KCNA7_MOUSE
ID KCNA7_MOUSE Reviewed; 489 AA.
AC Q17ST2; O70259;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Potassium voltage-gated channel subfamily A member 7;
DE AltName: Full=Voltage-gated potassium channel subunit Kv1.7;
GN Name=Kcna7; Synonyms=Kcnc7;
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 / MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=9488722; DOI=10.1074/jbc.273.10.5851;
RA Kalman K., Nguyen A., Tseng-Crank J., Dukes I.D., Chandy G., Hustad C.M.,
RA Copeland N.G., Jenkins N.A., Mohrenweiser H., Brandriff B., Cahalan M.,
RA Gutman G.A., Chandy K.G.;
RT "Genomic organization, chromosomal localization, tissue distribution, and
RT biophysical characterization of a novel mammalian Shaker-related voltage-
RT gated potassium channel, Kv1.7.";
RL J. Biol. Chem. 273:5851-5857(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=NMRI; TISSUE=Heart, and Skeletal muscle;
RX PubMed=16801386; DOI=10.1085/jgp.200609498;
RA Finol-Urdaneta R.K., Struever N., Terlau H.;
RT "Molecular and functional differences between heart mKv1.7 channel
RT isoforms.";
RL J. Gen. Physiol. 128:133-145(2006).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11896454; DOI=10.1038/sj.ejhg.5200739;
RA Bardien-Kruger S., Wulff H., Arieff Z., Brink P., Chandy K.G., Corfield V.;
RT "Characterisation of the human voltage-gated potassium channel gene, KCNA7,
RT a candidate gene for inherited cardiac disorders, and its exclusion as
RT cause of progressive familial heart block I (PFHBI).";
RL Eur. J. Hum. Genet. 10:36-43(2002).
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. Channels formed
CC by isoform 1 inactivate faster than channels formed by isoform 2.
CC {ECO:0000269|PubMed:11896454, ECO:0000269|PubMed:16801386,
CC ECO:0000269|PubMed:9488722}.
CC -!- SUBUNIT: Heterotetramer of potassium channel proteins. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:11896454,
CC ECO:0000269|PubMed:16801386, ECO:0000269|PubMed:9488722}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:11896454,
CC ECO:0000269|PubMed:16801386, ECO:0000269|PubMed:9488722}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=2;
CC Name=1; Synonyms=Kv1.7L;
CC IsoId=Q17ST2-1; Sequence=Displayed;
CC Name=2; Synonyms=Kv1.7S;
CC IsoId=Q17ST2-2; Sequence=VSP_028953;
CC -!- TISSUE SPECIFICITY: Detected in heart, skeletal muscle, brain, and
CC pancreatic islet cells. {ECO:0000269|PubMed:16801386,
CC ECO:0000269|PubMed:9488722}.
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 -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative initiation at Met-
CC 33 of isoform 1. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the potassium channel family. A (Shaker) (TC
CC 1.A.1.2) subfamily. Kv1.7/KCNA7 sub-subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC12271.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAC23664.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF032099; AAC12271.1; ALT_FRAME; mRNA.
DR EMBL; AF032101; AAC23664.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AF032100; AAC23664.1; JOINED; Genomic_DNA.
DR EMBL; AY779767; AAX11185.1; -; mRNA.
DR CCDS; CCDS39951.1; -. [Q17ST2-1]
DR PIR; S09047; S09047.
DR RefSeq; NP_034726.2; NM_010596.2. [Q17ST2-1]
DR AlphaFoldDB; Q17ST2; -.
DR SMR; Q17ST2; -.
DR STRING; 10090.ENSMUSP00000103403; -.
DR DrugCentral; Q17ST2; -.
DR GuidetoPHARMACOLOGY; 544; -.
DR GlyGen; Q17ST2; 1 site.
DR iPTMnet; Q17ST2; -.
DR PhosphoSitePlus; Q17ST2; -.
