KCNSK_CAEEL
ID KCNSK_CAEEL Reviewed; 536 AA.
AC Q8I4B0; E3W725; Q09658; Q14V33; Q6BEV2; Q8I4A9; Q8I4B1;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Potassium voltage-gated channel protein shk-1;
GN Name=shk-1 {ECO:0000312|EMBL:CAA88477.2}; ORFNames=ZK1321.2;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAA88477.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:CAA88477.2};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP ALTERNATIVE SPLICING, FUNCTION, AND TISSUE SPECIFICITY (ISOFORMS A; C AND
RP D).
RX PubMed=16899454; DOI=10.1074/jbc.m605814200;
RA Fawcett G.L., Santi C.M., Butler A., Harris T., Covarrubias M., Salkoff L.;
RT "Mutant analysis of the Shal (Kv4) voltage-gated fast transient K+ channel
RT in Caenorhabditis elegans.";
RL J. Biol. Chem. 281:30725-30735(2006).
RN [3] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=21059759; DOI=10.1113/jphysiol.2010.200683;
RA Liu P., Ge Q., Chen B., Salkoff L., Kotlikoff M.I., Wang Z.W.;
RT "Genetic dissection of ion currents underlying all-or-none action
RT potentials in C. elegans body-wall muscle cells.";
RL J. Physiol. (Lond.) 589:101-117(2011).
CC -!- FUNCTION: Mediates the voltage-dependent potassium ion permeability of
CC excitable membranes. Has an important role in repolarization and in
CC regulating the pattern of action potential firing. Isoform a expresses
CC currents in a more depolarized voltage range than isoform d.
CC {ECO:0000269|PubMed:16899454, ECO:0000269|PubMed:21059759}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P08510}; Multi-
CC pass membrane protein {ECO:0000250|UniProtKB:P08510}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=c {ECO:0000269|PubMed:9851916};
CC IsoId=Q8I4B0-1; Sequence=Displayed;
CC Name=b {ECO:0000269|PubMed:9851916};
CC IsoId=Q8I4B0-2; Sequence=VSP_044575;
CC Name=d {ECO:0000269|PubMed:9851916};
CC IsoId=Q8I4B0-3; Sequence=VSP_044572;
CC Name=a {ECO:0000269|PubMed:9851916};
CC IsoId=Q8I4B0-4; Sequence=VSP_044573, VSP_044575;
CC Name=e {ECO:0000269|PubMed:9851916};
CC IsoId=Q8I4B0-5; Sequence=VSP_044571, VSP_044575;
CC Name=f {ECO:0000269|PubMed:9851916};
CC IsoId=Q8I4B0-6; Sequence=VSP_044570, VSP_044575;
CC Name=g {ECO:0000269|PubMed:9851916};
CC IsoId=Q8I4B0-7; Sequence=VSP_044574;
CC -!- TISSUE SPECIFICITY: Expressed in a variety of interneurons and sensory
CC neurons, as well as body wall muscle. {ECO:0000269|PubMed:16899454,
CC ECO:0000269|PubMed:21059759}.
CC -!- DISRUPTION PHENOTYPE: Delayed spike repolarization.
CC {ECO:0000269|PubMed:21059759}.
CC -!- SIMILARITY: Belongs to the potassium channel family. A (Shaker) (TC
CC 1.A.1.2) subfamily. Shaker sub-subfamily. {ECO:0000255}.
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DR EMBL; Z48584; CAA88477.2; -; Genomic_DNA.
DR EMBL; Z48584; CAD57715.1; -; Genomic_DNA.
DR EMBL; Z48584; CAD57716.1; -; Genomic_DNA.
DR EMBL; Z48584; CAD57717.1; -; Genomic_DNA.
DR EMBL; Z48584; CAH04712.1; -; Genomic_DNA.
DR EMBL; Z48584; CAK55179.1; -; Genomic_DNA.
DR EMBL; Z48584; CBX53352.1; -; Genomic_DNA.
DR RefSeq; NP_001022516.1; NM_001027345.2. [Q8I4B0-5]
DR RefSeq; NP_001040829.1; NM_001047364.2. [Q8I4B0-6]
DR RefSeq; NP_001254226.1; NM_001267297.1.
DR RefSeq; NP_496104.2; NM_063703.4. [Q8I4B0-4]
DR RefSeq; NP_871934.1; NM_182134.3. [Q8I4B0-2]
DR RefSeq; NP_871935.1; NM_182135.4. [Q8I4B0-1]
DR RefSeq; NP_871936.1; NM_182136.4. [Q8I4B0-3]
DR AlphaFoldDB; Q8I4B0; -.
DR SMR; Q8I4B0; -.
DR STRING; 6239.ZK1321.2c; -.
DR TCDB; 1.A.1.2.20; the voltage-gated ion channel (vic) superfamily.
DR EPD; Q8I4B0; -.
DR PaxDb; Q8I4B0; -.
DR PeptideAtlas; Q8I4B0; -.
DR ABCD; Q8I4B0; 1 sequenced antibody.
