UN105_CAEEL
ID UN105_CAEEL Reviewed; 887 AA.
AC Q09274; A3FPK3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 3.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Degenerin-like protein unc-105;
DE AltName: Full=Uncoordinated protein 105;
GN Name=unc-105; ORFNames=C41C4.5;
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 B), AND TISSUE SPECIFICITY.
RX PubMed=8662524; DOI=10.1126/science.273.5273.361;
RA Liu J., Schrank B., Waterston R.H.;
RT "Interaction between a putative mechanosensory membrane channel and a
RT collagen.";
RL Science 273:361-364(1996).
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 MUTAGENESIS OF PRO-134 AND GLU-677.
RC STRAIN=Bristol N2;
RX PubMed=3744028; DOI=10.1093/genetics/113.4.821;
RA Park E.-C., Horvitz R.H.;
RT "Mutations with dominant effects on the behavior and morphology of the
RT nematode Caenorhabditis elegans.";
RL Genetics 113:821-852(1986).
RN [4]
RP MUTAGENESIS OF PRO-134 AND GLU-677.
RX PubMed=3744029; DOI=10.1093/genetics/113.4.853;
RA Park E.-C., Horvitz H.R.;
RT "C. elegans unc-105 mutations affect muscle and are suppressed by other
RT mutations that affect muscle.";
RL Genetics 113:853-867(1986).
RN [5]
RP FUNCTION.
RX PubMed=9655510; DOI=10.1016/s0896-6273(00)80503-6;
RA Garcia-Anoveros J., Garcia J.A., Liu J.-D., Corey D.P.;
RT "The nematode degenerin UNC-105 forms ion channels that are activated by
RT degeneration- or hypercontraction-causing mutations.";
RL Neuron 20:1231-1241(1998).
RN [6]
RP FUNCTION.
RX PubMed=15020702; DOI=10.1113/jphysiol.2003.057687;
RA Jospin M., Mariol M.-C., Segalat L., Allard B.;
RT "Patch clamp study of the UNC-105 degenerin and its interaction with the
RT LET-2 collagen in Caenorhabditis elegans muscle.";
RL J. Physiol. (Lond.) 557:379-388(2004).
RN [7]
RP FUNCTION.
RX PubMed=15254157; DOI=10.1113/jphysiol.2004.069971;
RA Jospin M., Allard B.;
RT "An amiloride-sensitive H+-gated Na+ channel in Caenorhabditis elegans body
RT wall muscle cells.";
RL J. Physiol. (Lond.) 559:715-720(2004).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-599, 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: Ion channel which is permeable to small monovalent cations.
CC Shown not to be H+-ion gated. May be mechanosensitive and is required
CC for growth and muscle development. {ECO:0000269|PubMed:15020702,
CC ECO:0000269|PubMed:15254157, ECO:0000269|PubMed:9655510}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=b;
CC IsoId=Q09274-1; Sequence=Displayed;
CC Name=a;
CC IsoId=Q09274-2; Sequence=VSP_025926;
CC -!- TISSUE SPECIFICITY: Expressed in body wall muscle.
CC {ECO:0000269|PubMed:8662524}.
CC -!- SIMILARITY: Belongs to the amiloride-sensitive sodium channel (TC
CC 1.A.6) family. {ECO:0000305}.
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DR EMBL; Z48045; CAA88101.2; -; Genomic_DNA.
DR EMBL; Z48045; CAM33500.1; -; Genomic_DNA.
DR PIR; H88226; H88226.
DR PIR; T19878; T19878.
DR RefSeq; NP_001122595.1; NM_001129123.1. [Q09274-1]
DR RefSeq; NP_495702.1; NM_063301.5. [Q09274-2]
DR AlphaFoldDB; Q09274; -.
DR STRING; 6239.C41C4.5e.1; -.
DR TCDB; 1.A.6.2.3; the epithelial na(+) channel (enac) family.
DR iPTMnet; Q09274; -.
DR PaxDb; Q09274; -.
DR EnsemblMetazoa; C41C4.5a.1; C41C4.5a.1; WBGene00006832. [Q09274-2]
DR EnsemblMetazoa; C41C4.5b.1; C41C4.5b.1; WBGene00006832. [Q09274-1]
DR GeneID; 174306; -.
DR UCSC; C41C4.5a.1; c. elegans. [Q09274-1]
DR CTD; 174306; -.
DR WormBase; C41C4.5a; CE23585; WBGene00006832; unc-105. [Q09274-2]
DR WormBase; C41C4.5b; CE40690; WBGene00006832; unc-105. [Q09274-1]
DR eggNOG; KOG4294; Eukaryota.
DR InParanoid; Q09274; -.
DR PhylomeDB; Q09274; -.
