SLO1_CAEEL
ID SLO1_CAEEL Reviewed; 1140 AA.
AC Q95V25; Q95V26; Q95V27; Q9U268;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Calcium-activated potassium channel slo-1;
DE AltName: Full=BK channel;
DE AltName: Full=Maxi K channel;
DE Short=MaxiK;
DE AltName: Full=Slo homolog;
DE AltName: Full=Slowpoke protein 1;
GN Name=slo-1 {ECO:0000312|WormBase:Y51A2D.19a};
GN ORFNames=Y51A2D.19 {ECO:0000312|WormBase:Y51A2D.19a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B AND C), FUNCTION, TISSUE
RP SPECIFICITY, AND MUTAGENESIS OF GLY-289.
RX PubMed=11738032; DOI=10.1016/s0896-6273(01)00522-0;
RA Wang Z.-W., Saifee O., Nonet M.L., Salkoff L.;
RT "SLO-1 potassium channels control quantal content of neurotransmitter
RT release at the C. elegans neuromuscular junction.";
RL Neuron 32:867-881(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
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 [3]
RP RESPONSE TO ETHANOL.
RX PubMed=14675531; DOI=10.1016/s0092-8674(03)00979-6;
RA Davies A.G., Pierce-Shimomura J.T., Kim H., VanHoven M.K., Thiele T.R.,
RA Bonci A., Bargmann C.I., McIntire S.L.;
RT "A central role of the BK potassium channel in behavioral responses to
RT ethanol in C. elegans.";
RL Cell 115:655-666(2003).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP GLU-350.
RX PubMed=28168949; DOI=10.7554/elife.24733;
RA Oh K.H., Haney J.J., Wang X., Chuang C.F., Richmond J.E., Kim H.;
RT "ERG-28 controls BK channel trafficking in the ER to regulate synaptic
RT function and alcohol response in C. elegans.";
RL Elife 6:0-0(2017).
CC -!- FUNCTION: Potassium channel activated by both membrane depolarization
CC or increase in cytosolic Ca(2+) that mediates export of K(+)
CC (PubMed:11738032). Its activation dampens the excitatory events that
CC elevate the cytosolic Ca(2+) concentration and/or depolarize the cell
CC membrane (PubMed:11738032). It therefore contributes to repolarization
CC of the membrane potential (PubMed:11738032). Essential for the
CC regulation of neurotransmitter release at synapses (PubMed:11738032,
CC PubMed:28168949). {ECO:0000269|PubMed:11738032,
CC ECO:0000269|PubMed:28168949}.
CC -!- SUBUNIT: Homotetramer; which constitutes the calcium-activated
CC potassium channel. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:28168949};
CC Multi-pass membrane protein {ECO:0000305}. Synapse
CC {ECO:0000269|PubMed:28168949}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=a;
CC IsoId=Q95V25-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q95V25-2; Sequence=VSP_009998;
CC Name=c;
CC IsoId=Q95V25-3; Sequence=VSP_009996, VSP_009997, VSP_009998;
CC -!- TISSUE SPECIFICITY: Expressed in synaptic regions of the nervous system
CC including in both the nerve ring and nerve cords, as well as in the
CC body-wall and vulval muscle. {ECO:0000269|PubMed:11738032,
CC ECO:0000269|PubMed:28168949}.
CC -!- DOMAIN: The S4 segment, which is characterized by a series of
CC positively charged amino acids at every third position, is part of the
CC voltage-sensor. {ECO:0000250}.
CC -!- DOMAIN: The pore-forming domain (also referred as P region) is imbedded
CC into the membrane, and forms the selectivity filter of the pore. It
CC contains the signature sequence of potassium channels that displays
CC selectivity to potassium (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The RCK N-terminal domain mediates the homotetramerization,
CC thereby promoting the assembly of monomers into functional potassium
CC channel. It includes binding sites for Ca(2+) and Mg(2+) (By
CC similarity). {ECO:0000250}.
CC -!- DOMAIN: The calcium bowl constitutes one of the Ca(2+) sensors and
CC probably acts as a Ca(2+)-binding site. {ECO:0000250}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
CC -!- MISCELLANEOUS: Its activity is activated by ethanol, leading to the
CC inhibition of neuronal activity.
CC -!- SIMILARITY: Belongs to the potassium channel family. Calcium-activated
CC (TC 1.A.1.3) subfamily. Slo sub-subfamily. {ECO:0000305}.
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DR EMBL; AF431891; AAL28102.1; -; mRNA.
DR EMBL; AF431892; AAL28103.1; -; mRNA.
