SID1_CAEEL
ID SID1_CAEEL Reviewed; 776 AA.
AC Q9GZC8;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Systemic RNA interference defective protein 1;
DE AltName: Full=Systemic RNAi enabling protein;
DE Flags: Precursor;
GN Name=sid-1 {ECO:0000312|WormBase:C04F5.1};
GN Synonyms=rde-7 {ECO:0000312|WormBase:C04F5.1},
GN rsd-8 {ECO:0000312|WormBase:C04F5.1};
GN ORFNames=C04F5.1 {ECO:0000312|WormBase:C04F5.1};
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}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF PRO-199; SER-536 AND
RP ARG-565.
RC STRAIN=Bristol N2 {ECO:0000269|PubMed:11834782};
RX PubMed=11834782; DOI=10.1126/science.1068836;
RA Winston W.M., Molodowitch C., Hunter C.P.;
RT "Systemic RNAi in C. elegans requires the putative transmembrane protein
RT SID-1.";
RL Science 295:2456-2459(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=14738731; DOI=10.1016/j.cub.2003.12.029;
RA Tijsterman M., May R.C., Simmer F., Okihara K.L., Plasterk R.H.;
RT "Genes required for systemic RNA interference in Caenorhabditis elegans.";
RL Curr. Biol. 14:111-116(2004).
RN [3]
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 [4] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=12970568; DOI=10.1126/science.1087117;
RA Feinberg E.H., Hunter C.P.;
RT "Transport of dsRNA into cells by the transmembrane protein SID-1.";
RL Science 301:1545-1547(2003).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=17381285; DOI=10.1101/sqb.2006.71.060;
RA Hunter C.P., Winston W.M., Molodowitch C., Feinberg E.H., Shih J.,
RA Sutherlin M., Wright A.J., Fitzgerald M.C.;
RT "Systemic RNAi in Caenorhabditis elegans.";
RL Cold Spring Harb. Symp. Quant. Biol. 71:95-100(2006).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-290, 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 [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19168628; DOI=10.1073/pnas.0809760106;
RA Jose A.M., Smith J.J., Hunter C.P.;
RT "Export of RNA silencing from C. elegans tissues does not require the RNA
RT channel SID-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:2283-2288(2009).
RN [8]
RP FUNCTION, SUBUNIT, AND MUTAGENESIS OF SER-536.
RX PubMed=19155320; DOI=10.1261/rna.1286409;
RA Shih J.D., Fitzgerald M.C., Sutherlin M., Hunter C.P.;
RT "The SID-1 double-stranded RNA transporter is not selective for dsRNA
RT length.";
RL RNA 15:384-390(2009).
RN [9]
RP FUNCTION.
RX PubMed=20512143; DOI=10.1038/nmeth.1463;
RA Calixto A., Chelur D., Topalidou I., Chen X., Chalfie M.;
RT "Enhanced neuronal RNAi in C. elegans using SID-1.";
RL Nat. Methods 7:554-559(2010).
RN [10]
RP FUNCTION, AND MUTAGENESIS OF SER-536.
RX PubMed=21474576; DOI=10.1261/rna.2596511;
RA Shih J.D., Hunter C.P.;
RT "SID-1 is a dsRNA-selective dsRNA-gated channel.";
RL RNA 17:1057-1065(2011).
RN [11]
RP FUNCTION.
RX PubMed=22178129; DOI=10.1016/j.ibmb.2011.11.007;
RA Kobayashi I., Tsukioka H., Komoto N., Uchino K., Sezutsu H., Tamura T.,
RA Kusakabe T., Tomita S.;
RT "SID-1 protein of Caenorhabditis elegans mediates uptake of dsRNA into
RT Bombyx cells.";
RL Insect Biochem. Mol. Biol. 42:148-154(2012).
RN [12]
RP FUNCTION, AND MUTAGENESIS OF SER-536.
RX PubMed=22902558; DOI=10.1016/j.molcel.2012.07.014;
RA McEwan D.L., Weisman A.S., Hunter C.P.;
RT "Uptake of extracellular double-stranded RNA by SID-2.";
RL Mol. Cell 47:746-754(2012).
RN [13]
RP FUNCTION.
RX PubMed=22293577; DOI=10.4161/rna.9.1.18084;
RA Mon H., Kobayashi I., Ohkubo S., Tomita S., Lee J., Sezutsu H., Tamura T.,
RA Kusakabe T.;
RT "Effective RNA interference in cultured silkworm cells mediated by
RT overexpression of Caenorhabditis elegans SID-1.";
RL RNA Biol. 9:40-46(2012).
RN [14]
RP FUNCTION, AND MUTAGENESIS OF ALA-173 AND PRO-199.
