DUS11_CAEEL
ID DUS11_CAEEL Reviewed; 233 AA.
AC Q22707;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=RNA/RNP complex-1-interacting phosphatase homolog {ECO:0000305};
DE EC=3.1.3.- {ECO:0000269|PubMed:33378643};
DE AltName: Full=Dual specificity protein phosphatase 11 homolog {ECO:0000250|UniProtKB:O75319};
DE AltName: Full=Phosphatase interacting with RNA/RNP complex-1 {ECO:0000312|WormBase:T23G7.5a};
GN Name=pir-1 {ECO:0000312|WormBase:T23G7.5a};
GN ORFNames=T23G7.5 {ECO:0000312|WormBase:T23G7.5a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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, INTERACTION WITH DCR-1, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=16439208; DOI=10.1016/j.cell.2005.11.036;
RA Duchaine T.F., Wohlschlegel J.A., Kennedy S., Bei Y., Conte D. Jr.,
RA Pang K., Brownell D.R., Harding S., Mitani S., Ruvkun G., Yates J.R. III,
RA Mello C.C.;
RT "Functional proteomics reveals the biochemical niche of C. elegans DCR-1 in
RT multiple small-RNA-mediated pathways.";
RL Cell 124:343-354(2006).
RN [3]
RP FUNCTION, INTERACTION WITH DCR-1; RRF-3; ERI-1; DRH-3 AND RDE-8, CATALYTIC
RP ACTIVITY, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF
RP CYS-150.
RX PubMed=33378643; DOI=10.1016/j.molcel.2020.12.004;
RA Chaves D.A., Dai H., Li L., Moresco J.J., Oh M.E., Conte D. Jr.,
RA Yates J.R. III, Mello C.C., Gu W.;
RT "The RNA phosphatase PIR-1 regulates endogenous small RNA pathways in C.
RT elegans.";
RL Mol. Cell 0:0-0(2020).
CC -!- FUNCTION: RNA polyphosphatase which has RNA 5'-triphosphatase and
CC diphosphatase activities (PubMed:33378643). Displays poor protein-
CC tyrosine phosphatase activity (By similarity). Binds to 5'-
CC triphosphorylated RNAs (also called ppp-RNAs) (PubMed:33378643).
CC Dephosphorylates ppp-RNAs converting them to 5'-monophosphorylated RNAs
CC (also called p-RNAs) (PubMed:33378643). During small-RNA-mediated gene-
CC silencing or RNA interference (RNAi), involved in the dcr-1-mediated
CC processing of an amplified dsRNA intermediate (PubMed:16439208). This
CC is most likely in association with several components of the ERI/DICER
CC complex including dcr-1, eri-1 and rrf-3 (PubMed:33378643). Plays a
CC role in the biogenesis of 26G small interfering RNAs (26G-siRNAs),
CC which are a class of 26 nucleotide siRNAs that possess a guanine
CC residue at the 5'-end, by dephosphorylating 5'-triphosphorylated 26G-
CC siRNAs prior to their maturation by the ERI/DICER complex
CC (PubMed:33378643). Plays a role in the biogenesis of csr-1-bound 22G
CC small interfering RNAs (22G-siRNAs), which are a class of 22 nucleotide
CC siRNAs that possess a guanine residue at the 5'-end (PubMed:33378643).
CC Not required for the biogenesis of microRNAs (miRNA) or for the
CC biogenesis of a class of 21 nucleotide PIWI-interacting RNAs (piRNAs)
CC that possess a uracil residue at the 5'-end (also called 21U-RNAs)
CC (PubMed:33378643). {ECO:0000250|UniProtKB:O75319,
CC ECO:0000269|PubMed:16439208, ECO:0000269|PubMed:33378643}.
CC -!- SUBUNIT: Interacts with the ERI/DICER complex component dcr-1
CC (PubMed:16439208, PubMed:33378643). Interacts with ERI/DICER complex
CC components rrf-3 and isoform b of eri-1 (PubMed:33378643). Interacts
CC with drh-3 and rde-8 (PubMed:33378643). {ECO:0000269|PubMed:16439208,
CC ECO:0000269|PubMed:33378643}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:33378643}. Nucleus
CC {ECO:0000269|PubMed:33378643}.
