DEL10_CAEEL
ID DEL10_CAEEL Reviewed; 1069 AA.
AC Q10025;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 5.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Degenerin-like protein del-10 {ECO:0000312|WormBase:T28D9.7};
GN Name=del-10 {ECO:0000312|WormBase:T28D9.7};
GN ORFNames=T28D9.7 {ECO:0000312|WormBase:T28D9.7};
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 [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 [2]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-216 AND ASN-374, IDENTIFICATION
RP BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:17761667}; Multi-
CC pass membrane protein {ECO:0000269|PubMed:17761667}.
CC -!- SIMILARITY: Belongs to the amiloride-sensitive sodium channel (TC
CC 1.A.6) family. {ECO:0000305}.
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DR EMBL; FO081595; CCD72711.1; -; Genomic_DNA.
DR PIR; T16948; T16948.
DR RefSeq; NP_495302.3; NM_062901.5.
DR AlphaFoldDB; Q10025; -.
DR STRING; 6239.T28D9.7; -.
DR iPTMnet; Q10025; -.
DR EPD; Q10025; -.
DR PaxDb; Q10025; -.
DR PeptideAtlas; Q10025; -.
DR PRIDE; Q10025; -.
DR EnsemblMetazoa; T28D9.7.1; T28D9.7.1; WBGene00020897.
DR GeneID; 174069; -.
DR KEGG; cel:CELE_T28D9.7; -.
DR UCSC; T28D9.7; c. elegans.
DR CTD; 174069; -.
DR WormBase; T28D9.7; CE41940; WBGene00020897; del-10.
DR eggNOG; KOG4294; Eukaryota.
DR GeneTree; ENSGT00940000160549; -.
DR HOGENOM; CLU_010323_0_0_1; -.
DR InParanoid; Q10025; -.
DR OMA; LCWAINT; -.
DR OrthoDB; 686369at2759; -.
DR Reactome; R-CEL-2672351; Stimuli-sensing channels.
DR PRO; PR:Q10025; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00020897; Expressed in larva and 2 other tissues.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0015280; F:ligand-gated sodium channel activity; IBA:GO_Central.
DR GO; GO:0035725; P:sodium ion transmembrane transport; IBA:GO_Central.
DR InterPro; IPR001873; ENaC.
DR PANTHER; PTHR11690; PTHR11690; 1.
DR Pfam; PF00858; ASC; 2.
DR PRINTS; PR01078; AMINACHANNEL.
PE 1: Evidence at protein level;
KW Glycoprotein; Ion channel; Ion transport; Membrane; Reference proteome;
KW Sodium; Sodium channel; Sodium transport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1069
FT /note="Degenerin-like protein del-10"
FT /evidence="ECO:0000305"
FT /id="PRO_0000181316"
FT TOPO_DOM 1..95
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 117..830
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 831..851
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 852..1069
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 898..948
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 960..1069
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 898..933
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 934..948
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1046..1069
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 216
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 374
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 454
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 539
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 545
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 584
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1069 AA; 123336 MW; 11E31AB5EDC07800 CRC64;
MVRMAERLAE NFIPEANQRN ENEPAYSRYK RVGQNRSRLN SRASLGSSMG RRITLIETDS
GVIEVESDKQ FLDAFKDANM DAVHHLNAAS PVTRGLWCMI IIAFVILVLV QCYSQIKLYI
SEPVATNIEA EYPSKISFPT VAICNNNQFR LTYLTGGRIM NRRSKSISGS LLSTGHDVES
VFDTVLRKSW DMDAVKFLRS AAHWKSRMIL GCTWPNGTSC KLSDFKAVWT TTGLCWAINT
DPHNPYEVTG SGEGHGLRLL LNVESYERVD ACTKHFRTKT LPGLKILIYN QTDIPDSSMN
GVNVPSGYSM DIPFKMQHRS KLTGVHCIEE NDEQIEASTD FNNPENIRTC TLRRYMTEVE
NSCHCTLRRA YTSNSTDVKM KACNVDQYFG CAQKAMQRIR EEGTASTCLP PCKSIDYTAW
QDMNRLPQNL MPALIEEQEE DDEDDVEQEE LDENVSFSTV SGGETFSCED SAYLDDKQVM
RIKRDAHRAY EMQARHQEDI FLRSRRLIAR LRNAINSIER YKWGWHYDTF SGVADRLSNL
TCFSNFSERH RDIISILESR PITSEEKKAN QMFFLLDETA FNRNATRYMS VGDLKSRYGD
KVDDVAEEIA VILRIMEKLW HVFMPDSYIR TMTGDFSRMD RIIELMNQYE LNKLQRRAWA
EKMQSRQMKH FFEDDFYESY YQPLIKDLDT TLVKQIDEVE ADWPKVEYYL QRGSAGKTGA
IMFFGDGNKD NRQKFEKLIV EMHECASGKM RKEAGKMLSS FKKSYRELQA AYGKLFKEEL
PDYLENFQFG NKFVGDNFAM VNIFLHRMNL EVWSQDRTYG FWSLACDIGG ALGLFLGASL
LTIIEIVYLC IQYGLCGKRA RNMKCIPMDA LTRQMKKVAT CSCCKKPIEK SREPIYKKKS
QSYQRRFTAD DEDQGDKFRS RASSEESKRR KNIWAQMNDP SGNSTLTPSE IKNFLDQVQR
NSQPPSYHDD HHPEDHYYYN DPNYLTISPP SDRPEDNREG STSGYYSSPR APPQANPRDE
SPIPDTEPIS VSEFSDALAP PLFKTPPRER RTRKEQKIDE EDDDKHSYV
