
DR GO; GO:0030424; C:axon; ISO:RGD.
DR GO; GO:0044305; C:calyx of Held; IDA:SynGO.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IMP:UniProtKB.
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:0045121; C:membrane raft; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IBA:GO_Central.
DR GO; GO:0005251; F:delayed rectifier potassium channel activity; IMP:RGD.
DR GO; GO:0015271; F:outward rectifier potassium channel activity; IMP:RGD.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IMP:UniProtKB.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IMP:UniProtKB.
DR GO; GO:0006813; P:potassium ion transport; TAS:RGD.
DR GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
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; IPR003972; K_chnl_volt-dep_Kv1.
DR InterPro; IPR004050; K_chnl_volt-dep_Kv1.3.
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; PR01510; KV13CHANNEL.
DR PRINTS; PR01491; KVCHANNEL.
DR PRINTS; PR01496; SHAKERCHANEL.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Ion channel; Ion transport; Lipoprotein;
KW Membrane; Palmitate; Phosphoprotein; Potassium; Potassium channel;
KW Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..525
FT /note="Potassium voltage-gated channel subfamily A member
FT 3"
FT /id="PRO_0000053979"
FT TOPO_DOM 1..184
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..203
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 204..244
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..266
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 267..277
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..298
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 299..312
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 313..331
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 332..347
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 348..367
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 368..408
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 409..431
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 432..525
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 394..399
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT MOTIF 523..525
FT /note="PDZ-binding"
FT SITE 228
FT /note="Not glycosylated"
FT /evidence="ECO:0000269|PubMed:22613618"
FT MOD_RES 470
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000255"
FT LIPID 267
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22613618"
FT CONFLICT 106
FT /note="F -> L (in Ref. 1; CAA34132)"
FT /evidence="ECO:0000305"
FT CONFLICT 181
FT /note="G -> R (in Ref. 3; AAA42035)"
FT /evidence="ECO:0000305"
FT CONFLICT 430
FT /note="V -> L (in Ref. 3; AAA42035)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 525 AA; 58425 MW; 6DA8869D5471C401 CRC64;
MTVVPGDHLL EPEAAGGGGG DPPQGGCVSG GGCDRYEPLP PALPAAGEQD CCGERVVINI
SGLRFETQLK TLCQFPETLL GDPKRRMRYF DPLRNEYFFD RNRPSFDAIL YYYQSGGRIR
RPVNVPIDIF SEEIRFYQLG EEAMEKFRED EGFLREEERP LPRRDFQRQV WLLFEYPESS
GPARGIAIVS VLVILISIVI FCLETLPEFR DEKDYPASPS QDVFEAANNS TSGASSGASS
FSDPFFVVET LCIIWFSFEL LVRFFACPSK ATFSRNIMNL IDIVAIIPYF ITLGTELAER
QGNGQQAMSL AILRVIRLVR VFRIFKLSRH SKGLQILGQT LKASMRELGL LIFFLFIGVI
LFSSAVYFAE ADDPSSGFNS IPDAFWWAVV TMTTVGYGDM HPVTIGGKIV GSLCAIAGVL
TIALPVPVIV SNFNYFYHRE TEGEEQAQYM HVGSCQHLSS SAEELRKARS NSTLSKSEYM
VIEEGGMNHS AFPQTPFKTG NSTATCTTNN NPNSCVNIKK IFTDV
