SID3_CAEEL
ID SID3_CAEEL Reviewed; 1237 AA.
AC Q10925; Q7JP57; Q7JP58; Q7JP59; Q95ZZ7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Tyrosine-protein kinase sid-3;
DE EC=2.7.10.2;
DE AltName: Full=Systemic RNA interference defective protein 3;
DE AltName: Full=Systemic RNAi enabling protein;
GN Name=sid-3; ORFNames=B0302.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
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]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP DOMAIN, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLY-124; LYS-139 AND
RP ARG-353.
RX PubMed=22912399; DOI=10.1073/pnas.1201153109;
RA Jose A.M., Kim Y.A., Leal-Ekman S., Hunter C.P.;
RT "Conserved tyrosine kinase promotes the import of silencing RNA into
RT Caenorhabditis elegans cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:14520-14525(2012).
CC -!- FUNCTION: Tyrosine-protein kinase which plays a role in RNA-mediated
CC gene silencing by mediating import of double-stranded RNA (dsRNA) into
CC cells. Not required for import of ingested dsRNA into intestinal cells
CC but involved in subsequent export from intestinal cells to internal
CC tissues. {ECO:0000269|PubMed:22912399}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22912399}.
CC Note=Displays diffuse localization in cytoplasm and cytoplasmic foci,
CC and also in a punctate pattern.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=a;
CC IsoId=Q10925-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q10925-2; Sequence=VSP_004999;
CC Name=c;
CC IsoId=Q10925-3; Sequence=VSP_014534, VSP_014535;
CC -!- TISSUE SPECIFICITY: Ubiquitously present in all tissues tested.
CC Expressed in the somatic cells of gut, pharynx, body wall muscle,
CC neurons, skin and excretory canal cells. {ECO:0000269|PubMed:22912399}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout all developmental stages.
CC {ECO:0000269|PubMed:22912399}.
CC -!- DOMAIN: The kinase domain is required for import of dsRNA into cells.
CC {ECO:0000269|PubMed:22912399}.
CC -!- DISRUPTION PHENOTYPE: Defective in transport of silencing RNAs but not
CC defective in execution of RNAi. Marginal enhancement of cell-autonomous
CC RNAi. Mildly defective in silencing the intestine-expressed gene, act-
CC 5. {ECO:0000269|PubMed:22912399}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. SYK/ZAP-70 subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
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DR EMBL; FO080160; CCD61695.1; -; Genomic_DNA.
DR EMBL; FO080160; CCD61696.1; -; Genomic_DNA.
DR EMBL; FO080160; CCD61697.1; -; Genomic_DNA.
DR PIR; T15316; T15316.
DR RefSeq; NP_510783.2; NM_078382.6. [Q10925-1]
DR RefSeq; NP_510784.2; NM_078383.4. [Q10925-2]
DR AlphaFoldDB; Q10925; -.
DR SMR; Q10925; -.
DR BioGRID; 46633; 1.
DR STRING; 6239.B0302.1a.2; -.
DR iPTMnet; Q10925; -.
DR EPD; Q10925; -.
DR PaxDb; Q10925; -.
DR PeptideAtlas; Q10925; -.
DR EnsemblMetazoa; B0302.1a.1; B0302.1a.1; WBGene00002207. [Q10925-1]
DR EnsemblMetazoa; B0302.1b.1; B0302.1b.1; WBGene00002207. [Q10925-2]
DR GeneID; 181756; -.
DR KEGG; cel:CELE_B0302.1; -.
DR UCSC; B0302.1b; c. elegans. [Q10925-1]
DR CTD; 181756; -.
DR WormBase; B0302.1a; CE33506; WBGene00002207; sid-3. [Q10925-1]
DR WormBase; B0302.1b; CE33548; WBGene00002207; sid-3. [Q10925-2]
DR eggNOG; KOG0199; Eukaryota.
DR HOGENOM; CLU_009070_0_0_1; -.
DR InParanoid; Q10925; -.
DR OMA; FLESKHC; -.
DR OrthoDB; 254943at2759; -.
DR Reactome; R-CEL-8863795; Downregulation of ERBB2 signaling.
DR PRO; PR:Q10925; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00002207; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0035194; P:post-transcriptional gene silencing by RNA; IMP:WormBase.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR Gene3D; 4.10.680.10; -; 1.
DR InterPro; IPR015116; Cdc42-bd-like.
DR InterPro; IPR037085; Cdc42-bd-like_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR Pfam; PF09027; GTPase_binding; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF07653; SH3_2; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW Reference proteome; RNA-mediated gene silencing; SH3 domain; Transferase;
KW Tyrosine-protein kinase.
