SUP10_CAEEL
ID SUP10_CAEEL Reviewed; 332 AA.
AC Q17374; Q21879;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 2.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Putative potassium channel regulatory protein sup-10;
DE AltName: Full=Suppressor of unc-93 protein 10;
DE Flags: Precursor;
GN Name=sup-10 {ECO:0000312|EMBL:AAB61087.1}; ORFNames=R09G11.1;
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:0000305, ECO:0000312|EMBL:AAB61087.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND MUTAGENESIS OF GLU-88; GLY-323 AND 322-TRP--ASP-332.
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:AAB61087.1};
RX PubMed=14534247; DOI=10.1523/jneurosci.23-27-09133.2003;
RA de la Cruz I.P., Levin J.Z., Cummins C., Anderson P., Horvitz H.R.;
RT "sup-9, sup-10, and unc-93 may encode components of a two-pore K+ channel
RT that coordinates muscle contraction in Caenorhabditis elegans.";
RL J. Neurosci. 23:9133-9145(2003).
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 GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-61, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA Taoka M., Takahashi N., Isobe T.;
RT "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT elegans and suggests an atypical translocation mechanism for integral
RT membrane proteins.";
RL Mol. Cell. Proteomics 6:2100-2109(2007).
RN [4]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=24586202; DOI=10.1371/journal.pgen.1004175;
RA de la Cruz I.P., Ma L., Horvitz H.R.;
RT "The Caenorhabditis elegans iodotyrosine deiodinase ortholog SUP-18
RT functions through a conserved channel SC-box to regulate the muscle two-
RT pore domain potassium channel SUP-9.";
RL PLoS Genet. 10:E1004175-E1004175(2014).
CC -!- FUNCTION: May contribute to coordination of muscle contraction as
CC regulatory subunit of a nonessential potassium channel complex.
CC {ECO:0000303|PubMed:14534247}.
CC -!- SUBUNIT: May form a complex with sup-9 and unc-93 where sup-10 and unc-
CC 93 act as regulatory subunits of the two pore potassium channel sup-9.
CC Sup-10 may regulate sup-9 via sup-18. {ECO:0000303|PubMed:14534247,
CC ECO:0000305|PubMed:24586202}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000303|PubMed:14534247}; Single-
CC pass type I membrane protein {ECO:0000303|PubMed:14534247}. Note=In
CC body-wall muscle cells, localizes to dense body-like structure which
CC connect the myofibril lattice to the cell membrane. Colocalizes with
CC sup-18. {ECO:0000269|PubMed:14534247, ECO:0000269|PubMed:24586202}.
CC -!- TISSUE SPECIFICITY: Low levels in body-wall muscles, eight vulval
CC muscles, intestinal muscles and anal depressor muscle.
CC {ECO:0000269|PubMed:14534247}.
CC -!- MISCELLANEOUS: Gain of function uncoordinated rubber band response is
CC phenocopied by exposure to the unc-49 agonist muscimol.
CC {ECO:0000269|PubMed:14534247}.
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DR EMBL; U43891; AAB61087.1; -; mRNA.
DR EMBL; FO081263; CCD70295.1; -; Genomic_DNA.
DR PIR; T28882; T28882.
DR RefSeq; NP_510835.1; NM_078434.4.
DR AlphaFoldDB; Q17374; -.
DR STRING; 6239.R09G11.1; -.
DR TCDB; 8.A.119.1.1; the potassium channel regulatory protein sup-10 (sup-10) family.
DR iPTMnet; Q17374; -.
DR EPD; Q17374; -.
DR PaxDb; Q17374; -.
DR PeptideAtlas; Q17374; -.
DR EnsemblMetazoa; R09G11.1.1; R09G11.1.1; WBGene00006319.
DR GeneID; 181784; -.
DR KEGG; cel:CELE_R09G11.1; -.
DR UCSC; R09G11.1; c. elegans.
DR CTD; 181784; -.
DR WormBase; R09G11.1; CE12656; WBGene00006319; sup-10.
DR eggNOG; ENOG502S7BA; Eukaryota.
DR HOGENOM; CLU_912872_0_0_1; -.
DR InParanoid; Q17374; -.
DR OMA; ETITYYY; -.
DR OrthoDB; 924681at2759; -.
DR BRENDA; 1.21.1.1; 1045.
DR PRO; PR:Q17374; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00006319; Expressed in larva and 2 other tissues.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:WormBase.
DR GO; GO:0055120; C:striated muscle dense body; IDA:WormBase.
DR GO; GO:0015459; F:potassium channel regulator activity; IGI:UniProtKB.
DR GO; GO:0006813; P:potassium ion transport; IEA:UniProtKB-KW.
DR GO; GO:0006937; P:regulation of muscle contraction; IMP:UniProtKB.
DR GO; GO:0043266; P:regulation of potassium ion transport; IGI:UniProtKB.
PE 1: Evidence at protein level;
KW Glycoprotein; Ion transport; Membrane; Potassium; Potassium transport;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..332
FT /note="Putative potassium channel regulatory protein sup-
FT 10"
FT /evidence="ECO:0000255"
FT /id="PRO_0000022440"
FT TOPO_DOM 19..301
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 302..322
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 323..332
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 88
FT /note="E->K: In n619; loss of function."
FT /evidence="ECO:0000269|PubMed:14534247"
FT MUTAGEN 322..332
FT /note="Missing: In n983; gain of function, uncoordinated
FT rubber band response."
FT /evidence="ECO:0000269|PubMed:14534247"
FT MUTAGEN 323
FT /note="G->R: In n240; loss of function."
FT /evidence="ECO:0000269|PubMed:14534247"
SQ SEQUENCE 332 AA; 38064 MW; 03BE5EB28A15D897 CRC64;
MRYAVFIFLI VLIDLIYCWN SKRSFFIPDF LGSGDGTPKS KTESVIEERM EYGRMILLVC
NKTCAKHRSD IPLWLKEFNQ KKGYQEPETI TYYYHTYRQA VSFIDTNETD VFPNLIYFIG
VKRVVFNGDV NIREDVNDWI ASLDQLILLE PRVYEDLNVI LSDTSNCSSK YLLLADRPKC
PQPSWSIVAR IAQDHGIQPV KIGHPLDGLT HVLLYKRMPY LSEASCHLSV LLYENSYSDF
GDDINPLVVS DWITTLLPLE EGSCPALFET YWHPIVDELT ELQQIFYSAE LEISERNKRP
AFVLVGLTGG IAVIILAFSI FWGLNGSGFN KD