RX PubMed=26067272; DOI=10.1074/jbc.m115.658864;
RA Li W., Koutmou K.S., Leahy D.J., Li M.;
RT "Systemic RNA interference deficiency-1 (SID-1) extracellular domain
RT selectively binds long double-stranded RNA and is required for RNA
RT transport by SID-1.";
RL J. Biol. Chem. 290:18904-18913(2015).
RN [15]
RP FUNCTION, AND MUTAGENESIS OF ASP-130.
RX PubMed=32908307; DOI=10.1038/s41586-020-2699-5;
RA Kaletsky R., Moore R.S., Vrla G.D., Parsons L.R., Gitai Z., Murphy C.T.;
RT "C. elegans interprets bacterial non-coding RNAs to learn pathogenic
RT avoidance.";
RL Nature 586:445-451(2020).
CC -!- FUNCTION: Plays a role in RNA-mediated gene silencing by acting cell-
CC autonomously as a channel for the transport of double-stranded RNA
CC (dsRNA) between cells. Mediates the spread of dsRNA and subsequent
CC silencing of genes in cells distant from the site of dsRNA
CC introduction. Selective for dsRNA. Preferentially binds long dsRNA,
CC from 50 base pairs up to 700. Short 20 base-pair long molecules are not
CC bound. May also bind dsDNA, but with lower affinity. Binding may be
CC sequence-independent (PubMed:26067272). Required for avoidance behavior
CC induced by small RNAs derived from pathogenic bacteria such as
CC P.aeruginosa (PubMed:32908307). {ECO:0000269|PubMed:11834782,
CC ECO:0000269|PubMed:12970568, ECO:0000269|PubMed:14738731,
CC ECO:0000269|PubMed:17381285, ECO:0000269|PubMed:19155320,
CC ECO:0000269|PubMed:19168628, ECO:0000269|PubMed:20512143,
CC ECO:0000269|PubMed:21474576, ECO:0000269|PubMed:22178129,
CC ECO:0000269|PubMed:22293577, ECO:0000269|PubMed:22902558,
CC ECO:0000269|PubMed:26067272, ECO:0000269|PubMed:32908307}.
CC -!- SUBUNIT: May self-associate to form multimers.
CC {ECO:0000269|PubMed:19155320}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11834782,
CC ECO:0000269|PubMed:12970568, ECO:0000269|PubMed:17381285}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:11834782,
CC ECO:0000269|PubMed:12970568, ECO:0000269|PubMed:17381285}.
CC Note=Enriched at the cell periphery and also to the punctate structures
CC of cytoplasm.
CC -!- TISSUE SPECIFICITY: Expressed in most non-neuronal cells, including
CC body wall muscle cells. {ECO:0000269|PubMed:11834782,
CC ECO:0000269|PubMed:17381285}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout all developmental stages.
CC {ECO:0000269|PubMed:11834782, ECO:0000269|PubMed:17381285}.
CC -!- DISRUPTION PHENOTYPE: Absence of silencing in adjacent cells or
CC tissues. Decrease in transgene silencing when combined with eri-1.
CC {ECO:0000269|PubMed:12970568, ECO:0000269|PubMed:19168628}.
CC -!- MISCELLANEOUS: This avoidance behavior is transgenerationally
CC inherited, and thus progeny display this same aversion despite never
CC been exposed to this pathogenic bacteria.
CC {ECO:0000269|PubMed:32908307}.
CC -!- SIMILARITY: Belongs to the SID1 family. {ECO:0000305}.
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DR EMBL; AF478687; AAL78657.1; -; mRNA.
DR EMBL; BX284605; CCD63011.1; -; Genomic_DNA.
DR RefSeq; NP_504372.2; NM_071971.6.
DR AlphaFoldDB; Q9GZC8; -.
DR STRING; 6239.C04F5.1; -.
DR TCDB; 1.A.79.1.1; the cholesterol uptake protein (chup) or double stranded rna uptake family.
DR iPTMnet; Q9GZC8; -.
DR EPD; Q9GZC8; -.
DR PaxDb; Q9GZC8; -.
DR EnsemblMetazoa; C04F5.1.1; C04F5.1.1; WBGene00004795.
DR GeneID; 178900; -.
DR KEGG; cel:CELE_C04F5.1; -.
DR UCSC; C04F5.1; c. elegans.
DR CTD; 178900; -.
DR WormBase; C04F5.1; CE30331; WBGene00004795; sid-1.
DR eggNOG; ENOG502QUXZ; Eukaryota.
DR GeneTree; ENSGT00390000010091; -.
DR HOGENOM; CLU_373491_0_0_1; -.
DR InParanoid; Q9GZC8; -.
DR OMA; MANRDEM; -.
DR OrthoDB; 139174at2759; -.
DR PhylomeDB; Q9GZC8; -.
