KCNAG_CAEEL
ID KCNAG_CAEEL Reviewed; 558 AA.
AC G5EFC3; O17535;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Potassium voltage-gated channel protein egl-36 {ECO:0000303|PubMed:9247272};
DE AltName: Full=Egg-laying defective protein 36 {ECO:0000303|PubMed:9247272, ECO:0000312|EMBL:CAA91765.1};
GN Name=egl-36 {ECO:0000312|EMBL:CAA91765.1, ECO:0000312|WormBase:R07A4.1};
GN ORFNames=R07A4.1;
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:0000312|EMBL:CAA91765.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:CAA91765.1};
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, ECO:0000312|EMBL:AAB95119.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-558, FUNCTION, TISSUE SPECIFICITY,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLU-142; GLY-408; SER-424 AND
RP PRO-439.
RX PubMed=9247271; DOI=10.1016/s0896-6273(00)80355-4;
RA Johnstone D.B., Wei A., Butler A., Salkoff L., Thomas J.H.;
RT "Behavioral defects in C. elegans egl-36 mutants result from potassium
RT channels shifted in voltage-dependence of activation.";
RL Neuron 19:151-164(1997).
RN [3] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP GLU-142; ALA-435 AND PRO-439.
RX PubMed=9247272; DOI=10.1016/s0896-6273(00)80356-6;
RA Elkes D.A., Cardozo D.L., Madison J., Kaplan J.M.;
RT "EGL-36 Shaw channels regulate C. elegans egg-laying muscle activity.";
RL Neuron 19:165-174(1997).
CC -!- FUNCTION: Voltage-dependent potassium channel involved in the
CC excitation of muscles operating egg-laying and defecation.
CC {ECO:0000269|PubMed:9247271, ECO:0000269|PubMed:9247272}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P08510}; Multi-
CC pass membrane protein {ECO:0000250|UniProtKB:P08510}.
CC -!- TISSUE SPECIFICITY: Expressed in muscles for egg-laying, anal depressor
CC and sphincter, and the four most anterior head muscles. Found in
CC neurons including enteric motor neurons AVL and DVB and the sensory
CC neuron PHB, the spermatheca, and the distal tip cells of the somatic
CC gonad. {ECO:0000269|PubMed:9247271, ECO:0000269|PubMed:9247272}.
CC -!- DISRUPTION PHENOTYPE: Egg-laying defects; retain many more eggs in
CC utero, laid eggs appear later in development. Moderately defective in
CC generating the expulsion step of defecation. Hyperpolarizing shifts in
CC the voltage dependence of channel activation.
CC {ECO:0000269|PubMed:9247271, ECO:0000269|PubMed:9247272}.
CC -!- SIMILARITY: Belongs to the potassium channel family. C (Shaw) (TC
CC 1.A.1.2) subfamily. Shaw sub-subfamily. {ECO:0000255}.
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DR EMBL; Z67756; CAA91765.1; -; Genomic_DNA.
DR EMBL; Z68010; CAA91765.1; JOINED; Genomic_DNA.
DR EMBL; AF005246; AAB95119.1; -; mRNA.
DR PIR; T23991; T23991.
DR RefSeq; NP_509795.1; NM_077394.3.
DR AlphaFoldDB; G5EFC3; -.
DR SMR; G5EFC3; -.
DR STRING; 6239.R07A4.1; -.
DR PaxDb; G5EFC3; -.
DR EnsemblMetazoa; R07A4.1.1; R07A4.1.1; WBGene00001202.
DR GeneID; 181269; -.
DR KEGG; cel:CELE_R07A4.1; -.
DR UCSC; R07A4.1; c. elegans.
DR CTD; 181269; -.
DR WormBase; R07A4.1; CE18123; WBGene00001202; egl-36.
DR eggNOG; KOG3713; Eukaryota.
DR HOGENOM; CLU_011722_4_3_1; -.
DR InParanoid; G5EFC3; -.
DR OMA; ELNTACN; -.
DR OrthoDB; 818306at2759; -.