DR jPOST; Q17ST2; -.
DR PaxDb; Q17ST2; -.
DR PRIDE; Q17ST2; -.
DR ProteomicsDB; 263592; -. [Q17ST2-1]
DR ProteomicsDB; 263593; -. [Q17ST2-2]
DR ABCD; Q17ST2; 1 sequenced antibody.
DR Antibodypedia; 18500; 79 antibodies from 21 providers.
DR DNASU; 16495; -.
DR Ensembl; ENSMUST00000107774; ENSMUSP00000103403; ENSMUSG00000038201. [Q17ST2-1]
DR GeneID; 16495; -.
DR KEGG; mmu:16495; -.
DR UCSC; uc009guz.1; mouse. [Q17ST2-1]
DR CTD; 3743; -.
DR MGI; MGI:96664; Kcna7.
DR VEuPathDB; HostDB:ENSMUSG00000038201; -.
DR eggNOG; KOG1545; Eukaryota.
DR GeneTree; ENSGT00940000162339; -.
DR HOGENOM; CLU_011722_4_0_1; -.
DR InParanoid; Q17ST2; -.
DR OMA; MPFDDPF; -.
DR OrthoDB; 818306at2759; -.
DR PhylomeDB; Q17ST2; -.
DR TreeFam; TF313103; -.
DR Reactome; R-MMU-1296072; Voltage gated Potassium channels.
DR BioGRID-ORCS; 16495; 2 hits in 71 CRISPR screens.
DR PRO; PR:Q17ST2; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q17ST2; protein.
DR Bgee; ENSMUSG00000038201; Expressed in hindlimb stylopod muscle and 14 other tissues.
DR Genevisible; Q17ST2; MM.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IBA:GO_Central.
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 Alternative initiation; Alternative splicing; Glycoprotein; Ion channel;
KW Ion transport; Lipoprotein; Membrane; Palmitate; Potassium;
KW Potassium channel; Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..489
FT /note="Potassium voltage-gated channel subfamily A member
FT 7"
FT /id="PRO_0000308274"
FT TRANSMEM 176..196
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TRANSMEM 242..262
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..294
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TRANSMEM 309..328
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TRANSMEM 345..365
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TRANSMEM 406..426
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT MOTIF 391..396
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT LIPID 264
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 224
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..32
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16801386"
FT /id="VSP_028953"
FT CONFLICT 86
FT /note="R -> A (in Ref. 1; AAC12271)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="V -> L (in Ref. 2; AAX11185)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="P -> S (in Ref. 1; AAC12271)"
FT /evidence="ECO:0000305"
FT CONFLICT 260
FT /note="R -> H (in Ref. 1; AAC12271)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 489 AA; 53948 MW; 80E92AB7697B6D2A CRC64;
MLFLPADTGH PTGVAAASGP HVRSPVARAV RAMEPRCPPP CGCCERLVLN VAGLRFETRA
RTLGRFPDTL LGDPVRRSRF YDGARREYFF DRHRPSFDAV LYYYQSGGRL RRPAHVPLDV
FLEEVSFYGL GAAALARLRE DEGCAVPPER PLPRRAFARQ LWLLFEFPES SQAARVLAVV
SVLVILVSIV VFCLETLPDF RDDRDDPGLA PVAAATGPFL ARLNGSSPMP GAPPRQPFND
PFFVVETLCI CWFSFELLVR LVACPSKAVF FKNVMNLIDF VAILPYFVAL GTELARQRGV
GQPAMSLAIL RVIRLVRVFR IFKLSRHSKG LQILGQTLRA SMRELGLLIF FLFIGVVLFS
SAVYFAEVDR VDTHFTSIPE SFWWAVVTMT TVGYGDMAPV TVGGKIVGSL CAIAGVLTIS
LPVPVIVSNF SYFYHRETEG EEAGMYSHVD TQPCGTLEGK ANGGLVDSEV PELLPPLWPP
AGKHMVTEV
