KCNA3_MOUSE
ID KCNA3_MOUSE Reviewed; 528 AA.
AC P16390; A3KMM2;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 3.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Potassium voltage-gated channel subfamily A member 3;
DE AltName: Full=MK3;
DE AltName: Full=Voltage-gated potassium channel subunit Kv1.3;
GN Name=Kcna3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2305265; DOI=10.1126/science.2305265;
RA Chandy K.G., Williams C.B., Spencer R.H., Aguilar B.A., Ghanshani S.,
RA Tempel B.L., Gutman G.A.;
RT "A family of three mouse potassium channel genes with intronless coding
RT regions.";
RL Science 247:973-975(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 expression.";
RL Cell 143:1174-1189(2010).
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. Binds PDZ
CC domains of DLG4 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein.
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:0000250}.
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; M30441; AAA39716.1; -; Genomic_DNA.
DR EMBL; CH466607; EDL01888.1; -; Genomic_DNA.
DR EMBL; BC132349; AAI32350.1; -; mRNA.
DR EMBL; BC137667; AAI37668.1; -; mRNA.
DR CCDS; CCDS17730.1; -.
DR PIR; C40090; I84205.
DR PIR; S09044; S09044.
DR RefSeq; NP_032444.2; NM_008418.2.
DR AlphaFoldDB; P16390; -.
DR SMR; P16390; -.
DR BioGRID; 200878; 211.
DR IntAct; P16390; 1.
DR STRING; 10090.ENSMUSP00000050680; -.
DR BindingDB; P16390; -.
DR ChEMBL; CHEMBL4818; -.
DR GuidetoPHARMACOLOGY; 540; -.
DR GlyGen; P16390; 1 site.
DR iPTMnet; P16390; -.
DR PhosphoSitePlus; P16390; -.
DR EPD; P16390; -.
DR jPOST; P16390; -.
DR MaxQB; P16390; -.
DR PaxDb; P16390; -.
DR PeptideAtlas; P16390; -.
DR PRIDE; P16390; -.
DR ProteomicsDB; 269196; -.
DR ABCD; P16390; 1 sequenced antibody.
DR Antibodypedia; 33788; 380 antibodies from 37 providers.
DR DNASU; 16491; -.
DR Ensembl; ENSMUST00000052718; ENSMUSP00000050680; ENSMUSG00000047959.
DR GeneID; 16491; -.
DR KEGG; mmu:16491; -.
DR UCSC; uc008qwp.2; mouse.
DR CTD; 3738; -.
DR MGI; MGI:96660; Kcna3.
DR VEuPathDB; HostDB:ENSMUSG00000047959; -.
DR eggNOG; KOG1545; Eukaryota.
DR GeneTree; ENSGT00940000160210; -.
DR HOGENOM; CLU_011722_4_0_1; -.
DR InParanoid; P16390; -.
DR OMA; GMNSAFK; -.
DR OrthoDB; 695337at2759; -.
DR PhylomeDB; P16390; -.
DR TreeFam; TF313103; -.
DR Reactome; R-MMU-1296072; Voltage gated Potassium channels.
DR BioGRID-ORCS; 16491; 0 hits in 71 CRISPR screens.
DR PRO; PR:P16390; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P16390; protein.
DR Bgee; ENSMUSG00000047959; Expressed in embryonic brain and 70 other tissues.
DR Genevisible; P16390; MM.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:0044305; C:calyx of Held; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; ISO:MGI.
DR GO; GO:0099056; C:integral component of presynaptic membrane; ISO:MGI.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IBA:GO_Central.
DR GO; GO:0005251; F:delayed rectifier potassium channel activity; ISO:MGI.
DR GO; GO:0015271; F:outward rectifier potassium channel activity; ISO:MGI.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; ISO:MGI.
DR GO; GO:0071805; P:potassium ion transmembrane transport; ISO:MGI.
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..528
FT /note="Potassium voltage-gated channel subfamily A member
FT 3"
FT /id="PRO_0000053978"
FT TOPO_DOM 1..187
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..206
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 207..247
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 248..269
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 270..280
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 281..301
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 302..315
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 316..334
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 335..350
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 351..370
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 371..411
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 412..434
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 435..528
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 397..402
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT MOTIF 526..528
FT /note="PDZ-binding"
FT /evidence="ECO:0000250"
FT MOD_RES 473
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000255"
FT LIPID 270
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 369
FT /note="V -> A (in Ref. 1; AAA39716)"
FT /evidence="ECO:0000305"
FT CONFLICT 492
FT /note="H -> Q (in Ref. 1; AAA39716)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 528 AA; 58564 MW; 12AC94FB13A523E7 CRC64;
MTVVPGDHLL EPEAAGGGGG DPPQGGCGSG GGGGGCDRYE PLPPALPAAG EQDCCGERVV
INISGLRFET QLKTLCQFPE TLLGDPKRRM RYFDPLRNEY FFDRNRPSFD AILYYYQSGG
RIRRPVNVPI DIFSEEIRFY QLGEEAMEKF REDEGFLREE ERPLPRRDFQ RQVWLLFEYP
ESSGPARGIA IVSVLVILIS IVIFCLETLP EFRDEKDYPA SPSQDVFEAA NNSTSGAPSG
ASSFSDPFFV VETLCIIWFS FELLVRFFAC PSKATFSRNI MNLIDIVAII PYFITLGTEL
AERQGNGQQA MSLAILRVIR LVRVFRIFKL SRHSKGLQIL GQTLKASMRE LGLLIFFLFI
GVILFSSAVY FAEADDPSSG FNSIPDAFWW AVVTMTTVGY GDMHPVTIGG KIVGSLCAIA
GVLTIALPVP VIVSNFNYFY HRETEGEEQA QYMHVGSCQH LSSSAEELRK ARSNSTLSKS
EYMVIEEGGM NHSAFPQTPF KTGNSTATCT TNNNPNSCVN IKKIFTDV