DR EnsemblMetazoa; ZK1321.2a.1; ZK1321.2a.1; WBGene00014261. [Q8I4B0-4]
DR EnsemblMetazoa; ZK1321.2b.1; ZK1321.2b.1; WBGene00014261. [Q8I4B0-2]
DR EnsemblMetazoa; ZK1321.2c.1; ZK1321.2c.1; WBGene00014261. [Q8I4B0-1]
DR EnsemblMetazoa; ZK1321.2d.1; ZK1321.2d.1; WBGene00014261. [Q8I4B0-3]
DR EnsemblMetazoa; ZK1321.2e.1; ZK1321.2e.1; WBGene00014261. [Q8I4B0-5]
DR EnsemblMetazoa; ZK1321.2f.1; ZK1321.2f.1; WBGene00014261. [Q8I4B0-6]
DR GeneID; 174536; -.
DR KEGG; cel:CELE_ZK1321.2; -.
DR UCSC; ZK1321.2a; c. elegans.
DR CTD; 174536; -.
DR WormBase; ZK1321.2a; CE32769; WBGene00014261; shk-1. [Q8I4B0-4]
DR WormBase; ZK1321.2b; CE32770; WBGene00014261; shk-1. [Q8I4B0-2]
DR WormBase; ZK1321.2c; CE32771; WBGene00014261; shk-1. [Q8I4B0-1]
DR WormBase; ZK1321.2d; CE32772; WBGene00014261; shk-1. [Q8I4B0-3]
DR WormBase; ZK1321.2e; CE36966; WBGene00014261; shk-1. [Q8I4B0-5]
DR WormBase; ZK1321.2f; CE40295; WBGene00014261; shk-1. [Q8I4B0-6]
DR eggNOG; KOG1545; Eukaryota.
DR GeneTree; ENSGT00940000164717; -.
DR InParanoid; Q8I4B0; -.
DR OMA; MPFDDPF; -.
DR OrthoDB; 695337at2759; -.
DR PhylomeDB; Q8I4B0; -.
DR PRO; PR:Q8I4B0; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00014261; Expressed in larva and 3 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; HDA:WormBase.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IBA:GO_Central.
DR GO; GO:0005251; F:delayed rectifier potassium channel activity; IDA:WormBase.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IBA:GO_Central.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IDA:WormBase.
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; IPR005821; Ion_trans_dom.
DR InterPro; IPR003968; K_chnl_volt-dep_Kv.
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 SUPFAM; SSF54695; SSF54695; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Ion channel; Ion transport; Membrane; Potassium;
KW Potassium channel; Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..536
FT /note="Potassium voltage-gated channel protein shk-1"
FT /id="PRO_0000420623"
FT TOPO_DOM 1..275
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..296
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 297..322
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 323..343
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 344..356
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 357..377
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 378..425
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 426..446
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 447..458
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 459..479
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 480..486
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 487..507
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 508..536
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 87..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..89
FT /note="Missing (in isoform f)"
FT /evidence="ECO:0000303|PubMed:9851916"
FT /id="VSP_044570"
FT VAR_SEQ 1..85
FT /note="MRFGGQRRCIESSDDNDSIDSMSIQQKNKEKEEWKWAQSLARRLEQVLNVHP
FT EKYQNGCSSQRPSRQPSPVEQLAPIRSHSADFG -> MWRFNRIKS (in isoform
FT e)"
FT /evidence="ECO:0000303|PubMed:9851916"
FT /id="VSP_044571"
FT VAR_SEQ 1..41
FT /note="MRFGGQRRCIESSDDNDSIDSMSIQQKNKEKEEWKWAQSLA -> MIDSLI
FT (in isoform d)"
FT /evidence="ECO:0000303|PubMed:9851916"
FT /id="VSP_044572"
FT VAR_SEQ 42..85
FT /note="RRLEQVLNVHPEKYQNGCSSQRPSRQPSPVEQLAPIRSHSADFG -> S
FT (in isoform a)"
FT /evidence="ECO:0000303|PubMed:9851916"
FT /id="VSP_044573"
FT VAR_SEQ 126..536
FT /note="Missing (in isoform g)"
FT /evidence="ECO:0000303|PubMed:9851916"
FT /id="VSP_044574"
FT VAR_SEQ 185..196
FT /note="Missing (in isoform b, isoform a, isoform e and
FT isoform f)"
FT /evidence="ECO:0000303|PubMed:9851916"
FT /id="VSP_044575"
SQ SEQUENCE 536 AA; 61234 MW; 9662A84009CF0632 CRC64;
MRFGGQRRCI ESSDDNDSID SMSIQQKNKE KEEWKWAQSL ARRLEQVLNV HPEKYQNGCS
SQRPSRQPSP VEQLAPIRSH SADFGRAAEM ASGNSEEGKG MLLRNGDDRI RLPSPQRGTP
DTSSTQGHPY TDQIVTINVS GMRFQTFEST LSRYPNSLLG DRNKRQHFFV SDTNEFFFDR
HRTTSSSFTF EIRNYLFESI LYIYQSGGRV KRPEIVPIDI FLKEMRFFQM GDDLLEEFWI
AEGYEKPKEV MMPNNKTQRK IWELMEYPDS SLSARIIAFI SIAVIALSII SFCWETVPSD
IEEKPINNSA TAELLDEMDE KHYSPFFWIE LMCILWFTIE LILRFISCPC KVTFATSVLN
IIDFVAIAPF FVNFFFADTS KSNSSMSFAV LRVLRLVRVF RVFKLSRHSV GLQILGKTFR
SSVQEFCLLI FFMAIALVLF ASGMYFAEQG EPNSKFTSIP ASFWFVLVTM TTVGYGDLVP
LSPFGKVVGG MCAMIGVLTL ALPVPIIVAN FKHFYRQENR LASMKSKGDD ADDDIA
