UN103_CAEEL
ID UN103_CAEEL Reviewed; 829 AA.
AC G5EFJ9; G5ECG3; G5EDE3; G5EE47; G5EFT6; G5EG15; G5EG91; G5EGQ1; M1Z8A0;
AC M1ZJW5;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Potassium voltage-gated channel unc-103 {ECO:0000305};
DE AltName: Full=Ether-a-go-go-related gene potassium channel homolog {ECO:0000250|UniProtKB:Q12809};
DE Short=ERG homolog {ECO:0000250|UniProtKB:Q12809};
DE Short=Eag-related protein homolog {ECO:0000250|UniProtKB:Q12809};
DE Short=Ether-a-go-go-related protein homolog {ECO:0000250|UniProtKB:Q12809};
DE AltName: Full=Uncoordinated protein 103 {ECO:0000303|PubMed:10647014};
GN Name=unc-103 {ECO:0000303|PubMed:10647014, ECO:0000312|WormBase:C30D11.1a};
GN ORFNames=C30D11.1 {ECO:0000312|WormBase:C30D11.1a};
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] (ISOFORM F).
RX PubMed=10647014; DOI=10.1038/46072;
RA Reiner D.J., Newton E.M., Tian H., Thomas J.H.;
RT "Diverse behavioural defects caused by mutations in Caenorhabditis elegans
RT unc-43 CaM kinase II.";
RL Nature 402:199-203(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 FUNCTION, AND MUTAGENESIS OF HIS-203; TRP-282; GLY-344 AND PRO-464.
RX PubMed=12684455; DOI=10.1523/jneurosci.23-07-02696.2003;
RA Garcia L.R., Sternberg P.W.;
RT "Caenorhabditis elegans UNC-103 ERG-like potassium channel regulates
RT contractile behaviors of sex muscles in males before and during mating.";
RL J. Neurosci. 23:2696-2705(2003).
RN [4]
RP MUTAGENESIS OF ALA-369.
RX PubMed=15280551; DOI=10.1073/pnas.0306005101;
RA Petersen C.I., McFarland T.R., Stepanovic S.Z., Yang P., Reiner D.J.,
RA Hayashi K., George A.L. Jr., Roden D.M., Thomas J.H., Balser J.R.;
RT "In vivo identification of genes that modify ether-a-go-go-related gene
RT activity in Caenorhabditis elegans may also affect human cardiac
RT arrhythmia.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:11773-11778(2004).
RN [5]
RP SUBUNIT, INTERACTION WITH DNJ-1, AND MUTAGENESIS OF ALA-369.
RX PubMed=27916661; DOI=10.1016/j.molcel.2016.10.027;
RA Li K., Jiang Q., Bai X., Yang Y.F., Ruan M.Y., Cai S.Q.;
RT "Tetrameric assembly of K(+) channels requires ER-located chaperone
RT proteins.";
RL Mol. Cell 65:52-65(2017).
CC -!- FUNCTION: Pore-forming (alpha) subunit of voltage-gated inwardly
CC rectifying potassium channel. Channel properties are modulated by cAMP
CC and subunit assembly (By similarity). Regulates the movements of the
CC male's copulatory spicules before and during male mating behavior
CC (PubMed:12684455). {ECO:0000250|UniProtKB:Q12809,
CC ECO:0000269|PubMed:12684455}.
CC -!- SUBUNIT: The potassium channel is composed of a homo- or
CC heterotetrameric complex (PubMed:27916661). Interacts with dnj-1; dnj-1
CC chaperone promotes tetramerization (PubMed:27916661).
CC {ECO:0000269|PubMed:27916661}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q12809};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=10;
CC Name=a;
CC IsoId=G5EFJ9-1; Sequence=Displayed;
CC Name=c;
CC IsoId=G5EFJ9-2; Sequence=VSP_058897;
CC Name=b;
CC IsoId=G5EFJ9-3; Sequence=VSP_058896;
CC Name=h;
CC IsoId=G5EFJ9-4; Sequence=VSP_058900, VSP_058903, VSP_058904,
CC VSP_058905;
CC Name=e;
CC IsoId=G5EFJ9-5; Sequence=VSP_058899;
CC Name=d;
CC IsoId=G5EFJ9-6; Sequence=VSP_058898;
CC Name=g;
CC IsoId=G5EFJ9-7; Sequence=VSP_058900, VSP_058903;
CC Name=f;
CC IsoId=G5EFJ9-8; Sequence=VSP_058900;
CC Name=i;
CC IsoId=G5EFJ9-9; Sequence=VSP_058901;
CC Name=j;
CC IsoId=G5EFJ9-10; Sequence=VSP_058902;
CC -!- SIMILARITY: Belongs to the potassium channel family. H (Eag) (TC
CC 1.A.1.20) subfamily. Kv11.1/KCNH2 sub-subfamily. {ECO:0000305}.