DR PRO; PR:Q9GZC8; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00004795; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:WormBase.
DR GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:WormBase.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:WormBase.
DR GO; GO:0051033; F:RNA transmembrane transporter activity; IDA:WormBase.
DR GO; GO:0033227; P:dsRNA transport; IDA:WormBase.
DR GO; GO:0035194; P:post-transcriptional gene silencing by RNA; IDA:WormBase.
DR GO; GO:0050658; P:RNA transport; IBA:GO_Central.
DR InterPro; IPR025958; SID1_TM_fam.
DR PANTHER; PTHR12185; PTHR12185; 1.
DR Pfam; PF13965; SID-1_RNA_chan; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Membrane; Reference proteome; RNA-binding;
KW RNA-mediated gene silencing; Signal; Transmembrane; Transmembrane helix;
KW Transport.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..776
FT /note="Systemic RNA interference defective protein 1"
FT /id="PRO_0000032574"
FT TOPO_DOM 18..319
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 320..340
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 341..429
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 430..450
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 451..481
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 482..502
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 503..510
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 511..531
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 532..543
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 544..564
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 565..575
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 576..596
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 597..599
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 600..620
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 621..633
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 634..654
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 655..659
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 660..680
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 681..691
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 692..712
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 713..741
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 742..762
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 763..776
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 22..312
FT /note="Involved in dsRNA-binding"
FT /evidence="ECO:0000269|PubMed:26067272"
FT REGION 360..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 19
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 20
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 234
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 130
FT /note="D->N: In pk3321; defective avoidance behavior in
FT response to P.aeruginosa."
FT /evidence="ECO:0000269|PubMed:32908307"
FT MUTAGEN 173
FT /note="A->T: Loss of binding to shorter than 100 base-pair
FT long dsRNA and decreased affinity for longer RNA species.
FT Decreased RNA transport."
FT /evidence="ECO:0000269|PubMed:26067272"
FT MUTAGEN 199
FT /note="P->L: In qt10; Failure to spread gene silencing
FT signal. Loss of binding to shorter than 100 base-pair long
FT dsRNA and decreased affinity for longer RNA species.
FT Decreased RNA transport."
FT /evidence="ECO:0000269|PubMed:11834782,
FT ECO:0000269|PubMed:26067272"
FT MUTAGEN 536
FT /note="S->I: In qt2; Defective in dsRNA transport."
FT /evidence="ECO:0000269|PubMed:11834782,
FT ECO:0000269|PubMed:19155320, ECO:0000269|PubMed:21474576,
FT ECO:0000269|PubMed:22902558"
FT MUTAGEN 565
FT /note="R->C: In qt4; Failure to spread gene silencing
FT signal."
FT /evidence="ECO:0000269|PubMed:11834782"
SQ SEQUENCE 776 AA; 87931 MW; 0CCD247D9E3FB61B CRC64;
MIRVYLIILM HLVIGLTQNN STTPSPIITS SNSSVLVFEI SSKMKMIEKK LEANTVHVLR
LELDQSFILD LTKVAAEIVD SSKYSKEDGV ILEVTVSNGR DSFLLKLPTV YPNLKLYTDG
KLLNPLVEQD FGAHRKRHRI GDPHFHQNLI VTVQSRLNAD IDYRLHVTHL DRAQYDFLKF
KTGQTTKTLS NQKLTFVKPI GFFLNCSEQN ISQFHVTLYS EDDICANLIT VPANESIYDR
SVISDKTHNR RVLSFTKRAD IFFTETEISM FKSFRIFVFI APDDSGCSTN TSRKSFNEKK
KISFEFKKLE NQSYAVPTAL MMIFLTTPCL LFLPIVINII KNSRKLAPSQ SNLISFSPVP
SEQRDMDLSH DEQQNTSSEL ENNGEIPAAE NQIVEEITAE NQETSVEEGN REIQVKIPLK
QDSLSLHGQM LQYPVAIILP VLMHTAIEFH KWTTSTMANR DEMCFHNHAC ARPLGELRAW
NNIITNIGYT LYGAIFIVLS ICRRGRHEYS HVFGTYECTL LDVTIGVFMV LQSIASATYH
ICPSDVAFQF DTPCIQVICG LLMVRQWFVR HESPSPAYTN ILLVGVVSLN FLISAFSKTS
YVRFIIAVIH VIVVGSICLA KERSLGSEKL KTRFFIMAFS MGNFAAIVMY LTLSAFHLNQ
IATYCFIINC IMYLMYYGCM KVLHSERITS KAKLCGALSL LAWAVAGFFF FQDDTDWTRS
AAASRALNKP CLLLGFFGSH DLWHIFGALA GLFTFIFVSF VDDDLINTRK TSINIF