DR PhylomeDB; G5EFC3; -.
DR Reactome; R-CEL-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
DR PRO; PR:G5EFC3; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00001202; Expressed in larva and 3 other tissues.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0032590; C:dendrite membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0032809; C:neuronal cell body 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:0005244; F:voltage-gated ion channel activity; IDA:WormBase.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IBA:GO_Central.
DR GO; GO:0034220; P:ion transmembrane transport; IDA:WormBase.
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; IPR003974; K_chnl_volt-dep_Kv3.
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; PR01498; SHAWCHANNEL.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
PE 1: Evidence at protein level;
KW Ion channel; Ion transport; Membrane; Potassium; Potassium channel;
KW Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..558
FT /note="Potassium voltage-gated channel protein egl-36"
FT /id="PRO_0000420622"
FT TRANSMEM 203..223
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..312
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TRANSMEM 358..378
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TRANSMEM 390..410
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TRANSMEM 422..442
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT REGION 516..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..546
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 142
FT /note="E->K: Channels open at more negative voltages than
FT wild-type and single mutants; when associated with S-439."
FT /evidence="ECO:0000269|PubMed:9247271,
FT ECO:0000269|PubMed:9247272"
FT MUTAGEN 142
FT /note="E->K: In n728; Channels open at more negative
FT voltages than wild-type."
FT /evidence="ECO:0000269|PubMed:9247271,
FT ECO:0000269|PubMed:9247272"
FT MUTAGEN 408
FT /note="G->E: In sa630; Premature egg laying with fewer eggs
FT retained."
FT /evidence="ECO:0000269|PubMed:9247271"
FT MUTAGEN 424
FT /note="S->L: In sa631: Reduced egg laying."
FT /evidence="ECO:0000269|PubMed:9247271"
FT MUTAGEN 435
FT /note="A->T: Restores egg-laying activity to n728 mutants."
FT /evidence="ECO:0000269|PubMed:9247272"
FT MUTAGEN 439
FT /note="P->S: Channels open at more negative voltages than
FT wild-type; when associated with K-142."
FT /evidence="ECO:0000269|PubMed:9247271,
FT ECO:0000269|PubMed:9247272"
FT MUTAGEN 439
FT /note="P->S: In n2332; Channels open at more negative
FT voltages than wild-type and increase in the rate of
FT activation."
FT /evidence="ECO:0000269|PubMed:9247271,
FT ECO:0000269|PubMed:9247272"
FT CONFLICT 520
FT /note="H -> D (in Ref. 2; AAB95119)"
FT /evidence="ECO:0000305|PubMed:9247271"
SQ SEQUENCE 558 AA; 63640 MW; B8610A559EEE28F3 CRC64;
MLDACSFNRF DSNRSSARRF SRRGSDYFGD KGISMDERIV LNVGGVRHET YQATLKKIPA
TRLSRLTPSL ANFDPLLNEY FFDRHPAVFA MILNYYRTGK LHYPTDVCGP LFEEELQYWG
LDASDTEPCC WMQLLHAKDT QETLAVLDRM DADHEDDPQL REQDTMKKFG WEEDYFQGKR
TRWMKLKPQM WSLFDEPYSS QAAKLIAGIS VLFIFISIFS FCLKTHQSFR LPVLIGQNIT
MPGGVVQPSI ERVSTEPLPI FGQIEMLCNI WFTLELIIRF VFCPSKIRFF KSPLNMIDLV
ATLSFYADAM MVRVVEDEPK DVVEFLSMIR IFRLFKLTQH HQGLQILIHT FRASAKELIL
LVFFLILGIV IFAALVYYAE KMEANPNNQF QSIPLGLWWA ICTMTTVGYG DMTPHTSFGR
LVGSLCAVMG VLTIALPVPV IVSNFAMFYS HNQARDKLPK RRRRVLPVEQ IRLQARRHAA
VLEPSASQGG LGGGQAIRRR NMPILIDQNC CDEENHNHKH REKSENSDEG TNSSSTTGVD
TVVKLGPSET AITTTIIS