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DR EMBL; AF257518; AAF68999.1; -; mRNA.
DR EMBL; BX284603; CAA84644.2; -; Genomic_DNA.
DR EMBL; BX284603; CAO78712.1; -; Genomic_DNA.
DR EMBL; BX284603; CAO78713.1; -; Genomic_DNA.
DR EMBL; BX284603; CAO78714.1; -; Genomic_DNA.
DR EMBL; BX284603; CAO78715.1; -; Genomic_DNA.
DR EMBL; BX284603; CAO78716.1; -; Genomic_DNA.
DR EMBL; BX284603; CAO78717.1; -; Genomic_DNA.
DR EMBL; BX284603; CAO78718.1; -; Genomic_DNA.
DR EMBL; BX284603; CCU83367.1; -; Genomic_DNA.
DR EMBL; BX284603; CCU83368.1; -; Genomic_DNA.
DR PIR; T19579; T19579.
DR RefSeq; NP_001122682.1; NM_001129210.2.
DR RefSeq; NP_001122683.1; NM_001129211.1.
DR RefSeq; NP_001122684.1; NM_001129212.1.
DR RefSeq; NP_001122685.1; NM_001129213.1.
DR RefSeq; NP_001122686.1; NM_001129214.1.
DR RefSeq; NP_001122687.1; NM_001129215.1. [G5EFJ9-7]
DR RefSeq; NP_001122688.1; NM_001129216.1.
DR RefSeq; NP_001293649.1; NM_001306720.1. [G5EFJ9-9]
DR RefSeq; NP_001293650.1; NM_001306721.1.
DR RefSeq; NP_497824.1; NM_065423.5.
DR AlphaFoldDB; G5EFJ9; -.
DR SMR; G5EFJ9; -.
DR STRING; 6239.C30D11.1j; -.
DR EnsemblMetazoa; C30D11.1a.1; C30D11.1a.1; WBGene00006830. [G5EFJ9-1]
DR EnsemblMetazoa; C30D11.1b.1; C30D11.1b.1; WBGene00006830. [G5EFJ9-3]
DR EnsemblMetazoa; C30D11.1c.1; C30D11.1c.1; WBGene00006830. [G5EFJ9-2]
DR EnsemblMetazoa; C30D11.1d.1; C30D11.1d.1; WBGene00006830. [G5EFJ9-6]
DR EnsemblMetazoa; C30D11.1e.1; C30D11.1e.1; WBGene00006830. [G5EFJ9-5]
DR EnsemblMetazoa; C30D11.1f.1; C30D11.1f.1; WBGene00006830. [G5EFJ9-8]
DR EnsemblMetazoa; C30D11.1g.1; C30D11.1g.1; WBGene00006830. [G5EFJ9-7]
DR EnsemblMetazoa; C30D11.1h.1; C30D11.1h.1; WBGene00006830.
DR EnsemblMetazoa; C30D11.1i.1; C30D11.1i.1; WBGene00006830. [G5EFJ9-9]
DR EnsemblMetazoa; C30D11.1j.1; C30D11.1j.1; WBGene00006830. [G5EFJ9-10]
DR GeneID; 175527; -.
DR KEGG; cel:CELE_C30D11.1; -.
DR CTD; 175527; -.
DR WormBase; C30D11.1a; CE41297; WBGene00006830; unc-103. [G5EFJ9-1]
DR WormBase; C30D11.1b; CE41298; WBGene00006830; unc-103. [G5EFJ9-3]
DR WormBase; C30D11.1c; CE41299; WBGene00006830; unc-103. [G5EFJ9-2]
DR WormBase; C30D11.1d; CE41300; WBGene00006830; unc-103. [G5EFJ9-6]
DR WormBase; C30D11.1e; CE41301; WBGene00006830; unc-103. [G5EFJ9-5]
DR WormBase; C30D11.1f; CE27805; WBGene00006830; unc-103. [G5EFJ9-8]
DR WormBase; C30D11.1g; CE41302; WBGene00006830; unc-103. [G5EFJ9-7]
DR WormBase; C30D11.1h; CE41303; WBGene00006830; unc-103.
DR WormBase; C30D11.1i; CE48274; WBGene00006830; unc-103. [G5EFJ9-9]
DR WormBase; C30D11.1j; CE48244; WBGene00006830; unc-103. [G5EFJ9-10]
DR eggNOG; KOG0498; Eukaryota.
DR GeneTree; ENSGT00940000171203; -.
DR OMA; IERMQNK; -.
DR OrthoDB; 247304at2759; -.