DR PRO; PR:Q09274; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00006832; Expressed in larva and 3 other tissues.
DR ExpressionAtlas; Q09274; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IC:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005216; F:ion channel activity; IDA:UniProtKB.
DR GO; GO:0015280; F:ligand-gated sodium channel activity; IBA:GO_Central.
DR GO; GO:0006816; P:calcium ion transport; IDA:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0015693; P:magnesium ion transport; IDA:UniProtKB.
DR GO; GO:0007517; P:muscle organ development; IMP:UniProtKB.
DR GO; GO:0035725; P:sodium ion transmembrane transport; IBA:GO_Central.
DR InterPro; IPR004726; Deg-1.
DR InterPro; IPR001873; ENaC.
DR InterPro; IPR020903; ENaC_CS.
DR PANTHER; PTHR11690; PTHR11690; 1.
DR Pfam; PF00858; ASC; 1.
DR PRINTS; PR01078; AMINACHANNEL.
DR TIGRFAMs; TIGR00867; deg-1; 1.
DR PROSITE; PS01206; ASC; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; Differentiation; Glycoprotein;
KW Ion channel; Ion transport; Membrane; Myogenesis; Reference proteome;
KW Sodium; Sodium channel; Sodium transport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..887
FT /note="Degenerin-like protein unc-105"
FT /id="PRO_0000181314"
FT TOPO_DOM 1..93
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 115..698
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 699..719
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 720..887
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 794..815
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 859..887
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 871..887
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 244
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 450
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 473
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 581
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 599
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT VAR_SEQ 1..53
FT /note="MAEDRIKSKLRRPASIESTMSSRTKPRHKPSPMSILMPHLMVGESFRKYRPH
FT G -> MLHLAASRNSQINSS (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_025926"
FT MUTAGEN 134
FT /note="P->S: In n490; worms appear reduced in size with
FT defective body muscles."
FT /evidence="ECO:0000269|PubMed:3744028,
FT ECO:0000269|PubMed:3744029"
FT MUTAGEN 134
FT /note="P->T: In n1274; worms appear reduced in size with
FT defective body muscles."
FT /evidence="ECO:0000269|PubMed:3744028,
FT ECO:0000269|PubMed:3744029"
FT MUTAGEN 677
FT /note="E->K: In n506; worms appear hypercontracted and
FT paralyzed."
FT /evidence="ECO:0000269|PubMed:3744028,
FT ECO:0000269|PubMed:3744029"
SQ SEQUENCE 887 AA; 100333 MW; BE5833546B93AF41 CRC64;
MAEDRIKSKL RRPASIESTM SSRTKPRHKP SPMSILMPHL MVGESFRKYR PHGLRNIRMN
GHLDWNQLRK SFEKQSTFHG ISHAATADGK WRWFWYTAFT ICLLALLIQI FFLISKYRQY
GKTVDLDLKF ENAPFPSITI CNLNPYKKSA IQSNPNTKAM MEAYSRRIGS GDKTEGIAAA
LSATGGLHAK VRRAKRKAKG KPRLRDRRYH QAFAQCLCDI EQLTGDRKGS CFAAFKGKIE
IDTNNTAGFM NLHTSRCLCQ LDTVSKALWP CFPYSSWKEK LCSECVDNTG HCPMRFYKGN
ELYENIKEQV DLCLCHKEYN HCVSTRDDGI ILEISPNDEL NDLDIGKKIA SQLSAQQEKQ
AEVTTTEAPT VTQALGFEEL TDDIAITSQA QENLMFAVGE MSEKAKESMS YELDELVLKC
SFNQKDCQMD RDFTLHYDNT FGNCYTFNYN RTAEVASHRA GANYGLRVLL YANVSEYLPT
TEAVGFRITV HDKHIVPFPD AFGYSAPTGF MSSFGVRMKQ FIRLEPPYGH CRHGGEDAAT
FVYTGFQYSV EACHRSCAQK VIVEACGCAD PMYPVAEMFG NNTKPCQAVN MDQRECLRNT
TLWLGELYSK GKEAIIPDCY CHQPCQETNY EVTYSSARWP SGSAKVMECL PGDFLCLEKY
RKNAAMVQIF YEELNYETMQ ESPAYTLTSV LADLGGLTGL WIGASVVSLL EIVTLIVFAT
QAYVRKRKGS ISAQSHHSVP VHRASRVSLN TLHKSSTTQS VKLSVMDIRS IKSIHSNHSS
KSKQSILIED LPPAIQEQSD DEEETTESSR TNGSCRYLAP GEDLPCLCKY HPDGSIRIMK
ALCPVHGYMV RRNYDYSVSN SEEEDAEDEV HREPEPFYSA PYEHRKK