DR EMBL; AF431893; AAL28104.1; -; mRNA.
DR EMBL; AL021497; CAB54459.2; -; Genomic_DNA.
DR EMBL; AL021497; CAD27617.1; -; Genomic_DNA.
DR EMBL; AL021497; CAD27618.1; -; Genomic_DNA.
DR PIR; T27083; T27083.
DR RefSeq; NP_001024259.1; NM_001029088.1. [Q95V25-1]
DR RefSeq; NP_001024260.1; NM_001029089.1. [Q95V25-2]
DR RefSeq; NP_001024261.1; NM_001029090.2. [Q95V25-3]
DR AlphaFoldDB; Q95V25; -.
DR SMR; Q95V25; -.
DR BioGRID; 45173; 3.
DR MINT; Q95V25; -.
DR STRING; 6239.Y51A2D.19d; -.
DR ChEMBL; CHEMBL3085614; -.
DR TCDB; 1.A.1.3.3; the voltage-gated ion channel (vic) superfamily.
DR iPTMnet; Q95V25; -.
DR EPD; Q95V25; -.
DR PaxDb; Q95V25; -.
DR EnsemblMetazoa; Y51A2D.19a.1; Y51A2D.19a.1; WBGene00004830. [Q95V25-1]
DR EnsemblMetazoa; Y51A2D.19b.1; Y51A2D.19b.1; WBGene00004830. [Q95V25-2]
DR EnsemblMetazoa; Y51A2D.19c.1; Y51A2D.19c.1; WBGene00004830. [Q95V25-3]
DR GeneID; 180203; -.
DR UCSC; Y51A2D.19a; c. elegans. [Q95V25-1]
DR CTD; 180203; -.
DR WormBase; Y51A2D.19a; CE30364; WBGene00004830; slo-1. [Q95V25-1]
DR WormBase; Y51A2D.19b; CE30365; WBGene00004830; slo-1. [Q95V25-2]
DR WormBase; Y51A2D.19c; CE30366; WBGene00004830; slo-1. [Q95V25-3]
DR eggNOG; KOG1420; Eukaryota.
DR GeneTree; ENSGT00940000168407; -.
DR InParanoid; Q95V25; -.
DR PhylomeDB; Q95V25; -.
DR Reactome; R-CEL-1300642; Sperm Motility And Taxes.
DR PRO; PR:Q95V25; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00004830; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR ExpressionAtlas; Q95V25; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031430; C:M band; IDA:WormBase.
DR GO; GO:0045211; C:postsynaptic membrane; IBA:GO_Central.
DR GO; GO:0055120; C:striated muscle dense body; IDA:WormBase.
DR GO; GO:0045202; C:synapse; IDA:WormBase.
DR GO; GO:0015269; F:calcium-activated potassium channel activity; IDA:WormBase.
DR GO; GO:0060072; F:large conductance calcium-activated potassium channel activity; IBA:GO_Central.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IDA:WormBase.
DR GO; GO:0048149; P:behavioral response to ethanol; IMP:WormBase.
DR GO; GO:0040011; P:locomotion; IGI:WormBase.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IGI:WormBase.
DR GO; GO:0043050; P:pharyngeal pumping; IMP:WormBase.
DR GO; GO:0006813; P:potassium ion transport; IDA:WormBase.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0046928; P:regulation of neurotransmitter secretion; IMP:WormBase.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IMP:WormBase.
DR GO; GO:0045214; P:sarcomere organization; IGI:WormBase.
DR Gene3D; 1.20.120.350; -; 1.
DR InterPro; IPR024939; Ca-act_K_channel_Slo-1.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR003929; K_chnl_BK_asu.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR10027:SF28; PTHR10027:SF28; 1.