FT CHAIN 1..1237
FT /note="Tyrosine-protein kinase sid-3"
FT /id="PRO_0000088119"
FT DOMAIN 107..369
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 366..426
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 683..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 741..802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 826..919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 940..986
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 999..1018
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1134..1156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 747..790
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 826..868
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 879..910
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 230
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 113..121
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 139
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 107..211
FT /note="IKLYELIGEGSFAVVKRGTWTQSNGTHVNVAVKILRDISPNIMDDLRVEASH
FT LLKLQHPSLIRLYGIVRQPAMMVFELCEGGSLLDRLRDDKKAILLVSRLHDYC -> TL
FT HRSNSDRSHRHLFQRSNHNPFNTFRSLSNRNKFVYRHQQLPFRNQFKSQLLPIVMWHPQ
FT LHLKRLQMHAIRYLQKQAHQLATRLSQLLLFTRHQLLRHHQLRC (in isoform
FT c)"
FT /evidence="ECO:0000305"
FT /id="VSP_014534"
FT VAR_SEQ 212..1045
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_014535"
FT VAR_SEQ 482..588
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_004999"
FT MUTAGEN 124
FT /note="G->D: In qt32; induces defects in mobile RNA
FT silencing."
FT /evidence="ECO:0000269|PubMed:22912399"
FT MUTAGEN 139
FT /note="K->A: Failure to rescue silencing defect in sid-3
FT mutants."
FT /evidence="ECO:0000269|PubMed:22912399"
FT MUTAGEN 353
FT /note="R->Q: In qt38; induces defects in mobile RNA
FT silencing."
FT /evidence="ECO:0000269|PubMed:22912399"
SQ SEQUENCE 1237 AA; 134491 MW; 05531196D8F865CB CRC64;
MASTSGALVD DNVLEVLRKA QLDAFISQFV FLFNVRRFDH FSHVRDKDML EIGMQQVQIR
QLREQILKMS REMWNRSDPK QVYIQADQSM PAQNSIDEKA LIPNEQIKLY ELIGEGSFAV
VKRGTWTQSN GTHVNVAVKI LRDISPNIMD DLRVEASHLL KLQHPSLIRL YGIVRQPAMM
VFELCEGGSL LDRLRDDKKA ILLVSRLHDY CMQIAKALQF LESKHCVHRD VAARNILLAR
DERTVKICDF GLMRALKENE QMYTMAPQKK VPFAWCPPEA LRHRKFSHAS DVWSYGVTIW
EVFTFGEEPW VGCRAIDVLK NIDAGERLEK PKYCSERIYQ IMKNCWKFNP AERCKFGAIR
EDLVAAMFLD AVARETYNSI QPGALQLTKG DEVVVVENTG QDWFGQNKKN QKFGTFPRSV
VFAQTNNAVA AATAVTPQKV PTAPTIRIPP SHPPPAPLKP LNNNTKTSLN DRTSKISMPV
AGSFIHTGHG DPLGGQSWGN PATIADMYLK NPVNGAPLSS MSSGAEIIAS KELLTNGGRS
THQPAAPSPA VMSKIRGLSL DLPEYDDFDR AFDDGFSPSK IELPREFCGN DSVISGGSNS
IGLANTYVME PPKQAFDIRG NRVLPPTNKA PVLIPTNPAP SVISSTASAG ITLSTNSSQM
FTSQDRHSNM PANLFPELQH RLNQGSSTGN GVRPRPASSI GIQNNDLSML NPQVNRPFSV
VNVPIVQQPA NIPCLVPTPA PPAPAHFSQP VSSQRVAQQQ QNTLQKALND ELKGNLNKRP
TGTTAPPSNG FNAPRADVAP VQQRPISSAS IPALQPQPIQ HIQKPIQPQQ VRIPPSTAPV
QKPVQVSAPT HSNVAPTTSS QASADARNPL PPKTSPPVSN TPITVAPVHA APTTSAPSTS
VVTRRPTSTT AQMSDEERRS RIAMDISSAL PAPSALLYGS NSTSSLPSAA VSTASSVPST
ARDNPVETRP SQPHVTMPPK KSSEPILSSE VLQPTRLPSA TTSQAKPVTQ PIRHPSPPVA
TVIPTAVVDK KPVSQNQGSN VPLFNITNSS NGYPQLNGYP NYGNGFQAYG YGMNYHQGYP
GYQGYNSYGN GMGQLALTHN AVTSLPPLVP SENRFSGTAQ PLGESDIMEF LGTQQRQAGS
SSRAVPPASA STSAASGITD LSMADKMEVL YREADFTHKG NCDTMVSQCN GNTEQALKLL
KQQHLVDMEL AMSTETARQA LEARQYDLPA AANMLLG