CC -!- DEVELOPMENTAL STAGE: Expressed from embryogenesis to adulthood
CC (PubMed:33378643). Expressed in the germline and somatic cells of L4
CC stage larvae (PubMed:33378643). In the germline of L4 stage
CC hermaphrodites, uniformally expressed in germ cells from the
CC proliferative mitotic zone to the meiotic mid-pachytene region
CC (PubMed:33378643). Expression reduces in germ cells transitioning
CC through diplotene and meiosis I and II and increases again before cells
CC begin spermatogenesis (PubMed:33378643). During oogenesis, expressed in
CC the distal germline and through the bend in the ovotestis
CC (PubMed:33378643). Not expressed in maturing oocytes or the embryonic
CC germline (PubMed:33378643). Expressed in most somatic cells throughout
CC development, with high expression in intestinal cells
CC (PubMed:33378643). {ECO:0000269|PubMed:33378643}.
CC -!- DISRUPTION PHENOTYPE: Arrests at the L4 larval stage due to a failure
CC to undergo the L4 to adult molt. Sterile due to the lack of functional
CC gametes. In RNAi-mediated knockdown assays, fails to process dsRNA
CC which results in the accumulation of high molecular weight dsRNA-
CC derived RNA species. {ECO:0000269|PubMed:16439208}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class dual specificity subfamily. {ECO:0000305}.
CC -!- CAUTION: Two isoforms have been reported, however the molecular basis
CC and sequence differences have not been determined. Both isoforms
CC interact with components of the ERI/DICER complex and both are detected
CC at all larval and adult stages, but only pir-1b is expressed in embryos
CC (PubMed:33378643). Furthermore, pir-1a expression depends on drh-3
CC activity and pir-1b expression depends on dcr-1 activity
CC (PubMed:33378643). {ECO:0000269|PubMed:33378643,
CC ECO:0000305|PubMed:33378643}.
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DR EMBL; BX284602; CAA92703.2; -; Genomic_DNA.
DR PIR; T25206; T25206.
DR RefSeq; NP_495959.2; NM_063558.4.
DR AlphaFoldDB; Q22707; -.
DR SMR; Q22707; -.
DR DIP; DIP-35121N; -.
DR IntAct; Q22707; 2.
DR STRING; 6239.T23G7.5a.1; -.
DR EPD; Q22707; -.
DR PaxDb; Q22707; -.
DR PeptideAtlas; Q22707; -.
DR EnsemblMetazoa; T23G7.5a.1; T23G7.5a.1; WBGene00011967.
DR GeneID; 174460; -.
DR KEGG; cel:CELE_T23G7.5; -.
DR UCSC; T23G7.5a; c. elegans.
DR CTD; 174460; -.
DR WormBase; T23G7.5a; CE48135; WBGene00011967; pir-1.
DR eggNOG; KOG2386; Eukaryota.
DR GeneTree; ENSGT00940000168004; -.
DR HOGENOM; CLU_057587_3_0_1; -.
DR InParanoid; Q22707; -.
DR OMA; NTFKYYD; -.
DR OrthoDB; 1544021at2759; -.
DR PRO; PR:Q22707; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00011967; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004651; F:polynucleotide 5'-phosphatase activity; IBA:GO_Central.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0050355; F:triphosphatase activity; IDA:UniProtKB.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR Pfam; PF00782; DSPc; 1.
DR SMART; SM00195; DSPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Nucleus; Protein phosphatase; Reference proteome;
KW RNA-binding; RNA-mediated gene silencing.
FT CHAIN 1..233
FT /note="RNA/RNP complex-1-interacting phosphatase homolog"
FT /id="PRO_0000444001"
FT DOMAIN 34..206
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 150
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT ACT_SITE 156
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255"
FT BINDING 151..156
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O75319"
FT MUTAGEN 150
FT /note="C->S: In wg1000; catalytically inactive. Binds to
FT 5'-triphosphorylated RNAs, but does not convert them to 5'-
FT monophosphorylated RNAs. Reduces levels of 26G small
FT interfering RNAs (siRNAs), which are a classes of 26
FT nucleotide siRNAs that possess a guanine residue at the 5'-
FT end. Furthermore, 40% of the 26G-siRNAs present are 5'-
FT triphosphorylated."
FT /evidence="ECO:0000269|PubMed:33378643"
SQ SEQUENCE 233 AA; 27061 MW; 1677EE45A8263239 CRC64;
MSNYHHNHNY QHRPRGYERL PGKRLPDRWN IYDNVGRDID GTRFVPFKTP LDSSFFDGKN
MPVELQFGVK TLISLAQQAN KQIGLVIDLT NTDRYYKKTE WADHGVKYLK LNCPGHEVNE
REDLVQDFIN AVKEFVNDKE NDGKLIGVHC THGLNRTGYL ICRYMIDVDN YSASDAISMF
EYYRGHPMER EHYKKSLYEA ERKKKYGKSS GKSSGNSADS TISSEQLHRN NSQ
