ID UNC58_CAEEL Reviewed; 591 AA.
AC Q22271; Q8MPX9;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 24-JAN-2024, entry version 147.
DE RecName: Full=Uncoordinated protein 58;
GN Name=unc-58 {ECO:0000312|EMBL:CAA90066.2}; ORFNames=T06H11.1;
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:CAA90066.2}
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 [2] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=8582640; DOI=10.1093/genetics/141.3.961;
RA Reiner D.J., Weinshenker D., Thomas J.H.;
RT "Analysis of dominant mutations affecting muscle excitation in
RT Caenorhabditis elegans.";
RL Genetics 141:961-976(1995).
RN [3] {ECO:0000305}
RP FUNCTION.
RX PubMed=11830642; DOI=10.1073/pnas.032671599;
RA Degtyareva N.P., Greenwell P., Hofmann E.R., Hengartner M.O., Zhang L.,
RA Culotti J.G., Petes T.D.;
RT "Caenorhabditis elegans DNA mismatch repair gene msh-2 is required for
RT microsatellite stability and maintenance of genome integrity.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:2158-2163(2002).
RN [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-226, 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).
CC -!- FUNCTION: Has a role in mobility, possibly in the transport of
CC potassium in muscles. {ECO:0000269|PubMed:11830642,
CC ECO:0000269|PubMed:8582640}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000269|PubMed:9851916};
CC IsoId=Q22271-1; Sequence=Displayed;
CC Name=b {ECO:0000269|PubMed:9851916};
CC IsoId=Q22271-2; Sequence=VSP_052547;
CC -!- DISRUPTION PHENOTYPE: Worms exhibit defects in mobility. Mutation
CC causes a dumpy (dpy) phenotype thought to be due to hyper-activation of
CC body-wall muscle. Severe mutations cause paralysis thought to be a
CC result of fully contracted muscles. {ECO:0000269|PubMed:8582640}.
CC -!- SIMILARITY: Belongs to the two pore domain potassium channel (TC
CC 1.A.1.8) family. {ECO:0000255}.
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DR EMBL; Z49889; CAA90066.2; -; Genomic_DNA.
DR EMBL; Z49889; CAD44149.1; -; Genomic_DNA.
DR PIR; T24626; T24626.
DR RefSeq; NP_741880.1; NM_171758.3. [Q22271-2]
DR RefSeq; NP_741881.1; NM_171759.3. [Q22271-1]
DR AlphaFoldDB; Q22271; -.
DR STRING; 6239.T06H11.1a.1; -.
DR GlyCosmos; Q22271; 1 site, No reported glycans.
DR iPTMnet; Q22271; -.
DR PaxDb; 6239-T06H11-1a; -.
DR EnsemblMetazoa; T06H11.1a.1; T06H11.1a.1; WBGene00006792. [Q22271-1]
DR EnsemblMetazoa; T06H11.1b.1; T06H11.1b.1; WBGene00006792. [Q22271-2]
DR GeneID; 181224; -.
DR UCSC; T06H11.1b; c. elegans. [Q22271-1]
DR AGR; WB:WBGene00006792; -.
DR WormBase; T06H11.1a; CE31594; WBGene00006792; unc-58. [Q22271-1]
DR WormBase; T06H11.1b; CE31595; WBGene00006792; unc-58. [Q22271-2]
DR eggNOG; KOG1418; Eukaryota.
DR HOGENOM; CLU_032755_1_0_1; -.
DR InParanoid; Q22271; -.
DR OMA; VSCICLY; -.
DR PhylomeDB; Q22271; -.
DR Reactome; R-CEL-1299503; TWIK related potassium channel (TREK).
DR Reactome; R-CEL-5576886; Phase 4 - resting membrane potential.
DR PRO; PR:Q22271; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00006792; Expressed in larva and 3 other cell types or tissues.
DR ExpressionAtlas; Q22271; baseline and differential.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015271; F:outward rectifier potassium channel activity; IDA:WormBase.
DR GO; GO:0022841; F:potassium ion leak channel activity; IBA:GO_Central.
DR GO; GO:0040011; P:locomotion; IMP:UniProtKB.
DR GO; GO:0006936; P:muscle contraction; IMP:UniProtKB.
DR GO; GO:0007567; P:parturition; IMP:UniProtKB.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006937; P:regulation of muscle contraction; IMP:WormBase.
DR GO; GO:0030322; P:stabilization of membrane potential; IBA:GO_Central.
DR Gene3D; 1.10.287.70; -; 1.
DR InterPro; IPR003280; 2pore_dom_K_chnl.
DR InterPro; IPR013099; K_chnl_dom.
DR PANTHER; PTHR11003; POTASSIUM CHANNEL, SUBFAMILY K; 1.
DR PANTHER; PTHR11003:SF310; UNCOORDINATED PROTEIN 58; 1.
DR Pfam; PF07885; Ion_trans_2; 1.
DR PRINTS; PR01333; 2POREKCHANEL.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Glycoprotein; Ion channel; Ion transport; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..591
FT /note="Uncoordinated protein 58"
FT /id="PRO_0000306199"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 289..309
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 318..338
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 400..420
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 428..448
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 453..473
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT VAR_SEQ 1..126
FT /note="MFFYSPNVAPQPSSTSHRRPTLTHQHHLHVGHLDTRLSVQIPEILSRSLVHD
FT PERTRLVPEQLRFIIDENQELWTGSQPPTGFLELCASPVSSVFSNADARRMSQRKLVLR
FT RPTISIQEDGKIIID -> MAPLTVKSSPPKKAKGISKFRRKKKQPPPDSTVFVAWALR
FT SVRESLIQVDPLAAALAHQARKTNSVPAVSRTPLLLQFTPFGPPLSAY (in
FT isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_052547"
SQ SEQUENCE 591 AA; 67391 MW; C7C26EB0EDBE24A7 CRC64;
MFFYSPNVAP QPSSTSHRRP TLTHQHHLHV GHLDTRLSVQ IPEILSRSLV HDPERTRLVP
EQLRFIIDEN QELWTGSQPP TGFLELCASP VSSVFSNADA RRMSQRKLVL RRPTISIQED
GKIIIDHVTA RWEGANINSQ SALLDADDGA TVITDTIKDD QDDKEPKSCP QQTVKYIKIL
TPHVILVSVL IGYLCLGAWI LMLLETRTEL LARSKKLVRL TNLMSNFTAE SWKMLNNAQH
GVSNMDEGEW AATFREWMVR VSETVDDRRP IRRELNRPDD LSNMHNKWTF PTAILYVLTV
LTTCGYGEVS VDTDVGKVFS VAFALVGIPL MFITAADIGK FLSETLLQFV SFWNRSVRKV
KQWMSRIRHG RRKSLQSTGG PNDTLDILGV DGTEEKLWFP IGAYVSCICI YCSIGSAMFI
TWERTWSFIH AFHFGFNLIV TVGLGDIVVT DYIFLSLIVA FVIVGLSVVT MCVDLASTHL
KAYFTRIHYF GRAKRFLGMS EELKEIVALL GAMRRKKGGK VTWNDVRDFL DNELRDRPFE
PHELLMKLRF IDETSSGMST IRHNSFQSDF FRESEYIRRV AALRPEQPAY L
//