DR PRO; PR:G5EFJ9; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00006830; Expressed in larva and 3 other tissues.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005242; F:inward rectifier potassium channel activity; IBA:GO_Central.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IBA:GO_Central.
DR GO; GO:0007617; P:mating behavior; IMP:WormBase.
DR GO; GO:0086011; P:membrane repolarization during action potential; IBA:GO_Central.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
DR GO; GO:0006937; P:regulation of muscle contraction; IMP:WormBase.
DR GO; GO:0046662; P:regulation of oviposition; NAS:WormBase.
DR CDD; cd00038; CAP_ED; 1.
DR Gene3D; 2.60.120.10; -; 1.
DR InterPro; IPR018490; cNMP-bd-like.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR003938; K_chnl_volt-dep_EAG/ELK/ERG.
DR InterPro; IPR003967; K_chnl_volt-dep_ERG.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR PRINTS; PR01463; EAGCHANLFMLY.
DR PRINTS; PR01470; ERGCHANNEL.
DR SMART; SM00100; cNMP; 1.
DR SUPFAM; SSF51206; SSF51206; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Glycoprotein; Ion channel;
KW Ion transport; Membrane; Potassium; Potassium channel; Potassium transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport;
KW Voltage-gated channel.
FT CHAIN 1..829
FT /note="Potassium voltage-gated channel unc-103"
FT /id="PRO_0000439645"
FT TOPO_DOM 1..123
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 124..144
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 145..158
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 159..179
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 180..203
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 204..224
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 225..234
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 235..255
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 256..261
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 262..282
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 283..327
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 328..348
FT /note="Pore-forming; Name=Segment H5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 349..354
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 355..375
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 376..829
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..654
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 458..559
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00060"
FT CARBOHYD 313
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 1..87
FT /note="MKTAVFGRDSGEPGSPCGAPPSLTFTPPATLVPPTHHHSRSTNRGGVSGTGG
FT GGSGGLQGAPGAGGPRASHSSRRTSRLHNNVSALG -> MDRTRPSVRNYSLDLTRHRK
FT LTADAKAVSPSSCSVKFMPEVLDNHGTTTSARKHSSLSQPALRCHSKQHHNILSPHALA
FT (in isoform b)"
FT /id="VSP_058896"
FT VAR_SEQ 1..87
FT /note="MKTAVFGRDSGEPGSPCGAPPSLTFTPPATLVPPTHHHSRSTNRGGVSGTGG
FT GGSGGLQGAPGAGGPRASHSSRRTSRLHNNVSALG -> MDSSVPMIDLSSGDDEEVEV
FT AMRRSYLLPPVPERPDGFPSLLFGNGNLSRSTLSINQEISMAPSPFSEITVSSQRPLVA
FT RSGSNSSEHNLQIKEAVKKKPVADIAHVSGTFVCVCVRGAQK (in isoform c)"
FT /id="VSP_058897"
FT VAR_SEQ 1..87
FT /note="MKTAVFGRDSGEPGSPCGAPPSLTFTPPATLVPPTHHHSRSTNRGGVSGTGG
FT GGSGGLQGAPGAGGPRASHSSRRTSRLHNNVSALG -> MPRRPPLLRLAPVPEDEEDD
FT EVFFEPADKNDDKQRFLPKQSRGSSRFVSEDVLNNSDDEEENK (in isoform d)"
FT /id="VSP_058898"
FT VAR_SEQ 1..87
