KCA10_MOUSE
ID KCA10_MOUSE Reviewed; 511 AA.
AC B2RQA1; B2RXZ4;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Potassium voltage-gated channel subfamily A member 10 {ECO:0000305};
DE AltName: Full=Voltage-gated potassium channel subunit Kv1.8 {ECO:0000250|UniProtKB:Q16322};
GN Name=Kcna10 {ECO:0000312|MGI:MGI:3037820};
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 {ECO:0000312|Proteomes:UP000000589};
RN [1] {ECO:0000312|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2] {ECO:0000312|EMBL:AAI37829.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain {ECO:0000312|EMBL:AAI37829.1};
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 [3] {ECO:0000305}
RP DEVELOPMENTAL STAGE.
RX PubMed=22446089; DOI=10.1016/j.gep.2012.03.001;
RA Carlisle F.A., Steel K.P., Lewis M.A.;
RT "Specific expression of Kcna10, Pxn and Odf2 in the organ of Corti.";
RL Gene Expr. Patterns 12:172-179(2012).
RN [4] {ECO:0000305}
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=23528307; DOI=10.1016/j.heares.2013.02.009;
RA Lee S.I., Conrad T., Jones S.M., Lagziel A., Starost M.F.,
RA Belyantseva I.A., Friedman T.B., Morell R.J.;
RT "A null mutation of mouse Kcna10 causes significant vestibular and mild
RT hearing dysfunction.";
RL Hear. Res. 300:1-9(2013).
CC -!- FUNCTION: Mediates 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. The channel
CC activity is up-regulated by cAMP. {ECO:0000250|UniProtKB:Q16322}.
CC -!- SUBUNIT: Homotetramer. Interacts with KCN4B/POMP. Interaction with
CC KCN4B/POMP is necessary for the modulation of channel activity by cAMP.
CC {ECO:0000250|UniProtKB:Q16322}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed strongly in the inner ear and weakly in
CC skeletal muscle. Not detected in other tissues.
CC {ECO:0000269|PubMed:23528307}.
CC -!- DEVELOPMENTAL STAGE: Detected in the cochlear duct from 14.5 dpc
CC (PubMed:22446089). Detected in the organ of Corti and the vestibular
CC system from 16.5 dpc onwards, where it is most strongly expressed in
CC hair cells (PubMed:22446089, PubMed:23528307).
CC {ECO:0000269|PubMed:22446089, ECO:0000269|PubMed:23528307}.
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. {ECO:0000250|UniProtKB:Q16322}.
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:0000250|UniProtKB:P63142}.
CC -!- DISRUPTION PHENOTYPE: Viable with no gross defects. Vestibular evoked
CC potentials (VsEPs) are highly abnormal suggesting impaired function of
CC the balance organ, although mice do not display any obvious imbalance
CC behaviors. {ECO:0000269|PubMed:23528307}.
CC -!- SIMILARITY: Belongs to the potassium channel family. A (Shaker) (TC
CC 1.A.1.2) subfamily. Kv1.8/KCNA10 sub-subfamily. {ECO:0000305}.
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DR EMBL; AC121825; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC132405; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC137828; AAI37829.1; -; mRNA.
DR EMBL; BC137829; AAI37830.1; -; mRNA.
DR EMBL; BC158036; AAI58037.1; -; mRNA.
DR CCDS; CCDS38587.1; -.
DR RefSeq; NP_001074609.1; NM_001081140.1.
DR AlphaFoldDB; B2RQA1; -.
DR SMR; B2RQA1; -.
DR STRING; 10090.ENSMUSP00000088118; -.
DR PhosphoSitePlus; B2RQA1; -.
DR MaxQB; B2RQA1; -.
DR PaxDb; B2RQA1; -.
DR PeptideAtlas; B2RQA1; -.
DR PRIDE; B2RQA1; -.
DR ProteomicsDB; 269244; -.
DR Antibodypedia; 20099; 88 antibodies from 22 providers.
DR DNASU; 242151; -.
DR Ensembl; ENSMUST00000055064; ENSMUSP00000088118; ENSMUSG00000042861.
DR GeneID; 242151; -.
DR KEGG; mmu:242151; -.
DR UCSC; uc008qwt.1; mouse.
DR CTD; 3744; -.
DR MGI; MGI:3037820; Kcna10.
DR VEuPathDB; HostDB:ENSMUSG00000042861; -.
DR eggNOG; KOG1545; Eukaryota.
DR GeneTree; ENSGT00940000159534; -.
DR HOGENOM; CLU_011722_4_0_1; -.
DR InParanoid; B2RQA1; -.
DR OMA; TACIAWF; -.
DR OrthoDB; 695337at2759; -.
DR PhylomeDB; B2RQA1; -.
DR TreeFam; TF313103; -.
DR Reactome; R-MMU-1296072; Voltage gated Potassium channels.
DR BioGRID-ORCS; 242151; 2 hits in 72 CRISPR screens.
DR PRO; PR:B2RQA1; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; B2RQA1; protein.
DR Bgee; ENSMUSG00000042861; Expressed in quadriceps femoris and 4 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; ISO:MGI.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006813; P:potassium ion 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; 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; PR01491; KVCHANNEL.
DR PRINTS; PR01496; SHAKERCHANEL.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
PE 2: Evidence at transcript level;
KW Ion channel; Ion transport; Lipoprotein; Membrane; Palmitate; Potassium;
KW Potassium channel; Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..511
FT /note="Potassium voltage-gated channel subfamily A member
FT 10"
FT /id="PRO_0000437460"
FT TRANSMEM 218..238
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..292
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TRANSMEM 303..323
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TRANSMEM 339..358
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TRANSMEM 375..395
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TRANSMEM 436..456
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT REGION 25..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 489..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 421..426
FT /note="Selectivity filter"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT COMPBIAS 489..504
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 293
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q09470"
FT CONFLICT 250
FT /note="V -> A (in Ref. 2; AAI58037)"
FT /evidence="ECO:0000305"
FT CONFLICT 479
FT /note="E -> S (in Ref. 2; AAI58037)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 511 AA; 57968 MW; 31FB404011B4BF29 CRC64;
MDVCSWKEME VALVNFDNSD EIHEEPGYAT DFDPTSSKGR PGSSPFSNWR VLISDNTNHE
TAFSKIPGEY VDPPGPEPVV LNEGNQRVII NIAGLRFETQ LRTLNQFPET LLGDREKRMQ
FFDSMRNEYF FDRNRPSFDG ILYYYQSGGK IRRPANVPID VFADEISFYE LGSEAMDQFR
EDEGFIKDPE TLLPTNDFHR QFWLLFEYPE SSSAARGVAV VSVLVVVISI TIFCLETLPE
FREDRELKVV RDPSINTNKT GLSQTMFTDP FFMVESTCIV WFTFELVLRF VVCPSKTDFF
KNIMNIIDII SIIPYFATLI TELVQETEPS AQQNMSLAIL RIIRLVRVFR IFKLSRHSKG
LQILGQTLKA SMRELGLLIF FLFIGVILFS SAVYFAEVDE PESHFSSIPD GFWWAVVTMT
TVGYGDMCPT TPGGKIVGTL CAIAGVLTIA LPVPVIVSNF NYFYHRETEN EEKPNIPGEL
DKILNSMGSR MGSTESLNKT NGSCSAEKSR K