DR Pfam; PF03493; BK_channel_a; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell membrane; Ion channel; Ion transport;
KW Membrane; Phosphoprotein; Potassium; Potassium channel;
KW Potassium transport; Reference proteome; Synapse; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..1140
FT /note="Calcium-activated potassium channel slo-1"
FT /id="PRO_0000054140"
FT TOPO_DOM 1..44
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 45..65
FT /note="Helical; Name=Segment S0"
FT /evidence="ECO:0000255"
FT TOPO_DOM 66..139
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..161
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 162..178
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..199
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 200..203
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 225..228
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..249
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 250..264
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 265..285
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 286..299
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 300..322
FT /note="Pore-forming; Name=P region"
FT /evidence="ECO:0000255"
FT TOPO_DOM 323..331
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 332..352
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 353..1140
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 353..519
FT /note="RCK N-terminal"
FT REGION 520..540
FT /note="Segment S7"
FT REGION 578..598
FT /note="Segment S8"
FT REGION 797..817
FT /note="Segment S9"
FT REGION 984..1004
FT /note="Segment S10"
FT MOTIF 316..319
FT /note="Selectivity for potassium"
FT MOTIF 955..977
FT /note="Calcium bowl"
FT VAR_SEQ 549..585
FT /note="QTTPDWLNLYLCGAGMEMYTDTLSHSFVGMTFPEAVD -> PHTPLWLNDYL
FT RGAGMEMYTESLSPSFANMSFPEAAN (in isoform c)"
FT /evidence="ECO:0000303|PubMed:11738032"
FT /id="VSP_009996"
FT VAR_SEQ 678
FT /note="R -> RDYSDFDALFYQND (in isoform c)"
FT /evidence="ECO:0000303|PubMed:11738032"
FT /id="VSP_009997"
FT VAR_SEQ 713..735
FT /note="SSTSDTHLNTKSLRFAYEIKKLM -> R (in isoform b and
FT isoform c)"
FT /evidence="ECO:0000303|PubMed:11738032"
FT /id="VSP_009998"
FT MUTAGEN 289
FT /note="G->E: In md1715; induces prolonged synaptic
FT release."
FT /evidence="ECO:0000269|PubMed:11738032"
FT MUTAGEN 350
FT /note="E->K: In ky399gf; gain of function. Insensitive to
FT the acetylcholinesterase inhibitor aldicarb, and locomotory
FT speed defects. In an erg-28 mutant background, these
FT defects are suppressed."
FT /evidence="ECO:0000269|PubMed:28168949"
SQ SEQUENCE 1140 AA; 129530 MW; 15670CB2CEA0F412 CRC64;
MGEIYSPSQS KGFNQPYGYP MNCNLSRVFM EMTEEDRKCL EERKYWCFLL SSITTFCASM
ILVVIWRVVT HLCCQRREKE FVEPIPAPEA VQINMNGSKH APSETDPFLK QQEEKHLGWM
TEAKDWAGEL ISGQSLTGRF LVLLVFILSI GSLIIYFYDA SFQNFQVETC IPWQDSPSQQ
IDLGFNIFFL VYFFIRFIAA SDKVWFLLEM YSWIDFFTIP PSFVAIYLQR NWLGFRFLRA
LRLMTVPDIL QYLNILKTSS SIRLTQLVTI FVAVCLTGAG LVHLLENSGD FFKGFINPHR
ITYADSVYFV LVTMSTVGYG DIYCTTLCGR LFMIFFILFG LAMFASYVPE IADLIGNRQK
YGGEYKGEHG KKHIVVCGHI TYDSVSHFLQ DFLHEDRDDV DVEVVFLHRV VPDLELEGLF
KRHFTKVEFF TGTVMDSLDL SRVKIGDADA CLVLANKYST NPDAEDAANI MRVISIKNYS
SDIRVIVQLM QYHNKAYLLN IPSWDWKRGD DVICLAELKL GFIAQSCLAP GFSTMMANLF
AMRSFKTSQT TPDWLNLYLC GAGMEMYTDT LSHSFVGMTF PEAVDLLFNR LGLLLLAIEL
KDEENKECNI AINPGPHIVI QPQTQGFFIA QSADEVKRAF FWCKQCHDDI KDVSLIKKCK
CKNLALFRRN TKHSTAARAR ATDVLQQFQP QAPAGPMGHL GQQVQLRMIN QQSSTSDTHL
NTKSLRFAYE IKKLMPSSGG RRNSMSIPPD GRGVDFSKDF EQQFQDMKYD STGMFHWCPS
RNLEDCVLER HQAAMTVLNG HVVVCLFADQ DSPLIGLRNF IMPLRSSNFH YHELKHVVIV
GDLEYLRKEW KTLYNLPKIS ILNGSPLSRA DLRAVNINLC DMCVIISARV PNTEDTTLAD
KEAILASLNI KAMQFDDTLG FFPMRHQTGD RSPLGSPISM QKKGAKFGTN VPMITELVND
SNVQFLDQDD DDDPDTELYL TQPFACGTAF AISVLDSLMS TTYFNDSALT LIRTLVTGGA
TPELELILAE GAGLRGGYST PETLSNRDRC RIAQISLQDN PYDGVVHNTT YGAMFTIALR
RYGQLCIGLY RLHDQDNPDS MKRYVITNPP AELRIKNTDY VYVLEQFDPG LEYEPGKRHF