FT /note="MKTAVFGRDSGEPGSPCGAPPSLTFTPPATLVPPTHHHSRSTNRGGVSGTGG
FT GGSGGLQGAPGAGGPRASHSSRRTSRLHNNVSALG -> MVGGGGGGGAGGSSTRRNAA
FT IASTSSTTSSAAGRRASAFVRRMSMAIPTLSADPVPFSA (in isoform e)"
FT /id="VSP_058899"
FT VAR_SEQ 1..87
FT /note="MKTAVFGRDSGEPGSPCGAPPSLTFTPPATLVPPTHHHSRSTNRGGVSGTGG
FT GGSGGLQGAPGAGGPRASHSSRRTSRLHNNVSALG -> MSSSTNHTGIIQHHPSQSQQ
FT QATTSSGAGNAVASQAKQLMVVLQSGSYK (in isoform h, isoform g and
FT isoform f)"
FT /id="VSP_058900"
FT VAR_SEQ 1..87
FT /note="MKTAVFGRDSGEPGSPCGAPPSLTFTPPATLVPPTHHHSRSTNRGGVSGTGG
FT GGSGGLQGAPGAGGPRASHSSRRTSRLHNNVSALG -> MRA (in isoform i)"
FT /id="VSP_058901"
FT VAR_SEQ 1..87
FT /note="MKTAVFGRDSGEPGSPCGAPPSLTFTPPATLVPPTHHHSRSTNRGGVSGTGG
FT GGSGGLQGAPGAGGPRASHSSRRTSRLHNNVSALG -> MPRRPPLLRLAPVPEDEEDD
FT EVFFEPADKNDDKQRFLPKQSRGSSRFVSEDVLNNSDDEEENKRCHLVSSSHASLRSLS
FT PCPSLQSSSSIGGCGGGGMVGGGGGGGAGGSSTRRNAAIASTSSTTSSAAGRRASAFVR
FT RMSMAIPTLSADPVPFSA (in isoform j)"
FT /id="VSP_058902"
FT VAR_SEQ 645..722
FT /note="SSSRCSPPHAALTATRSEATPLLRRSTNHHEEDDALFDDIRAFARGNTVTMS
FT PTVAGNSVSPTTAIHNDGIHSQQLSD -> N (in isoform h and isoform
FT g)"
FT /id="VSP_058903"
FT VAR_SEQ 779..781
FT /note="EPN -> RRR (in isoform h)"
FT /id="VSP_058904"
FT VAR_SEQ 782..829
FT /note="Missing (in isoform h)"
FT /id="VSP_058905"
FT MUTAGEN 203
FT /note="H->N: In sy557; causes spontaneous contractions of
FT the spicule muscles, inducing spicule protraction in the
FT absence of mating cues; when associated with R-282."
FT /evidence="ECO:0000269|PubMed:12684455"
FT MUTAGEN 282
FT /note="W->R: In sy557; causes spontaneous contractions of
FT the spicule muscles, inducing spicule protraction in the
FT absence of mating cues; when associated with N-203."
FT /evidence="ECO:0000269|PubMed:12684455"
FT MUTAGEN 344
FT /note="G->E: In sy670; causes spontaneous contractions of
FT the spicule muscles, inducing spicule protraction in the
FT absence of mating cues."
FT /evidence="ECO:0000269|PubMed:12684455"
FT MUTAGEN 369
FT /note="A->T: In n500 and e1597; gain-of-function mutation
FT which causes locomotive and egg-laying defects as well as
FT pharyngeal-pumping defect."
FT /evidence="ECO:0000269|PubMed:15280551,
FT ECO:0000269|PubMed:27916661"
FT MUTAGEN 464
FT /note="P->S: In sy674; causes mild contractions of the
FT spicule muscles, inducing spicule protraction in the
FT absence of mating cues."
FT /evidence="ECO:0000269|PubMed:12684455"
SQ SEQUENCE 829 AA; 91928 MW; C35EBA4C27C94597 CRC64;
MKTAVFGRDS GEPGSPCGAP PSLTFTPPAT LVPPTHHHSR STNRGGVSGT GGGGSGGLQG
APGAGGPRAS HSSRRTSRLH NNVSALGVLS LGADVLPEYK LQPTRIHHCT IVHYSPFKAV
WDWIILLLVI YTAVFTPYVA AFLLRELQDT AKKSRFTEPL EIVDLIVDIM FIVDIIINFR
TTYVNENDEA CQVVSDPGKI ATHYFKGWFI IDMVAAVPFD LLLVSTNSDE TTTLIGLLKT
ARLLRLVRVA RKLDRYSEYG AAVLLLLMAT FALIAHWLAC IWYAIGSAEL SHKEYTWLHQ
LSKQLAQPYT STNGTIPTGG PTLKSRYVTS LYFTLSTITS IGFGNVSATT DSEKIFTIIM
MILGSLMYAS VFGNVSAIIQ RLYSGTARYH TEMSRLREFI RFHQIPNPLR QRLEEYFQHA
WSYTNGIDMN LVLKGFPDCL QADICLHLNR NLLSGCAAFA GSTPGCLRAL SMRFRTTHSP
PGDTLVHRGD ILTGLYFIAR GSVEILNDDN TVMGILGKDD IFGENPLLYD EVGKSSCNVR
ALTYCDLHKI LRDDLLDVLD MYPEFAETFC KNLTITYNLR DDAQSLRKKF DRHKLLRMSS
SMNKDRYTTP PDGDHGNAAV RRSAESVSRC DSNPIDRRQS AGSRSSSRCS PPHAALTATR
SEATPLLRRS TNHHEEDDAL FDDIRAFARG NTVTMSPTVA GNSVSPTTAI HNDGIHSQQL
SDRSDDYEER RANMFGRRLE SIESQMERMQ NKFNSDMETL IKLVKEQSII RNNGSSNEEP
NARYRPNNYI SSAIRLPNGG GGGVVDEMRV SRLSSHEPPT PTQETDTIL
